|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-252 |
3.61e-112 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 322.01 E-value: 3.61e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTGQ 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLIMIAKLRGVSNP--AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKeaRERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 164 GLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKEMFppakveyiekqptLEEIF 243
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL-------------LEDVF 227
|
....*....
gi 1256329087 244 LAIIGKKEE 252
Cdd:COG1131 228 LELTGEEAR 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-222 |
4.17e-94 |
|
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: 275.40 E-value: 4.17e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTGQ 85
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLIMIAKLRGVSNP--AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAerRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 164 GLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELK 222
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-223 |
1.42e-93 |
|
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: 277.35 E-value: 1.42e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 13 KSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTGQFAALDGM 92
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 93 LTGRENLIMIAKLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEAR 170
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEaeERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 171 IEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKR 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-222 |
4.98e-84 |
|
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: 250.11 E-value: 4.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKE--VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLT 83
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLIMIAKLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEP 161
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEikEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 162 TTGLDPEARIEVWDTVKELaGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELK 222
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-252 |
1.95e-80 |
|
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: 241.69 E-value: 1.95e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTGQ 85
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLIMIAKLRGVS--NPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFdeELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 164 GLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKEmfppakveyIEKQPTLEEIF 243
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE---------EIGEENLEDAF 232
|
....*....
gi 1256329087 244 LAIIGKKEE 252
Cdd:COG4555 233 VALIGSEEG 241
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-212 |
1.93e-78 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 234.21 E-value: 1.93e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTGQ 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLimiaklrgvsnpaqvadnllarfsltdaanqradQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGL 165
Cdd:cd03230 81 EPSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1256329087 166 DPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKI 212
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-223 |
3.02e-60 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 192.33 E-value: 3.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSI 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQFAALDGMLTGRENLIMIAKLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFL 158
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAarALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 159 DEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-231 |
2.18e-58 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 187.24 E-value: 2.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRqpdHVRQSIsltg 84
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP---EDRRRI---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 85 qfaaldGML----------TGRENLIMIAKLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGA 152
Cdd:COG4152 74 ------GYLpeerglypkmKVGEQLVYLARLKGLSKAEakRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 153 PAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKEMFPPAKVE 231
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLR 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-216 |
2.21e-58 |
|
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: 184.34 E-value: 2.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTgQ 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLIMIAKLRGVSNpaQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGL 165
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRK--KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 166 DPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:cd03268 158 DPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-216 |
1.62e-56 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 183.88 E-value: 1.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSI 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQFAALDGMLTGRENLIMIAKLRGVS--NPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFL 158
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYFGMStrEIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 159 DEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-216 |
8.75e-56 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 177.77 E-value: 8.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGeIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTGQ 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLIMIAKLRGVSN---PAQVaDNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSkevKARV-DEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 163 TGLDPEARIEVWDTVKELaGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:cd03264 159 AGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-191 |
4.50e-54 |
|
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: 173.05 E-value: 4.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 4 AAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLT 83
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLIMIAKLRGVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180
....*....|....*....|....*...
gi 1256329087 164 GLDPEARIEVWDTVKELAGSGTTILLTT 191
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARGGAVLLTT 188
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-223 |
1.54e-52 |
|
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: 170.55 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH----V 76
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyeL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 77 RQSISLTGQFAALDGMLTGREN----LIMIAKLrgvsNPAQV---ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSL 149
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENvafpLREHTDL----SEAEIrelVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 150 IGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-221 |
1.09e-51 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 168.28 E-value: 1.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 3 NAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRqsisl 82
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 83 tgqfaALDGM------------LTGRENLIMIAKLRGVSNPAQ--VADNLLARFSLTDAANQRADQYSGGMKRRLDIAMS 148
Cdd:COG1137 76 -----ARLGIgylpqeasifrkLTVEDNILAVLELRKLSKKEReeRLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 149 LIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-216 |
1.94e-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: 166.77 E-value: 1.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKE----VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSIS 81
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 82 LTGQFAALDGMLTGRENLIMIAKLRGVSNPAQVA--DNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLD 159
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTArlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 160 EPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-212 |
1.98e-50 |
|
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: 164.20 E-value: 1.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKD----KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH-----V 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 77 RQSISLTGQFAALDGMLTGRENLIMIAKLRGVSNP--AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPA 154
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKerRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 155 IIFLDEPTTGLDPEARIEVWDTVKELA-GSGTTILLTTQYLEEAEqLADRIAILHGGKI 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-222 |
3.51e-49 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 165.29 E-value: 3.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTttvnilstlmkQDGGEVSICGFDVQRQP----------D 74
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**-----------RGALPAHV*GPDAGRRPwrf*twcanrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 75 HVRQSISLTGQF-AALDGMLTGRENLIMIAKLRGVS--NPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIG 151
Cdd:NF000106 82 ALRRTIG*HRPVr*GRRESFSGRENLYMIGR*LDLSrkDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 152 APAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELK 222
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-230 |
5.98e-49 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 163.72 E-value: 5.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 7 SIKGL-KKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFD-VQRQPDHVRQsISL-T 83
Cdd:COG4586 23 ALKGLfRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpFKRRKEFARR-IGVvF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLIMIAKLRGVsnPAQVADNLLARFS----LTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLD 159
Cdd:COG4586 102 GQRSQLWWDLPAIDSFRLLKAIYRI--PDAEYKKRLDELVelldLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 160 EPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKEMFPPAKV 230
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKT 251
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-223 |
6.33e-49 |
|
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: 160.79 E-value: 6.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH--VRQSISLT 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHkrARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLIMIAKLRGVSNPAQV--ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEP 161
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREekLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 162 TTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-220 |
8.16e-49 |
|
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: 160.68 E-value: 8.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH--VRQSISLT 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHeiARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLIMIAKLRGVSNPAQV------------ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIG 151
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLArarreerearerAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 152 APAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAE 220
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-223 |
1.20e-48 |
|
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: 159.91 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH--VRQSISLT 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHerARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLIMIAKLRGVSNPAQVADNLLARFS-LTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPrLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 163 TGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-216 |
4.03e-48 |
|
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: 158.07 E-value: 4.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRqSISLTGQ 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR-NIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLIMIAKLRGVSNP--AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAeiRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 164 GLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:cd03259 160 ALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-216 |
1.18e-47 |
|
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: 157.06 E-value: 1.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQrqpDHVRQSISLTGQ 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLIMIAKLRGV--SNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLkkEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 164 GLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-222 |
3.31e-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: 156.51 E-value: 3.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR----QPDHVRQSIS 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 82 LTGQFAALDGMLTGRENLIMiaKLRGVSN-PAQVADNL----LARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAII 156
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF--PLREHTRlSEEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 157 FLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELK 222
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-221 |
8.25e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 155.18 E-value: 8.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKD-KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVRQSISLT 83
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKkNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAalDGMLTGR----------ENLimiaklrGVSnPAQV---ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLI 150
Cdd:COG1122 81 FQNP--DDQLFAPtveedvafgpENL-------GLP-REEIrerVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 151 GAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-221 |
1.05e-46 |
|
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: 155.51 E-value: 1.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQS--ISLT 83
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARlgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLIMIAKLRGVSNPAQV---ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDE 160
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRKDLDRAEReerLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 161 PTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-220 |
6.40e-46 |
|
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: 154.04 E-value: 6.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 2 SNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH--VRQS 79
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHriARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 80 ISLTGQFAALDGMLTGRENLIMIAKLRGVSNPAQV-----------------ADNLLARFSLTDAANQRADQYSGGMKRR 142
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGLLAAllrlprarreerearerAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 143 LDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTtqyleeaE-------QLADRIAILHGGKIIT 214
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLI-------EhdmdlvmGLADRIVVLDFGRVIA 233
|
....*.
gi 1256329087 215 TGTLAE 220
Cdd:COG0411 234 EGTPAE 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-213 |
1.86e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 151.73 E-value: 1.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 3 NAAISIKGLKKSFKDKE----VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHV-- 76
Cdd:COG1136 2 SPLLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 77 ---RQSISLTGQFAALDGMLTGRENLIMIAKLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIG 151
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKErrERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 152 APAIIFLDEPTTGLDPEARIEVWDTVKELA-GSGTTILLTTQYLEEAEQlADRIAILHGGKII 213
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAAR-ADRVIRLRDGRIV 223
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
8-248 |
1.95e-45 |
|
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: 151.78 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 8 IKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHvrqSISLTGQFA 87
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLH---KIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 88 ALDGMLTGRENLIMIAKLRGVsnPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDP 167
Cdd:TIGR03740 80 PLYENLTARENLKVHTTLLGL--PDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 168 EARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTlaelkemfppakveyIEKQPTLEEIFLAII 247
Cdd:TIGR03740 158 IGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGK---------------INKSENLEKLFVEVV 222
|
.
gi 1256329087 248 G 248
Cdd:TIGR03740 223 K 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-221 |
2.02e-45 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 152.07 E-value: 2.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV---QRQPDHVRQSIsl 82
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdsKKDINKLRRKV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 83 tgqfaaldGM----------LTGRENlIMIA--KLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMS 148
Cdd:COG1126 80 --------GMvfqqfnlfphLTVLEN-VTLApiKVKKMSKAEaeERAMELLERVGLADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 149 LIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-221 |
2.23e-45 |
|
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: 152.51 E-value: 2.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPD-HVRQSISLT 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLIM--IAKLRGVSNPA----QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIF 157
Cdd:COG1120 81 PQEPPAPFGLTVRELVALgrYPHLGLFGRPSaedrEAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 158 LDEPTTGLDPEARIEVWDTVKELA-GSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-223 |
4.88e-45 |
|
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: 150.90 E-value: 4.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 7 SIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH--VRQSISLTG 84
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriARLGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 85 Q----FAAldgmLTGRENLIMIAKLR-GVSNPAQVADNLLARF-SLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFL 158
Cdd:COG0410 85 EgrriFPS----LTVEENLLLGAYARrDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 159 DEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-211 |
8.80e-44 |
|
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: 145.08 E-value: 8.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 7 SIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH-VRQSISLTGQ 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEeLRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FaaldgmltgrenlimiaklrgvsnpaqvadnllarfsltdaanqradqySGGMKRRLDIAMSLIGAPAIIFLDEPTTGL 165
Cdd:cd00267 81 L-------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1256329087 166 DPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGK 211
Cdd:cd00267 112 DPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-225 |
1.19e-43 |
|
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: 157.48 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 28 VQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTGQFAALDGMLTGRENLIMIAKLRG 107
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 108 VsnPAQ----VADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS 183
Cdd:TIGR01257 2042 V--PAEeiekVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE 2119
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1256329087 184 GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKEMF 225
Cdd:TIGR01257 2120 GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKF 2161
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-211 |
4.75e-43 |
|
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: 144.92 E-value: 4.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 7 SIKGLKKSFKDKE--VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH-VRQSISLT 83
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKeLRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAalDGMLTG---RENLIMIAKLRGVSNP--AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFL 158
Cdd:cd03225 81 FQNP--DDQFFGptvEEEVAFGLENLGLPEEeiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 159 DEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGK 211
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-216 |
5.52e-43 |
|
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: 145.34 E-value: 5.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDK----EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV----QRQPDHVR 77
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQ--FAALDGMLTGRENLIMIAKLRGVSNPAQ----VADNLLARFSLTDA-ANQRADQYSGGMKRRLDIAMSLI 150
Cdd:cd03257 82 KEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEarkeAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 151 GAPAIIFLDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-212 |
2.76e-42 |
|
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: 143.05 E-value: 2.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV---QRQPDHVRQSISL 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 83 TGQFAALDGMLTGRENlIMIA--KLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFL 158
Cdd:cd03262 81 VFQQFNLFPHLTVLEN-ITLApiKVKGMSKAEaeERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 159 DEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKI 212
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-216 |
3.05e-42 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 144.01 E-value: 3.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 7 SIKGL-KKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFD-VQRQPDHVRQSISLTG 84
Cdd:cd03267 22 SLKSLfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpWKRRKKFLRRIGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 85 QFAALDGMLTGRENLIMIAKLRGVSnPAQVADNlLARFS----LTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDE 160
Cdd:cd03267 102 QKTQLWWDLPVIDSFYLLAAIYDLP-PARFKKR-LDELSelldLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 161 PTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-221 |
1.21e-41 |
|
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: 148.90 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 3 NAAISIKGLKKSF--KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDG---GEVSICGFDVQRQPDHVR 77
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 -QSISLTGQ--FAALDGmLTGRENLIMIAKLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGA 152
Cdd:COG1123 82 gRRIGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEarARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 153 PAIIFLDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-221 |
1.58e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 145.24 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQsI 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRN-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQFAALDGMLTGRENlimIA---KLRGVSNP--AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAI 155
Cdd:COG3842 80 GMVFQDYALFPHLTVAEN---VAfglRMRGVPKAeiRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 156 IFLDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-216 |
3.30e-40 |
|
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: 136.80 E-value: 3.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 7 SIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRqpdhvrqsisltgqf 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 87 aaldgmLTGREnlimIAKLRGVSnpAQVadnlLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLD 166
Cdd:cd03214 66 ------LSPKE----LARKIAYV--PQA----LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 167 PEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:cd03214 130 IAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-215 |
3.87e-40 |
|
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: 137.99 E-value: 3.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDK----EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHvrqsIS 81
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD----RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 82 LTGQFAALDGMLTGRENLIMIAKLRGVSNP--AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLD 159
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAeaRERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 160 EPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHG--GKIITT 215
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-213 |
5.88e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 138.68 E-value: 5.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSF----KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHV 76
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 77 R---QSISLtgqfaaldgM--LTGRENLIMIAKLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSL 149
Cdd:COG1116 83 GvvfQEPAL---------LpwLTVLDNVALGLELRGVPKAErrERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 150 IGAPAIIFLDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAIL--HGGKII 213
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIV 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-245 |
5.91e-40 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 146.81 E-value: 5.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG-------FDVQRQPDHVR 77
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpvdagdIATRRRVGYMS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQfaaldgmLTGRENLIMIAKLRGVSnPAQVA---DNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPA 154
Cdd:NF033858 346 QAFSLYGE-------LTVRQNLELHARLFHLP-AAEIAarvAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 155 IIFLDEPTTGLDPEARIEVWDTVKELA-GSGTTILLTTQYLEEAEQlADRIAILHGGKIITTGTLAELKEMFppakveyi 233
Cdd:NF033858 418 LLILDEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAAR-------- 488
|
250
....*....|..
gi 1256329087 234 eKQPTLEEIFLA 245
Cdd:NF033858 489 -GAATLEEAFIA 499
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
5.99e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 138.30 E-value: 5.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH---VR 77
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigyVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQFAA--LDGMLTGRenLIMIAKLRGVSNPA-QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPA 154
Cdd:COG1121 82 QRAEVDWDFPItvRDVVLMGR--YGRRGLFRRPSRADrEAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 155 IIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKI 212
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-221 |
1.17e-39 |
|
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: 143.51 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSF-----KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV----QRQPDHV 76
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklsRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 77 RQSISLTGQ--FAALDGMLTGRENLIMIAKLRGVSNPAQV---ADNLLARFSL-TDAANQRADQYSGGMKRRLDIAMSLI 150
Cdd:COG1123 341 RRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERrerVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 151 GAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-211 |
7.73e-39 |
|
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: 133.08 E-value: 7.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHV---RQSISL 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 83 TGQFAALDGMLTGRENLimiaklrgvsnpaqvadnllaRFSLtdaanqradqySGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:cd03229 81 VFQDFALFPHLTVLENI---------------------ALGL-----------SGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1256329087 163 TGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGK 211
Cdd:cd03229 129 SALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-225 |
9.60e-39 |
|
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: 143.62 E-value: 9.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFK--DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISL 82
Cdd:TIGR01257 928 GVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 83 TGQFAALDGMLTGRENLIMIAKLRGVS-NPAQVA-DNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDE 160
Cdd:TIGR01257 1008 CPQHNILFHHLTVAEHILFYAQLKGRSwEEAQLEmEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 161 PTTGLDPEARIEVWDTVKELAgSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKEMF 225
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCF 1151
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-225 |
9.53e-38 |
|
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: 132.62 E-value: 9.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSF----KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPD-HVRQS 79
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 80 ISLTGQ--FAALDGMLTGRENLIMIAKLRGVSNPAQVADNLLARFSLTDA-ANQRADQYSGGMKRRLDIAMSLIGAPAII 156
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPELL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 157 FLDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKEMF 225
Cdd:COG1124 161 LLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-223 |
9.89e-38 |
|
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: 132.31 E-value: 9.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKD-KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH----VR--- 77
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqLRrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 ----QSISLTGQFAALDGMLTGRenLIMIAKLRGVSNP-----AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMS 148
Cdd:cd03256 81 gmifQQFNLIERLSVLENVLSGR--LGRRSTWRSLFGLfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 149 LIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
1.09e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 132.49 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 4 AAISIKGLKKSFK-DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQ----RQPDHVR- 77
Cdd:COG3638 1 PMLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTalrgRALRRLRr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 ------QSISLTGQFAALDGMLTGRenLIMIAKLRGVSN---PAQV--ADNLLARFSLTDAANQRADQYSGGMKRRLDIA 146
Cdd:COG3638 81 rigmifQQFNLVPRLSVLTNVLAGR--LGRTSTWRSLLGlfpPEDRerALEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 147 MSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-216 |
3.26e-37 |
|
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: 130.47 E-value: 3.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 12 KKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDG---GEVSICGfdVQRQPDHVRQSISLTGQFAA 88
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNG--QPRKPDQFQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 89 LDGMLTGRENLIMIAKLRG--VSNPAQ----VADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:cd03234 92 LLPGLTVRETLTYTAILRLprKSSDAIrkkrVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 163 TGLDPEARIEVWDTVKELAGSGTTILLTT-QYLEEAEQLADRIAILHGGKIITTG 216
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIhQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-163 |
1.60e-36 |
|
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: 126.22 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQP-DHVRQSISLTGQFAALDGMLTGRENL 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 100 IMIAKLRGVSNPA--QVADNLLARFSLTDAANQRAD----QYSGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:pfam00005 81 RLGLLLKGLSKREkdARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-212 |
1.69e-36 |
|
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: 128.42 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 7 SIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH---VRQSISLT 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigyVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQF--AALDGMLTGRenLIMIAKLRGVSNPA-QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDE 160
Cdd:cd03235 81 RDFpiSVRDVVLMGL--YGHKGLFRRLSKADkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 161 PTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKI 212
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-223 |
4.40e-36 |
|
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: 128.18 E-value: 4.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSF-KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH----VRQSI 80
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrkLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQFAALDGMLTGRENLIM--------IAKLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLI 150
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHgrlgykptWRSLLGRFSEEdkERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 151 GAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-221 |
6.27e-36 |
|
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: 129.79 E-value: 6.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKE----VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMK---QDGGEVSICGFDV----QRQPD 74
Cdd:COG0444 2 LEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLlklsEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 75 HVR-QSISLTGQ--FAALDGMLTGRENLIMIAKLRGVSNPAQV---ADNLLARFSLTDAAnQRADQY----SGGMKRRLD 144
Cdd:COG0444 82 KIRgREIQMIFQdpMTSLNPVMTVGDQIAEPLRIHGGLSKAEArerAIELLERVGLPDPE-RRLDRYphelSGGMRQRVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 145 IAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-221 |
1.29e-35 |
|
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: 126.54 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDK----EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPD----HVR 77
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQFAALDGMLTGRENL---IMIAKLRGVSNPAQVADnLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPA 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENValpLEIAGVPKAEIEERVLE-LLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 155 IIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-215 |
1.71e-35 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 124.08 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRqpdhvrqsisltgq 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 faaldgmltgrenlimiaklrgvSNPAQVADNLLARFSltdaanqradQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGL 165
Cdd:cd03216 67 -----------------------ASPRDARRAGIAMVY----------QLSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1256329087 166 DPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITT 215
Cdd:cd03216 114 TPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-212 |
3.16e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 124.93 E-value: 3.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVRQSISLTG 84
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 85 QFAALDGMlTGRENLIMIAKLRGVSNPAQVADNLLARFSLT-DAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1256329087 164 GLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKI 212
Cdd:COG4619 160 ALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-221 |
4.24e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 128.27 E-value: 4.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 4 AAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRqSISLT 83
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR-NIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAAL-DGMlTGRENlimIA---KLRGVSnPAQVA---DNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAII 156
Cdd:COG3839 81 FQSYALyPHM-TVYEN---IAfplKLRKVP-KAEIDrrvREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 157 FLDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-217 |
8.17e-35 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 124.74 E-value: 8.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG--FDVQRQPD-----HVR 77
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSdkairELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQFAALDGMLTGRENLIMI-AKLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPA 154
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQalARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 155 IIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGT 217
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-216 |
3.98e-34 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 122.67 E-value: 3.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTT---TVNILSTLMKQ--DGGEVSICG---FDVQRQPDHVR 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIPGapDEGEVLLDGkdiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQFAALDGMlTGRENLIMIAKLRGVSNPAQVAD---NLLARFSLTDAANQRADQY--SGGMKRRLDIAMSLIGA 152
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEELDErveEALRKAALWDEVKDRLHALglSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 153 PAIIFLDEPTTGLDPEARIEVWDTVKELAGSgTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-224 |
1.40e-33 |
|
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: 121.19 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQsISLTGQ 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP-VNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLIMIAKLRGVSNP---AQVADnLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAeikERVAE-ALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 163 TGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKEM 224
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-221 |
1.99e-33 |
|
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: 121.77 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKE--VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVqRQPDHV---RQSI 80
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT-LDEENLweiRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SL-----TGQFAAL---DGMLTGRENLimiaklrGVSNP--AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLI 150
Cdd:TIGR04520 80 GMvfqnpDNQFVGAtveDDVAFGLENL-------GVPREemRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 151 GAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQlADRIAILHGGKIITTGTLAEL 221
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREI 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-228 |
5.42e-33 |
|
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: 120.10 E-value: 5.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKD-KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQ-PDHVRQSISLT 83
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLIMIAKLRGVSNP--AQVADNLLARFSLTDA--ANQRADQYSGGMKRRLDIAMSLIGAPAIIFLD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEkiRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 160 EPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELkeMFPPA 228
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI--LRSPA 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-219 |
7.05e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 119.73 E-value: 7.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG--FDVQRQPDH-----VR 77
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDFSQKPSEkairlLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQFAALDGMLTGRENLIMI-AKLRGVSNPAQV--ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPA 154
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQARekAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 155 IIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLA 219
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-221 |
9.96e-33 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 119.42 E-value: 9.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 3 NAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQ-DGGEVSICGF-----DVQRqpdhV 76
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGErrggeDVWE----L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 77 RQSI-----SLTGQFA----ALDGMLTGRENLIMIAklRGVSnPAQV--ADNLLARFSLTDAANQRADQYSGGMKRRLDI 145
Cdd:COG1119 77 RKRIglvspALQLRFPrdetVLDVVLSGFFDSIGLY--REPT-DEQRerARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 146 AMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSG-TTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
24-221 |
1.21e-32 |
|
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: 119.67 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 24 VDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHV-----RQSISLTGQFAALDGMLTGREN 98
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrRKKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 99 LIMIAKLRGVS--NPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDT 176
Cdd:cd03294 123 VAFGLEVQGVPraEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1256329087 177 VKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:cd03294 203 LLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-225 |
2.44e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 118.70 E-value: 2.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 4 AAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV---------QRQPD 74
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqqKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 75 HVRQSISLTGQFAALDGMLTGRENLI---MIAKLRGVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIG 151
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIegpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 152 APAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGtlaELKEMF 225
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG---PAKALF 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-221 |
3.40e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 120.18 E-value: 3.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDK----EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH----VR 77
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelraAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQFAALDGMLTGRENlimIA---KLRGVSNP--AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGA 152
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAEN---VAlplEIAGVPKAeiRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 153 PAIIFLDEPTTGLDPE---------ARIEvwdtvKELagsGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG1135 159 PKVLLCDEATSALDPEttrsildllKDIN-----REL---GLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-211 |
4.31e-32 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 115.56 E-value: 4.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLkkSF----KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVRQSI 80
Cdd:cd03228 1 IEFKNV--SFsypgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQFAAL-DGMltgrenlimiaklrgvsnpaqVADNLLarfsltdaanqradqySGGMKRRLDIAMSLIGAPAIIFLD 159
Cdd:cd03228 79 AYVPQDPFLfSGT---------------------IRENIL----------------SGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 160 EPTTGLDPEARIEVWDTVKELAGsGTTILLTTQYLEEAEQlADRIAILHGGK 211
Cdd:cd03228 122 EATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-213 |
4.62e-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: 116.11 E-value: 4.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 12 KKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILS--TLMKQDGGEVSICGFdvQRQPDHVRQSISLTGQFAAL 89
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGR--PLDKRSFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 90 DGMLTGRENLIMIAKLRGVSnpaqvadnllarfsltdaanqradqysGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEA 169
Cdd:cd03213 94 HPTLTVRETLMFAAKLRGLS---------------------------GGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1256329087 170 RIEVWDTVKELAGSGTTILLTT-QYLEEAEQLADRIAILHGGKII 213
Cdd:cd03213 147 ALQVMSLLRRLADTGRTIICSIhQPSSEIFELFDKLLLLSQGRVI 191
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-213 |
7.88e-32 |
|
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: 115.82 E-value: 7.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 7 SIKGLKKSFKDK-EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGfdVQRQPDHVRQSISLTGQ 85
Cdd:cd03226 1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG--KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 faALDGMLTG---RENLIMIAKLrgVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:cd03226 79 --DVDYQLFTdsvREELLLGLKE--LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 163 TGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKII 213
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-221 |
5.19e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 119.35 E-value: 5.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 2 SNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGfdVQRQPDHVRQS-- 79
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG--EPVRFRSPRDAqa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 80 --ISLTGQFAALDGMLTGRENlIMIAKL---RGVSNPAQV---ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIG 151
Cdd:COG1129 79 agIAIIHQELNLVPNLSVAEN-IFLGREprrGGLIDWRAMrrrARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 152 APAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-213 |
6.22e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 113.99 E-value: 6.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFK-DKEVLKGVDFEVQRGEIFALLGSNGAGKTTtvnILSTLMKQ---DGGEVSICGFDVQRQPD----HVR 77
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKST---LLKLLYGEerpTSGQVLVNGQDLSRLKRreipYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSIsltgqfaaldGM-------LTGR---ENLIMIAKLRGVSnPAQVADN---LLARFSLTDAANQRADQYSGGMKRRLD 144
Cdd:COG2884 79 RRI----------GVvfqdfrlLPDRtvyENVALPLRVTGKS-RKEIRRRvreVLDLVGLSDKAKALPHELSGGEQQRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 145 IAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKII 213
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-221 |
7.44e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.42 E-value: 7.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV---QRQPDHVRQSISL 82
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 83 TGQFAALDGMLTGRENlIMIA--KLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFL 158
Cdd:PRK09493 82 VFQQFYLFPHLTALEN-VMFGplRVRGASKEEaeKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 159 DEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-221 |
8.83e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 116.78 E-value: 8.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSnaaISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQpDHVRQS- 79
Cdd:COG1118 1 MS---IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN-LPPRERr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 80 ISLTGQFAALDGMLTGRENlimIA---KLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPA 154
Cdd:COG1118 77 VGFVFQHYALFPHMTVAEN---IAfglRVRPPSKAEirARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 155 IIFLDEPTTGLDPEAR--IEVW--DTVKELagsGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG1118 154 VLLLDEPFGALDAKVRkeLRRWlrRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-224 |
9.21e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.98 E-value: 9.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGfdvqrqpdhvrQSI 80
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-----------KPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQFAALD---GM----------LTGRENLI--MIAKLRGVSNPAQVA---DNLLARFSLTDAANQRADQYSGGMKRR 142
Cdd:COG3845 70 RIRSPRDAIAlgiGMvhqhfmlvpnLTVAENIVlgLEPTKGGRLDRKAARariRELSERYGLDVDPDAKVEDLSVGEQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 143 LDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTG-----T 217
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVdtaetS 229
|
....*..
gi 1256329087 218 LAELKEM 224
Cdd:COG3845 230 EEELAEL 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-221 |
1.39e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 113.84 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 4 AAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH--VRQSIS 81
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHarARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 82 LTGQFAALDGMLTGRENLIMIAKLRGVSNPAQV---ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFL 158
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQRedrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 159 DEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-222 |
2.15e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 113.55 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH--VRQ 78
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqiARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 79 SISLTGQFAALDGMLTGRENLiMIAKLRGVSN---------PA---------QVADNLLARFSLTDAANQRADQYSGGMK 140
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENL-LVAQHQQLKTglfsgllktPAfrraesealDRAATWLERVGLLEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 141 RRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLA 219
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239
|
...
gi 1256329087 220 ELK 222
Cdd:PRK11300 240 EIR 242
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-216 |
4.85e-30 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 111.58 E-value: 4.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRqSISLTGQ 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR-DIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLIMIAKLRGVSNPA------QVADNLlarfSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLD 159
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEidervrEVAELL----QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 160 EPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-221 |
6.10e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.19 E-value: 6.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKE--VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGF--------DVQ 70
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 71 RQ-------PDHvrQSISLTGQfaalDGMLTGRENlimiaklRGVSNPAQV--ADNLLARFSLTDAANQRADQYSGGMKR 141
Cdd:PRK13635 81 RQvgmvfqnPDN--QFVGATVQ----DDVAFGLEN-------IGVPREEMVerVDQALRQVGMEDFLNREPHRLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 142 RLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQlADRIAILHGGKIITTGTLAE 220
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEE 226
|
.
gi 1256329087 221 L 221
Cdd:PRK13635 227 I 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-223 |
1.20e-29 |
|
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: 116.86 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLkkSFK----DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVRQS 79
Cdd:COG2274 473 DIELENV--SFRypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 80 ISLTGQfaalDGML---TGRENLIM------IAKLRGVsnpAQVADnllarfsLTDAANQRADQY-----------SGGM 139
Cdd:COG2274 551 IGVVLQ----DVFLfsgTIRENITLgdpdatDEEIIEA---ARLAG-------LHDFIEALPMGYdtvvgeggsnlSGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 140 KRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGsGTTILLTTQYLEEAeQLADRIAILHGGKIITTGTLA 219
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHE 694
|
....
gi 1256329087 220 ELKE 223
Cdd:COG2274 695 ELLA 698
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-216 |
1.95e-29 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 110.31 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGfdvqrqpdhvrQSISLTGQ 85
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----------RVSSLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLIMIAKLRGVSNP--AQVADNLLArFS-LTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:cd03220 92 GGGFNPELTGRENIYLNGRLLGLSRKeiDEKIDEIIE-FSeLGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 163 TGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-220 |
3.40e-29 |
|
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: 110.12 E-value: 3.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEvLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQsISLTGQ 85
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD-ISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLIMIAKLRGVSNP---AQVaDNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKeieRKV-LEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 163 TGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAE 220
Cdd:cd03299 158 SALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-223 |
3.75e-29 |
|
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: 109.74 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQsISLTG 84
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN-VGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 85 QFAALDGMLTGRENL---IMIAKLRGVSNPAQV---ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFL 158
Cdd:cd03296 81 QHYALFRHMTVFDNVafgLRVKPRSERPPEAEIrakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 159 DEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-225 |
6.85e-29 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 114.37 E-value: 6.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 18 KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQD---GGEVSICGFDVQRQPDHVRQSISLtgQFAALDGMLT 94
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISAYVQ--QDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 95 GRENLIMIAKLRGVSNPAQV-----ADNLLARFSLTDAANQRADQ------YSGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKKekrerVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 164 GLDPEARIEVWDTVKELAGSGTTILLTT-QYLEEAEQLADRIAILHGGKIITTGTLAELKEMF 225
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIhQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFF 258
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-212 |
8.65e-29 |
|
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: 107.13 E-value: 8.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 4 AAISIKGLkkSFKDKevLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRqpDHVRQSISLT 83
Cdd:cd03215 3 PVLEVRGL--SVKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR--RSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDgmltgRenlimiaKLRGVSNPAQVADNLLARFSLtdaanqradqySGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:cd03215 77 IAYVPED-----R-------KREGLVLDLSVAENIALSSLL-----------SGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1256329087 164 GLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKI 212
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-220 |
1.71e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 108.66 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH--------VR 77
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarrravLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQFAALDGMLTGRenlimIAKLRGVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLI------- 150
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGR-----APHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 151 GAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTIL-------LTTQYleeaeqlADRIAILHGGKIITTGTLAE 220
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVavlhdlnLAAQY-------ADRILLLHQGRLVAQGTPEE 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-217 |
2.03e-28 |
|
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: 107.90 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKE----VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV------Q 70
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldedA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 71 R---QPDH---VRQSisltgqFAALDGMlTGRENLIMIAKLRGVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLD 144
Cdd:COG4181 84 RarlRARHvgfVFQS------FQLLPTL-TALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 145 IAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQlADRIAILHGGKIITTGT 217
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTA 229
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-221 |
4.98e-28 |
|
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: 107.92 E-value: 4.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 18 KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPD----HVRQSISLTGQFAA----- 88
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkklkDLRKKVGLVFQFPEhqlfe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 89 ---LDGMLTGRENL---------IMIAKLRGVSNPAQVADnllaR--FSLtdaanqradqySGGMKRRLDIAMSLIGAPA 154
Cdd:TIGR04521 98 etvYKDIAFGPKNLglseeeaeeRVKEALELVGLDEEYLE----RspFEL-----------SGGQMRRVAIAGVLAMEPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 155 IIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:TIGR04521 163 VLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-223 |
5.40e-28 |
|
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: 111.78 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 4 AAISIKGLkkSFK----DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVRQ 78
Cdd:COG4987 332 PSLELEDV--SFRypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 79 SISLTGQ----FAAldgmlTGRENLiMIAklRGVSNPAQVADnLLARFSLTDAANQRADQY-----------SGGMKRRL 143
Cdd:COG4987 410 RIAVVPQrphlFDT-----TLRENL-RLA--RPDATDEELWA-ALERVGLGDWLAALPDGLdtwlgeggrrlSGGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 144 DIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQyLEEAEQlADRIAILHGGKIITTGTLAELKE 223
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHR-LAGLER-MDRILVLEDGRIVEQGTHEELLA 558
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-220 |
6.00e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 106.70 E-value: 6.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAaISIKGLKKSFK----------------------DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQD 58
Cdd:COG1134 1 MSSM-IEVENVSKSYRlyhepsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 59 GGEVSICGfdvqrqpdhvRQS--ISLTgqfAALDGMLTGRENLIMIAKLRGVSnPAQVADNL--LARFS-LTDAANQRAD 133
Cdd:COG1134 80 SGRVEVNG----------RVSalLELG---AGFHPELTGRENIYLNGRLLGLS-RKEIDEKFdeIVEFAeLGDFIDQPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 134 QYSGGMKRRLDIAMSLIGAPAIIFLDEPT-TGlDPE------ARIEvwdtvkELAGSGTTILLTTQYLEEAEQLADRIAI 206
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVLaVG-DAAfqkkclARIR------ELRESGRTVIFVSHSMGAVRRLCDRAIW 218
|
250
....*....|....
gi 1256329087 207 LHGGKIITTGTLAE 220
Cdd:COG1134 219 LEKGRLVMDGDPEE 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-223 |
8.39e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 111.00 E-value: 8.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 2 SNAAISIKGLkkSF---KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVR 77
Cdd:COG4988 333 GPPSIELEDV--SFsypGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQFAAL-DGmlTGRENlIMIAklRGVSNPAQVADnLLARFSLTDAANQRADQY-----------SGGMKRRLDI 145
Cdd:COG4988 411 RQIAWVPQNPYLfAG--TIREN-LRLG--RPDASDEELEA-ALEAAGLDEFVAALPDGLdtplgeggrglSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 146 AMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGsGTTILLTTQYLEEAEQlADRIAILHGGKIITTGTLAELKE 223
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLA 560
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-191 |
1.40e-27 |
|
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: 104.75 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 19 EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTGQFAALDGMLTGREN 98
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 99 LIMIAKLRGvsnPAQVA-DNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTV 177
Cdd:TIGR01189 94 LHFWAAIHG---GAQRTiEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
170
....*....|....
gi 1256329087 178 KELAGSGTTILLTT 191
Cdd:TIGR01189 171 RAHLARGGIVLLTT 184
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-238 |
1.62e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.77 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 4 AAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMK-----QDGGEVSICGFDVQRQP-DHVR 77
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDvIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQFAALDGMLTGRENLIMIAKL-RGVSNPAQVADNL---LARFSLTDAANQR----ADQYSGGMKRRLDIAMSL 149
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLnRLVKSKKELQERVrwaLEKAQLWDEVKDRldapAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 150 IGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSgTTILLTTQYLEEAEQLADRIAILHGGKIITTGTlaeLKEMFPPAK 229
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGP---TREVFTNPR 237
|
....*....
gi 1256329087 230 VEYIEKQPT 238
Cdd:PRK14247 238 HELTEKYVT 246
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-222 |
2.76e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 105.20 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH--VRQ 78
Cdd:COG4674 6 MHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHeiARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 79 SISLTGQFAALDGMLTGRENLIMIAK--------LRGVSNPAQVA--DNLLARFSLTDAANQRADQYSGGMKRRLDIAMS 148
Cdd:COG4674 86 GIGRKFQKPTVFEELTVFENLELALKgdrgvfasLFARLTAEERDriEEVLETIGLTDKADRLAGLLSHGQKQWLEIGML 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 149 LIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSgTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELK 222
Cdd:COG4674 166 LAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGK-HSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQ 238
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-235 |
3.66e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.55 E-value: 3.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 16 KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPD--HVRQSISLTgqFAALDGML 93
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMV--FQNPDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 94 T----------GRENLimiaklrGVSnPAQV---ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDE 160
Cdd:PRK13633 99 VativeedvafGPENL-------GIP-PEEIrerVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 161 PTTGLDPEARIEVWDTVKELAG-SGTTILLTTQYLEEAEQlADRIAILHGGKIITTGTlaeLKEMFPpaKVEYIEK 235
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKkYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT---PKEIFK--EVEMMKK 240
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-220 |
7.27e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.47 E-value: 7.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 4 AAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH-------- 75
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 76 VRQSISLTGQFAALD--GMltGRenlimIAKLRGVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLI--- 150
Cdd:PRK13548 81 LPQHSSLSFPFTVEEvvAM--GR-----APHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 151 ---GAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTIL-------LTTQYleeaeqlADRIAILHGGKIITTGTLA 219
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIvvlhdlnLAARY-------ADRIVLLHQGRLVADGTPA 226
|
.
gi 1256329087 220 E 220
Cdd:PRK13548 227 E 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-216 |
9.16e-27 |
|
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: 103.14 E-value: 9.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 24 VDFEVQrGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG---FDVQRQ---PDHVRQsISLTGQFAALDGMLTGRE 97
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKKinlPPQQRK-IGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 98 NLIMIAKLRGVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTV 177
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1256329087 178 KELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:cd03297 175 KQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-221 |
1.68e-26 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 103.34 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 2 SNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV------------ 69
Cdd:COG4598 5 APPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 70 --QRQPDHVRQSISLTGQFAALDGMLTGRENlIMIAKLR--GVSnPAQV---ADNLLARFSLTDAANQRADQYSGGMKRR 142
Cdd:COG4598 85 adRRQLQRIRTRLGMVFQSFNLWSHMTVLEN-VIEAPVHvlGRP-KAEAierAEALLAKVGLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 143 LDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-223 |
1.82e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.41 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQsISLTGQ 85
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH-VNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLIMIAKLRGVSNP---AQVADnLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPAAeitPRVME-ALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 163 TGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-237 |
3.57e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.47 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHV--------R 77
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElakrlailR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQfaaldgmLTGREnLIMIAKL---RGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGA 152
Cdd:COG4604 82 QENHINSR-------LTVRE-LVAFGRFpysKGRLTAEdrEIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 153 PAIIFLDEPTTGLDPEARIEVWDTVKELA-GSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAE------LKEMF 225
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEiitpevLSDIY 233
|
250
....*....|...
gi 1256329087 226 P-PAKVEYIEKQP 237
Cdd:COG4604 234 DtDIEVEEIDGKR 246
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-234 |
4.66e-26 |
|
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: 101.39 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQ-PDH--VRQSISLTGqfaaldgMLTGRE 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgPDRmvVFQNYSLLP-------WLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 98 NLIMIAK--LRGVSNPAQ--VADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEV 173
Cdd:TIGR01184 74 NIALAVDrvLPDLSKSERraIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 174 WDTVKELAG-SGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKEMFPPAKVEYIE 234
Cdd:TIGR01184 154 QEELMQIWEeHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVPFPRPRDRLEVVE 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-228 |
8.28e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.98 E-value: 8.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 25 DFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRqSISLTGQ----FAALdgmlTGRENli 100
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER-PVSMLFQennlFPHL----TVAQN-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 101 mIA-------KLrgvsNPAQVA--DNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARI 171
Cdd:COG3840 92 -IGlglrpglKL----TAEQRAqvEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 172 EVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKEMFPPA 228
Cdd:COG3840 167 EMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-210 |
1.40e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.09 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQrQPDHVRqsiSLTGQFAALDGMLTGR 96
Cdd:COG4525 19 PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT-GPGADR---GVVFQKDALLPWLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 97 ENLIMIAKLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARievw 174
Cdd:COG4525 95 DNVAFGLRLRGVPKAErrARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTR---- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1256329087 175 DTVKEL-----AGSGTTILLTTQYLEEAEQLADRIAILHGG 210
Cdd:COG4525 171 EQMQELlldvwQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-223 |
3.09e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.22 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRqSISLTGQ 85
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQR-PINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLIMIAKLRGVSNpAQVAD---NLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPK-AEIASrvnEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 163 TGLDPEAR----IEVWDTVKELagsGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:PRK11607 178 GALDKKLRdrmqLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-235 |
3.59e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.15 E-value: 3.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKD-KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPD---HVRQSIS 81
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 82 LTGQ------FA--ALDGMLTGRENLimiaKLRGVSNPAQVADNLlARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAP 153
Cdd:PRK13639 82 IVFQnpddqlFAptVEEDVAFGPLNL----GLSKEEVEKRVKEAL-KAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 154 AIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTlaeLKEMFppAKVEYI 233
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGT---PKEVF--SDIETI 231
|
..
gi 1256329087 234 EK 235
Cdd:PRK13639 232 RK 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-241 |
5.81e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 99.27 E-value: 5.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV----------- 69
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 70 ---QRQPDHVRQSISLTGQFAALDGMLTGRENlIMIAKLR--GVSNPA--QVADNLLARFSLTDAANQRADQY-SGGMKR 141
Cdd:PRK10619 81 vadKNQLRLLRTRLTMVFQHFNLWSHMTVLEN-VMEAPIQvlGLSKQEarERAVKYLAKVGIDERAQGKYPVHlSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 142 RLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIittgtlael 221
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI--------- 230
|
250 260
....*....|....*....|
gi 1256329087 222 KEMFPPAKVEYIEKQPTLEE 241
Cdd:PRK10619 231 EEEGAPEQLFGNPQSPRLQQ 250
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-213 |
9.25e-25 |
|
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: 96.93 E-value: 9.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 16 KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILStLMKQDG---GEVSICGfdvQRQPDHVRQSISLTGQFAALDGM 92
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA-GRKTAGvitGEILING---RPLDKNFQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 93 LTGRENLIMIAKLRGVSnpaqvadnllarfsltdaANQRadqysggmkRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIE 172
Cdd:cd03232 94 LTVREALRFSALLRGLS------------------VEQR---------KRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1256329087 173 VWDTVKELAGSGTTILLTT-QYLEEAEQLADRIAILH-GGKII 213
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIhQPSASIFEKFDRLLLLKrGGKTV 189
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-217 |
1.04e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 98.93 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQD---GGEVSICGFDVQRQ---PDHVRQS 79
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVQREgrlARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 80 ISLTG----QFAaLDGMLTGRENlIMIAKLRgvSNP-------------AQVADNLLARFSLTDAANQRADQYSGGMKRR 142
Cdd:PRK09984 85 RANTGyifqQFN-LVNRLSVLEN-VLIGALG--STPfwrtcfswftreqKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 143 LDIAMSLIGAPAIIFLDEPTTGLDPE-ARIeVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGT 217
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPEsARI-VMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-221 |
3.18e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.87 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH--VRQ 78
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 79 SISLTGQFAALDGMLTGRENLIMIAKLRGVSNPAQVADNLLARF-SLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIF 157
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 158 LDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-223 |
3.79e-24 |
|
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: 96.84 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQ-PDHVRQSISLTGQFAAL-DGmlT 94
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLnLRWLRSQIGLVSQEPVLfDG--T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 95 GRENLIMiaklrGVSNPAQVADNLLARF--------SLTDAAN----QRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:cd03249 93 IAENIRY-----GKPDATDEEVEEAAKKanihdfimSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 163 TGLDPEARIEVWDTVKELAGSGTTI-----LLTTQYleeaeqlADRIAILHGGKIITTGTLAELKE 223
Cdd:cd03249 168 SALDAESEKLVQEALDRAMKGRTTIviahrLSTIRN-------ADLIAVLQNGQVVEQGTHDELMA 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-220 |
6.08e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.33 E-value: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSF----KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV----QRQPDHVR 77
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSIsltgqfaaldGM-------LTGR---ENLIMIAKLRGVSN---PAQVADnLLARFSLTDAANQRADQYSGGMKRRLD 144
Cdd:PRK11153 82 RQI----------GMifqhfnlLSSRtvfDNVALPLELAGTPKaeiKARVTE-LLELVGLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 145 IAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVK----ELagsGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAE 220
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKdinrEL---GLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-217 |
7.70e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 98.23 E-value: 7.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSnaaISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQpdHVR-QS 79
Cdd:PRK10851 1 MS---IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARdRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 80 ISLTGQFAALDGMLTGRENL---IMIAKLRGVSNPA---QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAP 153
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFDNIafgLTVLPRRERPNAAaikAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 154 AIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGT 217
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-213 |
1.07e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.92 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFK-----DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVR-QS 79
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRaKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 80 IS------LTGQFAAldgmLTGRENLIMiAKLRGVS-------NPAQVAD--NLLARFS--LTDAANQRADQYSGGMKRR 142
Cdd:COG1101 82 IGrvfqdpMMGTAPS----MTIEENLAL-AYRRGKRrglrrglTKKRRELfrELLATLGlgLENRLDTKVGLLSGGQRQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 143 LDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWD-TVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKII 213
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALVLElTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-221 |
1.39e-23 |
|
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: 98.99 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAI-SIKGLKKSFKD----KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVniLSTL------MKQDGGEVSICGFDV 69
Cdd:COG4172 1 MMSMPLlSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTA--LSILrllpdpAAHPSGSILFDGQDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 70 QRQPD----HVR-QSISLTGQ--FAALDGMLT-GR---ENLIMIAKLRGVSNPAQVADnLLARFSLTDAAnQRADQY--- 135
Cdd:COG4172 79 LGLSErelrRIRgNRIAMIFQepMTSLNPLHTiGKqiaEVLRLHRGLSGAAARARALE-LLERVGIPDPE-RRLDAYphq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 136 -SGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKII 213
Cdd:COG4172 157 lSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
....*...
gi 1256329087 214 TTGTLAEL 221
Cdd:COG4172 237 EQGPTAEL 244
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-207 |
1.97e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.45 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 20 VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG-----FDVQRQ------PDHVRQSISLtGQFA- 87
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvaYVPQRSevpdslPLTVRDLVAM-GRWAr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 88 -ALDGMLTGRENLimiaklrgvsnpaqVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLD 166
Cdd:NF040873 86 rGLWRRLTRDDRA--------------AVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1256329087 167 PEARIEVWDTVKELAGSGTTILLTTQYLEEAeQLADRIAIL 207
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-204 |
1.99e-23 |
|
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: 93.71 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 20 VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTGQFAALDGMLTGRENL 99
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 100 IMIAKLRGVSnpaQVADnLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDP--EARIEVwDTV 177
Cdd:cd03231 95 RFWHADHSDE---QVEE-ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKagVARFAE-AMA 169
|
170 180
....*....|....*....|....*..
gi 1256329087 178 KELAGSGTTILLTTQYLEEAEQLADRI 204
Cdd:cd03231 170 GHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-221 |
2.54e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.07 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKE-----VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGF------DVQRQPD 74
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdkkNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 75 H-----------VRQSISLTGQFAALDGMLTGRENLIMIAKLR-GVS--NPAQVADNLLARFSLTDAANQRAD-QYSGGM 139
Cdd:PRK13631 102 NpyskkiknfkeLRRRVSMVFQFPEYQLFKDTIEKDIMFGPVAlGVKksEAKKLAKFYLNKMGLDDSYLERSPfGLSGGQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 140 KRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLA 219
Cdd:PRK13631 182 KRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPY 261
|
..
gi 1256329087 220 EL 221
Cdd:PRK13631 262 EI 263
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-238 |
2.58e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.91 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 3 NAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDG-----GEVSICGFDVQRQ---PD 74
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPdvdPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 75 HVRQSISLTGQFAALDGMLTGRENLIMIAKLRGVSNPAQVADNL----LARFSLTDAANQRADQY----SGGMKRRLDIA 146
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERvewaLKKAALWDEVKDRLNDYpsnlSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 147 MSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAgSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGtlaELKEMFP 226
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELK-KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG---PTRKVFE 237
|
250
....*....|..
gi 1256329087 227 PAKVEYIEKQPT 238
Cdd:PRK14267 238 NPEHELTEKYVT 249
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-212 |
3.02e-23 |
|
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: 94.07 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQrQPDH--VRQSISLTGQFAALDGMlT 94
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHkyLHSKVSLVGQEPVLFAR-S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 95 GRENL---IMIAKLRGVSNPAQVAD-----NLLARFSLTDaANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLD 166
Cdd:cd03248 104 LQDNIaygLQSCSFECVKEAAQKAHahsfiSELASGYDTE-VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1256329087 167 PEARIEVWDTVKElAGSGTTILLTTQYLEEAEQlADRIAILHGGKI 212
Cdd:cd03248 183 AESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-219 |
3.96e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.40 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 13 KSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQrqPDHVRQSISL---------T 83
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR--IRSPRDAIRAgiayvpedrK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDgmLTGRENlIMIAKLRGVSNP--------AQVADNLLARFSL-TDAANQRADQYSGGMKRRLDIAMSLIGAPA 154
Cdd:COG1129 338 GEGLVLD--LSIREN-ITLASLDRLSRGglldrrreRALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 155 IIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIitTGTLA 219
Cdd:COG1129 415 VLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI--VGELD 477
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-243 |
5.27e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQ-RQPDHVRQSISLTG 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 85 QFAALDGMLTGRENLIM-----IAKLRGVSNPAQVA-DNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFL 158
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMgrtphRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 159 DEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGtlaelkemfPPAKVeyiEKQPT 238
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG---------PPADV---LTADT 231
|
....*
gi 1256329087 239 LEEIF 243
Cdd:PRK09536 232 LRAAF 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-221 |
5.51e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.04 E-value: 5.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVRQ-SISLT 83
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAKAHQlGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLI--MIAKLRGVSNPAQVADNLLARFSLTDAAN--QRADQysggmkRRLDIAMSLIGAPAIIFLD 159
Cdd:PRK15439 92 PQEPLLFPNLSVKENILfgLPKRQASMQKMKQLLAALGCQLDLDSSAGslEVADR------QIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 160 EPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK15439 166 EPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-216 |
7.18e-23 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 91.61 E-value: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKE--VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLT 83
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAAL-DGMLtgRENLimiaklrgvsnpaqvadnllarfsltdaanqrADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:cd03247 81 NQRPYLfDTTL--RNNL--------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 163 TGLDPEARIEVWDTVKELAgSGTTILLTTQYLEEAEQlADRIAILHGGKIITTG 216
Cdd:cd03247 127 VGLDPITERQLLSLIFEVL-KDKTLIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-216 |
7.78e-23 |
|
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: 92.56 E-value: 7.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 25 DFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRqSISLTGQFAALDGMLTGREN--LIMI 102
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR-PVSMLFQENNLFAHLTVEQNvgLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 103 AKLRGVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKEL-A 181
Cdd:cd03298 97 PGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhA 176
|
170 180 190
....*....|....*....|....*....|....*
gi 1256329087 182 GSGTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:cd03298 177 ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-221 |
7.84e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 96.77 E-value: 7.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 16 KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVRQSISLTGQfaalDGML- 93
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQ----DTFLf 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 94 --TGRENL------------IMIAKLrgvsnpAQVADNLLArfsLTD----AANQRADQYSGGMKRRLDIAMSLIGAPAI 155
Cdd:COG1132 427 sgTIRENIrygrpdatdeevEEAAKA------AQAHEFIEA---LPDgydtVVGERGVNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 156 IFLDEPTTGLDPEARIEVWDTVKELAGSGTTIL----LTTQyleeaeQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMKGRTTIViahrLSTI------RNADRILVLDDGRIVEQGTHEEL 561
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-213 |
1.14e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.33 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 3 NAAISIKGLKKSF----KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV-QRQPDHV- 76
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVaTLDADALa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 77 ---RQSISLTGQFAALDGMLTGRENLIMIAKLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIG 151
Cdd:PRK10535 82 qlrREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQrlLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 152 APAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQlADRIAILHGGKII 213
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-213 |
1.29e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSIcG-------FDvQRQpdhvrq 78
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GetvkigyFD-QHQ------ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 79 sisltgqfAALDGMLTGRENLIMIAKlrgvSNPAQVADNLLARFSLT-DAANQRADQYSGGMKRRLDIAMSLIGAPAIIF 157
Cdd:COG0488 388 --------EELDPDKTVLDELRDGAP----GGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 158 LDEPTTGLDPEARIEVWDTVKELAGsgtTILLTT--QYLeeAEQLADRIAILHGGKII 213
Cdd:COG0488 456 LDEPTNHLDIETLEALEEALDDFPG---TVLLVShdRYF--LDRVATRILEFEDGGVR 508
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-223 |
1.95e-22 |
|
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: 91.05 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTtvnILSTLM-----KQDGGEVSICGFDVQRQPDHVRqsi 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTIMghpkyEVTEGEILFKGEDITDLPPEER--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 sltgqfaALDGMLTGRENLIMIAklrGVSNpaqvaDNLLaRFsltdaANqraDQYSGGMKRRLDIAMSLIGAPAIIFLDE 160
Cdd:cd03217 75 -------ARLGIFLAFQYPPEIP---GVKN-----ADFL-RY-----VN---EGFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 161 PTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQL-ADRIAILHGGKIITTGTLAELKE 223
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALE 194
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-191 |
2.18e-22 |
|
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: 90.95 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV---QRQPDHVRQSISLTGQ------FA 87
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQdpddqlFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 88 A--LDGMLTGRENLimiaklrGVSnPAQV---ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:TIGR01166 84 AdvDQDVAFGPLNL-------GLS-EAEVerrVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180
....*....|....*....|....*....
gi 1256329087 163 TGLDPEARIEVWDTVKELAGSGTTILLTT 191
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVIST 184
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-221 |
2.74e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 94.33 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHV-----RQSISLTGQFAALDGMLTG 95
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 96 RENLIMIAKLRGV--SNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEV 173
Cdd:PRK10070 124 LDNTAFGMELAGInaEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1256329087 174 WDT-VKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK10070 204 QDElVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-212 |
3.72e-22 |
|
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: 90.93 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPD----HVRQSISLTGQFAALDGMLTGR 96
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraipYLRRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 97 ENlIMIAkLRGVSNPAQVADN----LLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIE 172
Cdd:cd03292 97 EN-VAFA-LEVTGVPPREIRKrvpaALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1256329087 173 VWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKI 212
Cdd:cd03292 175 IMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-212 |
5.42e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.28 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVsICGfdvqRQP-DHVRQSISLTG 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPlAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 85 QFAAL-------DGMLTGrenlimiakLRGVSNPAqvADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIF 157
Cdd:PRK11247 88 QDARLlpwkkviDNVGLG---------LKGQWRDA--ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 158 LDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKI 212
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-221 |
7.08e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.08 E-value: 7.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQpDH----- 75
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHklaaq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 76 -----VRQSISLTGQFAALDGMLTGRenlIMIAKLRGV-----SNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDI 145
Cdd:PRK09700 80 lgigiIYQELSVIDELTVLENLYIGR---HLTKKVCGVniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 146 AMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-246 |
9.86e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.26 E-value: 9.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGL-----KKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQP---DHVR 77
Cdd:PRK13637 3 IKIENLthiymEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQFAALDGMltgrENLIMIAKLRGVSNPAQVADNLLAR---------FSLTDAANQRADQYSGGMKRRLDIAMS 148
Cdd:PRK13637 83 KKVGLVFQYPEYQLF----EETIEKDIAFGPINLGLSEEEIENRvkramnivgLDYEDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 149 LIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL-KEmfp 226
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVfKE--- 235
|
250 260
....*....|....*....|
gi 1256329087 227 pakVEyiekqpTLEEIFLAI 246
Cdd:PRK13637 236 ---VE------TLESIGLAV 246
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-212 |
1.41e-21 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 88.04 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLkkSFK----DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQ-PDHVRQSI 80
Cdd:cd03246 1 LEVENV--SFRypgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 sltGQFAALDGMLTGrenlimiaklrgvsnpaQVADNLLarfsltdaanqradqySGGMKRRLDIAMSLIGAPAIIFLDE 160
Cdd:cd03246 79 ---GYLPQDDELFSG-----------------SIAENIL----------------SGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 161 PTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQlADRIAILHGGKI 212
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-225 |
1.42e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.07 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV-QRQPDHVRQSISLTG 84
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 85 QFAALDGMLTGRE--------NLIMIAKLRGvsNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAII 156
Cdd:PRK11231 83 QHHLTPEGITVRElvaygrspWLSLWGRLSA--EDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 157 FLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAE------LKEMF 225
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEvmtpglLRTVF 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-221 |
1.94e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 90.24 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKD--KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGE---VSICGFDV-QRQPD 74
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLtAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 75 HVRQSISLT-----GQFAAL---DGMLTGRENlimiaklRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLD 144
Cdd:PRK13640 81 DIREKVGIVfqnpdNQFVGAtvgDDVAFGLEN-------RAVPRPEmiKIVRDVLADVGMLDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 145 IAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELA-GSGTTILLTTQYLEEAEQlADRIAILHGGKIITTGTLAEL 221
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEI 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-214 |
2.04e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 8 IKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSIcgfdvqrQPD----HVRQSISLT 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-------PKGlrigYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLI-MIAKLRGVS--------NPAQVADnLLARFSLTDA--ANQRADQ------------------ 134
Cdd:COG0488 74 DDLTVLDTVLDGDAELRaLEAELEELEaklaepdeDLERLAE-LQEEFEALGGweAEARAEEilsglgfpeedldrpvse 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 135 YSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEArIEvW--DTVKELAGsgtTILLTT--QYLeeAEQLADRIAILHGG 210
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES-IE-WleEFLKNYPG---TVLVVShdRYF--LDRVATRILELDRG 225
|
....
gi 1256329087 211 KIIT 214
Cdd:COG0488 226 KLTL 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
2.21e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.05 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 2 SNAAISIKGLKKSFKDKE--VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQP-DHVRQ 78
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 79 SISLT-----GQF---AALDGMLTGRENlimiaKLRGVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLI 150
Cdd:PRK13632 84 KIGIIfqnpdNQFigaTVEDDIAFGLEN-----KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 151 GAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGT-TILLTTQYLEEAeQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-213 |
2.21e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 89.71 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 2 SNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTT---TVNILSTLmkQDG----GEVSICG---FDVQR 71
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDL--IPGarveGEILLDGediYDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 72 QPDHVRQSIsltgqfaaldGM---------LTGRENLIMIAKLRGVSNPAQVADnlLARFSLTDAA---------NQRAD 133
Cdd:COG1117 86 DVVELRRRV----------GMvfqkpnpfpKSIYDNVAYGLRLHGIKSKSELDE--IVEESLRKAAlwdevkdrlKKSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 134 QYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEA--RIEvwDTVKELAGSgTTILLTTQYLEEAEQLADRIAILHGGK 211
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStaKIE--ELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGE 230
|
..
gi 1256329087 212 II 213
Cdd:COG1117 231 LV 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-191 |
2.26e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 88.32 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 23 GVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTGQFAALDGMLTGRENLIMI 102
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 103 AKLRGVSNPAQVADnLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEArievwdtVKEL-- 180
Cdd:PRK13538 99 QRLHGPGDDEALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG-------VARLea 170
|
170
....*....|....*.
gi 1256329087 181 -----AGSGTTILLTT 191
Cdd:PRK13538 171 llaqhAEQGGMVILTT 186
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-221 |
3.20e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.79 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAaISIKGLK---KSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG--------FDV 69
Cdd:PRK13650 1 MSNI-IEVKNLTfkyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 70 QRQPDHVRQSISltGQFAAL---DGMLTGRENlimiaklRGVSNPAQV--ADNLLARFSLTDAANQRADQYSGGMKRRLD 144
Cdd:PRK13650 80 RHKIGMVFQNPD--NQFVGAtveDDVAFGLEN-------KGIPHEEMKerVNEALELVGMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 145 IAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAeQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-191 |
3.74e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.01 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDvQRQPDHvRQSISLTGQFAALDGMLTGR 96
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPDV-AEACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 97 ENLIMIAKLRGvSNPAQVADNlLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDT 176
Cdd:PRK13539 92 ENLEFWAAFLG-GEELDIAAA-LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAEL 169
|
170
....*....|....*
gi 1256329087 177 VKELAGSGTTILLTT 191
Cdd:PRK13539 170 IRAHLAQGGIVIAAT 184
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-204 |
3.88e-21 |
|
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: 88.26 E-value: 3.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 3 NAAISIKGLKKSF-------KDKEVLKGVDFEVQRGEIFALLGSNGAGKtttvnilSTLMKQ-------DGGEVSIC--- 65
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGK-------STLLKCiygnylpDSGSILVRhdg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 66 -GFDVQRQPDHV-----RQSISLTGQF-------AALDgmltgrenlIMIAKL--RGVSNPA--QVADNLLARFSL---- 124
Cdd:COG4778 75 gWVDLAQASPREilalrRRTIGYVSQFlrviprvSALD---------VVAEPLleRGVDREEarARARELLARLNLperl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 125 ------TdaanqradqYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAE 198
Cdd:COG4778 146 wdlppaT---------FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVRE 216
|
....*.
gi 1256329087 199 QLADRI 204
Cdd:COG4778 217 AVADRV 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-216 |
4.05e-21 |
|
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: 88.03 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV-QRQPDHVRQSISLTGQfaalDGML-- 93
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrQLDPADLRRNIGYVPQ----DVTLfy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 94 -TGRENLIMiaklrgvSNPAqVADNLL---ARFS-LTDAANQ-----------RADQYSGGMKRRLDIAMSLIGAPAIIF 157
Cdd:cd03245 92 gTLRDNITL-------GAPL-ADDERIlraAELAgVTDFVNKhpngldlqigeRGRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 158 LDEPTTGLDPEARIEVWDTVKELAGSGTTILLT--TQYLeeaeQLADRIAILHGGKIITTG 216
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLGDKTLIIIThrPSLL----DLVDRIIVMDSGRIVADG 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-221 |
4.24e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.95 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFD---VQRQPdhVRQSISLTGQFAAL------DG 91
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDirtVTRAS--LRRNIAVVFQDAGLfnrsieDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 92 MLTGRENLIMiAKLRGVSNPAQVADNLLARFSLTDA-ANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEAR 170
Cdd:PRK13657 429 IRVGRPDATD-EEMRAAAERAQAHDFIERKPDGYDTvVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 171 IEVWDTVKELAGSGTTILLttqyleeAEQL-----ADRIAILHGGKIITTGTLAEL 221
Cdd:PRK13657 508 AKVKAALDELMKGRTTFII-------AHRLstvrnADRILVFDNGRVVESGSFDEL 556
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-252 |
4.38e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.63 E-value: 4.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 7 SIKGLK-KSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPdhVRQSISL--- 82
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS--PRERRRLgva 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 83 ------TGQFAALDgmLTGRENLIM-------IAKlRGVSNPAQV---ADNLLARFSL-TDAANQRADQYSGGMKRRLDI 145
Cdd:COG3845 337 yipedrLGRGLVPD--MSVAENLILgryrrppFSR-GGFLDRKAIrafAEELIEEFDVrTPGPDTPARSLSGGNQQKVIL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 146 AMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTgtlaelkemF 225
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGE---------V 484
|
250 260
....*....|....*....|....*..
gi 1256329087 226 PPAKVeyiekqpTLEEIFLAIIGKKEE 252
Cdd:COG3845 485 PAAEA-------TREEIGLLMAGVKEE 504
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-221 |
4.88e-21 |
|
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: 88.05 E-value: 4.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 16 KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH-VRQSISLTGQfaalDGML- 93
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKsLRSMIGVVLQ----DTFLf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 94 --TGRENLIM---IAKLRGVSNPAQV--ADNLLARF--SLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTG 164
Cdd:cd03254 90 sgTIMENIRLgrpNATDEEVIEAAKEagAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 165 LDPEARIEVWDTVKELAGSGTTI-----LLTTQYleeaeqlADRIAILHGGKIITTGTLAEL 221
Cdd:cd03254 170 IDTETEKLIQEALEKLMKGRTSIiiahrLSTIKN-------ADKILVLDDGKIIEEGTHDEL 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-221 |
5.34e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.41 E-value: 5.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 24 VDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV-----QRQPDHVRQSISLTGQF--------AALD 90
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstskQKEIKPVRKKVGVVFQFpesqlfeeTVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 91 GMLTGRENLimiaklrGVSN--PAQVADNLLARFSLTDAANQRAD-QYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDP 167
Cdd:PRK13643 105 DVAFGPQNF-------GIPKekAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 168 EARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-221 |
6.41e-21 |
|
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: 87.81 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 23 GVDFEVQRGEIFALLGSNGAGKTTT----VNILSTLMKQDGGEVSICGFDVQrqPDHVRQ---SISLTGQFAALDGMLTG 95
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTclaiLGLLPPGLTQTSGEILLDGRPLL--PLSIRGrhiATIMQNPRTAFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 96 RENLIMIAKLRGV--SNPAQVADNLLARFSLTDAA---NQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEAR 170
Cdd:TIGR02770 82 GNHAIETLRSLGKlsKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 171 IEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:TIGR02770 162 ARVLKLLRELRQLfGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEI 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-221 |
6.70e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.16 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV------QRQPD 74
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthrsiqQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 75 HVRQSisltgqFAALDGMLTGrENLIMIAKLRGVSNP--AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGA 152
Cdd:PRK11432 82 MVFQS------YALFPHMSLG-ENVGYGLKMLGVPKEerKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 153 PAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-235 |
9.70e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.26 E-value: 9.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH-----VRQSISLTGQFA-------- 87
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikqIRKKVGLVFQFPesqlfeet 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 88 ALDGMLTGRENLimiaklrGVSNPAQVAdnlLARFSLT------DAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEP 161
Cdd:PRK13649 103 VLKDVAFGPQNF-------GVSQEEAEA---LAREKLAlvgiseSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 162 TTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGtlaELKEMFppAKVEYIEK 235
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG---KPKDIF--QDVDFLEE 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-204 |
9.71e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.56 E-value: 9.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 19 EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVR-----QSISLTGQFAALDGML 93
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 94 TGRENLIMiAKLRGVSNPAQV---ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEAR 170
Cdd:PRK11629 103 TALENVAM-PLLIGKKKPAEInsrALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190
....*....|....*....|....*....|....*
gi 1256329087 171 IEVWDTVKEL-AGSGTTILLTTQYLeeaeQLADRI 204
Cdd:PRK11629 182 DSIFQLLGELnRLQGTAFLVVTHDL----QLAKRM 212
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-221 |
1.37e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.43 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 7 SIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTtvnILSTLM-----KQDGGEVSICGFDV------QRqpdh 75
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKST---LAKVLMghpkyEVTSGSILLDGEDIlelspdER---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 76 VRQSISLTGQF-AALDGMLTgrENLIMIA--KLRGVSNPAQ----VADNLLARFSLTDAANQRA--DQYSGGMKRRLDIA 146
Cdd:COG0396 75 ARAGIFLAFQYpVEIPGVSV--SNFLRTAlnARRGEELSAReflkLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 147 MSLIGAPAIIFLDEPTTGLDPEA-RIeVWDTVKELAGSGTTILLTTQY---LEEAEqlADRIAILHGGKIITTGTlAEL 221
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLDIDAlRI-VAEGVNKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGRIVKSGG-KEL 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-233 |
1.51e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 87.73 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKG--LKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVR 77
Cdd:PRK10253 1 MTESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQFAALDGMLTGREnliMIAKLRGVSNP----------AQVADNLLARfSLTDAANQRADQYSGGMKRRLDIAM 147
Cdd:PRK10253 81 RRIGLLAQNATTPGDITVQE---LVARGRYPHQPlftrwrkedeEAVTKAMQAT-GITHLADQSVDTLSGGQRQRAWIAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 148 SLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTlaeLKEMFP 226
Cdd:PRK10253 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA---PKEIVT 233
|
....*..
gi 1256329087 227 PAKVEYI 233
Cdd:PRK10253 234 AELIERI 240
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-223 |
1.52e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.55 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVqRQPDHV--RQSISLTGQFAALDGMlT 94
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL-VQYDHHylHRQVALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 95 GRENL---IMIAKLRGVSNPAQV--ADNLLARFSLTDAAN--QRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDp 167
Cdd:TIGR00958 571 VRENIaygLTDTPDEEIMAAAKAanAHDFIMEFPNGYDTEvgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 168 eARIEvwDTVKELAGSGT-TILLTTQYLEEAEQlADRIAILHGGKIITTGTLAELKE 223
Cdd:TIGR00958 650 -AECE--QLLQESRSRASrTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLME 702
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-228 |
2.01e-20 |
|
nickel import ATP-binding protein NikE; This family represents the NikE 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. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 87.17 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 18 KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR----QPDHVRQSISLTGQ--FAALDG 91
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldrkQRRAFRRDVQLVFQdsPSAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 92 MLTGR----ENLIMIAKLRGVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDP 167
Cdd:TIGR02769 104 RMTVRqiigEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 168 EARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKEMFPPA 228
Cdd:TIGR02769 184 VLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKHPA 245
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-211 |
2.97e-20 |
|
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: 83.65 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVsicgfdvqRQPDHVRqsislTGQ 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------TWGSTVK-----IGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FaaldgmltgrenlimiaklrgvsnpaqvadnllarfsltdaanqraDQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGL 165
Cdd:cd03221 68 F----------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1256329087 166 DPEARIEVWDTVKELAGsgtTILLTT--QYLeeAEQLADRIAILHGGK 211
Cdd:cd03221 102 DLESIEALEEALKEYPG---TVILVShdRYF--LDQVATKIIELEDGK 144
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-245 |
3.30e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.41 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVqRQPDHvRQSIS--- 81
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM-ADARH-RRAVCpri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 82 ------------LTgqfaaldgmLTGRENLIMIAKLRGVSNP--AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAM 147
Cdd:NF033858 79 aympqglgknlyPT---------LSVFENLDFFGRLFGQDAAerRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 148 SLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS--GTTILLTTQYLEEAEQLaDRIAILHGGKIITTGTLAELKEMf 225
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLAR- 227
|
250 260
....*....|....*....|
gi 1256329087 226 ppakveyiEKQPTLEEIFLA 245
Cdd:NF033858 228 --------TGADTLEAAFIA 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-228 |
4.55e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 86.28 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 10 GLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV----QRQPDHVRQSISLTGQ 85
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 --FAALDGMLTGREnlIMIAKLR---GVSNPAQVA--DNLLARFSLTDA-ANQRADQYSGGMKRRLDIAMSLIGAPAIIF 157
Cdd:PRK10419 97 dsISAVNPRKTVRE--IIREPLRhllSLDKAERLAraSEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 158 LDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKEMFPPA 228
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSSPA 246
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-213 |
5.55e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.42 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH-----VRQSISLTGQF----- 86
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkkLRKKVSLVFQFpeaql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 87 ---AALDGMLTGRENLimiaklrGVSN--PAQVADNLLARFSL-TDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDE 160
Cdd:PRK13641 99 fenTVLKDVEFGPKNF-------GFSEdeAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 161 PTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKII 213
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-221 |
6.27e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 86.37 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPD-----HVRQSISLTGQFAALD- 90
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirPVRKRIGMVFQFPESQl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 91 -------GMLTGRENLIMiaklrGVSNPAQVADNLLARFSLT-DAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:PRK13646 99 fedtverEIIFGPKNFKM-----NLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 163 TGLDPEARIEVWDTVKELA-GSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-216 |
6.44e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 85.75 E-value: 6.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG-----FDVQRQPDH 75
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 76 VRQSISLTG-----QFAAlDGmltgrenlimiakLR-GVSNPAQVADNLLA---RF--SLTDAANQ----------RAD- 133
Cdd:PRK11701 82 ERRRLLRTEwgfvhQHPR-DG-------------LRmQVSAGGNIGERLMAvgaRHygDIRATAGDwlerveidaaRIDd 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 134 ---QYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHG 209
Cdd:PRK11701 148 lptTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
....*..
gi 1256329087 210 GKIITTG 216
Cdd:PRK11701 228 GRVVESG 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-233 |
1.89e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.44 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTT---TVNILSTLMKQ--DGGEVSICGFDV-QRQPD 74
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPEvtITGSIVYNGHNIySPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 75 HV--RQSISLTGQ----FAaldgmLTGRENLIMIAKLRGVSNPA---QVADNLLARFSLTDAANQR----ADQYSGGMKR 141
Cdd:PRK14239 81 TVdlRKEIGMVFQqpnpFP-----MSIYENVVYGLRLKGIKDKQvldEAVEKSLKGASIWDEVKDRlhdsALGLSGGQQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 142 RLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSgTTILLTTQYLEEAEQLADRIAILHGGKIITTGtlaEL 221
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYN---DT 231
|
250
....*....|....*.
gi 1256329087 222 KEMF-PPAKVE---YI 233
Cdd:PRK14239 232 KQMFmNPKHKEtedYI 247
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-235 |
2.33e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.14 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDK-----EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSI 80
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTgqfaaldgmltgrENLIMIAKLRGVSNPAQVADNL-----LARFSLTDA-------------------ANQRADQY- 135
Cdd:PRK13651 83 VLE-------------KLVIQKTRFKKIKKIKEIRRRVgvvfqFAEYQLFEQtiekdiifgpvsmgvskeeAKKRAAKYi 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 136 -----------------SGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAE 198
Cdd:PRK13651 150 elvgldesylqrspfelSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVL 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1256329087 199 QLADRIAILHGGKIITTG----TLAELK-----EMFPPAKVEYIEK 235
Cdd:PRK13651 230 EWTKRTIFFKDGKIIKDGdtydILSDNKflienNMEPPKLLNFVNK 275
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-221 |
2.58e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.47 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH-VRQSISLTGQFAALDGMLTG 95
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIReVRKFVGLVFQNPDDQIFSPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 96 RENLIMIAKLRGVSNPAQVA---DNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIE 172
Cdd:PRK13652 96 VEQDIAFGPINLGLDEETVAhrvSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1256329087 173 VWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK13652 176 LIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-194 |
4.47e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 85.88 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQP-DHVRQSISLTGQ----FAAldg 91
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqDEVRRRVSVCAQdahlFDT--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 92 mlTGRENLiMIAklRGVSNPAQVADnLLARFSLTDAANQRADQY-----------SGGMKRRLDIAMSLIGAPAIIFLDE 160
Cdd:TIGR02868 424 --TVRENL-RLA--RPDATDEELWA-ALERVGLADWLRALPDGLdtvlgeggarlSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....
gi 1256329087 161 PTTGLDPEARIEVWDTVKElAGSGTTILLTTQYL 194
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-221 |
4.61e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.21 E-value: 4.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTT----VNILSTLMKQDGGEVSICGFDVQrqPDHVR-QSISLTGQ-----F 86
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVA--PCALRgRKIATIMQnprsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 87 AALDGMLT-GRENLimiaKLRGVSNPAQVADNLLARFSLTDAA---NQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:PRK10418 93 NPLHTMHThARETC----LALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 163 TGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-221 |
5.41e-19 |
|
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: 82.66 E-value: 5.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 16 KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVRQSISLTGQFAAL-DGml 93
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQDVFLfND-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 94 TGRENlIMIAKlRGVSnPAQVADnlLARfsltdAAN-----------------QRADQYSGGMKRRLDIAMSLIGAPAII 156
Cdd:cd03251 91 TVAEN-IAYGR-PGAT-REEVEE--AAR-----AANahefimelpegydtvigERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 157 FLDEPTTGLDPEARIEVWDTVKELAGSGTTILLttqyleeAEQL-----ADRIAILHGGKIITTGTLAEL 221
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVI-------AHRLstienADRIVVLEDGKIVERGTHEEL 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-221 |
5.57e-19 |
|
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: 84.78 E-value: 5.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 24 VDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG---FDVQRQ---PDHvRQSISLTGQFAALDGMLTGRE 97
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKGiflPPE-KRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 98 NLI-----MIAKLRGVSnPAQVADnLLARFSLTDaanQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIE 172
Cdd:TIGR02142 95 NLRygmkrARPSERRIS-FERVIE-LLGIGHLLG---RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1256329087 173 VWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:TIGR02142 170 ILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-221 |
6.76e-19 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 85.54 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVRQSISLTGQFAAL-DGMLT 94
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVALVSQDVVLfNDTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 95 greNLIMIAKLRGVSNpAQVADNLLARFsLTDAANQ-----------RADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:TIGR02203 424 ---NNIAYGRTEQADR-AEIERALAAAY-AQDFVDKlplgldtpigeNGVLLSGGQRQRLAIARALLKDAPILILDEATS 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 164 GLDPEARIEVWDTVKELAgSGTTILLTTQYLEEAEQlADRIAILHGGKIITTGTLAEL 221
Cdd:TIGR02203 499 ALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNEL 554
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-207 |
7.48e-19 |
|
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: 85.03 E-value: 7.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDK-EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVRQSISL 82
Cdd:TIGR02857 321 SLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 83 TGQ----FAAldgmlTGRENlimIAKLRGVSNPAQVAdNLLARFSLTDAANQRADQY-----------SGGMKRRLDIAM 147
Cdd:TIGR02857 401 VPQhpflFAG-----TIAEN---IRLARPDASDAEIR-EALERAGLDEFVAALPQGLdtpigeggaglSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 148 SLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAgSGTTILLTTQYLEEAEqLADRIAIL 207
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAA-LADRIVVL 529
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-239 |
1.02e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV---QRQPDHVRQSISL 82
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 83 TGQFAALDGMLTGRENLIMIAkLRGVSNP-AQVADNLLARFSLTDAANQRADQ---YSGGMKRRLDIAMSLIGAPAIIFL 158
Cdd:PRK13638 82 VFQDPEQQIFYTDIDSDIAFS-LRNLGVPeAEITRRVDEALTLVDAQHFRHQPiqcLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 159 DEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGtlaELKEMFppAKVEYIEK--- 235
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG---APGEVF--ACTEAMEQagl 235
|
....*
gi 1256329087 236 -QPTL 239
Cdd:PRK13638 236 tQPWL 240
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-225 |
1.30e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.62 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEV-LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPD----- 74
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTaLRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQknlva 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 75 HVRQSISLTGQFAAL--DGMLTGRENLIMIAKlRGVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGA 152
Cdd:PRK15056 82 YVPQSEEVDWSFPVLveDVVMMGRYGHMGWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 153 PAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHG-----GKIITTGTLAELKEMF 225
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGtvlasGPTETTFTAENLELAF 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-225 |
1.46e-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: 84.47 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTL--MKQDGGEV-------SICGFdVQRqPDHV 76
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcEKCGY-VER-PSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 77 RQSISLTGQ--------FAALDGMLTG---RENLIMIAKLRGVSNPAQVADNLL-----ARFSLTDAANQRAD------- 133
Cdd:TIGR03269 79 GEPCPVCGGtlepeevdFWNLSDKLRRrirKRIAIMLQRTFALYGDDTVLDNVLealeeIGYEGKEAVGRAVDliemvql 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 134 ---------QYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELA-GSGTTILLTTQYLEEAEQLADR 203
Cdd:TIGR03269 159 shrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDK 238
|
250 260
....*....|....*....|..
gi 1256329087 204 IAILHGGKIITTGTLAELKEMF 225
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVAVF 260
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
11-203 |
1.59e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.36 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 11 LKKSFKDKE----VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVR-----QSIS 81
Cdd:PRK10584 12 LKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklraKHVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 82 LTGQFAALDGMLTGRENLIMIAKLRGVSN--PAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLD 159
Cdd:PRK10584 92 FVFQSFMLIPTLNALENVELPALLRGESSrqSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1256329087 160 EPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQyleeAEQLADR 203
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNREhGTTLILVTH----DLQLAAR 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-221 |
1.79e-18 |
|
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: 83.23 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 24 VDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG---FDVQRQ---PDHVRQsISLTGQFAALDGMLTGRE 97
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGiflPPHRRR-IGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 98 NLIMIAKLRGVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTV 177
Cdd:COG4148 97 NLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1256329087 178 KELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG4148 177 ERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-221 |
2.00e-18 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 81.12 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV-QRQPDHVRQSISLTGQFAAL------ 89
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIrEVTLDSLRRAIGVVPQDTVLfndtig 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 90 DGMLTGR-----ENLIMIAKLrgvsnpAQVADNLLarfSLTDAAN----QRADQYSGGMKRRLDIAMSLIGAPAIIFLDE 160
Cdd:cd03253 93 YNIRYGRpdatdEEVIEAAKA------AQIHDKIM---RFPDGYDtivgERGLKLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 161 PTTGLDPEARIEVWDTVKELAGSGTTILLttqyleeAEQL-----ADRIAILHGGKIITTGTLAEL 221
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSKGRTTIVI-------AHRLstivnADKIIVLKDGRIVERGTHEEL 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-221 |
2.04e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.11 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 2 SNAAISIKGLKKSFKDKE--VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQP-DHVRQ 78
Cdd:PRK11160 335 DQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 79 SISLTGQ----FAAldgmlTGRENLIMIA------KLRGVSNpaQVA-DNLLarfsltdAANQRAD--------QYSGGM 139
Cdd:PRK11160 415 AISVVSQrvhlFSA-----TLRDNLLLAApnasdeALIEVLQ--QVGlEKLL-------EDDKGLNawlgeggrQLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 140 KRRLDIAMSLI-GAPaIIFLDEPTTGLDPEARIEVWDTVKELAgSGTTILLTTQYLEEAEQLaDRIAILHGGKIITTGTL 218
Cdd:PRK11160 481 QRRLGIARALLhDAP-LLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTH 557
|
...
gi 1256329087 219 AEL 221
Cdd:PRK11160 558 QEL 560
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
2.55e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.82 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKD-KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG--FDVQRQP-DHV 76
Cdd:PRK13636 1 MEDYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGlMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 77 RQSISLTGQ------FAA--LDGMLTGRENLIMIAKlrgvsNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMS 148
Cdd:PRK13636 81 RESVGMVFQdpdnqlFSAsvYQDVSFGAVNLKLPED-----EVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 149 LIGAPAIIFLDEPTTGLDPEARIEVWDTVKELA-GSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL---KEM 224
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQkELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVfaeKEM 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-223 |
2.69e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQD--GGEVSICGFDVQRQpdHVRQ 78
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQAS--NIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 79 S----ISLTGQFAALDGMLTGRENLIMIAKLR--GVSNPAQV---ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSL 149
Cdd:PRK13549 79 TeragIAIIHQELALVKELSVLENIFLGNEITpgGIMDYDAMylrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 150 IGAPAIIFLDEPTTGLDpEARIEV-WDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:PRK13549 159 NKQARLLILDEPTASLT-ESETAVlLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTE 232
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
10-191 |
4.22e-18 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 79.89 E-value: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 10 GLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQpDHVRQsISLTGQFAAL 89
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-DRSRF-MAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 90 DGMLTGRENLIMIAKLRGvSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEA 169
Cdd:PRK13543 94 KADLSTLENLHFLCGLHG-RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
170 180
....*....|....*....|..
gi 1256329087 170 RIEVWDTVKELAGSGTTILLTT 191
Cdd:PRK13543 173 ITLVNRMISAHLRGGGAALVTT 194
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-246 |
1.07e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.16 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 3 NAAISIKGLKKSFKD-KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV-QRQPDHVRQSI 80
Cdd:PRK13647 2 DNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQ------FAA--LDGMLTGRENLimiaKLRGVSNPAQVADNLLArFSLTDAANQRADQYSGGMKRRLDIAMSLIGA 152
Cdd:PRK13647 82 GLVFQdpddqvFSStvWDDVAFGPVNM----GLDKDEVERRVEEALKA-VRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 153 PAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKEmfpPAKVEY 232
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD---EDIVEQ 233
|
250
....*....|....*
gi 1256329087 233 IE-KQPTLEEIFLAI 246
Cdd:PRK13647 234 AGlRLPLVAQIFEDL 248
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-217 |
1.55e-17 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 80.92 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 4 AAISIKGLKKSF--------------KDK-EVLK---------GVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDG 59
Cdd:COG4175 2 PKIEVRNLYKIFgkrperalklldqgKSKdEILEktgqtvgvnDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 60 GEVSICGFDVQRQPD----HVRQS-ISLTGQFAALDGMLTGRENlimIA---KLRGVSNPA--QVADNLLARFSLTDAAN 129
Cdd:COG4175 82 GEVLIDGEDITKLSKkelrELRRKkMSMVFQHFALLPHRTVLEN---VAfglEIQGVPKAErrERAREALELVGLAGWED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 130 QRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILH 208
Cdd:COG4175 159 SYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELqAKLKKTIVFITHDLDEALRLGDRIAIMK 238
|
....*....
gi 1256329087 209 GGKIITTGT 217
Cdd:COG4175 239 DGRIVQIGT 247
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-221 |
2.00e-17 |
|
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: 81.00 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFK--DKEVLKGVD---FEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFD-----VQRQPD- 74
Cdd:TIGR03269 280 IKVRNVSKRYIsvDRGVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDewvdmTKPGPDg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 75 --HVRQSISLTGQFAALDGMLTGRENLI---------MIAKLRGVSNPAQV------ADNLLARFSltdaanqraDQYSG 137
Cdd:TIGR03269 360 rgRAKRYIGILHQEYDLYPHRTVLDNLTeaiglelpdELARMKAVITLKMVgfdeekAEEILDKYP---------DELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 138 GMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTV----KELagsGTTILLTTQYLEEAEQLADRIAILHGGKII 213
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
....*...
gi 1256329087 214 TTGTLAEL 221
Cdd:TIGR03269 508 KIGDPEEI 515
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-216 |
2.42e-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: 78.72 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEV-----SICGFDVQRQPDHVRQSI 80
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyimrSGAELELYQLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTG----QFAALDGMLTG-------RENLIMIAKlRGVSNPAQVADNLLARFSL-TDAANQRADQYSGGMKRRLDIAMS 148
Cdd:TIGR02323 84 MRTEwgfvHQNPRDGLRMRvsaganiGERLMAIGA-RHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 149 LIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-212 |
2.50e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 19 EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRqpDHVRQSISL-----------TGQFa 87
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINA--LSTAQRLARglvylpedrqsSGLY- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 88 aLDGMLTGRENLIMIAKLRGVSNPAQVAdNLLARF------SLTDAaNQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEP 161
Cdd:PRK15439 354 -LDAPLAWNVCALTHNRRGFWIKPAREN-AVLERYrralniKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 162 TTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKI 212
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-221 |
6.49e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.51 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 2 SNAAISIKGLKKSFKDKE----VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPdhvR 77
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRS---R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQFAALDGMLTGrENLIMIAKLRGVS-NPA-----QVADNL-----LARFSLTDAANQRAD------------- 133
Cdd:PRK10261 86 QVIELSEQSAAQMRHVRG-ADMAMIFQEPMTSlNPVftvgeQIAESIrlhqgASREEAMVEAKRMLDqvripeaqtilsr 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 134 ---QYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTT-ILLTTQYLEEAEQLADRIAILHG 209
Cdd:PRK10261 165 yphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQ 244
|
250
....*....|..
gi 1256329087 210 GKIITTGTLAEL 221
Cdd:PRK10261 245 GEAVETGSVEQI 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-223 |
6.81e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.48 E-value: 6.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDG--GEVSICGFDVQRQP--DHVRQSIS 81
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNirDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 82 LTGQFAALDGMLTGRENLIM---IAKLRGVSNPAQV---ADNLLARFSLTDAANQRA-DQYSGGMKRRLDIAMSLIGAPA 154
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLgneITLPGGRMAYNAMylrAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 155 IIFLDEPTTGLDpEARIEV-WDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:TIGR02633 162 LLILDEPSSSLT-EKETEIlLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSE 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-235 |
8.11e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.72 E-value: 8.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQrQPDHVRQSISLTG--------QFAAL--- 89
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG-DFSKLQGIRKLVGivfqnpetQFVGRtve 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 90 DGMLTGRENL----IMIAKLrgvsnpaqvADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGL 165
Cdd:PRK13644 97 EDLAFGPENLclppIEIRKR---------VDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 166 DPEARIEVWDTVKELAGSGTTILLTTQYLEEAeQLADRIAILHGGKIITTGT----LAELK----EMFPPAKVEYIEK 235
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEpenvLSDVSlqtlGLTPPSLIELAEN 244
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-239 |
8.89e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.15 E-value: 8.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 13 KSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDG--GEVSICGfdvqRQPdhVRQSISLTGqFAALD 90
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN----RKP--TKQILKRTG-FVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 91 GML----TGRENLIMIAKLR-----GVSNPAQVADNLLARFSLTDAANQRADQ-----YSGGMKRRLDIAMSLIGAPAII 156
Cdd:PLN03211 149 DILyphlTVRETLVFCSLLRlpkslTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 157 FLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTT-QYLEEAEQLADRIAILHGGKIITTGTLAELKEMFppakvEYIEK 235
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMhQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYF-----ESVGF 303
|
....
gi 1256329087 236 QPTL 239
Cdd:PLN03211 304 SPSF 307
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-221 |
9.25e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 77.75 E-value: 9.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSIcGFDV------QRQPDHVRQSISLTGQFA------- 87
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkkNKKLKPLRKKVGIVFQFPehqlfee 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 88 -ALDGMLTGRENLimiaklrGVS--NPAQVADNLLARFSLTDAANQRAD-QYSGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:PRK13634 102 tVEKDICFGPMNF-------GVSeeDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 164 GLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-221 |
1.17e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 76.54 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 25 DFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDhVRQSISLTGQFAALDGMLTGREN--LIMI 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP-SRRPVSMLFQENNLFSHLTVAQNigLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 103 AKLRGVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAG 182
Cdd:PRK10771 98 PGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1256329087 183 S-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK10771 178 ErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-207 |
3.42e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.51 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQrQPDHVRqsisltG 84
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-GPGAER------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 85 QFAALDGMLTGRENLIMIA---KLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLD 159
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAfglQLAGVEKMQrlEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 160 EPTTGLDPEAR-------IEVWdtvkelAGSGTTILLTTQYLEEAEQLADRIAIL 207
Cdd:PRK11248 154 EPFGALDAFTReqmqtllLKLW------QETGKQVLLITHDIEEAVFMATELVLL 202
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-221 |
4.77e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.51 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG--------FDVQRQPDHVRQSISltGQFAA 88
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvWNLRRKIGMVFQNPD--NQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 89 L---DGMLTGRENlimiaklRGVSNPAQV--ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:PRK13642 97 AtveDDVAFGMEN-------QGIPREEMIkrVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 164 GLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQlADRIAILHGGKIITTGTLAEL 221
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-217 |
6.75e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.07 E-value: 6.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTlMKQDGGEVSICG---------FDVQRQPDH 75
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGrveffnqniYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 76 VRQSISLTGQFAALDGMlTGRENLIMIAKLRGVSNPAQVADnlLARFSLTDAA---------NQRADQYSGGMKRRLDIA 146
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPM-SVYDNVAYGVKIVGWRPKLEIDD--IVESALKDADlwdeikhkiHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 147 MSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELA-GSGTTILLTTQYLEEAEQLADRIAILHG-----GKIITTGT 217
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGL 239
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-212 |
9.26e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.98 E-value: 9.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 16 KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQ-RQP-DHVRQSISLTGQFAALDGML 93
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPlDAVKKGMAYITESRRDNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 94 TG---RENLIMIAKLR--------GVSNP---AQVADNLLARFSLTDAA-NQRADQYSGGMKRRLDIAMSLIGAPAIIFL 158
Cdd:PRK09700 354 PNfsiAQNMAISRSLKdggykgamGLFHEvdeQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 159 DEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKI 212
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-214 |
1.06e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.59 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 2 SNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVRQSI 80
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQFAALDGMlTGRENLIMIAKLRGVS-NPAQVADNlLARFSLTDAA-NQRADQYSGGMKRRLDIAMSLIGAPAIIFL 158
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLIFPWQIRNQQpDPAIFLDD-LERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 159 DEPTTGLDPEARIEVWDTVKELA-GSGTTILLTTQyleeaeqlaDRIAILHGGKIIT 214
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTH---------DKDEINHADKVIT 209
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-220 |
1.51e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 75.92 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTlmKQDGGEVS-----------------ICGFdVQRQPDHVRQS 79
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITggdrlvngrpldssfqrSIGY-VQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 80 isltgqfaaldgmlTGRENLIMIAKLRgvsNPAQVAD-----------NLLARFSLTDA----------ANQRadqysgg 138
Cdd:TIGR00956 852 --------------TVRESLRFSAYLR---QPKSVSKsekmeyveeviKLLEMESYADAvvgvpgeglnVEQR------- 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 139 mkRRLDIAMSLIGAPA-IIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQ-----YLEEaeqlADRIAILH-GGK 211
Cdd:TIGR00956 908 --KRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHqpsaiLFEE----FDRLLLLQkGGQ 981
|
....*....
gi 1256329087 212 IITTGTLAE 220
Cdd:TIGR00956 982 TVYFGDLGE 990
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-221 |
2.10e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFK----DKEVLKGVDFEVQRGEIFALLGSNGAGKT-TTVNILSTL----MKQDGGEVSICGFDV-- 69
Cdd:PRK15134 1 MTQPLLAIENLSVAFRqqqtVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLpsppVVYPSGDIRFHGESLlh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 70 --QRQPDHVR-QSISLTGQ--FAALDGMLTGRENLIMIAKL-RGVSNPAQVADNL--LARFSLTDAANQRAD---QYSGG 138
Cdd:PRK15134 81 asEQTLRGVRgNKIAMIFQepMVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILncLDRVGIRQAAKRLTDyphQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 139 MKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGT 217
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
....
gi 1256329087 218 LAEL 221
Cdd:PRK15134 241 AATL 244
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-235 |
2.11e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.54 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMK------QDGGEVSICGFDV-QRQPDHVRQSISLTGQFAAL 89
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 90 DGMLTGRENLIMIAKLRGVSNP---AQVADNLLARFSL----TDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKreiKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 163 TGLDPEARIEVWDTVKELAGSgTTILLTTQYLEEAEQLADRIAILHGGKIITTGTlaeLKEMFPPAKVEYIEK 235
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGS---SNEIFTSPKNELTEK 250
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-213 |
2.46e-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: 72.30 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 12 KKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDG---GEVSICGFDVQRQPDHVRQSISLTGQFAA 88
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 89 LDGMLTGRENLIMIAKLRGvsnpaqvadnllarfsltdaaNQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPE 168
Cdd:cd03233 94 HFPTLTVRETLDFALRCKG---------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1256329087 169 ARIEVWDTVKELAGS--GTTILLTTQYLEEAEQLADRIAILHGGKII 213
Cdd:cd03233 153 TALEILKCIRTMADVlkTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-223 |
3.74e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQ-RQPDHVRQS-ISLT 83
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAgIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLIMiakLRGVSNP---------AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPA 154
Cdd:PRK10762 85 HQELNLIPQLTIAENIFL---GREFVNRfgridwkkmYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 155 IIFLDEPTTGL-DPEARiEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:PRK10762 162 VIIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTE 230
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-242 |
4.81e-15 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 74.50 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 19 EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTlMKQDG---GEVSICGFDvQRQPDHVRQSiSLTGQFAALDGMLTG 95
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG-RKTGGyieGDIRISGFP-KKQETFARIS-GYCEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 96 RENLIMIAKLRgvsNPAQVADNLLARF-----------SLTDAANQRA--DQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:PLN03140 971 RESLIYSAFLR---LPKEVSKEEKMMFvdevmelveldNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 163 TGLDPEARIEVWDTVKELAGSGTTILLTTQY--LEEAEQLADRIAILHGGKIITTGTLAELKEMFppakVEYIEKQPTLE 240
Cdd:PLN03140 1048 SGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKI----IEYFEAIPGVP 1123
|
..
gi 1256329087 241 EI 242
Cdd:PLN03140 1124 KI 1125
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-166 |
5.76e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 72.84 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSF--------KDKEVLK---GVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV 69
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 70 ----QRQPDHVRQSISLTGQ--FAALDGMLTGRENL---IMIAKLRGVSNPAQVADNLLARFSL-TDAANQRADQYSGGM 139
Cdd:COG4608 83 tglsGRELRPLRRRMQMVFQdpYASLNPRMTVGDIIaepLRIHGLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQ 162
|
170 180
....*....|....*....|....*..
gi 1256329087 140 KRRLDIAMSLIGAPAIIFLDEPTTGLD 166
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-228 |
6.64e-15 |
|
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: 73.63 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVR--------QSISLtgqfaa 88
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELgrhigylpQDVEL------ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 89 LDGmlTGRENlimIAKLRGVsNPAQVadnllarfslTDAAnQRA----------DQY-----------SGGMKRRLDIAM 147
Cdd:COG4618 418 FDG--TIAEN---IARFGDA-DPEKV----------VAAA-KLAgvhemilrlpDGYdtrigeggarlSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 148 SLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLeEAEQLADRIAILHGGKIITTGTLAE-LKEMFP 226
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEvLARLAR 559
|
..
gi 1256329087 227 PA 228
Cdd:COG4618 560 PA 561
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-221 |
9.19e-15 |
|
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: 71.36 E-value: 9.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 19 EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV--------QRQPDHVRQSISLTGQFAALD 90
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaladpawlRRQVGVVLQENVLFNRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 91 GMLT----GRENLIMIAKLRGvsnpaqvADNLLARFSL--TDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTG 164
Cdd:cd03252 96 IALAdpgmSMERVIEAAKLAG-------AHDFISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 165 LDPEARIEVWDTVKELAgSGTTILLTTQYLEEAEQlADRIAILHGGKIITTGTLAEL 221
Cdd:cd03252 169 LDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-168 |
1.05e-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: 73.05 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSIcGFDVQrqpdhvrqsISLTGQ 85
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK---------LAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 F-AALDG------MLTGRENLIMIAKlRGVSNPAQVadnllARFSLTDAANQ-RADQYSGGMKRRLDIAMSLIGAPAIIF 157
Cdd:TIGR03719 393 SrDALDPnktvweEISGGLDIIKLGK-REIPSRAYV-----GRFNFKGSDQQkKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
170
....*....|.
gi 1256329087 158 LDEPTTGLDPE 168
Cdd:TIGR03719 467 LDEPTNDLDVE 477
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-236 |
1.13e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.37 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 4 AAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRqSISLT 83
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER-GVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLIMIAKLRGVSNPA------QVADNLlarfSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIF 157
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEinqrvnQVAEVL----QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 158 LDEPTTGLDP----EARIEVWDTVKELagsGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL------------ 221
Cdd:PRK11000 157 LDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhypanrfvagf 233
|
250
....*....|....*....
gi 1256329087 222 ----KEMFPPAKVEYIEKQ 236
Cdd:PRK11000 234 igspKMNFLPVKVTATAIE 252
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-225 |
1.73e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.83 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 2 SNAAISI--KGLKKSFKDKE-----VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILST----LMKQDGGEVSICGFDVQ 70
Cdd:TIGR00956 51 PNALLKIltRGFRKLKKFRDtktfdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 71 RQPDHVRQSISLTGQFAALDGMLTGRENLIMIAKLRGVSN----------PAQVADNLLARFSL-----TDAANQRADQY 135
Cdd:TIGR00956 131 EIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQNrpdgvsreeyAKHIADVYMATYGLshtrnTKVGNDFVRGV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 136 SGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAG-SGTTILLTT-QYLEEAEQLADRIAILHGGKII 213
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIyQCSQDAYELFDKVIVLYEGYQI 290
|
250
....*....|..
gi 1256329087 214 TTGTLAELKEMF 225
Cdd:TIGR00956 291 YFGPADKAKQYF 302
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-220 |
1.84e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.83 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 33 IFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG---FDVQRQ---PDHVRQsISLTGQFAALDGMLTGRENLimiakLR 106
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKGiclPPEKRR-IGYVFQDARLFPHYKVRGNL-----RY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 107 GV--SNPAQVAD--------NLLARFSLTdaanqradqYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLD-PEARiEVWD 175
Cdd:PRK11144 100 GMakSMVAQFDKivallgiePLLDRYPGS---------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKR-ELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1256329087 176 TVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAE 220
Cdd:PRK11144 170 YLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-250 |
2.82e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.57 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQ-RQP-DHVRQSISLTGQFAALDGMLTG--- 95
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPqDGLANGIVYISEDRKRDGLVLGmsv 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 96 RENLIMIAkLRGVSNPA---------QVADNLLARFSL-TDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGL 165
Cdd:PRK10762 348 KENMSLTA-LRYFSRAGgslkhadeqQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 166 DPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIitTGtlaelkemfppakvEYIEKQPTLEEIFLA 245
Cdd:PRK10762 427 DVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI--SG--------------EFTREQATQEKLMAA 490
|
....*
gi 1256329087 246 IIGKK 250
Cdd:PRK10762 491 AVGKL 495
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-212 |
5.07e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.13 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 18 KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH----VRQSISLTGQFAALDGML 93
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLRRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 94 TGRENLIMIAKLRGVS--NPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARI 171
Cdd:PRK10908 95 TVYDNVAIPLIIAGASgdDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1256329087 172 EVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKI 212
Cdd:PRK10908 175 GILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-224 |
7.10e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.05 E-value: 7.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTtvnILSTLMKQD-----GGEVSICGFDVqrqpdhvrqsI 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKST---LSATLAGREdyevtGGTVEFKGKDL----------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQFAALDGMLTGRENLIMIAklrGVSNP--AQVADNL---------LARFSLTDAANQRADQ--------------- 134
Cdd:PRK09580 69 ELSPEDRAGEGIFMAFQYPVEIP---GVSNQffLQTALNAvrsyrgqepLDRFDFQDLMEEKIALlkmpedlltrsvnvg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 135 YSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLA-DRIAILHGGKII 213
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIV 225
|
250
....*....|.
gi 1256329087 214 TTGTLAELKEM 224
Cdd:PRK09580 226 KSGDFTLVKQL 236
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-223 |
8.70e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.02 E-value: 8.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV----QRQPDHVRQSIS 81
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 82 LTGQFAALDGMLTGRENLIMiaKLRGVSN-PAQVADNL----LARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAII 156
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAY--PLREHTQlPAPLLHSTvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 157 FLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAELKE 223
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-215 |
8.84e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 8.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 2 SNAAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQP--DHVRQS 79
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASttAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 80 ISLTGQFAALDGMLTGRENLiMIAKL---RGVSNPAQV---ADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAP 153
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENL-YLGQLphkGGIVNRRLLnyeAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 154 AIIFLDEPTTGLdpEAR-IEV-WDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITT 215
Cdd:PRK11288 160 RVIAFDEPTSSL--SAReIEQlFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
15-192 |
9.92e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 9.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 15 FKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTGQFAALDGMLT 94
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 95 GRENLIMIAKLrgvSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVW 174
Cdd:PRK13540 91 LRENCLYDIHF---SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170
....*....|....*...
gi 1256329087 175 DTVKELAGSGTTILLTTQ 192
Cdd:PRK13540 168 TKIQEHRAKGGAVLLTSH 185
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-221 |
1.01e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.49 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 4 AAISIKGLKKSFKDK-EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV-QRQP---Dhvrq 78
Cdd:PRK11650 2 AGLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnELEPadrD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 79 sISLTGQFAALDGMLTGRENLIMIAKLRGVSNP------AQVA-----DNLLARfsltdaanqRADQYSGGMKRRldIAM 147
Cdd:PRK11650 78 -IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAeieervAEAArilelEPLLDR---------KPRELSGGQRQR--VAM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 148 --SLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK11650 146 grAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-221 |
1.46e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.58 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLM-KQDG----GEVSICGFDVQRQPD--HVR 77
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdKVSGyrysGDVLLGGRSIFNYRDvlEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQ------FAALDGMLTG--RENLIMIAKLRGVsnpaqvADNLLARFSLTDAANQRAD----QYSGGMKRRLDI 145
Cdd:PRK14271 101 RRVGMLFQrpnpfpMSIMDNVLAGvrAHKLVPRKEFRGV------AQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 146 AMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSgTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-217 |
2.25e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.85 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSicgFDVQRQPDH----VRQSISLTgqFAALDGMLTGR 96
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIF---YNNQAITDDnfekLRKHIGIV--FQNPDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 97 enlimIAKLR---GVSNPAQVADNL-------LARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLD 166
Cdd:PRK13648 100 -----IVKYDvafGLENHAVPYDEMhrrvseaLKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1256329087 167 PEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQlADRIAILHGGKIITTGT 217
Cdd:PRK13648 175 PDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGT 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
31-221 |
2.47e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 31 GEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG--FDVQRQPDHVRQSISLTGQFAALDGMlTGREnLIMIAKLR-- 106
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpLESWSSKAFARKVAYLPQQLPAAEGM-TVRE-LVAIGRYPwh 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 107 ------GVSNPAQVaDNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKEL 180
Cdd:PRK10575 115 galgrfGAADREKV-EEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1256329087 181 AGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK10575 194 SQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-221 |
2.79e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 69.08 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVRQSISLTGQfaalDGML-- 93
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGIVPQ----DTVLfn 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 94 -TGRENlimIAKLRGVSNPAQVAdnllarfsltdAANQRA----------DQY-----------SGGMKRRLDIAMSLIG 151
Cdd:COG5265 446 dTIAYN---IAYGRPDASEEEVE-----------AAARAAqihdfieslpDGYdtrvgerglklSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 152 APAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLttqyleeAEQL-----ADRIAILHGGKIITTGTLAEL 221
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVARGRTTLVI-------AHRLstivdADEILVLEAGRIVERGTHAEL 579
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-221 |
4.29e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.33 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 2 SNAAISI--KGLK-KSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDgGEVSICGFDV-QRQPDHVR 77
Cdd:PRK11174 344 SNDPVTIeaEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELrELDPESWR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 QSISLTGQ----FAAldgmlTGRENLIM------IAKLRGVSNPAQVAD--NLLARfSLTDAANQRADQYSGGMKRRLDI 145
Cdd:PRK11174 423 KHLSWVGQnpqlPHG-----TLRDNVLLgnpdasDEQLQQALENAWVSEflPLLPQ-GLDTPIGDQAAGLSVGQAQRLAL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 146 AMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQyLEEAEQLaDRIAILHGGKIITTGTLAEL 221
Cdd:PRK11174 497 ARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQ-LEDLAQW-DQIWVMQDGQIVQQGDYAEL 570
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
12-221 |
4.64e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.34 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 12 KKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQ------RQPDHVRQSISLTGQ 85
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPanlkkiKEVKRLRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLIMIAKLRGVSNPAQV---ADNLLARFSLTDAANQRAD-QYSGGMKRRLDIAMSLIGAPAIIFLDEP 161
Cdd:PRK13645 98 FPEYQLFQETIEKDIAFGPVNLGENKQEAykkVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 162 TTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-180 |
8.14e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.91 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAaISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVsicgfdvqRQPDHVRqsI 80
Cdd:PRK09544 1 MTSL-VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR--I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQFAALDGMLTGRENLIMiaKLRgvsnPAQVADNLLARFSLTDAA---NQRADQYSGGMKRRLDIAMSLIGAPAIIF 157
Cdd:PRK09544 70 GYVPQKLYLDTTLPLTVNRFL--RLR----PGTKKEDILPALKRVQAGhliDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180
....*....|....*....|...
gi 1256329087 158 LDEPTTGLDPEARIEVWDTVKEL 180
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQL 166
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
8-223 |
9.37e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.82 E-value: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 8 IKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILS--TLMKQDGGEV-----SICGFDVQrqpDHVRQSI 80
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDIlfkgeSILDLEPE---ERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQFAAldgMLTGRENlimIAKLRGVSNPAQVADNL-----LARFSLT----DAANQRA--------DQYSGGMKRRL 143
Cdd:CHL00131 87 FLAFQYPI---EIPGVSN---ADFLRLAYNSKRKFQGLpeldpLEFLEIIneklKLVGMDPsflsrnvnEGFSGGEKKRN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 144 DIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLA-DRIAILHGGKIITTG--TLAE 220
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGdaELAK 240
|
...
gi 1256329087 221 LKE 223
Cdd:CHL00131 241 ELE 243
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-221 |
1.77e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 66.45 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGfdvqrqpdhvrqSISLTGQFAALDGMLTGRENLI 100
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------------SAALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 101 MIAKLRGVSNP--AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVK 178
Cdd:PRK13545 108 LKGLMMGLTKEkiKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMN 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1256329087 179 ELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK13545 188 EFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-215 |
1.78e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.35 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 9 KGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKtttvnilSTLMK----------QDG-----GEVsiCGFDVQRQP 73
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGK-------STLMKvlsgvyphgsYEGeilfdGEV--CRFKDIRDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 74 DHVrqSISLTGQFAALDGMLTGRENLIM---IAKlRGVSNPAQV---ADNLLARFSLTDAANQRADQYSGGMKRRLDIAM 147
Cdd:NF040905 76 EAL--GIVIIHQELALIPYLSIAENIFLgneRAK-RGVIDWNETnrrARELLAKVGLDESPDTLVTDIGVGKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 148 SLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITT 215
Cdd:NF040905 153 ALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-212 |
2.27e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 24 VDFEVQRGEIFALLGSNGAGKTTTVN-ILSTLMKQDGGEVSICG--FDVQRQPDHVRQSISLTGQFAALDGMLT--GREN 98
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGkpVDIRNPAQAIRAGIAMVPEDRKRHGIVPilGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 99 LIMIAKLRGVSNPAQVADNllARFSLTDAANQRAD-----------QYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDP 167
Cdd:TIGR02633 359 NITLSVLKSFCFKMRIDAA--AELQIIGSAIQRLKvktaspflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1256329087 168 EARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKI 212
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-181 |
3.49e-12 |
|
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: 64.35 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 27 EVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTgqfaaLDGMLTGrenlimiaKLR 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGT-----VRDLLSS--------ITK 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 107 GVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLiGAPAIIFL-DEPTTGLDPEARIEVWDTVKELA 181
Cdd:cd03237 88 DFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACL-SKDADIYLlDEPSAYLDVEQRLMASKVIRRFA 162
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-221 |
3.54e-12 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 65.53 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 19 EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH-VRQSISLTGQ----FAA--LDG 91
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtLRQFINYLPQepyiFSGsiLEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 92 MLTGRENLIMIAKLRGVSNPAQVADNLlARFSL---TDAANQrADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLD-- 166
Cdd:TIGR01193 568 LLLGAKENVSQDEIWAACEIAEIKDDI-ENMPLgyqTELSEE-GSSISGGQKQRIALARALLTDSKVLILDESTSNLDti 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 167 PEARIevwdtVKELAG-SGTTILLTTQYLEEAEQlADRIAILHGGKIITTGTLAEL 221
Cdd:TIGR01193 646 TEKKI-----VNNLLNlQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-219 |
4.70e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 24 VDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG--FDVQRQPDHVRQSISLTGQFAALDGMLTG---REN 98
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGIMLCPEDRKAEGIIPVhsvADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 99 LIMIA-----KLRGVSNP---AQVADNLLARFSL-TDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEA 169
Cdd:PRK11288 352 INISArrhhlRAGCLINNrweAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGA 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1256329087 170 RIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIitTGTLA 219
Cdd:PRK11288 432 KHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI--AGELA 479
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-221 |
4.71e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.04 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDK---------EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHV 76
Cdd:PRK15112 5 LEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 77 R-QSISLTGQFAALDgmLTGREN--------LIMIAKLRGVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAM 147
Cdd:PRK15112 85 RsQRIRMIFQDPSTS--LNPRQRisqildfpLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 148 SLIGAPAIIFLDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-168 |
9.76e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 9.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSIcGFDVQrqpdhvrqsISLTGQ 85
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK---------LAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 F-AALDG------MLTGRENLIMIAKlRGVSNPAQVadnllARFSLTDAANQ-RADQYSGGMKRRLDIAMSLIGAPAIIF 157
Cdd:PRK11819 395 SrDALDPnktvweEISGGLDIIKVGN-REIPSRAYV-----GRFNFKGGDQQkKVGVLSGGERNRLHLAKTLKQGGNVLL 468
|
170
....*....|.
gi 1256329087 158 LDEPTTGLDPE 168
Cdd:PRK11819 469 LDEPTNDLDVE 479
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-217 |
1.93e-11 |
|
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: 61.66 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDK--EVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH-VRQSISL 82
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 83 TGQFAALdGMLTGRENLIMI-----AKLRGVSNPAQVADNLlarfsltdaanqradqySGGMKRRLDIAMSLIGAPAIIF 157
Cdd:cd03369 87 IPQDPTL-FSGTIRSNLDPFdeysdEEIYGALRVSEGGLNL-----------------SQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 158 LDEPTTGLDPEARIEVWDTVKELAgSGTTILLTTQYLEEAEQLaDRIAILHGGKIITTGT 217
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
5-209 |
3.48e-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: 62.49 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDKEVLK-GVD-FE------VQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGevsicgfDVQRQPD-- 74
Cdd:COG1245 65 AISIVNLPEELEEDPVHRyGENgFRlyglpvPKKGKVTGILGPNGIGKSTALKILSGELKPNLG-------DYDEEPSwd 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 75 ----HVRQSIsLTGQFAAL-DGML------------------TGREnLIMIAKLRGVsnpaqvADNLLARFSLTDAANQR 131
Cdd:COG1245 138 evlkRFRGTE-LQDYFKKLaNGEIkvahkpqyvdlipkvfkgTVRE-LLEKVDERGK------LDELAEKLGLENILDRD 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 132 ADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHG 209
Cdd:COG1245 210 ISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILYG 287
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
10-191 |
4.18e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.74 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 10 GLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTtvnILSTLMKQDGGEVSICGFDVqrQPDHVRQSISLTGQFAAL 89
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKST---LLRLLAGALKGTPVAGCVDV--PDNQFGREASLIDAIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 90 DGMLTGREnlimiaklrgvsnpaqvadnLLARFSLTDAANQRA--DQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDP 167
Cdd:COG2401 110 GDFKDAVE--------------------LLNAVGLSDAVLWLRrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*
gi 1256329087 168 EARIEVWDTVKELAGS-GTTILLTT 191
Cdd:COG2401 170 QTAKRVARNLQKLARRaGITLVVAT 194
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-216 |
4.39e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.57 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 24 VDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTGQF------AALDGMLTG-- 95
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFifqdpyASLDPRQTVgd 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 96 --RENLIMIAKLRGVSNPAQVADnLLARFSLT-DAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIE 172
Cdd:PRK10261 423 siMEPLRVHGLLPGKAAAARVAW-LLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1256329087 173 VWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:PRK10261 502 IINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
12-226 |
6.44e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 60.99 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 12 KKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILstlmkqdGGEVSICGFDVQRQPDhvrqsISLTGQFAALDG 91
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNII-------GGSLSPTVGKVDRNGE-----VSVIAISAGLSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 92 MLTGRENLIMIAKLRGVSNP--AQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEA 169
Cdd:PRK13546 99 QLTGIENIEFKMLCMGFKRKeiKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 170 RIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGtlaELKEMFP 226
Cdd:PRK13546 179 AQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG---ELDDVLP 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-226 |
7.36e-11 |
|
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: 61.85 E-value: 7.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 20 VLKGVDFEVQRGEIFALLGSNGAGKTTTVN-ILSTLMKQDGgevsicgfdvqrqpdHVRQS--ISLTGQFA-ALDGmlTG 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPSEG---------------KIKHSgrISFSPQTSwIMPG--TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 96 RENLIMIA-----KLRGVSNPAQVADNlLARFSLTDAA--NQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPE 168
Cdd:TIGR01271 504 KDNIIFGLsydeyRYTSVIKACQLEED-IALFPEKDKTvlGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 169 ARIEVWDT-VKELAGSGTTILLTTQyLEEAEQlADRIAILHGGKIITTGTLAELKEMFP 226
Cdd:TIGR01271 583 TEKEIFEScLCKLMSNKTRILVTSK-LEHLKK-ADKILLLHEGVCYFYGTFSELQAKRP 639
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-221 |
7.73e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.57 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 16 KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVRQSISLTGQ--------- 85
Cdd:PRK11176 354 KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVSQnvhlfndti 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 -----FAALDGMltGRENLIMIAKLRGVSNPAQVADNllarfSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDE 160
Cdd:PRK11176 434 anniaYARTEQY--SREQIEEAARMAYAMDFINKMDN-----GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 161 PTTGLDPEARIEVWDTVKELAgSGTTILLTTQYLEEAEQlADRIAILHGGKIITTGTLAEL 221
Cdd:PRK11176 507 ATSALDTESERAIQAALDELQ-KNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAEL 565
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-172 |
8.51e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.45 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEV------SIcGFDVQrqpDHvrq 78
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenaNI-GYYAQ---DH--- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 79 sislTGQFAaldgmltGRENLI-MIAKLRGVSNPAQVADNLLAR--FSlTDAANQRADQYSGGMKRRLDIAMSLIGAPAI 155
Cdd:PRK15064 392 ----AYDFE-------NDLTLFdWMSQWRQEGDDEQAVRGTLGRllFS-QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170
....*....|....*..
gi 1256329087 156 IFLDEPTTGLDPEArIE 172
Cdd:PRK15064 460 LVMDEPTNHMDMES-IE 475
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-221 |
8.75e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISikglKKSFK--DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVsICGFdvqRQPDHV-- 76
Cdd:PRK10938 1 MSSLQIS----QGTFRlsDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER-QSQF---SHITRLsf 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 77 ---RQSISLTGQFAALDgML------TGRENLIMIakLRGVSNPAQVADnLLARFSLTDAANQRADQYSGGMKRRLDIAM 147
Cdd:PRK10938 73 eqlQKLVSDEWQRNNTD-MLspgeddTGRTTAEII--QDEVKDPARCEQ-LAQQFGITALLDRRFKYLSTGETRKTLLCQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 148 SLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK10938 149 ALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-188 |
9.07e-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: 61.34 E-value: 9.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKD--KEVLKGvdfEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSicgFDVqrqpdhvrqSISLT 83
Cdd:COG1245 342 VEYPDLTKSYGGfsLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDL---------KISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLIMIAKLRGVSNPAQVadNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:COG1245 407 PQYISPDYDGTVEEFLRSANTDDFGSSYYKT--EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180
....*....|....*....|....*.
gi 1256329087 164 GLDPEARIEVWDTVKELA-GSGTTIL 188
Cdd:COG1245 485 HLDVEQRLAVAKAIRRFAeNRGKTAM 510
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-226 |
9.49e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 60.64 E-value: 9.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 20 VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGfdvqrqpdhvrqSISLTGQFA-ALDGmlTGREN 98
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------RISFSSQFSwIMPG--TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 99 LIMIA-----KLRGVSNPAQVADNlLARFSLTDAA--NQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARI 171
Cdd:cd03291 118 IIFGVsydeyRYKSVVKACQLEED-ITKFPEKDNTvlGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 172 EVWDT-VKELAGSGTTILLTTQYleEAEQLADRIAILHGGKIITTGTLAELKEMFP 226
Cdd:cd03291 197 EIFEScVCKLMANKTRILVTSKM--EHLKKADKILILHEGSSYFYGTFSELQSLRP 250
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-217 |
1.17e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.51 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSFK--DKEV--LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDG---GEVSICGFDV---- 69
Cdd:PRK09473 8 QADALLDVKDLRVTFStpDGDVtaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREIlnlp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 70 QRQPDHVR-QSISLTGQ--FAALDGMLTGRENLIMIAKL-RGVSNpaqvADNLLARFSLTDA-----ANQRADQY----S 136
Cdd:PRK09473 88 EKELNKLRaEQISMIFQdpMTSLNPYMRVGEQLMEVLMLhKGMSK----AEAFEESVRMLDAvkmpeARKRMKMYphefS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 137 GGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITT 215
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
|
..
gi 1256329087 216 GT 217
Cdd:PRK09473 244 GN 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-212 |
1.56e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 18 KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVN-ILSTLMKQDGGEVSICG--FDVQRQPDHVRQSISLTGQFAALDGMLT 94
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGkpVKIRNPQQAIAQGIAMVPEDRKRDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 95 G---RENlIMIAKLRGVSNPAQVADNL--------LARFSL-TDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPT 162
Cdd:PRK13549 355 VmgvGKN-ITLAALDRFTGGSRIDDAAelktilesIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1256329087 163 TGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKI 212
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-217 |
1.57e-10 |
|
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: 59.04 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKD--KEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH-VRQSISL 82
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHdLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 83 TGQFAAL-DGmlTGRENLimiaKLRGVSNPAQVAdNLLARFSLTDAANQRADQ-----------YSGGMKRRLDIAMSLI 150
Cdd:cd03244 83 IPQDPVLfSG--TIRSNL----DPFGEYSDEELW-QALERVGLKEFVESLPGGldtvveeggenLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 151 GAPAIIFLDEPTTGLDPEARIEVWDTVKElAGSGTTILLTTQYLEEAEQlADRIAILHGGKIITTGT 217
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-209 |
2.05e-10 |
|
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: 59.30 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 31 GEIFALLGSNGAGKTTTVNILSTLMKQDGGEVsicgfdvQRQPD------HVRQSiSLTGQFAALDGmltgrENLIMIAK 104
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKF-------DDPPDwdeildEFRGS-ELQNYFTKLLE-----GDVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 105 LRGVSN-PAQVA----------------DNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDP 167
Cdd:cd03236 93 PQYVDLiPKAVKgkvgellkkkdergklDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1256329087 168 EARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHG 209
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYG 214
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-189 |
2.36e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 14 SFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILS-----------TLM-KQDGGEVSIcgFDVQRQPDHVRQSIS 81
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndlTLFgRRRGSGETI--WDIKKHIGYVSSSLH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 82 LTGQFA--ALDGMLTGRENLIMIakLRGVSNPAQV-ADNLLARFSLTDA-ANQRADQYSGGMKRRLDIAMSLIGAPAIIF 157
Cdd:PRK10938 347 LDYRVStsVRNVILSGFFDSIGI--YQAVSDRQQKlAQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLLI 424
|
170 180 190
....*....|....*....|....*....|..
gi 1256329087 158 LDEPTTGLDPEARIEVWDTVKELAGSGTTILL 189
Cdd:PRK10938 425 LDEPLQGLDPLNRQLVRRFVDVLISEGETQLL 456
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-221 |
2.42e-10 |
|
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: 60.08 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 11 LKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQdGGEVSICGFDVQRQPDH----VRQSISLTGQ- 85
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRalrpLRRRMQVVFQd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 -FAALDGMLTGREnliMIA--------KLRGVSNPAQVADnLLARFSLTDAANQRadqY----SGGMKRRLDIAMSLIGA 152
Cdd:COG4172 371 pFGSLSPRMTVGQ---IIAeglrvhgpGLSAAERRARVAE-ALEEVGLDPAARHR---YphefSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 153 PAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG4172 444 PKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-211 |
3.81e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 57.86 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKDKE-----VLKGVDFEVQRGEIFALLGSNGAGKTTtvnILSTL---MKQDGGEVSICGfdvqrqpdhvr 77
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPG----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 78 qSISLTGQFAALDGMlTGRENLIMIAKL------RGVSNPAQVADnlLARFSLTDAAN--QRADQYSGGMKRRLDIAMSL 149
Cdd:cd03250 67 -SIAYVSQEPWIQNG-TIRENILFGKPFdeeryeKVIKACALEPD--LEILPDGDLTEigEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 150 IGAPAIIFLDEPTTGLDPEARIEVWDTV--KELAGSGTTILLT--TQYLEEaeqlADRIAILHGGK 211
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIFENCilGLLLNNKTRILVThqLQLLPH----ADQIVVLDNGR 204
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
6-221 |
3.91e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.95 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSF--KDKEVL-----------KGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQ 72
Cdd:PRK15079 9 LEVADLKVHFdiKDGKQWfwqppktlkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 73 PD----HVRQSISLTGQ--FAALDGMLTGREnliMIAKLRGVSNP----AQVAD---NLLARFSL-TDAANQRADQYSGG 138
Cdd:PRK15079 89 KDdewrAVRSDIQMIFQdpLASLNPRMTIGE---IIAEPLRTYHPklsrQEVKDrvkAMMLKVGLlPNLINRYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 139 MKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGS-GTTILLTTQYLEEAEQLADRIAILHGGKIITTGT 217
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGT 245
|
....
gi 1256329087 218 LAEL 221
Cdd:PRK15079 246 YDEV 249
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
9-221 |
4.62e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.82 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 9 KGLkksFKDKEVLK---GVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQrQPDHV-----RQSI 80
Cdd:PRK11308 19 RGL---FKPERLVKaldGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL-KADPEaqkllRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQ--FAALD-----GMLTGrENLIMIAKLRGVSNPAQVADnLLARFSL-TDAANQRADQYSGGMKRRLDIAMSLIGA 152
Cdd:PRK11308 95 QIVFQnpYGSLNprkkvGQILE-EPLLINTSLSAAERREKALA-MMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 153 PAIIFLDEPTTGLDPEARIEV----WDTVKELagsGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVlnlmMDLQQEL---GLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-166 |
5.19e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.95 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 11 LKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGevsiCGFDVQ-------RQPDHVRQSISLT 83
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGE----IWFDGQplhnlnrRQLLPVRHRIQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 gqFAALDGMLTGRENLIMI---------AKLRGVSNPAQVADnLLARFSLTDAANQR-ADQYSGGMKRRLDIAMSLIGAP 153
Cdd:PRK15134 368 --FQDPNSSLNPRLNVLQIieeglrvhqPTLSAAQREQQVIA-VMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKP 444
|
170
....*....|...
gi 1256329087 154 AIIFLDEPTTGLD 166
Cdd:PRK15134 445 SLIILDEPTSSLD 457
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-188 |
6.71e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKKSFKD--KEVLKGvdfEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSicgFDVqrqpdhvrqSISLT 83
Cdd:PRK13409 341 VEYPDLTKKLGDfsLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---PEL---------KISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 GQFAALDGMLTGRENLIMIAKLRGvSNPAQVadNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTT 163
Cdd:PRK13409 406 PQYIKPDYDGTVEDLLRSITDDLG-SSYYKS--EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170 180
....*....|....*....|....*.
gi 1256329087 164 GLDPEARIEVWDTVKELA-GSGTTIL 188
Cdd:PRK13409 483 HLDVEQRLAVAKAIRRIAeEREATAL 508
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-221 |
1.33e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFK---DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVN-ILSTLMKQDGGEVSIcgfdvqrqpdhvRQSI 80
Cdd:PLN03232 614 AISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI------------RGSV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQFAALDGMlTGRENLIMIAKL------RGVSNPAQVAD-NLLARFSLTDAAnQRADQYSGGMKRRLDIAMSLIGAP 153
Cdd:PLN03232 682 AYVPQVSWIFNA-TVRENILFGSDFeserywRAIDVTALQHDlDLLPGRDLTEIG-ERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 154 AIIFLDEPTTGLDPEARIEVWDT-VKELAGSGTTILLTTQ--YLEeaeqLADRIAILHGGKIITTGTLAEL 221
Cdd:PLN03232 760 DIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQlhFLP----LMDRIILVSEGMIKEEGTFAEL 826
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
5-209 |
1.42e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKGLKKSFKDKEVLK-GVD-FE------VQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGevsicgfDVQRQP--- 73
Cdd:PRK13409 65 AISIVNLPEELEEEPVHRyGVNgFKlyglpiPKEGKVTGILGPNGIGKTTAVKILSGELIPNLG-------DYEEEPswd 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 74 ---DHVRQS---------------ISLTGQF-----AALDGmlTGREnLIMIAKLRGvsnpaqVADNLLARFSLTDAANQ 130
Cdd:PRK13409 138 evlKRFRGTelqnyfkklyngeikVVHKPQYvdlipKVFKG--KVRE-LLKKVDERG------KLDEVVERLGLENILDR 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 131 RADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAgSGTTILLTTQYLEEAEQLADRIAILHG 209
Cdd:PRK13409 209 DISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDLAVLDYLADNVHIAYG 286
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-205 |
3.62e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.94 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTV---NILSTLMK--QDGGEVSICG---FDVQRQPDHVRQSISLTGQ----FAA 88
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPgfRVEGKVTFHGknlYAPDVDPVEVRRRIGMVFQkpnpFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 89 ldgmlTGRENLIMIAKLRGVSNPAqvaDNLLARfSLTDAA---------NQRADQYSGGMKRRLDIAMSLIGAPAIIFLD 159
Cdd:PRK14243 106 -----SIYDNIAYGARINGYKGDM---DELVER-SLRQAAlwdevkdklKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1256329087 160 EPTTGLDPEARIEVWDTVKELaGSGTTILLTTQYLEEAEQLADRIA 205
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-231 |
6.97e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 20 VLKGVDFEVQRGEIFALLGSNGAGKtttvnilSTLMKQDGGEvsICGfDVQRQPDHVRQSISLTGQ-FAALDGMltgren 98
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGK-------STLLKALAGD--LTG-GGAPRGARVTGDVTLNGEpLAAIDAP------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 99 liMIAKLRGV----SNPA----------------------------QVADNLLARFSLTDAANQRADQYSGGMKRRLDIA 146
Cdd:PRK13547 80 --RLARLRAVlpqaAQPAfafsareivllgrypharragalthrdgEIAWQALALAGATALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 147 MSL---------IGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQY-LEEAEQLADRIAILHGGKIITTG 216
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHdPNLAARHADRIAMLADGAIVAHG 237
|
250
....*....|....*
gi 1256329087 217 TLAelkEMFPPAKVE 231
Cdd:PRK13547 238 APA---DVLTPAHIA 249
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-242 |
7.21e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 5 AISIKG---LKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVN-ILSTLMKQDGGEVSIcgfdvqrqpdhvRQSI 80
Cdd:PLN03130 614 AISIKNgyfSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI------------RGTV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQ----FAAldgmlTGRENLIMIAKL------RGVSNPAQVAD-NLLARFSLTDAAnQRADQYSGGMKRRLDIAMSL 149
Cdd:PLN03130 682 AYVPQvswiFNA-----TVRDNILFGSPFdperyeRAIDVTALQHDlDLLPGGDLTEIG-ERGVNISGGQKQRVSMARAV 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 150 IGAPAIIFLDEPTTGLDPEARIEVWDT-VKELAGSGTTILLTTQyLEEAEQLaDRIAILHGGKIITTGTLAEL------- 221
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQ-LHFLSQV-DRIILVHEGMIKEEGTYEELsnngplf 833
|
250 260
....*....|....*....|..
gi 1256329087 222 -KEMFPPAKVEYIEKQPTLEEI 242
Cdd:PLN03130 834 qKLMENAGKMEEYVEENGEEED 855
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-221 |
7.46e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.13 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 4 AAISIKGLKKSFKDKEV-LKGVD---FEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDG----GEVSICGFDVQRQPDH 75
Cdd:PRK11022 2 ALLNVDKLSVHFGDESApFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 76 VRQSisLTGQFAAL---DGMLT-------GREnlIMIA-KLRGVSNPA---QVADNLLARFSLTDAANqRADQY----SG 137
Cdd:PRK11022 82 ERRN--LVGAEVAMifqDPMTSlnpcytvGFQ--IMEAiKVHQGGNKKtrrQRAIDLLNQVGIPDPAS-RLDVYphqlSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 138 GMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELA-GSGTTILLTTQYLEEAEQLADRIAILHGGKIITTG 216
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
....*
gi 1256329087 217 TLAEL 221
Cdd:PRK11022 237 KAHDI 241
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
17-190 |
7.86e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 54.02 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQD---GGEVSICGFDVQRQPDHVRQsISLTGQFAALDGML 93
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRR-IGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 94 TGRENLiMIAKLRGVSNPA--QVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARI 171
Cdd:COG4136 92 SVGENL-AFALPPTIGRAQrrARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180
....*....|....*....|...
gi 1256329087 172 E----VWDTVKELAGSgtTILLT 190
Cdd:COG4136 171 QfrefVFEQIRQRGIP--ALLVT 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-221 |
7.89e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 8 IKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH---------VRQ 78
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealengismVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 79 SISLTGQFAALDGMLTGRenlimiAKLRGV-SNPAQVADNLLARFSLTDA---ANQRADQYSGGMKRRLDIAMSLIGAPA 154
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGR------YPTKGMfVDQDKMYRDTKAIFDELDIdidPRAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1256329087 155 IIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-221 |
1.14e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.11 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 1 MSNAAISIKGLKKSF-KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHV-RQ 78
Cdd:PRK10790 336 LQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 79 SISLTGQFAAL--DGMLT----GREnlIMIAKLRGVSNPAQVADnlLARfSLTDAANQR----ADQYSGGMKRRLDIAMS 148
Cdd:PRK10790 416 GVAMVQQDPVVlaDTFLAnvtlGRD--ISEEQVWQALETVQLAE--LAR-SLPDGLYTPlgeqGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 149 LIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAgSGTTILLTTQYLEEAEQlADRIAILHGGKIITTGTLAEL 221
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVR-EHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-220 |
1.39e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.78 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 26 FEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGgEVSICGFDVQ--RQPDHVRQSISLTGQFAALDGM-----LTgren 98
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSG-SIQFAGQPLEawSAAELARHRAYLSQQQTPPFAMpvfqyLT---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 99 LIMIAKLRgVSNPAQVADNLLARFSLTDAANQRADQYSGGMKRRLDIAMSLIG-APAI------IFLDEPTTGLDPeARI 171
Cdd:PRK03695 92 LHQPDKTR-TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLDV-AQQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1256329087 172 EVWDT-VKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAE 220
Cdd:PRK03695 170 AALDRlLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-174 |
2.00e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 4 AAISIKGLKKSFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGfDV-----QRQP----- 73
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLivarlQQDPprnve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 74 ----DHVRQSISLTGQF-----AALDGMLT--GRENLIMIAKLRGV---SNPAQVAD---NLLARFSLTdaANQRADQYS 136
Cdd:PRK11147 81 gtvyDFVAEGIEEQAEYlkryhDISHLVETdpSEKNLNELAKLQEQldhHNLWQLENrinEVLAQLGLD--PDAALSSLS 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1256329087 137 GGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEArIEvW 174
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIET-IE-W 194
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-221 |
2.23e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 20 VLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQR-QPDHVRQSISLTGQFAAL-DGmlTGRE 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLfSG--TVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 98 NLIMI-----AKLRGVSNPAQVADNL-LARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARI 171
Cdd:PLN03232 1329 NIDPFsehndADLWEALERAHIKDVIdRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1256329087 172 EVWDTVKELAGSGTTILLttqyleeAEQL-----ADRIAILHGGKIITTGTLAEL 221
Cdd:PLN03232 1409 LIQRTIREEFKSCTMLVI-------AHRLntiidCDKILVLSSGQVLEYDSPQEL 1456
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-212 |
2.27e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDH---------VRQSISLTGQFAALDG 91
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeainhgfalVTEERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 92 MLTGrenliMIAKLRGVSNPAQVADNllARFS-----LTDAANQRADQY-------SGGMKRRLDIAMSLIGAPAIIFLD 159
Cdd:PRK10982 344 GFNS-----LISNIRNYKNKVGLLDN--SRMKsdtqwVIDSMRVKTPGHrtqigslSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 160 EPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKI 212
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-216 |
2.33e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.33 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTVNilstlmkqDGGEVSICgfdvqrqpdhvRQSISLTGQFAaldgmltgRENLI 100
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--------EGLYASGK-----------ARLISFLPKFS--------RNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 101 MIAKLRGVSnpaqvaDNLLARFSLtdaaNQRADQYSGGMKRRLDIAMSLIGAP--AIIFLDEPTTGLDPEARIEVWDTVK 178
Cdd:cd03238 64 FIDQLQFLI------DVGLGYLTL----GQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIK 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1256329087 179 ELAGSGTTILLtTQYLEEAEQLADRI------AILHGGKIITTG 216
Cdd:cd03238 134 GLIDLGNTVIL-IEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
122-192 |
1.63e-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: 1.63e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 122 FSLTDAANQRADQYSGGMKRRLDIAMSLIGA---PAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQ 192
Cdd:pfam13304 224 LENGGGGELPAFELSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-168 |
1.77e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 14 SFKDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSiCG-------FDVQRqpdhvrqsisltgqf 86
Cdd:PRK11147 328 QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGtklevayFDQHR--------------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 87 AALDGMLTGRENL------IMI-AKLRGVSNPAQvaDNLlarFSltdaaNQRADQ----YSGGMKRRLDIAMSLIGAPAI 155
Cdd:PRK11147 392 AELDPEKTVMDNLaegkqeVMVnGRPRHVLGYLQ--DFL---FH-----PKRAMTpvkaLSGGERNRLLLARLFLKPSNL 461
|
170
....*....|...
gi 1256329087 156 IFLDEPTTGLDPE 168
Cdd:PRK11147 462 LILDEPTNDLDVE 474
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-219 |
1.80e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTT----------VNILSTLMKqDGGEVSICgfDVQRQPDH----------- 75
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELamsvfgrsygRNISGTVFK-DGKEVDVS--TVSDAIDAglayvtedrkg 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 76 --------VRQSISLtgqfAALDGmltgrenlimIAKlRGVSNPA---QVADNLLARFSL-TDAANQRADQYSGGMKRRL 143
Cdd:NF040905 349 yglnliddIKRNITL----ANLGK----------VSR-RGVIDENeeiKVAEEYRKKMNIkTPSVFQKVGNLSGGNQQKV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 144 DIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQLADRIAILHGGKIitTGTLA 219
Cdd:NF040905 414 VLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI--TGELP 487
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-221 |
3.00e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.10 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 17 DKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVsicgfdvqrqpdHVRQSISLTGQFAALDGMlTGR 96
Cdd:TIGR00957 650 LPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV------------HMKGSVAYVPQQAWIQND-SLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 97 ENLIMIAKLRGVSNPAQV-ADNLLARFSLTDAANQ-----RADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEAR 170
Cdd:TIGR00957 717 ENILFGKALNEKYYQQVLeACALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 171 IEVWDTV---KELAGSGTTILLT--TQYLEEaeqlADRIAILHGGKIITTGTLAEL 221
Cdd:TIGR00957 797 KHIFEHVigpEGVLKNKTRILVThgISYLPQ----VDVIIVMSGGKISEMGSYQEL 848
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-209 |
3.29e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.11 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 27 EVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPdhvrQSISLtgqfaaldgmltgrenlimiaklr 106
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP----QYIDL------------------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 107 gvsnpaqvadnllarfsltdaanqradqySGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGT- 185
Cdd:cd03222 73 -----------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKk 123
|
170 180
....*....|....*....|....
gi 1256329087 186 TILLTTQYLEEAEQLADRIAILHG 209
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-191 |
1.25e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 38 GSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPdhvRQSISLTGQFAALDGMLTGRENLIMIAKlrgVSNPAQVADN 117
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA---KPYCTYIGHNLGLKLEMTVFENLKFWSE---IYNSAETLYA 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 118 LLARFSLTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTT 191
Cdd:PRK13541 107 AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSS 180
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
145-221 |
1.43e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.26 E-value: 1.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1256329087 145 IAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKEL-AGSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
145-223 |
2.15e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.98 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 145 IAMSLIGAPAIIFLDEPTTGLDP--EARI-EVWDTVKELagSGTTILLTTQYLEEAEQLADRIAILHGGKIITTGTLAEL 221
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESttQAQIfRLLARLNQL--QGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQI 246
|
..
gi 1256329087 222 KE 223
Cdd:COG4170 247 LK 248
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-207 |
2.52e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 16 KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSIC------------------------------ 65
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkdinlkwwrskigvvsqdpllfsns 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 66 -------------------------GFDVQRQPDHVRQ-------SISLTGQFAALDGMLTGRENLIMIAKLRGVSNPAQ 113
Cdd:PTZ00265 476 iknnikyslyslkdlealsnyynedGNDSQENKNKRNScrakcagDLNDMSNTTDSNELIEMRKNYQTIKDSEVVDVSKK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 114 VadnLLARF--SLTDA----ANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTI 187
Cdd:PTZ00265 556 V---LIHDFvsALPDKyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 632
|
250 260
....*....|....*....|
gi 1256329087 188 LLTTQYLEEAEQLADRIAIL 207
Cdd:PTZ00265 633 TIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
133-207 |
5.38e-06 |
|
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: 45.43 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 133 DQYSGGMKRRLDIAM-----SLIGAPaIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEqLADRIAIL 207
Cdd:cd03227 76 LQLSGGEKELSALALilalaSLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAE-LADKLIHI 153
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-168 |
1.08e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 46.08 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 7 SIKGLKKSF-KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVsicgfdvQRQPDHvrqSISLTGQ 85
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA-------RPQPGI---KVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLI--------MIAKLRGVSN----PAQVADNLLARFS----LTDAAN-------------------- 129
Cdd:TIGR03719 76 EPQLDPTKTVRENVEegvaeikdALDRFNEISAkyaePDADFDKLAAEQAelqeIIDAADawdldsqleiamdalrcppw 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1256329087 130 -QRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPE 168
Cdd:TIGR03719 156 dADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
136-209 |
1.36e-05 |
|
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: 44.07 E-value: 1.36e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 136 SGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELagsGTTIlLTTQYLEEAEQLADRIAILHG 209
Cdd:cd03223 93 SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITV-ISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
21-212 |
1.91e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.35 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 21 LKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDV-QRQPDHVRQSISLTGQFAALDGMLTGRENl 99
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRKLFSAVFTDFHLFDQLLGPEG- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 100 imiaklrGVSNPAQVaDNLLARFSLTD----AANQRAD-QYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVW 174
Cdd:PRK10522 418 -------KPANPALV-EKWLERLKMAHklelEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFY 489
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1256329087 175 -DTVKELAGSGTTILLTTQ---YLEeaeqLADRIAILHGGKI 212
Cdd:PRK10522 490 qVLLPLLQEMGKTIFAISHddhYFI----HADRLLEMRNGQL 527
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
6-191 |
2.11e-05 |
|
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: 44.99 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKkSFKDKEVlkgvDFEvqrGEIFALLGSNGAGKTTTVNILSTLMKQDGG-EVSICGFDVQRQPDHVRQSISLT- 83
Cdd:COG3593 6 IKIKNFR-SIKDLSI----ELS---DDLTVLVGENNSGKSSILEALRLLLGPSSSrKFDEEDFYLGDDPDLPEIEIELTf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 84 ----GQFAALDGMLTGRENLI----------------MIAKLRGVSNPAQVADNLLARFSLTDAANQRAD---QYSGGMK 140
Cdd:COG3593 78 gsllSRLLRLLLKEEDKEELEealeelneelkealkaLNELLSEYLKELLDGLDLELELSLDELEDLLKSlslRIEDGKE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 141 RRLD---------IAMSLI---------GAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTT 191
Cdd:COG3593 158 LPLDrlgsgfqrlILLALLsalaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITT 226
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
129-220 |
6.68e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 129 NQRADQYSGGMKRRLDIA----MSLIGAPAIifLDEPTTGLDPEARIEVWDTVKELAGSGTTILLttqyLEEAEQ---LA 201
Cdd:PRK00635 471 ERALATLSGGEQERTALAkhlgAELIGITYI--LDEPSIGLHPQDTHKLINVIKKLRDQGNTVLL----VEHDEQmisLA 544
|
90 100
....*....|....*....|....*
gi 1256329087 202 DRI------AILHGGKIITTGTLAE 220
Cdd:PRK00635 545 DRIidigpgAGIFGGEVLFNGSPRE 569
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-169 |
7.76e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 20 VLKGVDFEVQRGEIFALLGSNGAGKtttvnilSTLMKQDGGEVSICGFDVQRQPDhVRQSISLTGQFAALDgmLTGRENL 99
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGK-------STILKLISGELQPSSGTVFRSAK-VRMAVFSQHHVDGLD--LSSNPLL 593
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1256329087 100 IMIAKLRGVsnPAQVADNLLARFSLT-DAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEA 169
Cdd:PLN03073 594 YMMRCFPGV--PEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA 662
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-223 |
7.77e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 129 NQRADQYSGGMKRRLDIAmSLIGAP---AIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTtQYLEEAEQLADRI- 204
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLA-TQIGSGltgVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVV-EHDEDTIRAADYVi 560
|
90 100
....*....|....*....|....
gi 1256329087 205 -----AILHGGKIITTGTLAELKE 223
Cdd:TIGR00630 561 digpgAGEHGGEVVASGTPEEILA 584
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
36-166 |
9.46e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 36 LLGSNGAGKTTTVNILSTLMKQDGGEVSIcgfDVQRQPDHVRQSisltgQFA-----ALDGMLTGRENL--IMIAKLRGV 108
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSL---DPNERLGKLRQD-----QFAfeeftVLDTVIMGHTELweVKQERDRIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 109 SNPA-------QVADnLLARFSLTD--AANQRA-----------DQYSGGM-------KRRLDIAMSLIGAPAIIFLDEP 161
Cdd:PRK15064 104 ALPEmseedgmKVAD-LEVKFAEMDgyTAEARAgelllgvgipeEQHYGLMsevapgwKLRVLLAQALFSNPDILLLDEP 182
|
....*
gi 1256329087 162 TTGLD 166
Cdd:PRK15064 183 TNNLD 187
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-220 |
1.26e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 18 KEVLKGVDFEVQRGEIFALLGSNGAGKTTtvnILSTLMKQdggevsicgFDVQRQPDHVRQSISLTGQFAaldgmltgre 97
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKST---LLQSLLSQ---------FEISEGRVWAERSIAYVPQQA---------- 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 98 nLIMIAKLRG------VSNPAQVADNL--------LARFS--LTDAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEP 161
Cdd:PTZ00243 731 -WIMNATVRGnilffdEEDAARLADAVrvsqleadLAQLGggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 162 TTGLDPEARIEVwdtVKE-----LAGSgTTILLTTQYleEAEQLADRIAILHGGKIITTGTLAE 220
Cdd:PTZ00243 810 LSALDAHVGERV---VEEcflgaLAGK-TRVLATHQV--HVVPRADYVVALGDGRVEFSGSSAD 867
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
34-221 |
1.78e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 34 FALLGSNGAGKTTTVNILSTLMKQDGgeVSICGFDVQrqpdHVRQSISLTGQFAALDGMLT------GRENlimiAKLRG 107
Cdd:PTZ00265 1258 FSLTKEGGSGEDSTVFKNSGKILLDG--VDICDYNLK----DLRNLFSIVSQEPMLFNMSIyenikfGKED----ATRED 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 108 VSNPAQVA--DNLLArfSLTDAANQRADQY----SGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELA 181
Cdd:PTZ00265 1328 VKRACKFAaiDEFIE--SLPNKYDTNVGPYgkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1256329087 182 GSGTTILLTTQYLEEAEQLADRIAILH-----GGKIITTGTLAEL 221
Cdd:PTZ00265 1406 DKADKTIITIAHRIASIKRSDKIVVFNnpdrtGSFVQAHGTHEEL 1450
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
6-181 |
2.96e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.76 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKkSFKDKEVlkgVDFEvqrGEIFALLGSNGAGKTT---------------TVNILSTLMKQDGGEVSI-CGFDV 69
Cdd:COG0419 5 LRLENFR-SYRDTET---IDFD---DGLNLIVGPNGAGKSTileairyalygkarsRSKLRSDLINVGSEEASVeLEFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 70 QRQPDHV--RQsisltGQFAALdGMLTGRENLIMIAKLRGVSNPAQVADNL----------LARFSLTDAANQR------ 131
Cdd:COG0419 78 GGKRYRIerRQ-----GEFAEF-LEAKPSERKEALKRLLGLEIYEELKERLkeleealesaLEELAELQKLKQEilaqls 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 132 ----ADQYSGGMKRRLDIAMSLigapaIIFLDepTTGLDPEARIEVWDTVKELA 181
Cdd:COG0419 152 gldpIETLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEELA 198
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
136-188 |
4.19e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 41.33 E-value: 4.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1256329087 136 SGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKElAGSGTTIL 188
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVI 538
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-81 |
5.31e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 40.94 E-value: 5.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1256329087 24 VDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQ-PDHVRQSIS 81
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADnREAYRQLFS 409
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-206 |
6.14e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.28 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 30 RGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICGFDVQRQPDHVRQSISLTGQFAAldgmltgrenlimiaklrgvs 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 110 npaqvadnllarfsltdaanqradQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTV------KELAGS 183
Cdd:smart00382 60 ------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrlllLLKSEK 115
|
170 180
....*....|....*....|...
gi 1256329087 184 GTTILLTTQYLEEAEQLADRIAI 206
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
31-190 |
1.25e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 31 GEIFALLGSNGAGKTTTVNILSTLMKQDGGEVSICG-----FDVQRQP-------DHVrqsISLTGQFAALDGML---TG 95
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlaWVNQETPalpqpalEYV---IDGDREYRQLEAQLhdaNE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 96 RENLIMIAKLRGVSNPAQV------ADNLLARFSLTDAANQR-ADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPE 168
Cdd:PRK10636 104 RNDGHAIATIHGKLDAIDAwtirsrAASLLHGLGFSNEQLERpVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD 183
|
170 180
....*....|....*....|....
gi 1256329087 169 ARI--EVWdtVKELagSGTTILLT 190
Cdd:PRK10636 184 AVIwlEKW--LKSY--QGTLILIS 203
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
6-99 |
1.64e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.83 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKkSFKDKEVlkgvDFEVQRGeIFALLGSNGAGKTTTVNILSTLM--------------------KQDGGEVSIC 65
Cdd:COG3950 6 LTIENFR-GFEDLEI----DFDNPPR-LTVLVGENGSGKTTLLEAIALALsgllsrlddvkfrkllirngEFGDSAKLIL 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1256329087 66 GFDVQR------QPDHVRQSISLTGQFAALDGMLTGRENL 99
Cdd:COG3950 80 YYGTSRllldgpLKKLERLKEEYFSRLDGYDSLLDEDSNL 119
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-168 |
2.39e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.95 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 7 SIKGLKKSF-KDKEVLKGVDFEVQRGEIFALLGSNGAGKTTTVNILSTLMKQDGGEVsicgfdvQRQPDHvrqSISLTGQ 85
Cdd:PRK11819 8 TMNRVSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA-------RPAPGI---KVGYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 86 FAALDGMLTGRENLI--------MIAKLRGVS----NPAQVADNLLARFS----LTDAAN---------QRAD------- 133
Cdd:PRK11819 78 EPQLDPEKTVRENVEegvaevkaALDRFNEIYaayaEPDADFDALAAEQGelqeIIDAADawdldsqleIAMDalrcppw 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1256329087 134 -----QYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPE 168
Cdd:PRK11819 158 dakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
6-170 |
2.84e-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: 37.97 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 6 ISIKGLKkSFKDKEVlkgVDFevqRGEIFALLGSNGAGKTTtvnILSTLMKQDGGEVSICGFDVQRQPD-----HVRQSI 80
Cdd:cd03240 4 LSIRNIR-SFHERSE---IEF---FSPLTLIVGQNGAGKTT---IIEALKYALTGELPPNSKGGAHDPKliregEVRAQV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 81 SLTGQFAALDGMLTGR-----ENLIMIaklrgvsnPAQVADNLLARfsltdaanqRADQYSGGMKR------RLDIAMSL 149
Cdd:cd03240 74 KLAFENANGKKYTITRslailENVIFC--------HQGESNWPLLD---------MRGRCSGGEKVlasliiRLALAETF 136
|
170 180
....*....|....*....|.
gi 1256329087 150 IGAPAIIFLDEPTTGLDPEAR 170
Cdd:cd03240 137 GSNCGILALDEPTTNLDEENI 157
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
130-221 |
3.47e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 130 QRADQYSGGMKRRLDIAMSL---IGAPAIIFLDEPTTGLDPEARIEVWDTVKELAGSGTTILLTTQYLEEAEQlADRIAI 206
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKT-ADYIID 903
|
90 100
....*....|....*....|.
gi 1256329087 207 L------HGGKIITTGTLAEL 221
Cdd:TIGR00630 904 LgpeggdGGGTVVASGTPEEV 924
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
136-225 |
3.53e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 38.67 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1256329087 136 SGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEARIEVWDTVKELA--GSGTTILLTTQYLEEAEQLADRIAILHGGKII 213
Cdd:PLN03140 338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVhlTEATVLMSLLQPAPETFDLFDDIILLSEGQIV 417
|
90
....*....|..
gi 1256329087 214 TTGTLAELKEMF 225
Cdd:PLN03140 418 YQGPRDHILEFF 429
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
115-169 |
3.60e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.30 E-value: 3.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1256329087 115 ADNLLARFSLT-DAANQRADQYSGGMKRRLDIAMSLIGAPAIIFLDEPTTGLDPEA 169
Cdd:PLN03073 324 AASILAGLSFTpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA 379
|
|
| NAD-GH |
pfam10712 |
NAD-specific glutamate dehydrogenase; The members of this are annotated as being NAD-specific ... |
30-91 |
7.97e-03 |
|
NAD-specific glutamate dehydrogenase; The members of this are annotated as being NAD-specific glutamate dehydrogenase encoded in antisense gene pair with DnaK-J.
Pssm-ID: 402378 Cd Length: 576 Bit Score: 37.08 E-value: 7.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1256329087 30 RGEIFALLGSNGAgktttvnilstLMKQDGGEVSICGFDVQRQPDHVRQS--ISLTGQFAALDG 91
Cdd:pfam10712 152 GGEHLRLLGRDGG-----------VALDDLREHAAHHLDAQRQRGHVQQQhvLDLTGQDAALDR 204
|
|
| |
