|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-216 |
7.18e-105 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 305.45 E-value: 7.18e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVPD 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRENLLFMAKLYDAP----RERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTN 158
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPrkeaRERIDELLELFGLTdaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880368 159 GLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-296 |
6.42e-92 |
|
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: 275.04 E-value: 6.42e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 12 KRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVPDVSNLYDE 91
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 92 LTVRENLLFMAKLYDAP----RERVDELIREFEL--PADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSA 165
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPkdeaEERAEELLELFELgeAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 166 RAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAKLVGRKTVVRLSVEPLS----------- 234
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSlkvevsmliae 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880368 235 --SSLLRALERYNPSfEEGKLvfEVDDVDGFLEELCSLRVELGFRVTSLCTEIPGIEDVFVELT 296
Cdd:TIGR01188 241 lgETGLGLLAVTVDS-DRIKI--LVPDGDETVPEIVEAAIRNGIRIRSISTERPSLDDVFLKLT 301
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-216 |
7.40e-91 |
|
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: 269.24 E-value: 7.40e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVPD 84
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRENLLFMAKLYDAP----RERVDELIREFEL--PADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTN 158
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPgaerRERIDELLDFVGLleAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 159 GLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-207 |
1.82e-82 |
|
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: 246.16 E-value: 1.82e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVPD 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRENLlfmaklydaprervdelirefelpadkkfgRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHS 164
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1828880368 165 ARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRI 207
Cdd:cd03230 131 RREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-223 |
6.62e-81 |
|
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: 244.77 E-value: 6.62e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVPDVS 86
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDELTVRENLLFMAKLY----DAPRERVDELIREFEL--PADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGL 160
Cdd:COG4555 84 GLYDRLTVRENIRYFAELYglfdEELKKRIEELIELLGLeeFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 161 DVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAKLVGRK 223
Cdd:COG4555 164 DVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-216 |
6.36e-74 |
|
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: 226.23 E-value: 6.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFE--AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLV 82
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 PDVSNLYDELTVRENLLFMAKLYDAPR----ERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEP 156
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKseikEEVELLLRVLGLTdkANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 157 TNGLDVHSARAVRSLIRALnRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-297 |
1.79e-69 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 217.67 E-value: 1.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 4 AVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVkteRLAVRRSIGLVP 83
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVSNLYDELTVRENLLFMAKLYDAP----RERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPT 157
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSkaeaKRRADEWLERLGLGdrANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 158 NGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAKLVGRKTvVRLSVEpLSSSL 237
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNT-LRLEAD-GDAGW 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 238 LRALERYNP-SFEEGKLVFEVDDvDGFLEELCSLRVELGFrVTSLCTEIPGIEDVFVELTK 297
Cdd:COG4152 236 LRALPGVTVvEEDGDGAELKLED-GADAQELLRALLARGP-VREFEEVRPSLNEIFIEVVG 294
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-211 |
1.72e-68 |
|
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: 212.23 E-value: 1.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGD----FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIG 80
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 81 LVPDVSNLYDELTVRENLLFMAKLY----DAPRERVDELIREFELPA--DKKFGRLSTGFKRRVTIASALVHEPEVLFLD 154
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYglkgDELTARLEELADRLGMEEllDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 155 EPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-211 |
5.79e-66 |
|
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: 205.53 E-value: 5.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRsIGLVPD 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-IGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRENLLFMAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDV 162
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKdsAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1828880368 163 HSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:cd03268 160 DGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-211 |
4.55e-59 |
|
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: 187.87 E-value: 4.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGfnvKTERLAVRRSIGLVPDVS 86
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDELTVRENLLFMAKLYDAPRE----RVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGL 160
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLKGLKKEearrRIDEWLERLELSeyANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 161 DVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-261 |
9.14e-58 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 188.37 E-value: 9.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKR-YGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLV-PDVS 86
Cdd:COG4586 26 GLFRReYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVfGQRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDELTVRENLLFMAKLYDAP----RERVDELIREFEL------PADKkfgrLSTGFKRRVTIASALVHEPEVLFLDEP 156
Cdd:COG4586 106 QLWWDLPAIDSFRLLKAIYRIPdaeyKKRLDELVELLDLgelldtPVRQ----LSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 157 TNGLDVHSARAVRSLIRALNR-RGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAKLVGRKTVVRLS-VEPLS 234
Cdd:COG4586 182 TIGLDVVSKEAIREFLKEYNReRGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLElAEPVP 261
|
250 260
....*....|....*....|....*....
gi 1828880368 235 SSllrALERYNP--SFEEGKLVFEVDDVD 261
Cdd:COG4586 262 PL---ELPRGGEviEREGNRVRLEVDPRE 287
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-218 |
1.34e-56 |
|
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: 182.49 E-value: 1.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVV-ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT----ERLAV 75
Cdd:COG1127 1 MSEPMIeVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 76 RRSIGLVPDVSNLYDELTVRENLLF-MAKLYDAP----RERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEP 148
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFpLREHTDLSeaeiRELVLEKLELVGLPgaADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 149 EVLFLDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAK 218
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-187 |
5.05e-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: 174.97 E-value: 5.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVPDVS 86
Cdd:COG4133 5 AENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDELTVRENLLFMAKLY--DAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDV 162
Cdd:COG4133 85 GLKPELTVRENLRFWAALYglRADREAIDEALEAVGLAglADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDA 164
|
170 180
....*....|....*....|....*
gi 1828880368 163 HSARAVRSLIRALNRRGMTVFITTH 187
Cdd:COG4133 165 AGVALLAELIAAHLARGGAVLLTTH 189
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-216 |
8.19e-54 |
|
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: 175.21 E-value: 8.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRY-GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERL-AVRRSIGLV 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLrELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 ---PDvsnlyDEL---TVRENLLF------MAKlyDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEP 148
Cdd:COG1122 81 fqnPD-----DQLfapTVEEDVAFgpenlgLPR--EEIRERVEEALELVGLEhlADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880368 149 EVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-211 |
3.21e-53 |
|
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: 174.06 E-value: 3.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 10 LVKR-YGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLV-PDVSN 87
Cdd:cd03267 26 LFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 88 LYDELTVRENLLFMAKLYDAP----RERVDELIREFELPA--DKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLD 161
Cdd:cd03267 106 LWWDLPVIDSFYLLAAIYDLPparfKKRLDELSELLDLEEllDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 162 VHSARAVRSLIRALNR-RGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:cd03267 186 VVAQENIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-211 |
4.15e-53 |
|
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: 172.70 E-value: 4.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVkTERLAVRRSIGLVPD 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRENLLFMAKLYDAP----RERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTN 158
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPkaeiRARVRELLELVGLEglLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1828880368 159 GLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:cd03259 160 ALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-217 |
7.88e-53 |
|
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: 172.73 E-value: 7.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT----ERlaVRRSIGLV 82
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmhKR--ARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 PDVSNLYDELTVRENLL----FMAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEP 156
Cdd:cd03218 81 PQEASIFRKLTVEENILavleIRGLSKKEREEKLEELLEEFHIThlRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 157 TNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELA 217
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-211 |
2.05e-52 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 184.17 E-value: 2.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 4 AVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVP 83
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVSNLYDELTVRENLLFMAKLYDAPRE----RVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPT 157
Cdd:NF033858 346 QAFSLYGELTVRQNLELHARLFHLPAAeiaaRVAEMLERFDLAdvADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880368 158 NGLD-VhsARAV--RSLIRaLNRR-GMTVFITTHNMVEAETIpQRIAIMRDGRIVAEG 211
Cdd:NF033858 426 SGVDpV--ARDMfwRLLIE-LSREdGVTIFISTHFMNEAERC-DRISLMHAGRVLASD 479
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-216 |
9.48e-52 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 172.30 E-value: 9.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVA-NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSI 79
Cdd:PRK13537 3 MSVAPIDfRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 80 GLVPDVSNLYDELTVRENLLFMAKLYDAP----RERVDELIrEF---ELPADKKFGRLSTGFKRRVTIASALVHEPEVLF 152
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSaaaaRALVPPLL-EFaklENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880368 153 LDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-207 |
2.30e-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: 165.74 E-value: 2.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGD----FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVK----TERLAVR 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklseKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 77 R-SIGLVPDVSNLYDELTVREN----LLFMAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPE 149
Cdd:cd03255 81 RrHIGFVFQSFNLLPDLTALENvelpLLLAGVPKKERRERAEELLERVGLGdrLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 150 VLFLDEPTNGLDVHSARAVRSLIRALNR-RGMTVFITTHNMVEAEtIPQRIAIMRDGRI 207
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-216 |
4.61e-50 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 168.86 E-value: 4.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 4 AVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVP 83
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVSNLYDELTVRENLLFMAKLYDAPRERVDELIR---EF---ELPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPT 157
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPsllEFarlESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 158 NGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-218 |
5.08e-50 |
|
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: 165.75 E-value: 5.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV----KTERLAVRRSIGLVP 83
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVSNLYDELTVRENLLFMakLY---DAPRERVDELIRE----FELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLD 154
Cdd:cd03261 84 QSGALFDSLTVFENVAFP--LRehtRLSEEEIREIVLEkleaVGLRgaEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 155 EPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAK 218
Cdd:cd03261 162 EPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-206 |
1.02e-49 |
|
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: 162.74 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAV---RRSIGLVPDV 85
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGMVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 86 SNLYDELTVRENLLFmaklydaprervdelirefelpadkkfgRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSA 165
Cdd:cd03229 85 FALFPHLTVLENIAL----------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1828880368 166 RAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGR 206
Cdd:cd03229 137 REVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-211 |
1.74e-49 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 167.58 E-value: 1.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVkTERLAVRRSIG 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 81 LVPDVSNLYDELTVRENLLF---MAKLY-DAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLD 154
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFglrMRGVPkAEIRARVAELLELVGLEglADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880368 155 EPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVG 218
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
4-225 |
2.79e-49 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 163.62 E-value: 2.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 4 AVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVP 83
Cdd:TIGR03864 1 ALEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVSNLYDELTVRENLLFMAKLYDAPR----ERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPT 157
Cdd:TIGR03864 81 QQPTLDLDLSVRQNLRYHAALHGLSRaearARIAELLARLGLAerADDKVRELNGGHRRRVEIARALLHRPALLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 158 NGLDVHSARAVRSLIRALNR-RGMTVFITTHNMVEAETiPQRIAIMRDGRIVAEGKRGELAKLVGRKTV 225
Cdd:TIGR03864 161 VGLDPASRAAITAHVRALARdQGLSVLWATHLVDEIEA-SDRLVVLHRGRVLADGAAAELRGATGGADL 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-216 |
3.83e-49 |
|
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: 170.47 E-value: 3.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRY-----GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT----ERLAV 75
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 76 RRSIGLV---PDVSnLYDELTVRENLLFMAKLY-----DAPRERVDELIREFELPAD--KKF-GRLSTGFKRRVTIASAL 144
Cdd:COG1123 341 RRRVQMVfqdPYSS-LNPRMTVGDIIAEPLRLHgllsrAERRERVAELLERVGLPPDlaDRYpHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880368 145 VHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRR-GMT-VFItTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTyLFI-SHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-208 |
4.70e-49 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 166.40 E-value: 4.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEaVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVkTERLAVRRSIG 80
Cdd:COG3839 1 MAS-LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 81 LVPDVSNLYDELTVRENLLF---MAKLYDAPR-ERVDELIREFELPA--DKKFGRLSTGFKRRVTIASALVHEPEVLFLD 154
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFplkLRKVPKAEIdRRVREAAELLGLEDllDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 155 EPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIV 208
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-206 |
6.62e-49 |
|
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: 161.87 E-value: 6.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 6 VANNLVKRYGDFE--AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA-VRRSIGLV 82
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKeLRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 ---PDVSNLYDelTVRENLLFMAKLYDAPRE----RVDELIREFEL--PADKKFGRLSTGFKRRVTIASALVHEPEVLFL 153
Cdd:cd03225 81 fqnPDDQFFGP--TVEEEVAFGLENLGLPEEeieeRVEEALELVGLegLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 154 DEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGR 206
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-218 |
1.17e-48 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 162.12 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 6 VANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVktERLAV----RRSIGL 81
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI--THLPMhkraRLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 VPDVSNLYDELTVRENL---LFMAKL-YDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDE 155
Cdd:COG1137 83 LPQEASIFRKLTVEDNIlavLELRKLsKKEREERLEELLEEFGIThlRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 156 PTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAK 218
Cdd:COG1137 163 PFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-211 |
1.16e-47 |
|
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: 158.90 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGeAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVPDVSNL 88
Cdd:cd03264 5 NLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQEFGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 89 YDELTVRENLLFMAKLYDAP----RERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDV 162
Cdd:cd03264 84 YPNFTVREFLDYIAWLKGIPskevKARVDEVLELVNLGdrAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 163 HSARAVRSLIRAL--NRrgmTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:cd03264 164 EERIRFRNLLSELgeDR---IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-216 |
4.95e-47 |
|
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: 158.28 E-value: 4.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT-ERLAVRRSIGLVPDV 85
Cdd:COG1120 4 AENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 86 SNLYDELTVRENLL--------FMAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDE 155
Cdd:COG1120 84 PPAPFGLTVRELVAlgryphlgLFGRPSAEDREAVEEALERTGLEhlADRPVDELSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880368 156 PTNGLDVHSARAVRSLIRALNR-RGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:COG1120 164 PTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-206 |
2.65e-46 |
|
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: 153.55 E-value: 2.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV-KTERLAVRRSIGLVPDv 85
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 86 snlydeltvrenllfmaklydaprervdelirefelpadkkfgrLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSA 165
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1828880368 166 RAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGR 206
Cdd:cd00267 117 ERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-217 |
3.71e-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: 155.90 E-value: 3.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 6 VANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT----ERlaVRRSIGL 81
Cdd:TIGR04406 3 VAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlpmhER--ARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 VPDVSNLYDELTVRENLlfMAKL---YDAPR----ERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLF 152
Cdd:TIGR04406 81 LPQEASIFRKLTVEENI--MAVLeirKDLDRaereERLEALLEEFQIShlRDNKAMSLSGGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 153 LDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELA 217
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-208 |
4.53e-46 |
|
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: 154.72 E-value: 4.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVkTERLAVRRSIGLVPD 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRENLLFMAKLYDAPRERVDELIRE------FELPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTN 158
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREvaellqIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 159 GLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIV 208
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-217 |
1.22e-45 |
|
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: 153.74 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV---KTERLaVRRSIGLVPDV 85
Cdd:cd03224 5 NLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglPPHER-ARAGIGYVPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 86 SNLYDELTVRENLL--FMAKLYDAPRERVDELIREFelPA-----DKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTN 158
Cdd:cd03224 84 RRIFPELTVEENLLlgAYARRRAKRKARLERVYELF--PRlkerrKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 159 GLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELA 217
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-215 |
2.17e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 153.28 E-value: 2.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRY-GDFEAVRGISFKVRRGEaFALL-GPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT----ERLAVRRSIGLV 82
Cdd:COG2884 6 NVSKRYpGGREALSDVSLEIEKGE-FVFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLRRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 PDVSNLYDELTVRENLLFMAKLYDAP----RERVDELIREFELpADKKF---GRLSTGFKRRVTIASALVHEPEVLFLDE 155
Cdd:COG2884 85 FQDFRLLPDRTVYENVALPLRVTGKSrkeiRRRVREVLDLVGL-SDKAKalpHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 156 PTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGE 215
Cdd:COG2884 164 PTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-211 |
3.98e-45 |
|
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: 152.98 E-value: 3.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV--KTERLAVRRSIGLVPD 84
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItgLPPHEIARLGIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRENLL--------------FMAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEP 148
Cdd:cd03219 83 IPRLFPELTVLENVMvaaqartgsglllaRARREEREARERAEELLERVGLAdlADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 149 EVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-215 |
1.76e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.40 E-value: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKterlAVRRSIG 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----RARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 81 LVPDVSNLYDE--LTVRE--------NLLFMAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEP 148
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDvvlmgrygRRGLFRRPSRADREAVDEALERVGLEdlADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 149 EVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMrDGRIVAEGKRGE 215
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEE 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-211 |
2.94e-44 |
|
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: 149.99 E-value: 2.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERlavrRSIGLVPDVS 86
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER----KRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDE--LTVRENLL--------FMAKLYDAPRERVDELIRE---FELpADKKFGRLSTGFKRRVTIASALVHEPEVLFL 153
Cdd:cd03235 78 SIDRDfpISVRDVVLmglyghkgLFRRLSKADKAKVDEALERvglSEL-ADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880368 154 DEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMrDGRIVAEG 211
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-241 |
6.37e-44 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 152.92 E-value: 6.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRY----GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT----ERLAVRRSIG 80
Cdd:COG1135 6 NLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserELRAARRKIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 81 LVPDVSNLYDELTVRENLLFMAKLYDAP----RERVDELIREFELpADKKF---GRLSTGFKRRVTIASALVHEPEVLFL 153
Cdd:COG1135 86 MIFQHFNLLSSRTVAENVALPLEIAGVPkaeiRKRVAELLELVGL-SDKADaypSQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 154 DEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGK-------------------- 212
Cdd:COG1135 165 DEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPvldvfanpqseltrrflptv 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1828880368 213 ---------RGELAKLVGRKTVVRLS------VEPLSSSLLRAL 241
Cdd:COG1135 245 lndelpeelLARLREAAGGGRLVRLTfvgesaDEPLLSELARRF 288
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-216 |
7.17e-44 |
|
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: 150.23 E-value: 7.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 13 RYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSG-EAYVNGFNVKTERLA-VRRSIGLV-PDVSNLY 89
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWeLRKRIGLVsPALQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 90 DE-LTVRENLL--FMAK--LYDAP----RERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTN 158
Cdd:COG1119 92 PRdETVLDVVLsgFFDSigLYREPtdeqRERARELLELLGLAhlADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 159 GLDVHSARAVRSLIRALNRRGMT--VFITTHnmveAETIPQ---RIAIMRDGRIVAEGKRGEL 216
Cdd:COG1119 172 GLDLGARELLLALLDKLAAEGAPtlVLVTHH----VEEIPPgitHVLLLKDGRVVAAGPKEEV 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-216 |
7.82e-44 |
|
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: 149.25 E-value: 7.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSI-----TSGEAYVNGFNV---KTERLAVRRSIG 80
Cdd:cd03260 5 DLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydlDVDVLELRRRVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 81 LVPDVSNLYDeLTVRENLLFMAKLY-----DAPRERVDELIREFELPADKK----FGRLSTGFKRRVTIASALVHEPEVL 151
Cdd:cd03260 85 MVFQKPNPFP-GSIYDNVAYGLRLHgiklkEELDERVEEALRKAALWDEVKdrlhALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 152 FLDEPTNGLDVHSARAVRSLIRALNRRgMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
8-217 |
1.97e-43 |
|
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: 148.59 E-value: 1.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV---KTERLaVRRSIGLVPD 84
Cdd:COG0410 7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglPPHRI-ARLGIGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRENLL---FMAKLYDAPRERVDELireFEL-PADKKF-----GRLSTGFKRRVTIASALVHEPEVLFLDE 155
Cdd:COG0410 86 GRRIFPSLTVEENLLlgaYARRDRAEVRADLERV---YELfPRLKERrrqraGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 156 PTNGLdvhsA----RAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELA 217
Cdd:COG0410 163 PSLGL----AplivEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-211 |
6.35e-43 |
|
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: 145.27 E-value: 6.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT-ERLAVRRSIGLVPDV 85
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVPQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 86 snlydeltvrenllfMAKLydapreRVDELirefelpADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSA 165
Cdd:cd03214 82 ---------------LELL------GLAHL-------ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1828880368 166 RAVRSLIRALNR-RGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:cd03214 134 IELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-207 |
7.92e-43 |
|
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: 146.14 E-value: 7.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV---KTERLAVRRSIGL 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 VPDVSNLYDELTVRENLLF-------MAKlyDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLF 152
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLapikvkgMSK--AEAEERALELLEKVGLAdkADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 153 LDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRI 207
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-216 |
1.12e-42 |
|
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: 146.57 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGD----FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT----ERLAVRRSIG 80
Cdd:cd03258 6 NVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKARRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 81 LVPDVSNLYDELTVRENLLFMAKLYDAPR----ERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLD 154
Cdd:cd03258 86 MIFQHFNLLSSRTVFENVALPLEIAGVPKaeieERVLELLELVGLEdkADAYPAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 155 EPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-260 |
1.56e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 153.14 E-value: 1.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRY--GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTL---TSITSGEAYVNGFNVKTERLAV 75
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 76 R-RSIGLVP-DVSNLYDELTVRENLLFMAKLYDAP----RERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHE 147
Cdd:COG1123 81 RgRRIGMVFqDPMTQLNPVTVGDQIAEALENLGLSraeaRARVLELLEAVGLErrLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 148 PEVLFLDEPTNGLDVHSARAVRSLIRALNR-RGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAklvgrKTVV 226
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL-----AAPQ 235
|
250 260 270
....*....|....*....|....*....|....
gi 1828880368 227 RLSVEPlssSLLRALERYNPSFEEGKLVFEVDDV 260
Cdd:COG1123 236 ALAAVP---RLGAARGRAAPAAAAAEPLLEVRNL 266
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-211 |
2.60e-42 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 145.34 E-value: 2.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRY----GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV----KTERLAVRRS 78
Cdd:cd03257 4 VKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 79 IGLVP-D-VSNLYDELTVRENL------LFMAKLYDAPRERVDELIREFELPAD--KKF-GRLSTGFKRRVTIASALVHE 147
Cdd:cd03257 84 IQMVFqDpMSSLNPRMTIGEQIaeplriHGKLSKKEARKEAVLLLLVGVGLPEEvlNRYpHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 148 PEVLFLDEPTNGLDVHSARAVRSLIRAL-NRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-210 |
5.81e-42 |
|
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: 144.15 E-value: 5.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGD----FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKterlAVRRSIGLVPD 84
Cdd:cd03293 5 NVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----GPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRENLLFMAKLYDAP----RERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTN 158
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPkaeaRERAEELLELVGLSgfENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 159 GLDVHSARAVRSLI-RALNRRGMTVFITTHNMVEAETIPQRIAIM--RDGRIVAE 210
Cdd:cd03293 161 ALDALTREQLQEELlDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-212 |
5.99e-42 |
|
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: 145.18 E-value: 5.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV---KTERLAvRR 77
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHRIA-RL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 78 SIGLVPDVSNLYDELTVRENLL----------FMAKLYDAP---------RERVDELIREFELP--ADKKFGRLSTGFKR 136
Cdd:COG0411 80 GIARTFQNPRLFPELTVLENVLvaaharlgrgLLAALLRLPrarreereaRERAEELLERVGLAdrADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 137 RVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNR-RGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGK 212
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-208 |
1.05e-41 |
|
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: 143.92 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVkTERLAVRRSIGLVPDVSNL 88
Cdd:cd03300 5 NVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 89 YDELTVRENLLF---MAKLYDAP-RERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDV 162
Cdd:cd03300 84 FPHLTVFENIAFglrLKKLPKAEiKERVAEALDLVQLEgyANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1828880368 163 HSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIV 208
Cdd:cd03300 164 KLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-216 |
1.71e-41 |
|
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: 143.86 E-value: 1.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGD-FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERL----AVRRSIGLV 82
Cdd:cd03256 4 ENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrQLRRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 PDVSNLYDELTVRENLLF-----------MAKLYD-APRERVDELIREFELpADKKFGR---LSTGFKRRVTIASALVHE 147
Cdd:cd03256 84 FQQFNLIERLSVLENVLSgrlgrrstwrsLFGLFPkEEKQRALAALERVGL-LDKAYQRadqLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 148 PEVLFLDEPTNGLDVHSARAVRSLIRALNR-RGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRINReEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-216 |
1.96e-41 |
|
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: 143.60 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGD-FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVK-TERLAVRRSIGLVPDVS 86
Cdd:cd03295 5 NVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReQDPVELRRKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDELTVRENLLFMAKLYDAPRE----RVDELIREFELPADKKFGR----LSTGFKRRVTIASALVHEPEVLFLDEPTN 158
Cdd:cd03295 85 GLFPHMTVEENIALVPKLLKWPKEkireRADELLALVGLDPAEFADRypheLSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 159 GLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:cd03295 165 ALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-260 |
2.55e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 149.41 E-value: 2.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNG--FNVKTERLAVRRS 78
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 79 IGLVPDVSNLYDELTVRENLL------FMAKL-YDAPRERVDELIRE--FELPADKKFGRLSTGFKRRVTIASALVHEPE 149
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVlgleptKGGRLdRKAARARIRELSERygLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 150 VLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRG-----ELAKL-VGRK 223
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAetseeELAELmVGRE 241
|
250 260 270
....*....|....*....|....*....|....*..
gi 1828880368 224 tvVRLSVEPlsssllralerynPSFEEGKLVFEVDDV 260
Cdd:COG3845 242 --VLLRVEK-------------APAEPGEVVLEVENL 263
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-211 |
4.02e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 145.67 E-value: 4.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLV----- 82
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFVfqhya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 --PDvsnlydeLTVRENLLFMAKLYDAP----RERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLD 154
Cdd:COG1118 86 lfPH-------MTVAENIAFGLRVRPPSkaeiRARVEELLELVQLEglADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 155 EPTNGLDVHSARAVRSLIRALNRR--GMTVFItTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDElgGTTVFV-THDQEEALELADRVVVMNQGRIEQVG 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-210 |
6.30e-40 |
|
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: 137.17 E-value: 6.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNG--FNVKTERLAVRRSIGLV 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 PdvsnlydeltvrenllfmaklydaprervdelirefelpadkkfgRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDV 162
Cdd:cd03216 81 Y---------------------------------------------QLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1828880368 163 HSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAE 210
Cdd:cd03216 116 AEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-221 |
2.23e-39 |
|
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: 138.24 E-value: 2.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEaVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVkTERLAVRRSIGLVPD 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRENLLFMAKLYDAPRERVDELIRE------FELPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTN 158
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEiaemlgIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 159 GLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG---------KRGELAKLVG 221
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGkpeevfkkpKNEFVAEFLG 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-223 |
8.50e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 142.46 E-value: 8.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNG--FNVKTERLAVRRS 78
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 79 IGLVPDVSNLYDELTVRENLlFMAKL--------YDAPRERVDELIREF--ELPADKKFGRLSTGFKRRVTIASALVHEP 148
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENI-FLGREprrgglidWRAMRRRARELLARLglDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 149 EVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL------AKLVGR 222
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELtedelvRLMVGR 239
|
.
gi 1828880368 223 K 223
Cdd:COG1129 240 E 240
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-259 |
4.24e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 135.98 E-value: 4.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGD-FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTER---LAVRRSIGLV 82
Cdd:PRK13639 4 TRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKkslLEVRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 ---PDvsnlyDEL---TVRENLLFMAKLYDAPRERVDELIRE------FELPADKKFGRLSTGFKRRVTIASALVHEPEV 150
Cdd:PRK13639 84 fqnPD-----DQLfapTVEEDVAFGPLNLGLSKEEVEKRVKEalkavgMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 151 LFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL---AKLVgRKTVVR 227
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVfsdIETI-RKANLR 237
|
250 260 270
....*....|....*....|....*....|...
gi 1828880368 228 LsvePLSSSLLRALER-YNPSFEEGKLVFEVDD 259
Cdd:PRK13639 238 L---PRVAHLIEILNKeDNLPIKMGYTIGEARR 267
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-222 |
4.70e-38 |
|
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: 142.67 E-value: 4.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 4 AVVANNLVKRYGDFE--AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT-ERLAVRRSIG 80
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 81 LVPDVSNLYDElTVRENLLFMAKlyDAPRERVDELIR-----EF--ELPA--DKKFG----RLSTGFKRRVTIASALVHE 147
Cdd:COG2274 553 VVLQDVFLFSG-TIRENITLGDP--DATDEEIIEAARlaglhDFieALPMgyDTVVGeggsNLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 148 PEVLFLDEPTNGLDVHSARAVRSLIRALnRRGMTVFITTHNMveaETIPQ--RIAIMRDGRIVAEGKRGELAKLVGR 222
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRL---STIRLadRIIVLDKGRIVEDGTHEELLARKGL 702
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-208 |
1.50e-37 |
|
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: 132.38 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDF-EAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLavRRSIGLVP-DV- 85
Cdd:cd03226 4 NISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER--RKSIGYVMqDVd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 86 SNLYDElTVRENLLFMAKLYDAPRERVDELIREFEL--PADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVH 163
Cdd:cd03226 82 YQLFTD-SVREELLLGLKELDAGNEQAETVLKDLDLyaLKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1828880368 164 SARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIV 208
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-206 |
3.99e-37 |
|
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: 130.20 E-value: 3.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDF--EAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA-VRRSIGL 81
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEsLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 VPDVSNLYDElTVRENLlfmaklydaprervdelirefelpadkkfgrLSTGFKRRVTIASALVHEPEVLFLDEPTNGLD 161
Cdd:cd03228 81 VPQDPFLFSG-TIRENI-------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1828880368 162 VHSARAVRSLIRALnRRGMTVFITTHNMveaETIPQ--RIAIMRDGR 206
Cdd:cd03228 129 PETEALILEALRAL-AKGKTVIVIAHRL---STIRDadRIIVLDDGR 171
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-187 |
1.49e-36 |
|
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: 129.59 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTTVRMLT--TLTSITSGEAYVNGFNVKTERLavRRSIGLVPDVSNLYDELTVREN 97
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKRSF--RKIIGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 98 LLFMAKLYdaprervdelirefelpadkkfgRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNR 177
Cdd:cd03213 103 LMFAAKLR-----------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD 159
|
170
....*....|
gi 1828880368 178 RGMTVFITTH 187
Cdd:cd03213 160 TGRTIICSIH 169
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-216 |
4.41e-36 |
|
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: 129.77 E-value: 4.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 4 AVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVkTERLAVRRSIGLVP 83
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVSNLYDELTVRENLLF---MAKLYDAP-----RERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFL 153
Cdd:cd03296 81 QHYALFRHMTVFDNVAFglrVKPRSERPpeaeiRAKVHELLKLVQLDwlADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880368 154 DEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-238 |
1.32e-35 |
|
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: 136.30 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFE--AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVPDV 85
Cdd:TIGR01257 1941 NELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQF 2020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 86 SNLYDELTVRENLLFMAKLYDAPRERVDEL----IREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNG 159
Cdd:TIGR01257 2021 DAIDDLLTGREHLYLYARLRGVPAEEIEKVanwsIQSLGLSlyADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 160 LDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAKLVGRKTVVRLSVEPLSSSLL 238
Cdd:TIGR01257 2101 MDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKDDLL 2179
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-260 |
6.67e-35 |
|
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: 127.57 E-value: 6.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 17 FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV----KTERLAVRRSIGLV---PDvSNLY 89
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakkKKKLKDLRKKVGLVfqfPE-HQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 90 dELTVRENLLFMAKLYDAP----RERVDELIREFELPADKK----FgRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLD 161
Cdd:TIGR04521 97 -EETVYKDIAFGPKNLGLSeeeaEERVKEALELVGLDEEYLerspF-ELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 162 VHSARAVRSLIRALNR-RGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAKLVGRKTVVRLSVePLSSSLLRA 240
Cdd:TIGR04521 175 PKGRKEILDLFKRLHKeKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDELEKIGLDV-PEITELARK 253
|
250 260
....*....|....*....|
gi 1828880368 241 LERYNPSFEegKLVFEVDDV 260
Cdd:TIGR04521 254 LKEKGLPVP--KDPLTVEEA 271
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-211 |
1.41e-34 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 125.90 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYV--NGFNVKTER-----LAVRRSIG 80
Cdd:PRK11124 6 NGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKTPsdkaiRELRRNVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 81 LVPDVSNLYDELTVRENL-------LFMAKlyDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVL 151
Cdd:PRK11124 86 MVFQQYNLWPHLTVQQNLieapcrvLGLSK--DQALARAEKLLERLRLKpyADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 152 FLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
12-211 |
2.01e-34 |
|
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: 124.33 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 12 KRYGDFEAvrGISFKVRrGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAV-----RRSIGLVPDVS 86
Cdd:cd03297 8 KRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDELTVRENLLF-MAKLYDAP-RERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDV 162
Cdd:cd03297 85 ALFPHLNVRENLAFgLKRKRNREdRISVDELLDLLGLDhlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1828880368 163 HSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:cd03297 165 ALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-158 |
4.84e-34 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 121.60 E-value: 4.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV-KTERLAVRRSIGLVPDVSNLYDELTVRENL 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 99 LFMAKLY----DAPRERVDELIREFEL------PADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTN 158
Cdd:pfam00005 81 RLGLLLKglskREKDARAEEALEKLGLgdladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-221 |
5.59e-34 |
|
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: 130.26 E-value: 5.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 4 AVVANNLVKRYGD-FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA-VRRSIGL 81
Cdd:COG4988 336 SIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAsWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 VPDVSNLYdELTVRENLLFMAKlyDAPRERVDELIR-----EF--ELPA--DKKFG----RLSTGFKRRVTIASALVHEP 148
Cdd:COG4988 416 VPQNPYLF-AGTIRENLRLGRP--DASDEELEAALEaagldEFvaALPDglDTPLGeggrGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 149 EVLFLDEPTNGLDVHSARAVRSLIRALnRRGMTVFITTH---NMVEAEtipqRIAIMRDGRIVAEGKRGELAKLVG 221
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHrlaLLAQAD----RILVLDDGRIVEQGTHEELLAKNG 563
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-207 |
1.22e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 126.60 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVkTERLAVRRSIGLVPDVSNL 88
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENRHVNTVFQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 89 YDELTVRENLLFMAKLYDAP----RERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDV 162
Cdd:PRK09452 98 FPHMTVFENVAFGLRMQKTPaaeiTPRVMEALRMVQLEefAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1828880368 163 HSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRI 207
Cdd:PRK09452 178 KLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-222 |
1.85e-33 |
|
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: 128.73 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 4 AVVANNLVKRY--GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERL-AVRRSIG 80
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEdDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 81 LVPDVSNLYDElTVRENLLF------MAKLYDApRERV--DELIREfeLPA--DKKFG----RLSTGFKRRVTIASALVH 146
Cdd:COG4987 413 VVPQRPHLFDT-TLRENLRLarpdatDEELWAA-LERVglGDWLAA--LPDglDTWLGeggrRLSGGERRRLALARALLR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 147 EPEVLFLDEPTNGLDVHSARAVRSLIRALnRRGMTVFITTHNMVEAETIpQRIAIMRDGRIVAEGKRGELAKLVGR 222
Cdd:COG4987 489 DAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQNGR 562
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-211 |
2.12e-33 |
|
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: 122.26 E-value: 2.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 11 VKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGfnvkTERLAVRRSIGLVPdvsnlyd 90
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RVSSLLGLGGGFNP------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 91 ELTVRENLLFMAKLYDAPRERVDELIREF----ELPA--DKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHS 164
Cdd:cd03220 98 ELTGRENIYLNGRLLGLSRKEIDEKIDEIiefsELGDfiDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1828880368 165 ARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:cd03220 178 QEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-222 |
2.88e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 128.36 E-value: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 13 RY-GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA-VRRSIGLVP-DVSnLY 89
Cdd:COG1132 348 SYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEsLRRQIGVVPqDTF-LF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 90 DElTVRENLLFmAKLyDAPRERV---------DELIREFElpadKKF--------GRLSTGFKRRVTIASALVHEPEVLF 152
Cdd:COG1132 427 SG-TIRENIRY-GRP-DATDEEVeeaakaaqaHEFIEALP----DGYdtvvgergVNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880368 153 LDEPTNGLDVHSARAVRSLIRALnRRGMTVFITTHNMveaETIPQ--RIAIMRDGRIVAEGKRGELAKLVGR 222
Cdd:COG1132 500 LDEATSALDTETEALIQEALERL-MKGRTTIVIAHRL---STIRNadRILVLDDGRIVEQGTHEELLARGGL 567
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
9-216 |
9.02e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.97 E-value: 9.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVK----TERLaVRRSIGLVPD 84
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkvDERL-IRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRENLLF-------MAKlyDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDE 155
Cdd:PRK09493 85 QFYLFPHLTALENVMFgplrvrgASK--EEAEKQARELLAKVGLAerAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 156 PTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-211 |
1.32e-32 |
|
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: 120.07 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 22 GISFKVRRGEAFALLGPNGAGKTTTVRMLTTL---TSITSGEAYVNGfnVKTERLAVRRSIGLVPDVSNLYDELTVRENL 98
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNG--QPRKPDQFQKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 99 LFMAKLY------DAPRERVDELIREFELP----ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAV 168
Cdd:cd03234 103 TYTAILRlprkssDAIRKKRVEDVLLRDLAltriGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1828880368 169 RSLIRALNRRGMTVFITTHN-MVEAETIPQRIAIMRDGRIVAEG 211
Cdd:cd03234 183 VSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-216 |
1.84e-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: 120.83 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV----KTERLAVRR-SIGL 81
Cdd:cd03294 27 KEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRELRRkKISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 VPDVSNLYDELTVRENLLFMAKLYDAPR-ERVDELIREFELP-----ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDE 155
Cdd:cd03294 107 VFQSFALLPHRTVLENVAFGLEVQGVPRaEREERAAEALELVglegwEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 156 PTNGLDVHSARAVRSLIRAL--NRRGMTVFITtHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLqaELQKTIVFIT-HDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-238 |
2.35e-32 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 122.54 E-value: 2.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 4 AVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVrMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGL-V 82
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*hR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 PDVSNLYDELTVRENLLFMAKLYDAPRE----RVDELIREFEL--PADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEP 156
Cdd:NF000106 92 PVR*GRRESFSGRENLYMIGR*LDLSRKdaraRADELLERFSLteAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 157 TNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAKLVGRKTvvrLSVEPLSSS 236
Cdd:NF000106 172 TTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRT---LQIRPAHAA 248
|
..
gi 1828880368 237 LL 238
Cdd:NF000106 249 EL 250
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-222 |
2.76e-32 |
|
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: 119.64 E-value: 2.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFE--AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA-VRRSIGL 81
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAsLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 VPDVSNLYDElTVRENLLFMAKlyDAPRERV---------DELIREFELPADKKFG----RLSTGFKRRVTIASALVHEP 148
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGRP--GATREEVeeaaraanaHEFIMELPEGYDTVIGergvKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 149 EVLFLDEPTNGLDVHSARAVRSLIRALnRRGMTVFITTHNMveaETIPQ--RIAIMRDGRIVAEGKRGELAKLVGR 222
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRL---STIENadRIVVLEDGKIVERGTHEELLAQGGV 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-207 |
5.17e-32 |
|
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: 118.28 E-value: 5.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRY-GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV---KTERLA-VRRSIGLVP 83
Cdd:cd03292 5 NVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPyLRRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVSNLYDELTVRENLLFMAKLYDAP----RERVDELIREFELpADKKF---GRLSTGFKRRVTIASALVHEPEVLFLDEP 156
Cdd:cd03292 85 QDFRLLPDRNVYENVAFALEVTGVPpreiRKRVPAALELVGL-SHKHRalpAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 157 TNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRI 207
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-211 |
1.13e-31 |
|
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: 124.74 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 4 AVVANNLVKRYGDF--EAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGL 81
Cdd:TIGR01257 928 GVCVKNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 VPDVSNLYDELTVRENLLFMAKL----YDAPRERVDELIREFEL--PADKKFGRLSTGFKRRVTIASALVHEPEVLFLDE 155
Cdd:TIGR01257 1008 CPQHNILFHHLTVAEHILFYAQLkgrsWEEAQLEMEAMLEDTGLhhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 156 PTNGLDVHSARAVRSLIRALnRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-211 |
1.37e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 117.88 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRY----------------------GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITS 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 59 GEAYVNGfnvkteR----LAVrrSIGLVPdvsnlydELTVRENLLFMAKLYDAPRERVDEL---IREF-ELPA--DKKFG 128
Cdd:COG1134 81 GRVEVNG------RvsalLEL--GAGFHP-------ELTGRENIYLNGRLLGLSRKEIDEKfdeIVEFaELGDfiDQPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 129 RLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIV 208
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
...
gi 1828880368 209 AEG 211
Cdd:COG1134 226 MDG 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-211 |
1.73e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.58 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVA-NNLVKRYGDFE--AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERL-AVR 76
Cdd:PRK13635 1 MKEEIIRvEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 77 RSIGLV---PDvsNLYDELTVRENLLFMAKLYDAPR----ERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHE 147
Cdd:PRK13635 81 RQVGMVfqnPD--NQFVGATVQDDVAFGLENIGVPReemvERVDQALRQVGMEdfLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 148 PEVLFLDEPTNGLDVHSARAVRSLIRALNR-RGMTVFITTHNMVEAETiPQRIAIMRDGRIVAEG 211
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-216 |
2.09e-31 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 119.39 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRY----GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTL---TSITSGEAYVNGFNV----KTERLAVR 76
Cdd:COG0444 5 RNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLlklsEKELRKIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 77 -RSIGLVP-D-------VsnlydeLTVRENLLFMAKLY-----DAPRERVDELIREFELPADKKFGR-----LSTGFKRR 137
Cdd:COG0444 85 gREIQMIFqDpmtslnpV------MTVGDQIAEPLRIHgglskAEARERAIELLERVGLPDPERRLDrypheLSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 138 VTIASALVHEPEVLFLDEPTNGLDVhSARA-VRSLIRALNR-RGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGE 215
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDV-TIQAqILNLLKDLQReLGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
.
gi 1828880368 216 L 216
Cdd:COG0444 238 L 238
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-211 |
2.78e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.91 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRYGD-FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNG--FNVKTERlAVRR 77
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGreVNAENEK-WVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 78 SIGLV---PDvsnlyDEL---TVRENLLF----MAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALV 145
Cdd:PRK13647 80 KVGLVfqdPD-----DQVfssTVWDDVAFgpvnMGLDKDEVERRVEEALKAVRMWdfRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 146 HEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-188 |
3.20e-31 |
|
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: 115.60 E-value: 3.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 15 GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTER---LAVRRSIGLVpdVSNLYDE 91
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRkglLERRQRVGLV--FQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 92 L---TVRENLLF----MAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDV 162
Cdd:TIGR01166 81 LfaaDVDQDVAFgplnLGLSEAEVERRVREALTAVGASglRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180
....*....|....*....|....*.
gi 1828880368 163 HSARAVRSLIRALNRRGMTVFITTHN 188
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-188 |
5.66e-31 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 115.36 E-value: 5.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERlaVRRSIGLVPDVS 86
Cdd:PRK13539 5 GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD--VAEACHYLGHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDELTVRENLLFMAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHS 164
Cdd:PRK13539 83 AMKPALTVAENLEFWAAFLGGEELDIAAALEAVGLAplAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|....
gi 1828880368 165 ARAVRSLIRALNRRGMTVFITTHN 188
Cdd:PRK13539 163 VALFAELIRAHLAQGGIVIAATHI 186
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-216 |
9.83e-31 |
|
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: 115.41 E-value: 9.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 16 DFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERL-AVRRSIGLVPDVSNLYDElTV 94
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLdSLRRAIGVVPQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 95 RENLLFmAKLyDAPRE---------RVDELIREFELPADKKFG----RLSTGFKRRVTIASALVHEPEVLFLDEPTNGLD 161
Cdd:cd03253 92 GYNIRY-GRP-DATDEevieaakaaQIHDKIMRFPDGYDTIVGerglKLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880368 162 VHSARAV-RSLIRALNRRgmTVFITTHNMveaETIPQ--RIAIMRDGRIVAEGKRGEL 216
Cdd:cd03253 170 THTEREIqAALRDVSKGR--TTIVIAHRL---STIVNadKIIVLKDGRIVERGTHEEL 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-216 |
1.14e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 115.38 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERL--AVRRSIGLV 82
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhaRARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 PDVSNLYDELTVRENLLFMAKLYD-----APRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDE 155
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDdlsaeQREDRANELMEEFHIEhlRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 156 PTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-215 |
5.94e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 116.05 E-value: 5.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRY----GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV----KTERLAVRRSI 79
Cdd:PRK11153 5 KNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 80 GLVPDVSNLYDELTVRENLLFMAKLYDAPRE----RVDELIREFELpADKKF---GRLSTGFKRRVTIASALVHEPEVLF 152
Cdd:PRK11153 85 GMIFQHFNLLSSRTVFDNVALPLELAGTPKAeikaRVTELLELVGL-SDKADrypAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880368 153 LDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGE 215
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-216 |
9.60e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 115.59 E-value: 9.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVkTERLAVRRSIGLVPD 84
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRENLLFMAKLYDAPRERVDELIRE---------FElpaDKKFGRLSTGFKRRVTIASALVHEPEVLFLDE 155
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEalelvdlagFE---DRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880368 156 PTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-241 |
1.51e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.60 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 18 EAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA---VRRSIGLV---PDvSNLYDE 91
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdIRKKVGLVfqyPE-YQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 92 lTVRENLLFMAKLYDAPRERVDELIRE--------FELPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVH 163
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRamnivgldYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 164 SARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAKLVGRKTVVRLSVePLSSSLLRAL 241
Cdd:PRK13637 179 GRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESIGLAV-PQVTYLVRKL 256
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-271 |
1.87e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 113.26 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRYGDFE------AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTER-- 72
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 73 LAVRRSIGLV---PDvsNLYDELTVRENLLF----MAKLYDAPRERVDELIREFELPADKKFG--RLSTGFKRRVTIASA 143
Cdd:PRK13633 81 WDIRNKAGMVfqnPD--NQIVATIVEEDVAFgpenLGIPPEEIRERVDESLKKVGMYEYRRHAphLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 144 LVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETiPQRIAIMRDGRIVAEGKRGELAKLVGR 222
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEM 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1828880368 223 KTVVRLSVePLSSSLLRALERYNPSFEEgklvfEVDDVDGFLEELCSLR 271
Cdd:PRK13633 238 MKKIGLDV-PQVTELAYELKKEGVDIPS-----DILTIDEMVNELCQLK 280
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-211 |
2.59e-29 |
|
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: 111.14 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 18 EAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT-ERLAVRRSIGLVP-DVSNLYDelTVR 95
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPqDVTLFYG--TLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 96 ENLLFMAKLYD-------APRERVDELIRE----FELPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHS 164
Cdd:cd03245 96 DNITLGAPLADderilraAELAGVTDFVNKhpngLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1828880368 165 ARAVRSLIRALnRRGMTVFITTHNMVeAETIPQRIAIMRDGRIVAEG 211
Cdd:cd03245 176 EERLKERLRQL-LGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-216 |
3.60e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 114.36 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAeAVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGfnvktERL----AVR 76
Cdd:PRK11000 1 MA-SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE-----KRMndvpPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 77 RSIGLVPDVSNLYDELTVRENLLFMAKLYDAPRE----RVDELIREFELPA--DKKFGRLSTGFKRRVTIASALVHEPEV 150
Cdd:PRK11000 75 RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEeinqRVNQVAEVLQLAHllDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 151 LFLDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-216 |
3.93e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.89 E-value: 3.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 18 EAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNG--FNVKTERLAVRRSIGLVPD---VSNLYDEL 92
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDAIRAGIAYVPEdrkGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 93 TVRENL-------LFMAKLYDAPRER--VDELIREFELPA---DKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGL 160
Cdd:COG1129 346 SIRENItlasldrLSRGGLLDRRRERalAEEYIKRLRIKTpspEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 161 DVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:COG1129 426 DVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-211 |
6.19e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 110.98 E-value: 6.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV--KTERLAVRRSIG---LV 82
Cdd:COG4674 14 EDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLtgLDEHEIARLGIGrkfQK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 PDVsnlYDELTVRENLL------------FMAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEP 148
Cdd:COG4674 94 PTV---FEELTVFENLElalkgdrgvfasLFARLTAEERDRIEEVLETIGLTdkADRLAGLLSHGQKQWLEIGMLLAQDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 149 EVLFLDEPTNGLDVHSARAVRSLIRALnRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:COG4674 171 KLLLLDEPVAGMTDAETERTAELLKSL-AGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEG 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-222 |
7.03e-29 |
|
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: 110.71 E-value: 7.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 16 DFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERL-AVRRSIGLVPDVSNLYDeLTV 94
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrWLRSQIGLVSQEPVLFD-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 95 RENLLFmaKLYDAPRERVDELIR-----EF--ELP------ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLD 161
Cdd:cd03249 94 AENIRY--GKPDATDEEVEEAAKkanihDFimSLPdgydtlVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 162 VHSARAVRSlirALNR--RGMTVFITTHNMveaETI--PQRIAIMRDGRIVAEGKRGELAKLVGR 222
Cdd:cd03249 172 AESEKLVQE---ALDRamKGRTTIVIAHRL---STIrnADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-193 |
1.21e-28 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 109.24 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNG-----FNVKTERLAVRRSIGLVP 83
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGqetppLNSKKASKFRREKLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVSNLYDELTVRENLLFMAKLYDAPRERVDELIRE------FELPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPT 157
Cdd:TIGR03608 83 QNFALIENETVEENLDLGLKYKKLSKKEKREKKKEalekvgLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPT 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1828880368 158 NGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAE 193
Cdd:TIGR03608 163 GSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK 198
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-216 |
2.48e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.45 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 4 AVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTER---------LA 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkgliRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 75 VRRSIGLVPDVSNLYDELTVRENLL---FMAKlyDAPRERVDELIREfeLPAdkKFG----------RLSTGFKRRVTIA 141
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIegpVIVK--GEPKEEATARARE--LLA--KVGlagketsyprRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 142 SALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-218 |
2.62e-28 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 113.61 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNG--FNVKTERLAVRRSIGLVPD 84
Cdd:PRK15439 14 ARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpCARLTPAKAHQLGIYLVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRENLLFMAKLYDAPRERVDELIREF--ELPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDV 162
Cdd:PRK15439 94 EPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALgcQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 163 HSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAK 218
Cdd:PRK15439 174 AETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
7.33e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.20 E-value: 7.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRML---TTLTSI--TSGEAYVNGFNV---KTER 72
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPGarVEGEILLDGEDIydpDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 73 LAVRRSIGLVPDVSNLYdELTVRENLLFMAKLY-DAPRERVDELIREfelpADKKFG--------------RLSTGFKRR 137
Cdd:COG1117 88 VELRRRVGMVFQKPNPF-PKSIYDNVAYGLRLHgIKSKSELDEIVEE----SLRKAAlwdevkdrlkksalGLSGGQQQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 138 VTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRgMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGK 212
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGP 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-216 |
8.02e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 110.70 E-value: 8.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVkTERLAVRRSIGLVPDVSNL 88
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMFQSYAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 89 YDELTVRENLLFMAKLYDAPR----ERVDELI-----REFelpADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNG 159
Cdd:PRK11607 103 FPHMTVEQNIAFGLKQDKLPKaeiaSRVNEMLglvhmQEF---AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880368 160 LDVH-SARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK11607 180 LDKKlRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
15-242 |
9.64e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 108.74 E-value: 9.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 15 GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERL-AVRRSIGLVpdVSNLYDEL- 92
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIrEVRKFVGLV--FQNPDDQIf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 93 --TVRENLLF----MAKLYDAPRERVDELIREFELPA--DKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHS 164
Cdd:PRK13652 93 spTVEQDIAFgpinLGLDEETVAHRVSSALHMLGLEElrDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 165 ARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAKLVGRKTVVRLSVEPLsSSLLRALE 242
Cdd:PRK13652 173 VKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLDLPSL-PKLIRSLQ 250
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-207 |
1.01e-27 |
|
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: 105.98 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 19 AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV--KTERLAVRRSIGLVPD---VSNLYDELT 93
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAGIAYVPEdrkREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 94 VRENLLfmaklydaprervdelirefeLPAdkkfgRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIR 173
Cdd:cd03215 95 VAENIA---------------------LSS-----LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIR 148
|
170 180 190
....*....|....*....|....*....|....
gi 1828880368 174 ALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRI 207
Cdd:cd03215 149 ELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
8-212 |
1.67e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 107.38 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV------KTERLAVRRSIGL 81
Cdd:PRK11300 9 SGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghQIARMGVVRTFQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 VpdvsNLYDELTVRENLL----------FMAKLYDAPRERVDEL--------------IREFelpADKKFGRLSTGFKRR 137
Cdd:PRK11300 89 V----RLFREMTVIENLLvaqhqqlktgLFSGLLKTPAFRRAESealdraatwlervgLLEH---ANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 138 VTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGK 212
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-211 |
2.23e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.16 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV---KTERLAVRRsiGLVP 83
Cdd:PRK13548 5 ARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadwSPAELARRR--AVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVSNLYDELTVRE----NLLFMAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALV------HEPEVL 151
Cdd:PRK13548 83 QHSSLSFPFTVEEvvamGRAPHGLSRAEDDALVAAALAQVDLAhlAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880368 152 FLDEPTNGLDV----HSARAVRSLIRalnRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:PRK13548 163 LLDEPTSALDLahqhHVLRLARQLAH---ERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-221 |
2.53e-27 |
|
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: 106.16 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 19 AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT-ERLAVRRSIGLVPDVSNLYDElTVREN 97
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 98 LlfmakLYDAPRERVDELIREFELPADKKF----------------GRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLD 161
Cdd:cd03254 97 I-----RLGRPNATDEEVIEAAKEAGAHDFimklpngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880368 162 VHSARAVRSLIRALnRRGMTVFITTHNMveaETI--PQRIAIMRDGRIVAEGKRGELAKLVG 221
Cdd:cd03254 172 TETEKLIQEALEKL-MKGRTSIIIAHRL---STIknADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-211 |
3.26e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 106.74 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV---KTERLAVRRsiGLVP 83
Cdd:COG4559 4 AENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaawSPWELARRR--AVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVSNLYDELTVRENLLfMAKL-YDAPRERVDELIRE---------FelpADKKFGRLSTGFKRRVTIASAL--VHEPE-- 149
Cdd:COG4559 82 QHSSLAFPFTVEEVVA-LGRApHGSSAAQDRQIVREalalvglahL---AGRSYQTLSGGEQQRVQLARVLaqLWEPVdg 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 150 ---VLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTH--NMveAETIPQRIAIMRDGRIVAEG 211
Cdd:COG4559 158 gprWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHdlNL--AAQYADRILLLHQGRLVAQG 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-216 |
3.46e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 106.32 E-value: 3.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV---KTERLAVRRSIglvpd 84
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVattPSRELAKRLAI----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 vsnLYDE------LTVRENLLF------MAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEV 150
Cdd:COG4604 80 ---LRQEnhinsrLTVRELVAFgrfpysKGRLTAEDREIIDEAIAYLDLEdlADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 151 LFLDEPTNGLDVHSARAVRSLIRAL-NRRGMTVFITTH--NMveAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHdiNF--ASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-207 |
5.86e-27 |
|
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: 103.84 E-value: 5.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEA--VRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT-ERLAVRRSIGLVPDV 85
Cdd:cd03246 5 NVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 86 SNLYDElTVRENLLfmaklydaprervdelirefelpadkkfgrlSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSA 165
Cdd:cd03246 85 DELFSG-SIAENIL-------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1828880368 166 RAVRSLIRALNRRGMTVFITTHNMvEAETIPQRIAIMRDGRI 207
Cdd:cd03246 133 RALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-207 |
8.36e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 107.62 E-value: 8.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAeAVVANNLVKRY-GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAvRRSI 79
Cdd:PRK11650 1 MA-GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 80 GLVPDVSNLYDELTVRENLLF------MAKlyDAPRERVDELIREFELPA--DKKFGRLSTGFKRRVTIASALVHEPEVL 151
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYglkirgMPK--AEIEERVAEAARILELEPllDRKPRELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 152 FLDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRI 207
Cdd:PRK11650 157 LFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-219 |
1.05e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 109.75 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 22 GISFKVRRGEAFALLGPNGAGKTTTVRMLTTLT---SITSGEAYVNGfnVKTERLAVRRSIGLVPDVSNLYDELTVRENL 98
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNG--MPIDAKEMRAISAYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 99 LFMAKL-------YDAPRERVDELIREFELP--ADKKFGR------LSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVH 163
Cdd:TIGR00955 121 MFQAHLrmprrvtKKEKRERVDEVLQALGLRkcANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880368 164 SARAVRSLIRALNRRGMTVFITTHNmveaetiP--------QRIAIMRDGRIVAEGKRGELAKL 219
Cdd:TIGR00955 201 MAYSVVQVLKGLAQKGKTIICTIHQ-------PsselfelfDKIILMAEGRVAYLGSPDQAVPF 257
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-207 |
1.28e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.09 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVktERLAVR-RSIGLVPDVS 86
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV--SRLHARdRKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDELTVRENLLFMAKLY--------DAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEP 156
Cdd:PRK10851 84 ALFRHMTVFDNIAFGLTVLprrerpnaAAIKAKVTQLLEMVQLAhlADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 157 TNGLDVHSARAVRSLIRALNR--RGMTVFItTHNMVEAETIPQRIAIMRDGRI 207
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEelKFTSVFV-THDQEEAMEVADRVVVMSQGNI 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
9-216 |
1.59e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 105.15 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV----KTERLAVRRSIGLV-- 82
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQRKAFRRDIQMVfq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 --PDVSNLYDEL--TVRENLLFMAKLYDAPRE-RVDELIREFELP---ADKKFGRLSTGFKRRVTIASALVHEPEVLFLD 154
Cdd:PRK10419 97 dsISAVNPRKTVreIIREPLRHLLSLDKAERLaRASEMLRAVDLDdsvLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880368 155 EPTNGLDVHSARAVRSLIRALNRRGMT--VFItTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTacLFI-THDLRLVERFCQRVMVMDNGQIVETQPVGDK 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-187 |
1.61e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.61 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGfNVKterlavrrsIGLVPDVS 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR---------IGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDELTVRENLL-----------FMAKLYDAPRE------RVDELIREFE----------------------LPADKKF 127
Cdd:COG0488 71 PLDDDLTVLDTVLdgdaelraleaELEELEAKLAEpdedleRLAELQEEFEalggweaearaeeilsglgfpeEDLDRPV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 128 GRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSaraVRSLIRALNRRGMTVFITTH 187
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEWLEEFLKNYPGTVLVVSH 207
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-187 |
1.70e-26 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 103.21 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVPDVS 86
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDELTVRENLLFMAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHS 164
Cdd:TIGR01189 83 GLKPELSALENLHFWAAIHGGAQRTIEDALAAVGLTgfEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|...
gi 1828880368 165 ARAVRSLIRALNRRGMTVFITTH 187
Cdd:TIGR01189 163 VALLAGLLRAHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
8-254 |
1.75e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.07 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFE--AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA-VRRSIGLV-- 82
Cdd:PRK13632 11 ENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRKKIGIIfq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 -PDvsNLYDELTVRENLLFMAKLYDAPRERVDELIREFELPA------DKKFGRLSTGFKRRVTIASALVHEPEVLFLDE 155
Cdd:PRK13632 91 nPD--NQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVgmedylDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 156 PTNGLDVHSARAVRSLIRAL-NRRGMTVFITTHNMVEAeTIPQRIAIMRDGRIVAEGKRGELAKLVGRKTVVRLSVePLS 234
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLrKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNNKEILEKAKIDS-PFI 246
|
250 260
....*....|....*....|
gi 1828880368 235 SSLLRALERYNPSFEEGKLV 254
Cdd:PRK13632 247 YKLSKKLKGIDPTYNEEELI 266
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-260 |
1.92e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 108.33 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVA-NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNG--FNVKTERLAVRR 77
Cdd:PRK09700 1 MATPYISmAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 78 SIGLVPDVSNLYDELTVRENlLFMAKL------------YDAPRERVDELIREFELPAD--KKFGRLSTGFKRRVTIASA 143
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLEN-LYIGRHltkkvcgvniidWREMRVRAAMMLLRVGLKVDldEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 144 LVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGkrgeLAKLVGRK 223
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG----MVSDVSND 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1828880368 224 TVVRLSVEplsssllRALE-RYNPSFEE-----GKLVFEVDDV 260
Cdd:PRK09700 236 DIVRLMVG-------RELQnRFNAMKENvsnlaHETVFEVRNV 271
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-216 |
4.39e-26 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 108.29 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 4 AVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV--KTERLAVRRSIGL 81
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadARHRRAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 VPDV--SNLYDELTVRENLLFMAKLY--DAP--RERVDELIR-----EFelpADKKFGRLSTGFKRRVTIASALVHEPEV 150
Cdd:NF033858 81 MPQGlgKNLYPTLSVFENLDFFGRLFgqDAAerRRRIDELLRatglaPF---ADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880368 151 LFLDEPTNGLDVHSARAVRSLIRAL--NRRGMTVFITTHNMVEAETIPQRIAiMRDGRIVAEGKRGEL 216
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIDRIraERPGMSVLVATAYMEEAERFDWLVA-MDAGRVLATGTPAEL 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-228 |
1.18e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.00 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 13 RYGD-FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTER---LAVRRSIGLV---PDv 85
Cdd:PRK13636 14 NYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglMKLRESVGMVfqdPD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 86 snlydeltvreNLLFMAKLY--------------DAPRERVDELIRE--FELPADKKFGRLSTGFKRRVTIASALVHEPE 149
Cdd:PRK13636 93 -----------NQLFSASVYqdvsfgavnlklpeDEVRKRVDNALKRtgIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 150 VLFLDEPTNGLD-VHSARAVRSLIRALNRRGMTVFITTHNMveaETIP---QRIAIMRDGRIVAEGKRGEL--AKLVGRK 223
Cdd:PRK13636 162 VLVLDEPTAGLDpMGVSEIMKLLVEMQKELGLTIIIATHDI---DIVPlycDNVFVMKEGRVILQGNPKEVfaEKEMLRK 238
|
....*
gi 1828880368 224 TVVRL 228
Cdd:PRK13636 239 VNLRL 243
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-216 |
1.45e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 102.30 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSI-----TSGEAYVNGFNV-KTERLAVRRS 78
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIfKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 79 IGLVPDVSNLYDELTVRENL---LFMAKLYDAPRE---RVDELIREFELPADKK------FGRLSTGFKRRVTIASALVH 146
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENValgLKLNRLVKSKKElqeRVRWALEKAQLWDEVKdrldapAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 147 EPEVLFLDEPTNGLDVHSARAVRSLIRALnRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-187 |
1.70e-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: 100.40 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 22 GISFKVRRGEAFALLGPNGAGKTTTVRMLT--TLTSITSGEAYVNGFNVKTErlaVRRSIGLVPDVSNLYDELTVRENLL 99
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLDKN---FQRSTGYVEQQDVHSPNLTVREALR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 100 FMAKLydaprervdeliREfelpadkkfgrLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRG 179
Cdd:cd03232 102 FSALL------------RG-----------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSG 158
|
....*...
gi 1828880368 180 MTVFITTH 187
Cdd:cd03232 159 QAILCTIH 166
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-211 |
5.04e-25 |
|
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: 104.38 E-value: 5.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 12 KRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSiTSGEAYVNGFNV----KTERLAVRRSIGLV---Pd 84
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLdglsRRALRPLRRRMQVVfqdP- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRE------NLLFMAKLYDAPRERVDELIREFELPADkKFGR----LSTGFKRRVTIASALVHEPEVLFLD 154
Cdd:COG4172 372 FGSLSPRMTVGQiiaeglRVHGPGLSAAERRARVAEALEEVGLDPA-ARHRypheFSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880368 155 EPTNGLDVhSARA-VRSLIRALNRR-GMT-VFItTHNM--VEAetIPQRIAIMRDGRIVAEG 211
Cdd:COG4172 451 EPTSALDV-SVQAqILDLLRDLQREhGLAyLFI-SHDLavVRA--LAHRVMVMKDGKVVEQG 508
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-216 |
5.84e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 102.12 E-value: 5.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVV-ANNLVKRY----GDFE-------AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV 68
Cdd:COG4608 3 MAEPLLeVRDLKKHFpvrgGLFGrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 69 ----KTERLAVRRSIGLV---PdvsnlYDEL----TVRENL---LFMAKLYDA--PRERVDELIREFELPADKkFGR--- 129
Cdd:COG4608 83 tglsGRELRPLRRRMQMVfqdP-----YASLnprmTVGDIIaepLRIHGLASKaeRRERVAELLELVGLRPEH-ADRyph 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 130 -LSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVhSARA-VRSLIRALNRR-GMT-VFItTH--NMVeaETIPQRIAIMR 203
Cdd:COG4608 157 eFSGGQRQRIGIARALALNPKLIVCDEPVSALDV-SIQAqVLNLLEDLQDElGLTyLFI-SHdlSVV--RHISDRVAVMY 232
|
250
....*....|...
gi 1828880368 204 DGRIVAEGKRGEL 216
Cdd:COG4608 233 LGKIVEIAPRDEL 245
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-187 |
7.23e-25 |
|
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: 99.10 E-value: 7.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 22 GISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVPDVSNLYDELTVRENLLFM 101
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 102 AKLYDapRERVDELIREFELPA--DKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRG 179
Cdd:cd03231 98 HADHS--DEQVEEALARVGLNGfeDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARG 175
|
....*...
gi 1828880368 180 MTVFITTH 187
Cdd:cd03231 176 GMVVLTTH 183
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-187 |
1.01e-24 |
|
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: 103.52 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 2 AEAVVANNLVKRYGD-FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNG-----FNVKTerlaV 75
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladADADS----W 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 76 RRSIGLVPDVSNLYdELTVRENLLFMAKlyDAPRERV---------DELIREFELPADKKFG----RLSTGFKRRVTIAS 142
Cdd:TIGR02857 395 RDQIAWVPQHPFLF-AGTIAENIRLARP--DASDAEIrealeraglDEFVAALPQGLDTPIGeggaGLSGGQAQRLALAR 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1828880368 143 ALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALnRRGMTVFITTH 187
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTH 515
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-210 |
1.07e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 99.50 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGD----FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVR-----RS 78
Cdd:PRK11629 9 DNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 79 IGLVPDVSNLYDELTVREN----LLFMAKLYDAPRERVDELIRE--FELPADKKFGRLSTGFKRRVTIASALVHEPEVLF 152
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENvampLLIGKKKPAEINSRALEMLAAvgLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 153 LDEPTNGLDVHSARAVRSLIRALNRRGMTVF-ITTHNMVEAETIPQRIAiMRDGRIVAE 210
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFlVVTHDLQLAKRMSRQLE-MRDGRLTAE 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-211 |
1.48e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.23 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVK-TERLAVRRSIGLVPDVSN 87
Cdd:PRK09536 8 DLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 88 LYDELTVRE--------NLLFMAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPT 157
Cdd:PRK09536 88 LSFEFDVRQvvemgrtpHRSRFDTWTETDRAAVERAMERTGVAqfADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 158 NGLDVHsaRAVRSL--IRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:PRK09536 168 ASLDIN--HQVRTLelVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-234 |
1.67e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.32 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTT----VRMLTTLT-SITSGEAYVNGFNVKteRLAvrRSIGL 81
Cdd:PRK11231 5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLlkcfARLLTPQSgTVFLGDKPISMLSSR--QLA--RRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 VPDVSNLYDELTVRE--------NLLFMAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVL 151
Cdd:PRK11231 81 LPQHHLTPEGITVRElvaygrspWLSLWGRLSAEDNARVNQAMEQTRINhlADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 152 FLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL--AKLVgrKTVVRLS 229
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVmtPGLL--RTVFDVE 238
|
....*....
gi 1828880368 230 VE----PLS 234
Cdd:PRK11231 239 AEihpePVS 247
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-241 |
3.60e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.01 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRY---GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERL-AVR 76
Cdd:PRK13642 1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 77 RSIGLV---PDvsNLYDELTVRENLLFMAKLYDAPRE----RVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHE 147
Cdd:PRK13642 81 RKIGMVfqnPD--NQFVGATVEDDVAFGMENQGIPREemikRVDEALLAVNMLdfKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 148 PEVLFLDEPTNGLDVHSARAVRSLIRAL-NRRGMTVFITTHNMVEAETiPQRIAIMRDGRIVAEGKRGELAKLVGRKTVV 226
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIkEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
250
....*....|....*
gi 1828880368 227 RLSVePLSSSLLRAL 241
Cdd:PRK13642 238 GLDV-PFSSNLMKDL 251
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-216 |
3.67e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.90 E-value: 3.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAvrGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRrsiglvPdVS- 86
Cdd:COG3840 5 DDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER------P-VSm 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 -----NLYDELTVRENLLF----MAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDE 155
Cdd:COG3840 76 lfqenNLFPHLTVAQNIGLglrpGLKLTAEQRAQVEQALERVGLAglLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 156 PTNGLDVhsarAVR----SLIRALNR-RGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:COG3840 156 PFSALDP----ALRqemlDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-216 |
4.32e-24 |
|
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: 97.94 E-value: 4.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 18 EAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA-VRRSIGLVPDVSNLYDElTVRE 96
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwLRRQVGVVLQENVLFNR-SIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 97 NLlfmaKLYD--APRERVDE---------LIREFELPADKKFGR----LSTGFKRRVTIASALVHEPEVLFLDEPTNGLD 161
Cdd:cd03252 95 NI----ALADpgMSMERVIEaaklagahdFISELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 162 VHSARAVRSLIRALNrRGMTVFITTHNMVEAETiPQRIAIMRDGRIVAEGKRGEL 216
Cdd:cd03252 171 YESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-216 |
4.62e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 98.12 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTER-----LAV-------- 75
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgqLKVadknqlrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 76 -RRSIGLVPDVSNLYDELTVRENLLfmaklyDAP-----------RERVDELIREF---ELPADKKFGRLSTGFKRRVTI 140
Cdd:PRK10619 90 lRTRLTMVFQHFNLWSHMTVLENVM------EAPiqvlglskqeaRERAVKYLAKVgidERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 141 ASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-209 |
4.62e-24 |
|
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: 101.44 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTL--TSITSGEAYVNGFNVKTE--RLAVRRSIGLVP 83
Cdd:TIGR02633 5 KGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASniRDTERAGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVSNLYDELTVRENLLFMAKL--------YDAPRERVDELIREFELPAD---KKFGRLSTGFKRRVTIASALVHEPEVLF 152
Cdd:TIGR02633 85 QELTLVPELSVAENIFLGNEItlpggrmaYNAMYLRAKNLLRELQLDADnvtRPVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 153 LDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVA 209
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVA 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
8-210 |
7.24e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 97.26 E-value: 7.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV---KTERLaVRRSIGLVPD 84
Cdd:PRK11614 9 DKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwQTAKI-MREAVAIVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVRENLL---FMA--KLYDAPRERVDELIREFELPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNG 159
Cdd:PRK11614 88 GRRVFSRMTVEENLAmggFFAerDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 160 LDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAE 210
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-212 |
7.42e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 98.62 E-value: 7.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYG-----DFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSG------------------EA 61
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 62 YVNGFNVKTERL-------AVRRSIGLVPDVS--NLYDElTVRENLLFMAKLYDAPRERVDELIREF----ELPAD---- 124
Cdd:PRK13651 83 VLEKLVIQKTRFkkikkikEIRRRVGVVFQFAeyQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYielvGLDESylqr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 125 KKFGrLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRD 204
Cdd:PRK13651 162 SPFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....*...
gi 1828880368 205 GRIVAEGK 212
Cdd:PRK13651 241 GKIIKDGD 248
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-211 |
7.85e-24 |
|
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: 95.46 E-value: 7.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFE--AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLV 82
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 PDVSNLYDElTVRENLlfmaklydaprervdelirefelpadkkfG-RLSTGFKRRVTIASALVHEPEVLFLDEPTNGLD 161
Cdd:cd03247 81 NQRPYLFDT-TLRNNL-----------------------------GrRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 162 VHSARAVRSLI-RALnrRGMTVFITTHNMVEAETIpQRIAIMRDGRIVAEG 211
Cdd:cd03247 131 PITERQLLSLIfEVL--KDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-216 |
8.40e-24 |
|
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: 100.91 E-value: 8.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 15 GDFEAVRGISFKVRRGEAFALLGPNGAGKTTT----VRMLTTLTSITSGEAYVNGFNV--KTER--LAVR-RSIGLV--- 82
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLlgLSERelRRIRgNRIAMIfqe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 PDVS-N-LYdelTV----RENLLFMAKLYDAP-RERVDELIREFELP-ADKKFGR----LSTGFKRRVTIASALVHEPEV 150
Cdd:COG4172 101 PMTSlNpLH---TIgkqiAEVLRLHRGLSGAAaRARALELLERVGIPdPERRLDAyphqLSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 151 LFLDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:COG4172 178 LIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-216 |
8.75e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.93 E-value: 8.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 16 DFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV--KT---ERLAVRRSIGLV---PDvSN 87
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthKTkdkYIRPVRKRIGMVfqfPE-SQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 88 LYDElTVRENLLFMAKLYDAPRERVDEliREFELPADKKFGR---------LSTGFKRRVTIASALVHEPEVLFLDEPTN 158
Cdd:PRK13646 98 LFED-TVEREIIFGPKNFKMNLDEVKN--YAHRLLMDLGFSRdvmsqspfqMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 159 GLDVHSARAVRSLIRALN-RRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-216 |
9.57e-24 |
|
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: 100.65 E-value: 9.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRY-----GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVN-----------GFNvktER 72
Cdd:TIGR03269 284 NVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpGPD---GR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 73 LAVRRSIGLVPDVSNLYDELTVRENLLFMAKLydaprERVDELIR---------------EFELPADKKFGRLSTGFKRR 137
Cdd:TIGR03269 361 GRAKRYIGILHQEYDLYPHRTVLDNLTEAIGL-----ELPDELARmkavitlkmvgfdeeKAEEILDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 138 VTIASALVHEPEVLFLDEPTNGLDVHSARAV-RSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVtHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
8-223 |
1.37e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 96.67 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTS--ITSGEAYVNGFNVK----TERlaVRRSIGL 81
Cdd:COG0396 4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILelspDER--ARAGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 -------VPDVSNlydeltvrENLLFMA------KLYDAP--RERVDELIREFELPADkkFGR------LSTGFKRRVTI 140
Cdd:COG0396 82 afqypveIPGVSV--------SNFLRTAlnarrgEELSARefLKLLKEKMKELGLDED--FLDryvnegFSGGEKKRNEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 141 ASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNmveaETI-----PQRIAIMRDGRIVAEGKRgE 215
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHY----QRIldyikPDFVHVLVDGRIVKSGGK-E 226
|
....*...
gi 1828880368 216 LAKLVGRK 223
Cdd:COG0396 227 LALELEEE 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-212 |
2.56e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.06 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSIT-----SGEAYVNGFNVKTER--- 72
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDvdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 73 LAVRRSIGLVPDVSNLYDELTVRENLLFMAKLYD--APRERVDELIR----------EFELPADKKFGRLSTGFKRRVTI 140
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEwalkkaalwdEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880368 141 ASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALnRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGK 212
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-223 |
3.13e-23 |
|
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: 94.52 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTtvrMLTTL-----TSITSGEAYVNGfnvkterlavrrsiglv 82
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKG----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 PDVSNLydELTVRENL-LFMAklYDAPRE----RVDELIREFelpaDKKFgrlSTGFKRRVTIASALVHEPEVLFLDEPT 157
Cdd:cd03217 64 EDITDL--PPEERARLgIFLA--FQYPPEipgvKNADFLRYV----NEGF---SGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 158 NGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETI-PQRIAIMRDGRIVAEGKRgELAKLVGRK 223
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK-ELALEIEKK 198
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-212 |
5.20e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 95.97 E-value: 5.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 17 FE--AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT-----ERLAVRRSIGLV---PDvS 86
Cdd:PRK13649 18 FEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVfqfPE-S 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDElTVRENLLFMAKLYDAPRERVDELIRE-------FELPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNG 159
Cdd:PRK13649 97 QLFEE-TVLKDVAFGPQNFGVSQEEAEALAREklalvgiSESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 160 LDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGK 212
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-187 |
7.94e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 93.33 E-value: 7.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 21 RGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRS---IGLVPDVsnlYDELTVREN 97
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllyLGHQPGI---KTELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 98 LLFMAKLYDAPRE--RVDEL----IREFE-LPAdkkfGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRS 170
Cdd:PRK13538 95 LRFYQRLHGPGDDeaLWEALaqvgLAGFEdVPV----RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEA 170
|
170
....*....|....*..
gi 1828880368 171 LIRALNRRGMTVFITTH 187
Cdd:PRK13538 171 LLAQHAEQGGMVILTTH 187
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-222 |
1.01e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.11 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 19 AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA-VRRSIGLVPDVSNLYDElTVREN 97
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAsLRRNIAVVFQDAGLFNR-SIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 98 LLF------MAKLYDAPrERVDELirEFELPADKKFG--------RLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVH 163
Cdd:PRK13657 429 IRVgrpdatDEEMRAAA-ERAQAH--DFIERKPDGYDtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 164 SARAVRSLIRALnRRGMTVFITTHNMveaETI--PQRIAIMRDGRIVAEGKRGELAKLVGR 222
Cdd:PRK13657 506 TEAKVKAALDEL-MKGRTTFIIAHRL---STVrnADRILVFDNGRVVESGSFDELVARGGR 562
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-211 |
1.33e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.22 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAyvnGFNVKTERL------- 73
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV---HYRMRDGQLrdlyals 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 74 -AVRRSI--------------GLVPDVS---NlydeltVRENLlfMA---KLYDAPRERVDELIREFELPA---DKKFGR 129
Cdd:PRK11701 80 eAERRRLlrtewgfvhqhprdGLRMQVSaggN------IGERL--MAvgaRHYGDIRATAGDWLERVEIDAariDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 130 LSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVhSARA-----VRSLIRALnrrGMTVFITTHNMVEAETIPQRIAIMRD 204
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV-SVQArlldlLRGLVREL---GLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
....*..
gi 1828880368 205 GRIVAEG 211
Cdd:PRK11701 228 GRVVESG 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
15-209 |
1.43e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.87 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 15 GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT---ERLAV--RRSIGLVPDVSNLY 89
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldaDALAQlrREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 90 DELTVRENL----LFMAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVH 163
Cdd:PRK10535 99 SHLTAAQNVevpaVYAGLERKQRLLRAQELLQRLGLEdrVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1828880368 164 SARAVRSLIRALNRRGMTVFITTHN-MVEAETipQRIAIMRDGRIVA 209
Cdd:PRK10535 179 SGEEVMAILHQLRDRGHTVIIVTHDpQVAAQA--ERVIEIRDGEIVR 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-253 |
1.52e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.41 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRYGDFE---AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERL-AVR 76
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 77 RSIGLV---PDvsNLYDELTVRENLLF----MAKLYDAPRERVDELIR-----EFelpADKKFGRLSTGFKRRVTIASAL 144
Cdd:PRK13650 81 HKIGMVfqnPD--NQFVGATVEDDVAFglenKGIPHEEMKERVNEALElvgmqDF---KEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 145 VHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAeTIPQRIAIMRDGRIVAEGKRGELAKLVGRK 223
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGNDL 234
|
250 260 270
....*....|....*....|....*....|
gi 1828880368 224 TVVRLSVePLSSSLLRALERYNPSFEEGKL 253
Cdd:PRK13650 235 LQLGLDI-PFTTSLVQSLRQNGYDLPEGYL 263
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-211 |
1.59e-22 |
|
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: 92.94 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 27 VRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAvRRSIGLVPDVSNLYDELTVRENLLFMA---- 102
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-DRPVSMLFQENNLFAHLTVEQNVGLGLspgl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 103 KLYDAPRERVDELIREFELPA--DKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNR-RG 179
Cdd:cd03298 100 KLTAEDRQAIEVALARVGLAGleKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAeTK 179
|
170 180 190
....*....|....*....|....*....|..
gi 1828880368 180 MTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:cd03298 180 MTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-211 |
2.63e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.54 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTL-TSITSGEAYVN--GFNVKTE-RLA-- 74
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLiTGDKSAGSHIEllGRTVQREgRLArd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 75 VRRS---IGLVPDVSNLYDELTVRENLLFMAkLYDAPRERV-----DELIREFELPADKKFG-------RLST---GFKR 136
Cdd:PRK09984 81 IRKSranTGYIFQQFNLVNRLSVLENVLIGA-LGSTPFWRTcfswfTREQKQRALQALTRVGmvhfahqRVSTlsgGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 137 RVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-260 |
2.98e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.54 E-value: 2.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTL--TSITSGEAYVNGFNVK------TERLAV---R 76
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQasnirdTERAGIaiiH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 77 RSIGLVPdvsnlydELTVRENLLFMAKL-------YDAPRERVDELIREFELPAD--KKFGRLSTGFKRRVTIASALVHE 147
Cdd:PRK13549 89 QELALVK-------ELSVLENIFLGNEItpggimdYDAMYLRAQKLLAQLKLDINpaTPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 148 PEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL------AKLVG 221
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMteddiiTMMVG 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 1828880368 222 RKtvvrlsveplssslLRALERYNPSfEEGKLVFEVDDV 260
Cdd:PRK13549 242 RE--------------LTALYPREPH-TIGEVILEVRNL 265
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-256 |
3.83e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 93.74 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 23 ISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTER-----LAVRRSIGLV---PDvSNLYDElTV 94
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknlKKLRKKVSLVfqfPE-AQLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 95 RENLLFMAKLY----DAPRERVDELIREFELP---ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARA 167
Cdd:PRK13641 104 LKDVEFGPKNFgfseDEAKEKALKWLKKVGLSedlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 168 VRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAKlvGRKTVVR--LSvEPLSSSLLRALERYN 245
Cdd:PRK13641 184 MMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS--DKEWLKKhyLD-EPATSRFASKLEKGG 260
|
250
....*....|.
gi 1828880368 246 PSFEEGKLVFE 256
Cdd:PRK13641 261 FKFSEMPLTID 271
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-207 |
3.85e-22 |
|
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: 92.15 E-value: 3.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 16 DFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT-ERLAVRRSIGLVPDVSNLYDElTV 94
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 95 RENLLFmaKLYDAPRERVDEL---------IREFEL----PADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLD 161
Cdd:cd03248 105 QDNIAY--GLQSCSFECVKEAaqkahahsfISELASgydtEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1828880368 162 VHSARAVRSLIRALNRRgMTVFITTHNMVEAETiPQRIAIMRDGRI 207
Cdd:cd03248 183 AESEQQVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-208 |
6.77e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 6.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEaYVNGFNVKterlavrrsIGLVP- 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGETVK---------IGYFDq 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVSNLYDELTVRENLLFMAKlyDAPRERVDELIREFELP---ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGL 160
Cdd:COG0488 386 HQEELDPDKTVLDELRDGAP--GGTEQEVRGYLGRFLFSgddAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHL 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1828880368 161 DVHSARAvrsLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIV 208
Cdd:COG0488 464 DIETLEA---LEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-222 |
1.02e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.89 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGD--FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVK--TERlAVRRSIGLVP 83
Cdd:PRK11160 342 NNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdySEA-ALRQAISVVS 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVSNLYDElTVRENLLFMAKlyDAPRERVDELIREFELPA----DKKF-------GR-LSTGFKRRVTIASALVHEPEVL 151
Cdd:PRK11160 421 QRVHLFSA-TLRDNLLLAAP--NASDEALIEVLQQVGLEKlledDKGLnawlgegGRqLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 152 FLDEPTNGLDVHSARAVRSLIRALNrRGMTVFITTHNMVEAETIpQRIAIMRDGRIVAEGKRGELAKLVGR 222
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQGR 566
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-208 |
1.34e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.38 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVA-NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSI-----TSGEAYVNGFNV---KTE 71
Cdd:PRK14239 1 MTEPILQvSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIyspRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 72 RLAVRRSIGLVPDVSNLYdELTVRENLLFMAKLYDAP-RERVDELIREFELPA-----------DKKFGrLSTGFKRRVT 139
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIKdKQVLDEAVEKSLKGAsiwdevkdrlhDSALG-LSGGQQQRVC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 140 IASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALnRRGMTVFITTHNMVEAETIPQRIAIMRDGRIV 208
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-216 |
1.45e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.65 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 16 DFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV-------KTERLAVRRSIGLVPDVSNL 88
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 89 YDELTVRENLLFMAKLYDAPRER-----VDELIREFEL------PADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPT 157
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKReikkiVEECLRKVGLwkevydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 158 NGLDVHSARAVRSLIRALnRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK14246 182 SMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-223 |
1.46e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 94.30 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT----ERLAV--------RRSIGLVPDVSn 87
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspqDGLANgivyisedRKRDGLVLGMS- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 88 lydeltVRENLLFMAKLY----------DAPRERVDELIREFEL--PA-DKKFGRLSTGFKRRVTIASALVHEPEVLFLD 154
Cdd:PRK10762 347 ------VKENMSLTALRYfsraggslkhADEQQAVSDFIRLFNIktPSmEQAIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 155 EPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGE------LAKLVGRK 223
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQatqeklMAAAVGKL 495
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-212 |
2.20e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.40 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 14 YGDFE--AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTL--------TSITsgeayVNGFNVKTERL-AVRRSIGLV 82
Cdd:PRK13640 15 YPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKIT-----VDGITLTAKTVwDIREKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 ---PDvsNLYDELTVRENLLFMAKLYDAPRERVDELIR---------EFelpADKKFGRLSTGFKRRVTIASALVHEPEV 150
Cdd:PRK13640 90 fqnPD--NQFVGATVGDDVAFGLENRAVPRPEMIKIVRdvladvgmlDY---IDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 151 LFLDEPTNGLDVHSARAVRSLIRAL-NRRGMTVFITTHNMVEAETIPQRIaIMRDGRIVAEGK 212
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANMADQVL-VLDDGKLLAQGS 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-216 |
3.47e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 93.63 E-value: 3.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 21 RGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFN-VKTERLAVRRSIGLVPDVSNLYDElTVRENLL 99
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPlVQYDHHYLHRQVALVGQEPVLFSG-SVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 100 FmaKLYDAPRERV---------DELIREFELPADKKFG----RLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSAR 166
Cdd:TIGR00958 577 Y--GLTDTPDEEImaaakaanaHDFIMEFPNGYDTEVGekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1828880368 167 AVRSLiraLNRRGMTVFITTHNMVEAETIPQrIAIMRDGRIVAEGKRGEL 216
Cdd:TIGR00958 655 LLQES---RSRASRTVLLIAHRLSTVERADQ-ILVLKKGSVVEMGTHKQL 700
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-187 |
3.98e-21 |
|
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: 93.19 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 15 GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERL-AVRRSIGLVPDVSNLYDElT 93
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 94 VRENLLFMAK------LYDA-PRERVDELIREFELPADKKFG----RLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDV 162
Cdd:TIGR02868 425 VRENLRLARPdatdeeLWAAlERVGLADWLRALPDGLDTVLGeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....*
gi 1828880368 163 HSARAVRSLIRALNRRGMTVFITTH 187
Cdd:TIGR02868 505 ETADELLEDLLAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-243 |
4.32e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 90.85 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 17 FE--AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSG---------EAYVNGFNVKTerlaVRRSIGLV--- 82
Cdd:PRK13634 18 FErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigerviTAGKKNKKLKP----LRKKVGIVfqf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 PDvSNLYDElTVRENLLFMAKLYDAPRE----RVDELIREFELPAD---KKFGRLSTGFKRRVTIASALVHEPEVLFLDE 155
Cdd:PRK13634 94 PE-HQLFEE-TVEKDICFGPMNFGVSEEdakqKAREMIELVGLPEEllaRSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 156 PTNGLDVHSARAVRSLIRALNR-RGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAKLVGRKTVVRLSVePLS 234
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIGLDL-PET 250
|
....*....
gi 1828880368 235 SSLLRALER 243
Cdd:PRK13634 251 VKFKRALEE 259
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-223 |
6.62e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.87 E-value: 6.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 24 SFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNvKTERLAVRRSIGLVPDVSNLYDELTVRENL-LFMA 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQNIgLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 103 ---KLYDAPRERVDELIREFELPA--DKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDvhsaRAVRSLIRAL-- 175
Cdd:PRK10771 98 pglKLNAAQREKLHAIARQMGIEDllARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD----PALRQEMLTLvs 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880368 176 ---NRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL-------AKLVGRK 223
Cdd:PRK10771 174 qvcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELlsgkasaSALLGIK 231
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-216 |
8.15e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.79 E-value: 8.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRY----GDF------EAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV-- 68
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrGLFkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 69 --KTERLAVRRSIGLVpdVSNLYDELTVR--------ENLLFMAKLYDAPR-ERVDELIREFELPADkKFGR----LSTG 133
Cdd:PRK11308 82 adPEAQKLLRQKIQIV--FQNPYGSLNPRkkvgqileEPLLINTSLSAAERrEKALAMMAKVGLRPE-HYDRyphmFSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 134 FKRRVTIASALVHEPEVLFLDEPTNGLDVhSARA-VRSLIRALNRRGMT--VFItTHNMVEAETIPQRIAIMRDGRIVAE 210
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDV-SVQAqVLNLMMDLQQELGLsyVFI-SHDLSVVEHIADEVMVMYLGRCVEK 236
|
....*.
gi 1828880368 211 GKRGEL 216
Cdd:PRK11308 237 GTKEQI 242
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-222 |
9.83e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 89.28 E-value: 9.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVV---ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVktERLA--- 74
Cdd:PRK10253 1 MTESVArlrGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI--QHYAske 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 75 VRRSIGLVPDVSNLYDELTVREnLLFMAKLYDAP------RERVDELIREFELP-----ADKKFGRLSTGFKRRVTIASA 143
Cdd:PRK10253 79 VARRIGLLAQNATTPGDITVQE-LVARGRYPHQPlftrwrKEDEEAVTKAMQATgithlADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 144 LVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNR-RGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL--AKLV 220
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIvtAELI 237
|
..
gi 1828880368 221 GR 222
Cdd:PRK10253 238 ER 239
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-212 |
1.03e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 89.66 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 19 AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVK--TERLAVRRSIGLV---PDVSnlYDELT 93
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfSKLQGIRKLVGIVfqnPETQ--FVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 94 VRENLLFMAKLYDAP----RERVDELIREFELPADKKFG--RLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARA 167
Cdd:PRK13644 95 VEEDLAFGPENLCLPpieiRKRVDRALAEIGLEKYRHRSpkTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1828880368 168 VRSLIRALNRRGMTVFITTHNMVEAEtIPQRIAIMRDGRIVAEGK 212
Cdd:PRK13644 175 VLERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGE 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-216 |
1.18e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.38 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 2 AEAVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAY-----VNGFNVKTER--LA 74
Cdd:PRK14271 19 APAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNYRdvLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 75 VRRSIGLVPDVSNLYdELTVRENLLFMAK----------------------LYDAPRERVdelirefelpADKKFgRLST 132
Cdd:PRK14271 99 FRRRVGMLFQRPNPF-PMSIMDNVLAGVRahklvprkefrgvaqarltevgLWDAVKDRL----------SDSPF-RLSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 133 GFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRgMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGK 212
Cdd:PRK14271 167 GQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
....
gi 1828880368 213 RGEL 216
Cdd:PRK14271 246 TEQL 249
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-209 |
1.23e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.51 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNG----FNVKTERLA-----VRRS 78
Cdd:PRK11288 8 DGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrFASTTAALAagvaiIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 79 IGLVPdvsnlydELTVRENLLF-----------MAKLYDAPRERVDELirEFELPADKKFGRLSTGFKRRVTIASALVHE 147
Cdd:PRK11288 88 LHLVP-------EMTVAENLYLgqlphkggivnRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 148 PEVLFLDEPTNGLdvhSARAVR---SLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVA 209
Cdd:PRK11288 159 ARVIAFDEPTSSL---SAREIEqlfRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
15-215 |
1.43e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.01 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 15 GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV----KTERLAVRRSIGLVPDVSNLYD 90
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 91 ELTVREN----LLFMAKLYDAPRERVDELIREFELpADKKFG---RLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVH 163
Cdd:PRK10908 93 DRTVYDNvaipLIIAGASGDDIRRRVSAALDKVGL-LDKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1828880368 164 SARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVaEGKRGE 215
Cdd:PRK10908 172 LSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH-GGVGGE 222
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-187 |
6.19e-20 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 90.17 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 27 VRRGEAFALLGPNGAGKTTTVRML---TTLTSITSGEAYVNGFNVKTerlAVRRSIGLVPDVSNLYDELTVRENLLFMAK 103
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLaerVTTGVITGGDRLVNGRPLDS---SFQRSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 104 LY---DAPRER----VDELIR--EFELPADKKFGR----LSTGFKRRVTIASALVHEPEVL-FLDEPTNGLDVHSARAVR 169
Cdd:TIGR00956 863 LRqpkSVSKSEkmeyVEEVIKllEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLlFLDEPTSGLDSQTAWSIC 942
|
170
....*....|....*...
gi 1828880368 170 SLIRALNRRGMTVFITTH 187
Cdd:TIGR00956 943 KLMRKLADHGQAILCTIH 960
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-216 |
9.64e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.93 E-value: 9.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 11 VKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVktERLAVRRSI----------- 79
Cdd:COG3845 265 VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI--TGLSPRERRrlgvayipedr 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 80 ---GLVPDvsnlydeLTVRENLLFmaKLYDAP-------------RERVDELIREF-------ELPAdkkfGRLSTGFKR 136
Cdd:COG3845 343 lgrGLVPD-------MSVAENLIL--GRYRRPpfsrggfldrkaiRAFAEELIEEFdvrtpgpDTPA----RSLSGGNQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 137 RVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-189 |
1.38e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 86.24 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 4 AVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSItSGEAYVNG----FN-------VKTER 72
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrvefFNqniyerrVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 73 LavRRSIGLVPDVSNLYdELTVRENLLFMAKLYD-APRERVDELIREFELPAD----------KKFGRLSTGFKRRVTIA 141
Cdd:PRK14258 86 L--RRQVSMVHPKPNLF-PMSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADlwdeikhkihKSALDLSGGQQQRLCIA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1828880368 142 SALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRG-MTVFITTHNM 189
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNL 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-211 |
2.22e-19 |
|
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: 84.47 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFE--AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERL-AVRRSIGLVPD 84
Cdd:cd03244 6 KNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLhDLRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDElTVRENLLFMAKLYDAPRERVDELIREFELPADKKFG----------RLSTGFKRRVTIASALVHEPEVLFLD 154
Cdd:cd03244 86 DPVLFSG-TIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGldtvveeggeNLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 155 EPTNGLDVHSARAVRSLIRAlNRRGMTVFITTHNMveaETI--PQRIAIMRDGRIVAEG 211
Cdd:cd03244 165 EATASVDPETDALIQKTIRE-AFKDCTVLTIAHRL---DTIidSDRILVLDKGRVVEFD 219
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
9-187 |
2.47e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 84.23 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVPDVSNL 88
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 89 YDELTVRENLLFMAKLYDAPRErVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSAR 166
Cdd:PRK13540 86 NPYLTLRENCLYDIHFSPGAVG-ITELCRLFSLEhlIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|.
gi 1828880368 167 AVRSLIRALNRRGMTVFITTH 187
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-236 |
2.98e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 87.75 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 19 AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV--KTERLAVRRSIGLVPDVSNLYDELTVRE 96
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfNGPKSSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 97 NLL--------FMAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSAR 166
Cdd:PRK10762 99 NIFlgrefvnrFGRIDWKKMYAEADKLLARLNLRfsSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 167 AVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELAK------LVGRKTV------------VRL 228
Cdd:PRK10762 179 SLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEdsliemMVGRKLEdqyprldkapgeVRL 258
|
....*...
gi 1828880368 229 SVEPLSSS 236
Cdd:PRK10762 259 KVDNLSGP 266
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-216 |
3.81e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.83 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSI-----TSGEAYVNGFNVKTERL---AVRRS 78
Cdd:PRK14243 13 TENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDVdpvEVRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 79 IGLVPDVSNLYDElTVRENLLFMAKLyDAPRERVDELI-REFELPA------DK--KFG-RLSTGFKRRVTIASALVHEP 148
Cdd:PRK14243 93 IGMVFQKPNPFPK-SIYDNIAYGARI-NGYKGDMDELVeRSLRQAAlwdevkDKlkQSGlSLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 149 EVLFLDEPTNGLDVHSARAVRSLIRALNRRgMTVFITTHNMVEAETIPQRIAIMrDGRIVAEGKR-GEL 216
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFF-NVELTEGGGRyGYL 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-211 |
3.92e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.56 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 19 AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT-----ERLAVRRSIGLV---PDvSNLYD 90
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkEIKPVRKKVGVVfqfPE-SQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 91 ElTVRENLLFMAKLYDAPRERVDELIRE-FELPA------DKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVH 163
Cdd:PRK13643 100 E-TVLKDVAFGPQNFGIPKEKAEKIAAEkLEMVGladefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1828880368 164 SARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-216 |
4.46e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.38 E-value: 4.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 19 AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA-VRRSIGLVPDVSNLYDElTVREN 97
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAsLRNQVALVSQNVHLFND-TIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 98 LLFMAK-LYDapRERVD---------ELIREFELPADKKFGR----LSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVH 163
Cdd:PRK11176 437 IAYARTeQYS--REQIEeaarmayamDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 164 SARAVRSLIRAL--NRrgmTVFITTHNMveaETIPQ--RIAIMRDGRIVAEGKRGEL 216
Cdd:PRK11176 515 SERAIQAALDELqkNR---TSLVIAHRL---STIEKadEILVVEDGEIVERGTHAEL 565
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-221 |
7.44e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.44 E-value: 7.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 23 ISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITsGEAYVNGFNVKTERLAV-RRSIGLVPDVSNLYdELTVRENLLfM 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwRKHLSWVGQNPQLP-HGTLRDNVL-L 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 102 AKlYDAPRERVDELIR-----EF--ELPA--DKKFG----RLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAV 168
Cdd:PRK11174 446 GN-PDASDEQLQQALEnawvsEFlpLLPQglDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 169 rslIRALNR--RGMTVFITTHNMVEAETIPQrIAIMRDGRIVAEGKRGELAKLVG 221
Cdd:PRK11174 525 ---MQALNAasRRQTTLMVTHQLEDLAQWDQ-IWVMQDGQIVQQGDYAELSQAGG 575
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-215 |
7.79e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.74 E-value: 7.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 22 GISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSiTSGEAYVNGFNVKT---ERLAVRRSiglvpdvsnlYdeLTVRENL 98
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDwsaAELARHRA----------Y--LSQQQSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 99 LFMAKLY-------------DAPRERVDELIREFELpaDKKFGR----LSTGFKRRVTIASAL--VH-----EPEVLFLD 154
Cdd:COG4138 81 PFAMPVFqylalhqpagassEAVEQLLAQLAEALGL--EDKLSRpltqLSGGEWQRVRLAAVLlqVWptinpEGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 155 EPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGE 215
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-212 |
1.30e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 83.65 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 23 ISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA-VRRSIGLV---PDvsNLYDELTVRENL 98
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEkLRKHIGIVfqnPD--NQFVGSIVKYDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 99 LF----MAKLYDAPRERVDELIREFEL--PADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLI 172
Cdd:PRK13648 106 AFglenHAVPYDEMHRRVSEALKQVDMleRADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLV 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1828880368 173 RALNR-RGMTVFITTHNMVEAETIPQRIaIMRDGRIVAEGK 212
Cdd:PRK13648 186 RKVKSeHNITIISITHDLSEAMEADHVI-VMNKGTVYKEGT 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-206 |
1.48e-18 |
|
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: 82.13 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 21 RGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGfnvkterlavrrSIGLVPDVSNLYDElTVRENLLF 100
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWIQNG-TIRENILF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 101 MAKlYDAprERVDELIREFELPAD-KKFGR------------LSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARA 167
Cdd:cd03250 89 GKP-FDE--ERYEKVIKACALEPDlEILPDgdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRH 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1828880368 168 V-RSLIRALNRRGMTVFITTHNMveaETIPQ--RIAIMRDGR 206
Cdd:cd03250 166 IfENCILGLLLNNKTRILVTHQL---QLLPHadQIVVLDNGR 204
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-215 |
1.59e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.35 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 23 ISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNG--FNVKTERLAVRRSI----------GLVPDVSnlyd 90
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGImlcpedrkaeGIIPVHS---- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 91 eltVRENL--------LFMAKLYDAPRER--VDELIREFELP---ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPT 157
Cdd:PRK11288 348 ---VADNInisarrhhLRAGCLINNRWEAenADRFIRSLNIKtpsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880368 158 NGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGE 215
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-232 |
1.96e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 16 DFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT------ERLAVRRSIGLV---PDVs 86
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikEVKRLRKEIGLVfqfPEY- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDElTVRENLLFMAKLYDAPRE----RVDELIREFELPAD---KKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNG 159
Cdd:PRK13645 102 QLFQE-TIEKDIAFGPVNLGENKQeaykKVPELLKLVQLPEDyvkRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880368 160 LDVHSARAVRSLIRALNR-RGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGELakLVGRKTVVRLSVEP 232
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI--FSNQELLTKIEIDP 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-261 |
2.63e-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: 84.85 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSI--TSGE-----------AYVN----------- 64
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRiiyhvalcekcGYVErpskvgepcpv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 65 ------GFNV------KTERLAVRRSIGLVPDVS-NLYDELTVRENLlfMAKLYDAPRERVDELIREFELPADKKFGR-- 129
Cdd:TIGR03269 85 cggtlePEEVdfwnlsDKLRRRIRKRIAIMLQRTfALYGDDTVLDNV--LEALEEIGYEGKEAVGRAVDLIEMVQLSHri 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 130 ------LSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRS-LIRALNRRGMTVFITTHNMVEAETIPQRIAIM 202
Cdd:TIGR03269 163 thiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEVIEDLSDKAIWL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 203 RDGRIVAEG-------KRGELAKLVGRKTVVRLSVEPLSsslLRALERYNPSFEEGkLVFEVDDVD 261
Cdd:TIGR03269 243 ENGEIKEEGtpdevvaVFMEGVSEVEKECEVEVGEPIIK---VRNVSKRYISVDRG-VVKAVDNVS 304
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
23-206 |
2.90e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.68 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 23 ISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT---ERLavRRSIGLVPDVSNLYDElTVRENLL 99
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlkpEIY--RQQVSYCAQTPTLFGD-TVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 100 FMAKL-YDAPRER--VDELIReFELPA---DKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIR 173
Cdd:PRK10247 103 FPWQIrNQQPDPAifLDDLER-FALPDtilTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIH 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1828880368 174 ALNR-RGMTVFITTHNMVEAE------TIPQRIAIMRDGR 206
Cdd:PRK10247 182 RYVReQNIAVLWVTHDKDEINhadkviTLQPHAGEMQEAR 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-208 |
5.50e-18 |
|
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: 80.53 E-value: 5.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYG-DFEAV-RGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERL-AVRRSIGLVPD 84
Cdd:cd03369 10 ENLSVRYApDLPPVlKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLeDLRSSLTIIPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDElTVRENLlfmaklyDAPRERVDELIREfELPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHS 164
Cdd:cd03369 90 DPTLFSG-TIRSNL-------DPFDEYSDEEIYG-ALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1828880368 165 ARAVRSLIRALnRRGMTVFITTHNMveaETIP--QRIAIMRDGRIV 208
Cdd:cd03369 161 DALIQKTIREE-FTNSTILTIAHRL---RTIIdyDKILVMDAGEVK 202
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-216 |
5.54e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.98 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 13 RYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTER---LAVRRSIGLV---PDVS 86
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrglLALRQQVATVfqdPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDEltVRENLLFMAKLYDAPRERVDELIREFELPADKKFGR------LSTGFKRRVTIASALVHEPEVLFLDEPTNGL 160
Cdd:PRK13638 90 IFYTD--IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 161 DVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-210 |
5.64e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.07 E-value: 5.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRygDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV--KTERLAVRRSIGLVPD 84
Cdd:PRK09700 268 VRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 V---SNLYDELTVRENLLFMAKLYDA----------PRERVDELIREFELPA------DKKFGRLSTGFKRRVTIASALV 145
Cdd:PRK09700 346 SrrdNGFFPNFSIAQNMAISRSLKDGgykgamglfhEVDEQRTAENQRELLAlkchsvNQNITELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 146 HEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAE 210
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-216 |
8.19e-18 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 83.53 E-value: 8.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 24 SFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEaYVNGFNvKTERLAVRRSIGLVPD---------VSNLYDE--L 92
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE-RQSQFS-HITRLSFEQLQKLVSDewqrnntdmLSPGEDDtgR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 93 TVRENLLFMAKlydaPRERVDELIREFELPA--DKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRS 170
Cdd:PRK10938 101 TTAEIIQDEVK----DPARCEQLAQQFGITAllDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1828880368 171 LIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK10938 177 LLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-207 |
9.09e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 9.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNgfnvKTERLAVRRSIGLVPD 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG----TAPLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDELTVREN--LLFMAKLYDAPRERVDEL---IREFELPAdkkfgRLSTGFKRRVTIASALVHEPEVLFLDEPTNG 159
Cdd:PRK11247 89 DARLLPWKKVIDNvgLGLKGQWRDAALQALAAVglaDRANEWPA-----ALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1828880368 160 LDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRI 207
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-187 |
1.22e-17 |
|
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: 77.87 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEaYVNGFNVKterlavrrsIGLVPd 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-VTWGSTVK---------IGYFE- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 vsnlydeltvrenllfmaklydaprervdelirefelpadkkfgRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHS 164
Cdd:cd03221 70 --------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES 105
|
170 180
....*....|....*....|...
gi 1828880368 165 araVRSLIRALNRRGMTVFITTH 187
Cdd:cd03221 106 ---IEALEEALKEYPGTVILVSH 125
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-216 |
1.44e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.39 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 19 AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV----KTERLAVRR-SIGLVPDVSNLYDELT 93
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisDAELREVRRkKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 94 VRENLLFMAKLYDAP----RERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLD-VHSAR 166
Cdd:PRK10070 123 VLDNTAFGMELAGINaeerREKALDALRQVGLEnyAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDpLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1828880368 167 AVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-208 |
2.34e-17 |
|
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: 78.84 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 12 KRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSIT---SGEAYVNGFNVKTERLAVRRSIGLVPDVSNL 88
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 89 YDELTVRENLLFMAKLydapreRVDELIREFelpadkkfgrlSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAV 168
Cdd:cd03233 95 FPTLTVRETLDFALRC------KGNEFVRGI-----------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1828880368 169 RSLIRALNRR-GMTVFIT-------THNMVEaetipqRIAIMRDGRIV 208
Cdd:cd03233 158 LKCIRTMADVlKTTTFVSlyqasdeIYDLFD------KVLVLYEGRQI 199
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-216 |
2.50e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 79.81 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVK------RYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT---ERL-AVR 76
Cdd:PRK11831 4 VANLVDmrgvsfTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrSRLyTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 77 RSIGLVPDVSNLYDELTVRENLLFmaklydaP-RERV---DELIREFEL----------PADKKFGRLSTGFKRRVTIAS 142
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAY-------PlREHTqlpAPLLHSTVMmkleavglrgAAKLMPSELSGGMARRAALAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 143 ALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-262 |
2.72e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRygDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT----ERLAVRRSIGLV-- 82
Cdd:PRK10261 331 NRVTR--EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIfq 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 -PDVSnLYDELTVRENLLFMAKLY-----DAPRERVDELIREFELPADKKF---GRLSTGFKRRVTIASALVHEPEVLFL 153
Cdd:PRK10261 409 dPYAS-LDPRQTVGDSIMEPLRVHgllpgKAAAARVAWLLERVGLLPEHAWrypHEFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 154 DEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKrgelaklvgRKTVVRLSVEP 232
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP---------RRAVFENPQHP 558
|
250 260 270
....*....|....*....|....*....|
gi 1828880368 233 LSSSLLRALERYNPSFEEGKLVFEVDDVDG 262
Cdd:PRK10261 559 YTRKLMAAVPVADPSRQRPQRVLLSDDLPS 588
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-215 |
3.06e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.21 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 23 ISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSiTSGEAYVNGFNVKTER---LAVRRSiglvpdvsnlYdeLTVRENLL 99
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSaaeLARHRA----------Y--LSQQQTPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 100 FMAKLY-------------DAPRERVDELIREFELpaDKKFGR----LSTGFKRRVTIASAL--VH-----EPEVLFLDE 155
Cdd:PRK03695 82 FAMPVFqyltlhqpdktrtEAVASALNEVAEALGL--DDKLGRsvnqLSGGEWQRVRLAAVVlqVWpdinpAGQLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 156 PTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGE 215
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-210 |
7.29e-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: 80.64 E-value: 7.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 6 VANNLVKRYGDfeavrgISFKVRRGEAFALLGPNGAGKTTTVRML-TTLTSITSGEAYVNG--FNVKTERLAVRRSIGLV 82
Cdd:TIGR02633 268 VINPHRKRVDD------VSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGkpVDIRNPAQAIRAGIAMV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 PD-------VSNL----YDELTVRENLLFMAKLYDAPRER-VDELIREFELPADKKF---GRLSTGFKRRVTIASALVHE 147
Cdd:TIGR02633 342 PEdrkrhgiVPILgvgkNITLSVLKSFCFKMRIDAAAELQiIGSAIQRLKVKTASPFlpiGRLSGGNQQKAVLAKMLLTN 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 148 PEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAE 210
Cdd:TIGR02633 422 PRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-243 |
4.40e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.36 E-value: 4.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 17 FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEayvngfnVKTERLAVRRSIGLVPDVSNLYDELTVRE 96
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGL-------VQCDKMLLRRRSRQVIELSEQSAAQMRHV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 97 NLLFMAKLYDAPR----------ERVDELIR-------EFELPADKKF-----------------GRLSTGFKRRVTIAS 142
Cdd:PRK10261 102 RGADMAMIFQEPMtslnpvftvgEQIAESIRlhqgasrEEAMVEAKRMldqvripeaqtilsrypHQLSGGMRQRVMIAM 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 143 ALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGElaklvg 221
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQ------ 255
|
250 260
....*....|....*....|..
gi 1828880368 222 rktVVRLSVEPLSSSLLRALER 243
Cdd:PRK10261 256 ---IFHAPQHPYTRALLAAVPQ 274
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-194 |
4.73e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.92 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGeayvngfnvKTERLAVRRsIG 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG---------VIKRNGKLR-IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 81 LVPDVSNLYDELTVRENLLFMAKlydaPRERVDELirefeLPADKK----------FGRLSTGFKRRVTIASALVHEPEV 150
Cdd:PRK09544 71 YVPQKLYLDTTLPLTVNRFLRLR----PGTKKEDI-----LPALKRvqaghlidapMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1828880368 151 LFLDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHN--MVEAET 194
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDlhLVMAKT 188
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-211 |
5.25e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.81 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 3 EAVVANNLV-----KRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA--- 74
Cdd:PRK13631 20 IILRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNhel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 75 --------------VRRSIGLV---PDVSNLYDelTVRENLLFMAKLYDAPRERVDELIREF--ELPADKKF-----GRL 130
Cdd:PRK13631 100 itnpyskkiknfkeLRRRVSMVfqfPEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAKFYlnKMGLDDSYlerspFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 131 STGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAE 210
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
.
gi 1828880368 211 G 211
Cdd:PRK13631 258 G 258
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-209 |
6.06e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 77.85 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNG--FNVKTERLAVRRSIGLVPDVS 86
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDELTVRENL---------LFM--AKLYDAPRERVDELirEFELPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDE 155
Cdd:PRK10982 83 NLVLQRSVMDNMwlgryptkgMFVdqDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1828880368 156 PTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVA 209
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-189 |
6.21e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.07 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRYGD-FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVkteRLAVRRS- 78
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 79 IGLVPDVSNLYDELTVR-ENLLFM-----------AKLYDapRERVDELIREFELPA--DKKFGRLSTGFKRRVTIASAL 144
Cdd:PRK15056 80 VAYVPQSEEVDWSFPVLvEDVVMMgryghmgwlrrAKKRD--RQIVTAALARVDMVEfrHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1828880368 145 VHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNM 189
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNL 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-207 |
1.25e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.01 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 18 EAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLV--PD---VSNLYDE- 91
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylPEdrqSSGLYLDa 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 92 --------LTVRENLLFMAKLYDAPR-ERVDELIR-EFElPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLD 161
Cdd:PRK15439 357 plawnvcaLTHNRRGFWIKPARENAVlERYRRALNiKFN-HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1828880368 162 VhSARA-VRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRI 207
Cdd:PRK15439 436 V-SARNdIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
8-223 |
1.29e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 74.68 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLT--TLTSITSGEAYVNGFNVKTERLAVRRSIGL---- 81
Cdd:CHL00131 11 KNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEPEERAHLGIflaf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 -----VPDVSNlydeltvrENLLFMAklYDAPR--ERVDEL--IREFELPADK--------KF-GR-----LSTGFKRRV 138
Cdd:CHL00131 91 qypieIPGVSN--------ADFLRLA--YNSKRkfQGLPELdpLEFLEIINEKlklvgmdpSFlSRnvnegFSGGEKKRN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 139 TIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTH--NMVEAeTIPQRIAIMRDGRIVAEGKrGEL 216
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLDY-IKPDYVHVMQNGKIIKTGD-AEL 238
|
....*..
gi 1828880368 217 AKLVGRK 223
Cdd:CHL00131 239 AKELEKK 245
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
30-216 |
1.34e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.21 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 30 GEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT-ERLAVRRSIGLVPDVSNLYDELTVRENLLF-------- 100
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRELVAIgrypwhga 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 101 MAKLYDAPRERVDELIREFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNR- 177
Cdd:PRK10575 117 LGRFGAADREKVEEAISLVGLKplAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQe 196
|
170 180 190
....*....|....*....|....*....|....*....
gi 1828880368 178 RGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK10575 197 RGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-213 |
1.60e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 17 FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYvngFNVKTERLAVRRSIglVPDVSNLYDELTVRE 96
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC---VDVPDNQFGREASL--IDAIGRKGDFKDAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 97 nLLFMAKLYDAPrervdeLIRefelpadKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAV-RSLIRAL 175
Cdd:COG2401 118 -LLNAVGLSDAV------LWL-------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVaRNLQKLA 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 1828880368 176 NRRGMT-VFITTHNMVEAETIPQRIAIMRDGRIVAEGKR 213
Cdd:COG2401 184 RRAGITlVVATHHYDVIDDLQPDLLIFVGYGGVPEEKRR 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-211 |
2.99e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 10 LVKRYGDF-EAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSiTSGEAYVNG-----FNVKtERLAVRRSIGLV- 82
Cdd:PRK15134 291 ILKRTVDHnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGqplhnLNRR-QLLPVRHRIQVVf 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 83 --PDvSNLYDELTVR----ENL-LFMAKLYDAPRE-RVDELIREFELPADKKF---GRLSTGFKRRVTIASALVHEPEVL 151
Cdd:PRK15134 369 qdPN-SSLNPRLNVLqiieEGLrVHQPTLSAAQREqQVIAVMEEVGLDPETRHrypAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 152 FLDEPTNGLDVHSARAVRSLIRALNRRGMTVFI-TTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLfISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-210 |
3.48e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.27 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 22 GISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKT----ERLAVR-RSIGLVPDVSNLYDELTVRE 96
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKLRaKHVGFVFQSFMLIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 97 NLLFMAKLYDA----PRERVDELI-------REFELPAdkkfgRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSA 165
Cdd:PRK10584 108 NVELPALLRGEssrqSRNGAKALLeqlglgkRLDHLPA-----QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1828880368 166 RAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAiMRDGRIVAE 210
Cdd:PRK10584 183 DKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLR-LVNGQLQEE 227
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-185 |
4.61e-15 |
|
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: 75.36 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLT-----SITSGE----AYVNGFNvktERLAVRR 77
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEqpdsgTIEIGEtvklAYVDQSR---DALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 78 SIglVPDVSNLYDELTVrENLLFMAKLYdaprervdelIREFELP-AD--KKFGRLSTGFKRRVTIASALVHEPEVLFLD 154
Cdd:TIGR03719 402 TV--WEEISGGLDIIKL-GKREIPSRAY----------VGRFNFKgSDqqKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
170 180 190
....*....|....*....|....*....|.
gi 1828880368 155 EPTNGLDVHSARAVRSLIraLNRRGMTVFIT 185
Cdd:TIGR03719 469 EPTNDLDVETLRALEEAL--LNFAGCAVVIS 497
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-210 |
5.34e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.97 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTTVrmlttlTSI-------TSGEAYVNGFNVKTE--RLAVRRSIGLVPD---VSN 87
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELV------QCLfgaypgrWEGEIFIDGKPVKIRnpQQAIAQGIAMVPEdrkRDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 88 LYDELTVRENLLFMA-------KLYDAPRER--VDELIREFELPA---DKKFGRLSTGFKRRVTIASALVHEPEVLFLDE 155
Cdd:PRK13549 352 IVPVMGVGKNITLAAldrftggSRIDDAAELktILESIQRLKVKTaspELAIARLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1828880368 156 PTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAE 210
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-192 |
5.48e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.20 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVK---TERLAVRRSIGLVP 83
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAERGVVFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 dvsnlydELTVRENLLFMAKLYDAPRERVDELIREF----ELP-ADKKF-GRLSTGFKRRVTIASALVHEPEVLFLDEPT 157
Cdd:PRK11248 84 -------WRNVQDNVAFGLQLAGVEKMQRLEIAHQMlkkvGLEgAEKRYiWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1828880368 158 NGLDVHSARAVRS-LIRALNRRGMTVFITTHNMVEA 192
Cdd:PRK11248 157 GALDAFTREQMQTlLLKLWQETGKQVLLITHDIEEA 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-214 |
7.70e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.46 E-value: 7.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDF--EAVRGisfKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAyvngfnVKTERLAVRRSIgLVPDVs 86
Cdd:PRK13409 345 DLTKKLGDFslEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------DPELKISYKPQY-IKPDY- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 nlydELTVRENLLFMAKLYDAPRERVdELIREFELPA--DKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHS 164
Cdd:PRK13409 414 ----DGTVEDLLRSITDDLGSSYYKS-EIIKPLQLERllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1828880368 165 ----ARAVRSLIRalnRRGMTVFITTHNMVEAETIPQRIaimrdgrIVAEGKRG 214
Cdd:PRK13409 489 rlavAKAIRRIAE---EREATALVVDHDIYMIDYISDRL-------MVFEGEPG 532
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-187 |
1.39e-14 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 74.11 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTS--ITSGEAYVNGFNVKTERLAvrRSIGLVPDVSNLYDELTVREN 97
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKKQETFA--RISGYCEQNDIHSPQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 98 LLFMAKLyDAPRER--------VDELIREFELPA--DKKFGR-----LSTGFKRRVTIASALVHEPEVLFLDEPTNGLDV 162
Cdd:PLN03140 974 LIYSAFL-RLPKEVskeekmmfVDEVMELVELDNlkDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
170 180
....*....|....*....|....*
gi 1828880368 163 HSARAVRSLIRALNRRGMTVFITTH 187
Cdd:PLN03140 1053 RAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-199 |
3.15e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.26 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 18 EAVRG-ISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAvrRSIGLVPDVSNLYDELTVRE 96
Cdd:PRK13543 24 EPVFGpLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS--RFMAYLGHLPGLKADLSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 97 NLLFMAKLYDAPRERV--------------DELIREfelpadkkfgrLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDV 162
Cdd:PRK13543 102 NLHFLCGLHGRRAKQMpgsalaivglagyeDTLVRQ-----------LSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1828880368 163 HSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRI 199
Cdd:PRK13543 171 EGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRM 207
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-199 |
3.30e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.74 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTtvrmlttLTSITSG---EAYVNGFNVKTERLA------- 74
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKST-------LLSLITGdhpQGYSNDLTLFGRRRGsgetiwd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 75 VRRSIGLVPdvSNLYDE----LTVRENLL--FMAK--LYDAPRERVDELIREF-------ELPADKKFGRLSTGFKRRVT 139
Cdd:PRK10938 334 IKKHIGYVS--SSLHLDyrvsTSVRNVILsgFFDSigIYQAVSDRQQKLAQQWldilgidKRTADAPFHSLSWGQQRLAL 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880368 140 IASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMT--VFITTHnmveAETIPQRI 199
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFVSHH----AEDAPACI 469
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
8-252 |
4.39e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 71.31 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRYGD----FEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTS----ITSGEAYVNGFNVKTERLAVRRSI 79
Cdd:PRK11022 7 DKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 80 gLVPDVSNLYDE--------LTVRENLLFMAKLYD-----APRERVDELIREFELPA-----DKKFGRLSTGFKRRVTIA 141
Cdd:PRK11022 87 -VGAEVAMIFQDpmtslnpcYTVGFQIMEAIKVHQggnkkTRRQRAIDLLNQVGIPDpasrlDVYPHQLSGGMSQRVMIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 142 SALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGElaklv 220
Cdd:PRK11022 166 MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD----- 240
|
250 260 270
....*....|....*....|....*....|..
gi 1828880368 221 grktVVRLSVEPLSSSLLRALerynPSFEEGK 252
Cdd:PRK11022 241 ----IFRAPRHPYTQALLRAL----PEFAQDK 264
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-216 |
5.69e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.11 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTT----VRMLTTLTSITSGEAYVNGFNVKTERLAVRRSIGLVPDVSNLYDELT-- 93
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNPRSAFNPLHtm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 94 ---VRENLLFMAKLydAPRERVDELIREFELPADKKFGRL-----STGFKRRVTIASALVHEPEVLFLDEPTNGLD-VHS 164
Cdd:PRK10418 99 hthARETCLALGKP--ADDATLTAALEAVGLENAARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTDLDvVAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1828880368 165 ARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK10418 177 ARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-207 |
1.07e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.91 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 19 AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSG---------------EAYVNGFNVKTERlavRRSIGLVP 83
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGtitlhgkkinnhnanEAINHGFALVTEE---RRSTGIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 D--------VSNLyDELTVRENLLFMAKLYDAPRERVDELirEFELPADK-KFGRLSTGFKRRVTIASALVHEPEVLFLD 154
Cdd:PRK10982 340 YldigfnslISNI-RNYKNKVGLLDNSRMKSDTQWVIDSM--RVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 155 EPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRI 207
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-215 |
1.38e-13 |
|
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: 70.97 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDF--EAVRGisfKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYvngfnvKTERLAVRrsiglvPD-V 85
Cdd:COG1245 346 DLTKSYGGFslEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD------EDLKISYK------PQyI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 86 SNLYDElTVRENllfmakLYDAPRERVD------ELIREFELPA--DKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPT 157
Cdd:COG1245 411 SPDYDG-TVEEF------LRSANTDDFGssyyktEIIKPLGLEKllDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880368 158 NGLDV----HSARAVRSLIRAlnrRGMTVFITTHNMVEAETIPQRIaimrdgrIVAEGKRGE 215
Cdd:COG1245 484 AHLDVeqrlAVAKAIRRFAEN---RGKTAMVVDHDIYLIDYISDRL-------MVFEGEPGV 535
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-187 |
1.76e-13 |
|
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: 70.35 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRY-GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAyvngfnvkteRLAVRRSIGLVPDVS 86
Cdd:TIGR03719 8 NRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA----------RPQPGIKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 87 NLYDELTVRENL----------------LFMAklYDAPRERVDELIRE-------------FEL--------------PA 123
Cdd:TIGR03719 78 QLDPTKTVRENVeegvaeikdaldrfneISAK--YAEPDADFDKLAAEqaelqeiidaadaWDLdsqleiamdalrcpPW 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880368 124 DKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDvhsARAVRSLIRALNRRGMTVFITTH 187
Cdd:TIGR03719 156 DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPGTVVAVTH 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-187 |
2.17e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.29 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 22 GISFKVRRGEAFALLGPNGAGKTTtvrmlttLTSITSGEAYVNGF-------NVKTERLAVRRsIGLVPDVSNLYDELTV 94
Cdd:PLN03211 86 GVTGMASPGEILAVLGPSGSGKST-------LLNALAGRIQGNNFtgtilanNRKPTKQILKR-TGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 95 RENLLFMAkLYDAPRE--------RVDELIREFELPA------DKKFGR-LSTGFKRRVTIASALVHEPEVLFLDEPTNG 159
Cdd:PLN03211 158 RETLVFCS-LLRLPKSltkqekilVAESVISELGLTKcentiiGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180
....*....|....*....|....*...
gi 1828880368 160 LDVHSARAVRSLIRALNRRGMTVFITTH 187
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
7-216 |
4.98e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVK----RYGDF-----EAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNG------------ 65
Cdd:PRK15112 7 VRNLSKtfryRTGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 66 ------FNVKTERLAVRRSIGLVPDVS-NLYDELTVRENllfmaklydapRERVDELIREFELPADKKF---GRLSTGFK 135
Cdd:PRK15112 87 qrirmiFQDPSTSLNPRQRISQILDFPlRLNTDLEPEQR-----------EKQIIETLRQVGLLPDHASyypHMLAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 136 RRVTIASALVHEPEVLFLDEPTNGLDVhsarAVRSLIRAL-----NRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAE 210
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDM----SMRSQLINLmlelqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
....*.
gi 1828880368 211 GKRGEL 216
Cdd:PRK15112 232 GSTADV 237
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
15-243 |
8.33e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.83 E-value: 8.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 15 GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTS---ITSGEAYVNG---FNVKTERLAVRRS--IGLV---P 83
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGGSATFNGreiLNLPEKELNKLRAeqISMIfqdP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVS-NLYdeLTVRENLLFMAKLYD--APRERVDELIREFE---LPADKKFGRL-----STGFKRRVTIASALVHEPEVLF 152
Cdd:PRK09473 107 MTSlNPY--MRVGEQLMEVLMLHKgmSKAEAFEESVRMLDavkMPEARKRMKMyphefSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 153 LDEPTNGLDVHSARAVRSLIRALNRRGMTVFIT-THNMVEAETIPQRIAIMRDGRIVAEGKRGElaklvgrktVVRLSVE 231
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMiTHDLGVVAGICDKVLVMYAGRTMEYGNARD---------VFYQPSH 255
|
250
....*....|..
gi 1828880368 232 PLSSSLLRALER 243
Cdd:PRK09473 256 PYSIGLLNAVPR 267
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-216 |
1.98e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.42 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 18 EAVRGISFKVRRGEAFALLGPNGAGKTTT----VRMLTTLTSI-TSGEAYVNGFNV-----KTERLAVRRSIGLV---PD 84
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTalsiLRLLPSPPVVyPSGDIRFHGESLlhaseQTLRGVRGNKIAMIfqePM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VS---------NLYDELTVRENllfMAKlyDAPR-------ERVDelIREfelpADKKFG----RLSTGFKRRVTIASAL 144
Cdd:PRK15134 103 VSlnplhtlekQLYEVLSLHRG---MRR--EAARgeilnclDRVG--IRQ----AAKRLTdyphQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 145 VHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-215 |
2.49e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.12 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTTVRmlttltSI--------TSGEAYVNG--FNVKTERLAV----------RRSI 79
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAM------SVfgrsygrnISGTVFKDGkeVDVSTVSDAIdaglayvtedRKGY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 80 GLvpdvsNLYDelTVRENLLfMAKLYDAPRERVDELIREFELPAD-------------KKFGRLSTGFKRRVTIASALVH 146
Cdd:NF040905 350 GL-----NLID--DIKRNIT-LANLGKVSRRGVIDENEEIKVAEEyrkkmniktpsvfQKVGNLSGGNQQKVVLSKWLFT 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 147 EPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGE 215
Cdd:NF040905 422 DPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREE 490
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
10-215 |
2.52e-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: 65.51 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 10 LVKRYGDFE-AVRGISFkvRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAyvngfnvkterLAVRRSIGLVPDVSNL 88
Cdd:cd03237 6 MKKTLGEFTlEVEGGSI--SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-----------EIELDTVSYKPQYIKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 89 YDELTVREnLLF--MAKLYDAPRERVD-------ELIREFELPadkkfgRLSTGFKRRVTIASALVHEPEVLFLDEPTNG 159
Cdd:cd03237 73 DYEGTVRD-LLSsiTKDFYTHPYFKTEiakplqiEQILDREVP------ELSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880368 160 LDVHSARAVRSLIR--ALNRRGmTVFITTHNMVEAETIPQRIaimrdgrIVAEGKRGE 215
Cdd:cd03237 146 LDVEQRLMASKVIRrfAENNEK-TAFVVEHDIIMIDYLADRL-------IVFEGEPSV 195
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-167 |
2.54e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.07 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVnGFNVKterlavrrsIGLVpD 84
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK---------LAYV-D 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VS--NLYDELTVRENLlfmaklydapRERVDEL-IREFELP------------AD--KKFGRLSTGFKRRVTIASALVHE 147
Cdd:PRK11819 394 QSrdALDPNKTVWEEI----------SGGLDIIkVGNREIPsrayvgrfnfkgGDqqKKVGVLSGGERNRLHLAKTLKQG 463
|
170 180
....*....|....*....|
gi 1828880368 148 PEVLFLDEPTNGLDVHSARA 167
Cdd:PRK11819 464 GNVLLLDEPTNDLDVETLRA 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-208 |
2.58e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.74 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITS--GEAYVNG----FnvKTERLAVRRSI--- 79
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevcrF--KDIRDSEALGIvii 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 80 ----GLVPdvsnlydELTVRENLlFM----AKL----YDAPRERVDELIREFEL--PADKKFGRLSTGFKRRVTIASALV 145
Cdd:NF040905 84 hqelALIP-------YLSIAENI-FLgnerAKRgvidWNETNRRARELLAKVGLdeSPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 146 HEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIV 208
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-187 |
4.20e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.30 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 35 LLGPNGAGKTTTVRMLTTLTSITSGEAyvngfnvkteRLAVRRSIGLVPDVSNLYDELTVRENLL-----FMAKL----- 104
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEA----------RPAPGIKVGYLPQEPQLDPEKTVRENVEegvaeVKAALdrfne 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 105 ----YDAPRERVDELIREF-EL--------------------------PADKKFGRLSTGFKRRVTIASALVHEPEVLFL 153
Cdd:PRK11819 108 iyaaYAEPDADFDALAAEQgELqeiidaadawdldsqleiamdalrcpPWDAKVTKLSGGERRRVALCRLLLEKPDMLLL 187
|
170 180 190
....*....|....*....|....*....|....
gi 1828880368 154 DEPTNGLDvhsARAVRSLIRALNRRGMTVFITTH 187
Cdd:PRK11819 188 DEPTNHLD---AESVAWLEQFLHDYPGTVVAVTH 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-216 |
5.74e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.11 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 19 AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNV----KTERLAVRRSIGLV---PDVSnLYDE 91
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMIfqdPLAS-LNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 92 LTVRENLLFMAKLY--DAPRERVDELIREFELpadkKFGRL-----------STGFKRRVTIASALVHEPEVLFLDEPTN 158
Cdd:PRK15079 115 MTIGEIIAEPLRTYhpKLSRQEVKDRVKAMML----KVGLLpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 159 GLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEGKRGEL 216
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-190 |
1.13e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRYGD---FEavrGISFKVRRGEAFALLGPNGAGKTTTVRMLT-TLT------SITSGE----------AYVN 64
Cdd:PRK15064 2 LSTANITMQFGAkplFE---NISVKFGGGNRYGLIGANGCGKSTFMKILGgDLEpsagnvSLDPNErlgklrqdqfAFEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 65 gFNV-------KTERLAV---RRSIGLVPDVSNlYDELTVRENLLFMAKL--YDApRERVDELIREFELPADKKFGRLST 132
Cdd:PRK15064 79 -FTVldtvimgHTELWEVkqeRDRIYALPEMSE-EDGMKVADLEVKFAEMdgYTA-EARAGELLLGVGIPEEQHYGLMSE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 133 ---GFKRRVTIASALVHEPEVLFLDEPTNGLDVHSaraVRSLIRALNRRGMTVFITTH-----NMV 190
Cdd:PRK15064 156 vapGWKLRVLLAQALFSNPDILLLDEPTNNLDINT---IRWLEDVLNERNSTMIIISHdrhflNSV 218
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-187 |
1.63e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 62.20 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 37 GPNGAGKTTTVRMLTTLTSITSGEAYVNgfNVKTERLAvRRSIGLVPDVSNLYDELTVRENLLFMAKLYDAPrERVDELI 116
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYK--NCNINNIA-KPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSA-ETLYAAI 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828880368 117 REFELP--ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTH 187
Cdd:PRK13541 109 HYFKLHdlLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-184 |
2.13e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 25 FKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGfNVKTERLA--------------VRRSIGLVPDVSNLYD 90
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLIVARLQqdpprnvegtvydfVAEGIEEQAEYLKRYH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 91 ELTVR-------ENLLFMAKL-----------YDApreRVDELIREFELPADKKFGRLSTGFKRRVTIASALVHEPEVLF 152
Cdd:PRK11147 103 DISHLvetdpseKNLNELAKLqeqldhhnlwqLEN---RINEVLAQLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLL 179
|
170 180 190
....*....|....*....|....*....|..
gi 1828880368 153 LDEPTNGLDVHSARAVRSLIraLNRRGMTVFI 184
Cdd:PRK11147 180 LDEPTNHLDIETIEWLEGFL--KTFQGSIIFI 209
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-187 |
2.62e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 61.02 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGeayvngfnvKTERLAVRRSIgLVPDVSNLYDeLTVRENLL 99
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG---------RIGMPEGEDLL-FLPQRPYLPL-GTLREQLI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 100 FmaklydaPRERVdelirefelpadkkfgrLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRAlnrRG 179
Cdd:cd03223 86 Y-------PWDDV-----------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE---LG 138
|
....*...
gi 1828880368 180 MTVFITTH 187
Cdd:cd03223 139 ITVISVGH 146
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
9-229 |
3.05e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.84 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGD--FeAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRSI--GLVPD 84
Cdd:PRK10522 327 NVTFAYQDngF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLfsAVFTD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VsNLYDELTVRENLLFMAKLYDAPRERVdELIREFELpADKKFG--RLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDV 162
Cdd:PRK10522 406 F-HLFDQLLGPEGKPANPALVEKWLERL-KMAHKLEL-EDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1828880368 163 HSARAV-RSLIRALNRRGMTVFITTHN---MVEAEtipqRIAIMRDGRIvAEGKrGELAKLVGRKTVVRLS 229
Cdd:PRK10522 483 HFRREFyQVLLPLLQEMGKTIFAISHDdhyFIHAD----RLLEMRNGQL-SELT-GEERDAASRDAVARTA 547
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-208 |
4.65e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.99 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 4 AVVANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEayvngfnVKTERLAvrrSIGLVP 83
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-------VKWSENA---NIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 -DVS-------NLY-----------DELTVRE---NLLFMAklydaprervDElirefelpADKKFGRLSTGFKRRVTIA 141
Cdd:PRK15064 389 qDHAydfendlTLFdwmsqwrqegdDEQAVRGtlgRLLFSQ----------DD--------IKKSVKVLSGGEKGRMLFG 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 142 SALVHEPEVLFLDEPTNGLDVHSaraVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIV 208
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDMES---IESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-218 |
7.92e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 23 ISFKVRRGEAFALLGPNGAGKTTTVR-MLTTLTSITSGEAYVNGfnvkterlavrrSIGLVPDVSNLYDElTVRENLLFM 101
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG------------TVAYVPQVSWIFNA-TVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 102 AKlYDAPRE----RVDELIREFE-LPAD--KKFGR----LSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAV-- 168
Cdd:PLN03130 703 SP-FDPERYeraiDVTALQHDLDlLPGGdlTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfd 781
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1828880368 169 RSLIRALnrRGMTVFITTHNMveaETIPQ--RIAIMRDGRIVAEGKRGELAK 218
Cdd:PLN03130 782 KCIKDEL--RGKTRVLVTNQL---HFLSQvdRIILVHEGMIKEEGTYEELSN 828
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-218 |
8.72e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 8.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 23 ISFKVRRGEAFALLGPNGAGKTTTVR-MLTTLTsitsgeayvngfNVKTERLAVRRSIGLVPDVSNLYDElTVRENLLFM 101
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISaMLGELS------------HAETSSVVIRGSVAYVPQVSWIFNA-TVRENILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 102 AKlYDAPRE----RVDELIREFELPADKKFGRL-------STGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRS 170
Cdd:PLN03232 703 SD-FESERYwraiDVTALQHDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD 781
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1828880368 171 LIRALNRRGMTVFITTHNMveaETIPQ--RIAIMRDGRIVAEGKRGELAK 218
Cdd:PLN03232 782 SCMKDELKGKTRVLVTNQL---HFLPLmdRIILVSEGMIKEEGTFAELSK 828
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-212 |
9.19e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.81 E-value: 9.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 34 ALLGPNGAGKTTTVRMLTTLTSITSGEAYVN---------GFNVKTERlavrRSIGLVPDVSNLYDELTVRENLLF-MAK 103
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNgrvlfdaekGICLPPEK----RRIGYVFQDARLFPHYKVRGNLRYgMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 104 LYDAPRERVDEL--IRefelPADKKF-GRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVhsARAvRSLIRALNRRGM 180
Cdd:PRK11144 104 SMVAQFDKIVALlgIE----PLLDRYpGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL--PRK-RELLPYLERLAR 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1828880368 181 TVFI----TTHNMVEAETIPQRIAIMRDGRIVAEGK 212
Cdd:PRK11144 177 EINIpilyVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-189 |
9.76e-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: 62.11 E-value: 9.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFeavrgiSFK------VRRGEAFALLGPNGAGKTTTVRMLttltsitSGEAYVNGFNVKTE----------- 71
Cdd:COG1245 78 DPVHRYGEN------GFRlyglpvPKKGKVTGILGPNGIGKSTALKIL-------SGELKPNLGDYDEEpswdevlkrfr 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 72 ---------RLA---VRRS-----IGLVPDVSNLydelTVREnLLfmaKLYDApRERVDELIREFELPA--DKKFGRLST 132
Cdd:COG1245 145 gtelqdyfkKLAngeIKVAhkpqyVDLIPKVFKG----TVRE-LL---EKVDE-RGKLDELAEKLGLENilDRDISELSG 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 133 GFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNM 189
Cdd:COG1245 216 GELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-216 |
1.54e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA-VRRSIGLVPDVSNLYDElTVRENL 98
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTdLRRVLSIIPQSPVLFSG-TVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 99 LFMAKLYDA------PRERVDELIRE--FELPADKKFG--RLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAV 168
Cdd:PLN03232 1331 DPFSEHNDAdlwealERAHIKDVIDRnpFGLDAEVSEGgeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1828880368 169 RSLIRAlNRRGMTVFITTHNMveaETIP--QRIAIMRDGRIVAEGKRGEL 216
Cdd:PLN03232 1411 QRTIRE-EFKSCTMLVIAHRL---NTIIdcDKILVLSSGQVLEYDSPQEL 1456
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-221 |
1.81e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.27 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 19 AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAVRRS-IGLVPDVSNLYDElTVREN 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSrLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 98 LLFMAKlyDAPRERVDELIRE-------FELPA--DKKFGR----LSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHS 164
Cdd:PRK10789 409 IALGRP--DATQQEIEHVARLasvhddiLRLPQgyDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRT 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 165 ARAVRSLIRALnRRGMTVFITTHNMvEAETIPQRIAIMRDGRIVAEGKRGELAKLVG 221
Cdd:PRK10789 487 EHQILHNLRQW-GEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-261 |
2.65e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.33 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVngfnvkterlavRRSIGLVPDVSNLYDElTVRENLL 99
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA------------ERSIAYVPQQAWIMNA-TVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 100 FmaklYDAPRE-RVDELIREFELPAD-------------KKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVH-S 164
Cdd:PTZ00243 743 F----FDEEDAaRLADAVRVSQLEADlaqlgggleteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvG 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 165 ARAVRSLIR-ALnrRGMTVFITTHNmVEAETIPQRIAIMRDGRIVAEGKRGELAKlvgrktvvrlsvEPLSSSlLRALER 243
Cdd:PTZ00243 819 ERVVEECFLgAL--AGKTRVLATHQ-VHVVPRADYVVALGDGRVEFSGSSADFMR------------TSLYAT-LAAELK 882
|
250
....*....|....*...
gi 1828880368 244 YNPSFEEGKLVFEVDDVD 261
Cdd:PTZ00243 883 ENKDSKEGDADAEVAEVD 900
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-171 |
2.85e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 9 NLVKRYGDFeavrgiSFK------VRRGEAFALLGPNGAGKTTTVRMLT--------TLTSITSGEAYVNGF-------- 66
Cdd:PRK13409 78 EPVHRYGVN------GFKlyglpiPKEGKVTGILGPNGIGKTTAVKILSgelipnlgDYEEEPSWDEVLKRFrgtelqny 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 67 --NVKTERLAVRRSIGLVPDVSNLYDElTVRENLlfmaKLYDApRERVDELIREFELPA--DKKFGRLSTGFKRRVTIAS 142
Cdd:PRK13409 152 fkKLYNGEIKVVHKPQYVDLIPKVFKG-KVRELL----KKVDE-RGKLDEVVERLGLENilDRDISELSGGELQRVAIAA 225
|
170 180 190
....*....|....*....|....*....|...
gi 1828880368 143 ALVHEPEVLFLDEPTNGLDVH----SARAVRSL 171
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLDIRqrlnVARLIREL 258
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-211 |
2.94e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTtvrMLTTLTSITSGEAYVNGFNVKTE--------------RLAVRRSIglVPDV 85
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKST---LLKALAGDLTGGGAPRGARVTGDvtlngeplaaidapRLARLRAV--LPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 86 SNLYDELTVRENLLF----MAKLYDAPRERVDELI-REFELP-ADKKFGR----LSTGFKRRVTIASALVH--------- 146
Cdd:PRK13547 92 AQPAFAFSAREIVLLgrypHARRAGALTHRDGEIAwQALALAgATALVGRdvttLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 147 EPEVLFLDEPTNGLDVHSARAVRSLIRALNRR-GMTVFITTHNMVEAETIPQRIAIMRDGRIVAEG 211
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
16-211 |
6.94e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.26 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 16 DFEAVRGISFKVRRGEAFALLGPNGAGKTTtvrMLTTLT-----SITSGEAYVNGFNVKTERLAVRRSIGL--------- 81
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKST---LSATLAgredyEVTGGTVEFKGKDLLELSPEDRAGEGIfmafqypve 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 VPDVSNLYDELT----VREnllfmaklY--DAPRERVD------ELIREFELPADKKFGRLSTGF----KRRVTIASALV 145
Cdd:PRK09580 90 IPGVSNQFFLQTalnaVRS--------YrgQEPLDRFDfqdlmeEKIALLKMPEDLLTRSVNVGFsggeKKRNDILQMAV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 146 HEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETI-PQRIAIMRDGRIVAEG 211
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIkPDYVHVLYQGRIVKSG 228
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-222 |
1.04e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.96 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLV--------KRYGDFE--------AVRGISFKVRRGE-------------AF-ALLGPNGAGKTTTVRML 50
Cdd:PRK10790 308 LQQAVVAGERVfelmdgprQQYGNDDrplqsgriDIDNVSFAYRDDNlvlqninlsvpsrGFvALVGHTGSGKSTLASLL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 51 TTLTSITSGEAYVNGFNVKTERLAV-RRSIGLV---PDV--SNLYDELTVRENLLfMAKLYDApRERVD--ELIREFELP 122
Cdd:PRK10790 388 MGYYPLTEGEIRLDGRPLSSLSHSVlRQGVAMVqqdPVVlaDTFLANVTLGRDIS-EEQVWQA-LETVQlaELARSLPDG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 123 ADKKFG----RLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALnRRGMTVFITTHNM---VEAETi 195
Cdd:PRK10790 466 LYTPLGeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV-REHTTLVVIAHRLstiVEADT- 543
|
250 260
....*....|....*....|....*..
gi 1828880368 196 pqrIAIMRDGRIVAEGKRGELAKLVGR 222
Cdd:PRK10790 544 ---ILVLHRGQAVEQGTHQQLLAAQGR 567
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-216 |
4.34e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.65 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 15 GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLttLTSITSGEAYVngfnvkterlAVRRSIGLVPDVSNLYDElTV 94
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDKVEGHV----------HMKGSVAYVPQQAWIQND-SL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 95 RENLLFMAKLYDAPRERVDE---LIREFE-LPAD------KKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHS 164
Cdd:TIGR00957 716 RENILFGKALNEKYYQQVLEacaLLPDLEiLPSGdrteigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828880368 165 ARAVrsLIRALNRRGM----TVFITTHNMveaETIPQR--IAIMRDGRIVAEGKRGEL 216
Cdd:TIGR00957 796 GKHI--FEHVIGPEGVlknkTRILVTHGI---SYLPQVdvIIVMSGGKISEMGSYQEL 848
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
84-208 |
8.14e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 DVSNLYdELTVRENLLFMAKLY--------DAPRERV---------DELIREFELPADKKFG----RLSTGFKRRVTIAS 142
Cdd:PTZ00265 1293 DLRNLF-SIVSQEPMLFNMSIYenikfgkeDATREDVkrackfaaiDEFIESLPNKYDTNVGpygkSLSGGQKQRIAIAR 1371
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 143 ALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFItthnmveaeTIPQRIA-IMRDGRIV 208
Cdd:PTZ00265 1372 ALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII---------TIAHRIAsIKRSDKIV 1429
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-253 |
8.88e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 55.25 E-value: 8.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 5 VVANNLVKRY--GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSiTSGEAYVNGFNVKTERLAV-RRSIGL 81
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKwRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 82 VPDVSNLYDElTVRENLLFMAKLYDAPRERVDE------LIREFelPADKKFGR------LSTGFKRRVTIASALVHEPE 149
Cdd:cd03289 82 IPQKVFIFSG-TFRKNLDPYGKWSDEEIWKVAEevglksVIEQF--PGQLDFVLvdggcvLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 150 VLFLDEPTNGLDVHSARAVRSLIRAlNRRGMTVFITTHNmVEAETIPQRIAIMRDGRIvaeGKRGELAKLVGRKTVVRLS 229
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHR-IEAMLECQRFLVIEENKV---RQYDSIQKLLNEKSHFKQA 233
|
250 260
....*....|....*....|....
gi 1828880368 230 VEPlsSSLLRALERYNPSFEEGKL 253
Cdd:cd03289 234 ISP--SDRLKLFPRRNSSKSKRKP 255
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-189 |
2.34e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.91 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 11 VKRYGDFeavrgiSFK------VRRGEAFALLGPNGAGKTTTVRML-----------------TTLTSITSGEAYVNGF- 66
Cdd:cd03236 7 VHRYGPN------SFKlhrlpvPREGQVLGLVGPNGIGKSTALKILagklkpnlgkfddppdwDEILDEFRGSELQNYFt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 67 NVKTERLAVRRSIGLVPDVSNLYDElTVRENLlfmaKLYDApRERVDELIREFELPA--DKKFGRLSTGFKRRVTIASAL 144
Cdd:cd03236 81 KLLEGDVKVIVKPQYVDLIPKAVKG-KVGELL----KKKDE-RGKLDELVDQLELRHvlDRNIDQLSGGELQRVAIAAAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1828880368 145 VHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNM 189
Cdd:cd03236 155 ARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-184 |
3.91e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 16 DFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVN-GFNVKTERLAVRRS-IGLVP---------- 83
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSkIGVVSqdpllfsnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 84 -----------------------DVSNLYDELTVREN--------------------LLFMAKLYDAPRER--------- 111
Cdd:PTZ00265 477 knnikyslyslkdlealsnyyneDGNDSQENKNKRNScrakcagdlndmsnttdsneLIEMRKNYQTIKDSevvdvskkv 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 112 -----VDELIREFELPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRAL--NRRGMTVFI 184
Cdd:PTZ00265 557 lihdfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIII 636
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-247 |
4.07e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 8 NNLVKRY--GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSiTSGEAYVNGFNVKTERLAV-RRSIGLVPD 84
Cdd:TIGR01271 1221 QGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTwRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 85 VSNLYDElTVRENLLFMAKLYDAPRERVDE------LIREFelPADKKFGR------LSTGFKRRVTIASALVHEPEVLF 152
Cdd:TIGR01271 1300 KVFIFSG-TFRKNLDPYEQWSDEEIWKVAEevglksVIEQF--PDKLDFVLvdggyvLSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 153 LDEPTNGLDVHSARAVRSLIRAlNRRGMTVFITTHNmVEAETIPQRIAIMRDGRIvaeGKRGELAKLVGRKTVVRLSVEP 232
Cdd:TIGR01271 1377 LDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHR-VEALLECQQFLVIEGSSV---KQYDSIQKLLNETSLFKQAMSA 1451
|
250
....*....|....*
gi 1828880368 233 LSSSLLRALERYNPS 247
Cdd:TIGR01271 1452 ADRLKLFPLHRRNSS 1466
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-213 |
2.27e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 27 VRRGEAFALLGPNGAGKTTtvrMLTTLTSIT-------SGEAYVNGFNVKTERLAVRRSIGLVPDVSNLYDELTVRENLL 99
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCST---LLKTIASNTdgfhigvEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 100 FMAKLyDAPRERVDELIRE-------------FELP--ADKKFGR-----LSTGFKRRVTIASALVHEPEVLFLDEPTNG 159
Cdd:TIGR00956 161 FAARC-KTPQNRPDGVSREeyakhiadvymatYGLShtRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRG 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828880368 160 LDVHSA----RAVRSLIRALNrrgMTVFITTHNMVE-AETIPQRIAIMRDGRIVAEGKR 213
Cdd:TIGR00956 240 LDSATAlefiRALKTSANILD---TTPLVAIYQCSQdAYELFDKVIVLYEGYQIYFGPA 295
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-175 |
2.33e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 21 RGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAyvngFNVKTERLAVRRSiglvpdvsNLYDELTVREN-LL 99
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV----FRSAKVRMAVFSQ--------HHVDGLDLSSNpLL 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 100 FMAKLY-DAPRERVDELIREFELP---ADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHsarAVRSLIRAL 175
Cdd:PLN03073 594 YMMRCFpGVPEQKLRAHLGSFGVTgnlALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD---AVEALIQGL 670
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-208 |
2.79e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 22 GISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA-VRRSIGLVPDVSNLYDElTVRENLLF 100
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdLRKVLGIIPQAPVLFSG-TVRFNLDP 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 101 MAKLYDA------PRERVDELIREFELPADKKFGR----LSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRS 170
Cdd:PLN03130 1336 FNEHNDAdlweslERAHLKDVIRRNSLGLDAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQK 1415
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1828880368 171 LIRAlNRRGMTVFITTHNMveaETI--PQRIAIMRDGRIV 208
Cdd:PLN03130 1416 TIRE-EFKSCTMLIIAHRL---NTIidCDRILVLDAGRVV 1451
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
10-214 |
3.09e-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: 49.49 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 10 LVKRYGDFEA-VRGISFKvrRGEAFALLGPNGAGKTTTVRMLttltsitSGEAYVNGFNVKTERLAVrrsiglvpdvsnl 88
Cdd:cd03222 6 CVKRYGVFFLlVELGVVK--EGEVIGIVGPNGTGKTTAVKIL-------AGQLIPNGDNDEWDGITP------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 89 ydeltvrenllfmaklydaprervdelirefelPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDV----HS 164
Cdd:cd03222 64 ---------------------------------VYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNA 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1828880368 165 ARAVRSLIRALNRrgmTVFITTHNMVEAETIPQRIaimrdgrIVAEGKRG 214
Cdd:cd03222 111 ARAIRRLSEEGKK---TALVVEHDLAVLDYLSDRI-------HVFEGEPG 150
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
127-190 |
5.94e-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: 50.08 E-value: 5.94e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828880368 127 FGRLSTGFKRRVTIASAL---VHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMV 190
Cdd:pfam13304 234 AFELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-207 |
6.09e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.81 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 1 MAEAVVANNLVKRY--------------------GDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGE 60
Cdd:PRK13546 1 MNVSVNIKNVTKEYriyrtnkermkdalipkhknKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 61 AYVNGfnvkterlavrrSIGLVPDVSNLYDELTVRENLLFMAKLYDAPRERVDEL---IREFELPAD------KKFgrlS 131
Cdd:PRK13546 81 VDRNG------------EVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMtpkIIEFSELGEfiyqpvKKY---S 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 132 TGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRI 207
Cdd:PRK13546 146 SGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-189 |
3.93e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 19 AVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGfnvkterlavrrSIGLVPDVSNLYDELTVRENL 98
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------------SAALIAISSGLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 99 LFMAKLYDAPRERVDELIREFELPAD-KKF-----GRLSTGFKRRVTIASALVHEPEVLFLDEptnGLDVHSARAVRSLI 172
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADiGKFiyqpvKTYSSGMKSRLGFAISVHINPDILVIDE---ALSVGDQTFTKKCL 183
|
170 180
....*....|....*....|
gi 1828880368 173 RALN---RRGMTVFITTHNM 189
Cdd:PRK13545 184 DKMNefkEQGKTIFFISHSL 203
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
130-218 |
4.32e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.59 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 130 LSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRALNR-RGMTVFITTHNMveaETIPQ---RIAIMRDG 205
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDL---ESISQwadTITVLYCG 235
|
90
....*....|...
gi 1828880368 206 RIVAEGKRGELAK 218
Cdd:COG4170 236 QTVESGPTEQILK 248
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-173 |
4.46e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.40 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLA-VRRSIGLVPDVSNLYDElTVRENL 98
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHdLRFKITIIPQDPVLFSG-SLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 99 LFMAKLYDAPRERVDEL--IREF--ELPADKKFG------RLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAV 168
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELahLKTFvsALPDKLDHEcaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
....*
gi 1828880368 169 RSLIR 173
Cdd:TIGR00957 1461 QSTIR 1465
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-187 |
6.04e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 7 ANNLVKRYGDFEAVRGISFKVRRGEAFALLGPNGAGKTTTVR-MLTTLTSiTSGE---------AYvngFNVKTERLAVR 76
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQA-DSGRihcgtklevAY---FDQHRAELDPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 77 RSIglvpdVSNLYD---ELTVR----------ENLLFMAKlydapRERVdelirefelPADKkfgrLSTGFKRRVTIASA 143
Cdd:PRK11147 398 KTV-----MDNLAEgkqEVMVNgrprhvlgylQDFLFHPK-----RAMT---------PVKA----LSGGERNRLLLARL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1828880368 144 LVHEPEVLFLDEPTNGLDVHSARAVRSLIRalNRRGmTVFITTH 187
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETLELLEELLD--SYQG-TVLLVSH 495
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-205 |
6.23e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 46.17 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 16 DFEAVRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERLAV-----RRSIGLVPDVSNLYD 90
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 91 ElTVRENLLFMAKLydaPRERVDELIREFELPADKK---FG----------RLSTGFKRRVTIASALVHEPEVLFLDEPT 157
Cdd:cd03290 93 A-TVEENITFGSPF---NKQRYKAVTDACSLQPDIDllpFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1828880368 158 NGLDVHSARAV--RSLIRALNRRGMTVFITTHNMveaETIPQR--IAIMRDG 205
Cdd:cd03290 169 SALDIHLSDHLmqEGILKFLQDDKRTLVLVTHKL---QYLPHAdwIIAMKDG 217
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
34-187 |
7.29e-06 |
|
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: 46.92 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 34 ALLGPNGAGKTTTVRMLTTLTSITSGEAYVNG-FNVKTERLAVRRSIGLV--PDVSNLYDELTVRENLLFMAKLYDAPRE 110
Cdd:COG3593 27 VLVGENNSGKSSILEALRLLLGPSSSRKFDEEdFYLGDDPDLPEIEIELTfgSLLSRLLRLLLKEEDKEELEEALEELNE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 111 RVDELIRE-------------------FELPADKK------------------FGRLSTGFKRRVTIASALV-------H 146
Cdd:COG3593 107 ELKEALKAlnellseylkelldgldleLELSLDELedllkslslriedgkelpLDRLGSGFQRLILLALLSAlaelkraP 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1828880368 147 EPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTH 187
Cdd:COG3593 187 ANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
118-187 |
1.35e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 118 EFELPADKKFgrlSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHsarAVRSLIRALNRRGMTVFITTH 187
Cdd:PLN03073 336 EMQVKATKTF---SGGWRMRIALARALFIEPDLLLLDEPTNHLDLH---AVLWLETYLLKWPKTFIVVSH 399
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-244 |
1.60e-05 |
|
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: 45.62 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGfnvkterlavrrSIGLVPDVSNLYDElTVRENLL 99
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------RISFSSQFSWIMPG-TIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 100 FMAKlYDAPRERvdELIREFELPAD-KKFGR------------LSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSAR 166
Cdd:cd03291 120 FGVS-YDEYRYK--SVVKACQLEEDiTKFPEkdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 167 AV-RSLIRALNRRGMTVFITthNMVEAETIPQRIAIMRDGRIVAEGKRGEL--------AKLVGRKTVVRLSVEPLSSSL 237
Cdd:cd03291 197 EIfESCVCKLMANKTRILVT--SKMEHLKKADKILILHEGSSYFYGTFSELqslrpdfsSKLMGYDTFDQFSAERRNSIL 274
|
....*..
gi 1828880368 238 LRALERY 244
Cdd:cd03291 275 TETLRRF 281
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
121-189 |
1.68e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.68e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828880368 121 LPADKKFGRLSTGFKRRVTIASAL---VHEPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHNM 189
Cdd:PRK00635 801 LPLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM 872
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-208 |
2.98e-05 |
|
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: 43.52 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 29 RGEAFALLGPNGAGKTTTVRMLttltsitSGEAYVNGFNVKterlavrrsiglvpdvsnlydeltvrenllfmakLYDAP 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL-------ARELGPPGGGVI----------------------------------YIDGE 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 109 RERVDELIREFELPADKKFGRLSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSARAVRSLIRA------LNRRGMTV 182
Cdd:smart00382 40 DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrlllllKSEKNLTV 119
|
170 180
....*....|....*....|....*.
gi 1828880368 183 FITTHNmvEAETIPQRIAIMRDGRIV 208
Cdd:smart00382 120 ILTTND--EKDLGPALLRRRFDRRIV 143
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
130-248 |
3.32e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.79 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 130 LSTGFKRRVTIASALVHEPEVLFLDEPTNGLD-VHSARAVRSLIRALNRRGMTVFITTHNMVEAETIPQRIAIMRDGRIV 208
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEpTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1828880368 209 AEGKRGELaklvgrktvVRLSVEPLSSSLLRALerynPSF 248
Cdd:PRK15093 239 ETAPSKEL---------VTTPHHPYTQALIRAI----PDF 265
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-249 |
4.75e-05 |
|
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: 44.90 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGfnvkterlavrrSIGLVPDVSNLYDElTVRENLL 99
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQTSWIMPG-TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 100 FMAKlYDAPRERvdELIREFELPAD-KKFGR------------LSTGFKRRVTIASALVHEPEVLFLDEPTNGLDVHSAR 166
Cdd:TIGR01271 509 FGLS-YDEYRYT--SVIKACQLEEDiALFPEkdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 167 AV--RSLIRALNRRgmTVFITTHNMvEAETIPQRIAIMRDGRIVAEGKRGEL--------AKLVGRKTVVRLSVEPLSSS 236
Cdd:TIGR01271 586 EIfeSCLCKLMSNK--TRILVTSKL-EHLKKADKILLLHEGVCYFYGTFSELqakrpdfsSLLLGLEAFDNFSAERRNSI 662
|
250
....*....|...
gi 1828880368 237 LLRALERYNPSFE 249
Cdd:TIGR01271 663 LTETLRRVSIDGD 675
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
129-247 |
8.23e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.77 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 129 RLSTGFKRRVTIASALVH--EPEVLFLDEPTNGLDVHSARAVRSLIRALNRRGmTVFITTHN--MVEAETIPQRIAIMRD 204
Cdd:COG4637 258 ELSDGTLRFLALLAALLSprPPPLLCIEEPENGLHPDLLPALAELLREASERT-QVIVTTHSpaLLDALEPEEVLVLERE 336
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1828880368 205 GRivaegkrgelaklvGRKTVVRLSVEPLSssllRALERYNPS 247
Cdd:COG4637 337 DD--------------GETRIRRLSDLELP----EWLEGYSLG 361
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
117-188 |
1.50e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 42.72 E-value: 1.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 117 REFELPadkkFGRLSTGFKRRVTIASALV---HEPEVLFLDEPTNGLDVHSARA-VRSLIRALNRRGMTVFITTHN 188
Cdd:COG1106 194 GNVPLP----LSEESDGTKRLLALAGALLdalAKGGVLLIDEIEASLHPSLLRKlLKLFLDLANKNNAQLIFTTHS 265
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
129-188 |
2.10e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.19 E-value: 2.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828880368 129 RLSTGFKRRVTIASALVHE---PEVLF-LDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHN 188
Cdd:cd03227 77 QLSGGEKELSALALILALAslkPRPLYiLDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
121-188 |
2.42e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.15 E-value: 2.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 121 LPADKKFGRLSTGFKRRVTIASALVHEPE-VLF-LDEPTNGLDVHSARAVRSLIRALNRRGMTVFITTHN 188
Cdd:cd03238 79 LTLGQKLSTLSGGELQRVKLASELFSEPPgTLFiLDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-98 |
4.76e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.61 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828880368 20 VRGISFKVRRGEAFALLGPNGAGKTTTVRMLTTLTSITSGEAYVNGFNVKTERL-AVRRSIGLVPDVSNLYDElTVRENL 98
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLrELRRQFSMIPQDPVLFDG-TVRQNV 1404
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
130-189 |
8.33e-03 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 37.21 E-value: 8.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828880368 130 LSTGFKRRVTIASALVHE---PEVLFLDEPTNGLDVHSaraVRSLIRALNR---RGMTVFITTHNM 189
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHD---VKKLLEVLQRlvdKGNTVVVIEHNL 232
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