|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-236 |
1.06e-103 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 303.14 E-value: 1.06e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVVPQ 87
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 DLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 168 GIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLItkygENYLE 236
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK----ARLLE 224
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
15-310 |
2.31e-93 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 279.27 E-value: 2.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 15 KSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVVPQDLALYPT 94
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 95 LTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSR 174
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 175 NHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKYGENYLEIV----------ISNIPE 244
Cdd:TIGR01188 161 RAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRprdiqslkveVSMLIA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 245 EFIHKTKMIVDVkscTLVDKKVIIQCVDSFNVTREVMKLIQKYNLKIELFNVKNSNLENVFLHLTG 310
Cdd:TIGR01188 240 ELGETGLGLLAV---TVDSDRIKILVPDGDETVPEIVEAAIRNGIRIRSISTERPSLDDVFLKLTG 302
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-226 |
2.75e-90 |
|
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: 268.47 E-value: 2.75e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVVPQ 87
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 DLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 168 GIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-226 |
1.55e-77 |
|
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: 235.86 E-value: 1.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGD--YTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVV 85
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 86 PQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEP 165
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446051965 166 TVGIDPQSRNHIFNCIRHLVEELgiTVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-245 |
6.16e-73 |
|
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: 225.12 E-value: 6.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVVP 86
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 87 QDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPT 166
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 167 VGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKYGENYLE-IVISNIPEE 245
Cdd:COG4555 161 NGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEdAFVALIGSE 239
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-217 |
3.02e-71 |
|
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: 218.04 E-value: 3.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVVPQ 87
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 DLALYPTLTAYDNLSfyadlyglkgnrkksrikealqfaqledwahkridtFSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:cd03230 81 EPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446051965 168 GIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-219 |
1.34e-61 |
|
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: 195.28 E-value: 1.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGD----YTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNV 82
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFL 162
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446051965 163 DEPTVGIDPQSRNHIFNCIRHLvEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILD 219
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-314 |
7.20e-61 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 196.18 E-value: 7.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVVPQ 87
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 DLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 168 GIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLI-TKYGENYLEIVISNIPE-- 244
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIeSEIGCDVIEIYGPDPVAlr 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446051965 245 ----EFIHKTKMIVDVKSCTLVDKKVIiqcvdsfnvtreVMKLIQKYNLKielFNVKNSNLENVFLHLTGKNLR 314
Cdd:PRK13537 247 delaPLAERTEISGETLFCYVRDPEPL------------HARLKGRAGLR---YLHRPANLEDVFLRLTGREMQ 305
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-218 |
1.25e-58 |
|
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: 187.40 E-value: 1.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGeIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVVPQ 87
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 DLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446051965 168 GIDPQSRNHifncIRHLVEELG--ITVIYTTHHMEEAEMLCHRVAIYDKGEIL 218
Cdd:cd03264 160 GLDPEERIR----FRNLLSELGedRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-221 |
3.23e-55 |
|
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: 178.48 E-value: 3.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyTERNKIKKNVSVVPQ 87
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 DLALYPTLTAYDNLSFyadlyGLKGNRKKS-----RIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFL 162
Cdd:cd03259 80 DYALFPHLTVAENIAF-----GLKLRGVPKaeiraRVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 163 DEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDID 221
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-226 |
5.58e-55 |
|
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: 178.58 E-value: 5.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnyDLYTERNKI------KKN 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSG-------EILLDGKDItnlpphKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIF 161
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 162 LDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-312 |
1.26e-54 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 179.92 E-value: 1.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL-YTERNKIkknvSVV 85
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLdPEDRRRI----GYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 86 PQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEP 165
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 166 TVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKYGENYLEIVISNIPEE 245
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADGDAGW 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446051965 246 FihktKMIVDVKSCTLVDKKVIIQCVDSfNVTREVMKLIQKyNLKIELFNVKNSNLENVFLHLTGKN 312
Cdd:COG4152 236 L----RALPGVTVVEEDGDGAELKLEDG-ADAQELLRALLA-RGPVREFEEVRPSLNEIFIEVVGEK 296
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-217 |
2.48e-54 |
|
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: 176.32 E-value: 2.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTE-RNKIkknvSVVP 86
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAaRNRI----GYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 87 QDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPT 166
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446051965 167 VGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-313 |
1.30e-53 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 178.49 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSV 84
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 85 VPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDE 164
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 165 PTVGIDPQSRNHIFNCIRHLVeELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKY-GENYLEIVISNIP 243
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHiGCQVIEIYGGDPH 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446051965 244 E--EFIHKTKMIVDVKSCTLVdkkVIIQCVDSFNVtrevmKLIQKYNLKIELfnvKNSNLENVFLHLTGKNL 313
Cdd:PRK13536 278 ElsSLVKPYARRIEVSGETLF---CYAPDPEQVRV-----QLRGRAGLRLLQ---RPPNLEDVFLRLTGREM 338
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-226 |
1.14e-52 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 176.44 E-value: 1.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnydlyternKI------- 78
Cdd:COG3842 4 PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSG--------------RIlldgrdv 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 ------KKNVSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIG 152
Cdd:COG3842 70 tglppeKRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446051965 153 LLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-226 |
4.07e-51 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 172.18 E-value: 4.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGY----GTVCNyDLYTErnkiKKN 81
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEiligGRDVT-DLPPK----DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVVPQDLALYPTLTAYDNLSFyadlyGLKgNRKKS------RIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLN 155
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAF-----PLK-LRKVPkaeidrRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446051965 156 KPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-226 |
6.90e-51 |
|
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: 168.23 E-value: 6.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT----ERNKIKK 80
Cdd:COG1127 3 EPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 81 NVSVVPQDLALYPTLTAYDNLSFYadLY---GLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKP 157
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFP--LRehtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 158 KVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-198 |
2.49e-49 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 163.03 E-value: 2.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVVP 86
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 87 QDLALYPTLTAYDNLSFYADLYGLKGNRkkSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPT 166
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|..
gi 446051965 167 VGIDPQSRNHIFNCIRHLVEELGItVIYTTHH 198
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGA-VLLTTHQ 190
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-238 |
6.63e-49 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 163.72 E-value: 6.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 1 MTDINTMISIRYIKKSY----GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNydlyTERN 76
Cdd:COG1116 1 MSAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 77 KIKKNVSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNK 156
Cdd:COG1116 77 GPGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 157 PKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKG-----EILDIDTPK--NLITK 229
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARpgrivEEIDVDLPRprDRELR 236
|
....*....
gi 446051965 230 YGENYLEIV 238
Cdd:COG1116 237 TSPEFAALR 245
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-218 |
1.43e-48 |
|
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: 162.12 E-value: 1.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 14 KKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVV-PQDLALY 92
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 93 PTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQ 172
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446051965 173 SRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEIL 218
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-230 |
8.47e-48 |
|
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: 159.81 E-value: 8.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 16 SY-GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTE-RNKIKKNVSVVPQDlalyP 93
Cdd:COG1122 9 SYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnLRELRRKVGLVFQN----P 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 94 -----TLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVG 168
Cdd:COG1122 85 ddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446051965 169 IDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKY 230
Cdd:COG1122 165 LDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-219 |
1.09e-47 |
|
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: 158.92 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVcNYDLYTERNKIKKNVSVVPQ 87
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF-DGKSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 DLALYPTLTAYDNLSFYADLYGLkgnrKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446051965 168 GIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILD 219
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-228 |
3.55e-47 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 158.43 E-value: 3.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLY----TERNKIKKNVS 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQDLALYPTLTAYDNLSFYadlygLKGNRKKS------RIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKP 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFP-----LREHTRLSeeeireIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446051965 158 KVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-209 |
1.20e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 156.74 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGD----YTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT----ERN 76
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 77 KI-KKNVSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLN 155
Cdd:COG1136 82 RLrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446051965 156 KPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMlCHRV 209
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRV 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-217 |
1.51e-46 |
|
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: 156.50 E-value: 1.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGD----YTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIK---- 79
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 80 -KNVSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPK 158
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMlCHRVAIYDKGEI 217
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-216 |
7.42e-46 |
|
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: 154.55 E-value: 7.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 16 SYGDYT--VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL-YTERNKIKKNVSVVPQDlaly 92
Cdd:cd03225 8 SYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtKLSLKELRRKVGLVFQN---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 93 P-----TLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:cd03225 84 PddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446051965 168 GIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGE 216
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-221 |
1.15e-45 |
|
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: 154.17 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGD----YTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNydlyTERNKIKKNVS 83
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLD 163
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446051965 164 EPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDK-----GEILDID 221
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpgriVAEVEVD 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-167 |
1.22e-45 |
|
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: 151.65 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL-YTERNKIKKNVSVVPQDLALYPTLTAYDNL 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 102 SFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRID----TFSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-224 |
1.48e-45 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 158.57 E-value: 1.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 1 MTDINTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyTERNKIKK 80
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 81 NVSVVPQDLALYPTLTAYDNLSFyadlyGLKGNRK-----KSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLN 155
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENVAF-----GLRMQKTpaaeiTPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 156 KPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPK 224
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPR 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-304 |
3.72e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 156.02 E-value: 3.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 19 DYTVI---KNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVV-PQDLALYPT 94
Cdd:COG4586 31 EYREVeavDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVfGQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 95 LTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSR 174
Cdd:COG4586 111 LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 175 NHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEIL-DIDTpKNLITKYGeNYLEIVI---SNIPEEFIHKT 250
Cdd:COG4586 191 EAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIyDGSL-EELKERFG-PYKTIVLelaEPVPPLELPRG 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446051965 251 KMIVDVKsctlvDKKVIIQCVDSFNVTREVMKLIQKYNlkIELFNVKNSNLENV 304
Cdd:COG4586 269 GEVIERE-----GNRVRLEVDPRESLAEVLARLLARYP--VRDLTIEEPPIEEV 315
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-228 |
4.80e-45 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 153.66 E-value: 4.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK-IKKNVSVV 85
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRReLARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 86 PQDLALYPTLTAYDNLSF----YADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIF 161
Cdd:COG1120 81 PQEPPAPFGLTVRELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446051965 162 LDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-217 |
4.90e-45 |
|
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: 152.66 E-value: 4.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSY----GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIK--- 79
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 80 -KNVSVVPQD--LALYPTLTAYDnlSFYADLYGLKGNRKKSRIKEAL-----QFAQLEDWAHKRIDTFSGGMKRRINLVI 151
Cdd:cd03257 81 rKEIQMVFQDpmSSLNPRMTIGE--QIAEPLRIHGKLSKKEARKEAVllllvGVGLPEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 152 GLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
1.07e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.55 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 1 MTDiNTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLI-SILSTLTlPDEGYGTVCNYDLYTERNKIk 79
Cdd:COG1121 1 MMM-MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLkAILGLLP-PTSGTVRLFGKPPRRARRRI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 80 knvSVVPQDLALYPT--LTAYD--NLSFYADLYGLKGNRKKSR--IKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGL 153
Cdd:COG1121 78 ---GYVPQRAEVDWDfpITVRDvvLMGRYGRRGLFRRPSRADReaVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 154 LNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDK-----GEILDIDTPKNLIT 228
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRglvahGPPEEVLTPENLSR 233
|
...
gi 446051965 229 KYG 231
Cdd:COG1121 234 AYG 236
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-226 |
2.20e-44 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 154.53 E-value: 2.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGY----GTVCNYDLYT-ERnkikkNV 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRivlnGRDLFTNLPPrER-----RV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVVPQDLALYPTLTAYDNLSFyadlyGLKGN-----RKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKP 157
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAF-----GLRVRppskaEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 158 KVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-228 |
5.59e-44 |
|
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: 156.99 E-value: 5.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT----ERNKIKKNVS 83
Cdd:COG1123 266 LSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLRELRRRVQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQD--LALYPTLTAYDNLSFYADLYG-LKGNRKKSRIKEALQFAQL-EDWAHKRIDTFSGGMKRRINLVIGLLNKPKV 159
Cdd:COG1123 346 MVFQDpySSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKL 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 160 IFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:COG1123 426 LILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-216 |
7.74e-44 |
|
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: 148.10 E-value: 7.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERN---KIKKNVSV 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 85 VPQDLALYPTLTAYDNLSfyadlYGLkgnrkksrikealqfaqledwahkridtfSGGMKRRINLVIGLLNKPKVIFLDE 164
Cdd:cd03229 81 VFQDFALFPHLTVLENIA-----LGL-----------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446051965 165 PTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGE 216
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-223 |
1.48e-43 |
|
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: 149.41 E-value: 1.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyTERNKIKKNVSVVPQ 87
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 DLALYPTLTAYDNLSFyadlyGLKGNRKKSRIKEA---------LQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPK 158
Cdd:cd03296 82 HYALFRHMTVFDNVAF-----GLRVKPRSERPPEAeirakvhelLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTP 223
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-217 |
5.32e-43 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 147.73 E-value: 5.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGD----YTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT----ERNKI 78
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 KKNVSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPK 158
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-226 |
1.38e-41 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 147.56 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyTERNKIKKNVSV 84
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 85 VPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDE 164
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446051965 165 PTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-215 |
5.59e-40 |
|
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: 139.21 E-value: 5.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 16 SYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLI-SILSTLTlPDEGYGTVCNYDLYTERNKIkknvSVVPQDLAL--- 91
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLkAILGLLK-PTSGSIRVFGKPLEKERKRI----GYVPQRRSIdrd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 92 YPtLTAYD--NLSFYADLYGLKGNRK--KSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:cd03235 83 FP-ISVRDvvLMGLYGHKGLFRRLSKadKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446051965 168 GIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKG 215
Cdd:cd03235 162 GVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
10-217 |
1.22e-39 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 138.69 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 10 IRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLytERNKIKkNVSVVPQDL 89
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW--TRKDLH-KIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 90 ALYPTLTAYDNLSFYADLYGLKgnrkKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGI 169
Cdd:TIGR03740 80 PLYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446051965 170 DPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:TIGR03740 156 DPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-243 |
2.37e-39 |
|
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: 139.32 E-value: 2.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 13 IKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTE-----RNKIKKNVSVVPQ 87
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkelRELRRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 DLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 168 GIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKYGENYLEIVISNIP 243
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVD 265
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-228 |
4.41e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 143.89 E-value: 4.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSY--GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLtLPDEG--YGTVC--NYDLYTERNKI 78
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHGGriSGEVLldGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 K-KNVSVVPQD--LALYPtLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLN 155
Cdd:COG1123 81 RgRRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446051965 156 KPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-228 |
5.58e-39 |
|
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: 137.43 E-value: 5.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYT-VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyTERN--KIKKNVSV 84
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI-REQDpvELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 85 VPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLED--WAHKRIDTFSGGMKRRINLVIGLLNKPKVIFL 162
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 163 DEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-217 |
7.87e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.10 E-value: 7.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygTVCnYD--LYTERN--KIKKNVS 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSG--EIY-LDgkPLSAMPppEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQDLALYPTlTAYDNLSFYADLYGLKGNRKksRIKEALQFAQL-EDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFL 162
Cdd:COG4619 78 YVPQEPALWGG-TVRDNLPFPFQLRERKFDRE--RALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 163 DEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-223 |
9.38e-39 |
|
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: 137.48 E-value: 9.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnydlyternKIK---KNV 82
Cdd:COG0411 3 PLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSG--------------RILfdgRDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVVP-------------QDLALYPTLTAYDNL----------SFYADLYGLKGNRKKS-----RIKEALQFAQLEDWAHK 134
Cdd:COG0411 69 TGLPphriarlgiartfQNPRLFPELTVLENVlvaaharlgrGLLAALLRLPRARREEreareRAEELLERVGLADRADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 135 RIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDK 214
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF 228
|
....*....
gi 446051965 215 GEILDIDTP 223
Cdd:COG0411 229 GRVIAEGTP 237
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-221 |
1.07e-38 |
|
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: 135.85 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnyDLY------TERNKIKKN 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSG-------RIYiggrdvTDLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIF 161
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 162 LDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDID 221
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
8-229 |
1.18e-38 |
|
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: 136.31 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYtVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyTERNKIKKNVSVVPQ 87
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 DLALYPTLTAYDNLSfyadlYGLK--GNRKKSRIKEALQFAQLEDWAH---KRIDTFSGGMKRRINLVIGLLNKPKVIFL 162
Cdd:cd03299 79 NYALFPHMTVYKNIA-----YGLKkrKVDKKEIERKVLEIAEMLGIDHllnRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446051965 163 DEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITK 229
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-217 |
1.66e-38 |
|
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: 135.35 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTER---NKIKKNVSV 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKkniNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 85 VPQDLALYPTLTAYDNLSFyadlyGLKGNRKKSRiKEALQFA-------QLEDWAHKRIDTFSGGMKRRINLVIGLLNKP 157
Cdd:cd03262 81 VFQQFNLFPHLTVLENITL-----APIKVKGMSK-AEAEERAlellekvGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 158 KVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-228 |
2.46e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 135.51 E-value: 2.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLY---TERNKIKKNVS 83
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQDLALYPTLTAYDNLsfyadLYGLKGNRKKSRiKEALQFAQ-------LEDWAHKRIDTFSGGMKRRINLVIGLLNK 156
Cdd:COG1126 81 MVFQQFNLFPHLTVLENV-----TLAPIKVKKMSK-AEAEERAMellervgLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446051965 157 PKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
16-218 |
3.03e-38 |
|
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: 133.71 E-value: 3.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 16 SYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK-IKKNVSVVPQdlalypt 94
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKeLARKIAYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 95 ltaydnlsfyadlyglkgnrkksrikeALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSR 174
Cdd:cd03214 81 ---------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446051965 175 NHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEIL 218
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-216 |
4.33e-38 |
|
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: 132.37 E-value: 4.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 9 SIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL-YTERNKIKKNVSVVPQ 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 dlalyptltaydnlsfyadlyglkgnrkksrikealqfaqledwahkridtFSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446051965 168 GIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGE 216
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-218 |
1.94e-37 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 133.33 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygTV--CNYDLYTER-NKI-KKNVS 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSG--SVlfDGEDITGLPpHEIaRLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQDLALYPTLTAYDNL---------SFYADLYGLKGNRK-KSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGL 153
Cdd:cd03219 79 RTFQIPRLFPELTVLENVmvaaqartgSGLLLARARREEREaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 154 LNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEIL 218
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
7-221 |
2.92e-37 |
|
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: 132.03 E-value: 2.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRyIKKSYGDYTVikNLSIDIrKGEIIGLLGPNGAGKTTLISILSTLTLPDEGY----GTVcnydLYTERNKI---- 78
Cdd:cd03297 1 MLCVD-IEKRLPDFTL--KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTivlnGTV----LFDSRKKInlpp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 -KKNVSVVPQDLALYPTLTAYDNLsfyadLYGLKGNR---KKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLL 154
Cdd:cd03297 73 qQRKIGLVFQQYALFPHLNVRENL-----AFGLKRKRnreDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446051965 155 NKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDID 221
Cdd:cd03297 148 AQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-228 |
3.55e-37 |
|
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: 132.67 E-value: 3.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL--YTERNKIKKNVSVV 85
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItkLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 86 PQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEP 165
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446051965 166 TVGIDPQSRNHIFNCIRHLVeELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-219 |
4.85e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.71 E-value: 4.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSY-GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyterNKIKK----- 80
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL----SRLKRreipy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 81 ---NVSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKP 157
Cdd:COG2884 77 lrrRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446051965 158 KVIFLDEPTVGIDPQSRNHIfncIRHLVE--ELGITVIYTTHHMEEAEMLCHRVAIYDKGEILD 219
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEI---MELLEEinRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-235 |
8.15e-37 |
|
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: 140.15 E-value: 8.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVVPQDLALYPTLTAYDNLS 102
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 103 FYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIR 182
Cdd:TIGR01257 2035 LYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446051965 183 HLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKYGENYL 235
Cdd:TIGR01257 2115 SIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYI 2166
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-229 |
9.89e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 134.05 E-value: 9.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSY----GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT----ERNKI 78
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 KKNVSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRInlviG----LL 154
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRV----GiaraLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 155 NKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI------LDIDT-PKNLI 227
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIveqgpvLDVFAnPQSEL 236
|
..
gi 446051965 228 TK 229
Cdd:COG1135 237 TR 238
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-224 |
1.73e-36 |
|
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: 130.38 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTL-----TLPDEG----YGTVCnYDLYTERNKI 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGevllDGKDI-YDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 KKNVSVVPQDLALYPtLTAYDNLSFYADLYGLKGNRK-KSRIKEALQFAQLEDWAHKRID--TFSGGMKRRINLVIGLLN 155
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEElDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 156 KPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElgITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPK 224
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-217 |
2.16e-36 |
|
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: 130.77 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYT-VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK----IKKNV 82
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVVPQDLALYPTLTAYDN--------LSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLL 154
Cdd:cd03256 81 GMIFQQFNLIERLSVLENvlsgrlgrRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446051965 155 NKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-226 |
6.89e-35 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 126.84 E-value: 6.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDY----TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK-IKKN 81
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKaFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVVPQD--LALYPTLTAYDNLSfyADLYGLKGNRKKSRIKEALQFAQL-EDWAHKRIDTFSGGMKRRINLVIGLLNKPK 158
Cdd:COG1124 81 VQMVFQDpyASLHPRHTVDRILA--EPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-219 |
7.70e-34 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 123.97 E-value: 7.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCN--YDLYTERN-----KIKK 80
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSdkairELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 81 NVSVVPQDLALYPTLTAYDNL-SFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKV 159
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 160 IFLDEPTVGIDPQSRNHIFNCIRHLvEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILD 219
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-224 |
9.43e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 126.74 E-value: 9.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyTERNKIKKNVSVVPQ 87
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 DLALYPTLTAYDNLSFyadlyGLK--GNRK-------KSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPK 158
Cdd:PRK10851 82 HYALFRHMTVFDNIAF-----GLTvlPRRErpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPK 224
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
8-227 |
1.07e-33 |
|
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: 123.54 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT----ERNKIkkNVS 83
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlpmhERARL--GIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQDLALYPTLTAYDNLSFYADL-YGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFL 162
Cdd:TIGR04406 80 YLPQEASIFRKLTVEENIMAVLEIrKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 163 DEPTVGIDPQSRNHIFNCIRHLvEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLI 227
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
22-234 |
1.26e-33 |
|
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: 130.34 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL-YTERNKIKKNVSVVPQDLALYPTlTAYDN 100
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLrQIDPASLRRQIGVVLQDVFLFSG-TIREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 101 LSFYADLYGLKgnrkksRIKEALQFAQLEDWAHKR---IDT--------FSGGMKRRINLVIGLLNKPKVIFLDEPTVGI 169
Cdd:COG2274 569 ITLGDPDATDE------EIIEAARLAGLHDFIEALpmgYDTvvgeggsnLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 170 DPQSRNHIFNCIRHLVEelGITVIYTTHHMEEAEmLCHRVAIYDKGEILDIDTPKNLITKYGENY 234
Cdd:COG2274 643 DAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-247 |
1.27e-33 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 130.63 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 15 KSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG----YG-TVCNYDLYTernkiKKNVSVVPQDL 89
Cdd:NF033858 274 MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlFGqPVDAGDIAT-----RRRVGYMSQAF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 90 ALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGI 169
Cdd:NF033858 349 SLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 170 DPQSRNHIFnciRHLVE---ELGITVIYTTHHMEEAEmLCHRVAIYDKGEILDIDTPKNLITKYGENYLEivisnipEEF 246
Cdd:NF033858 429 DPVARDMFW---RLLIElsrEDGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTPAALVAARGAATLE-------EAF 497
|
.
gi 446051965 247 I 247
Cdd:NF033858 498 I 498
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-226 |
1.63e-33 |
|
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: 122.54 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEgyGTVcNYD------LYTERnKIKKN 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRS--GSI-RFDgrditgLPPHE-RARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVVPQDLALYPTLTAYDNLSFYAdlYGLKGNRKKSRIKEALQ-FAQLEDWAHKRIDTFSGG---MkrrinLVIG--LLN 155
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGA--YARRRAKRKARLERVYElFPRLKERRKQLAGTLSGGeqqM-----LAIAraLMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446051965 156 KPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-227 |
2.00e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 122.83 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG----YGT-VCNYDLYtERNKik 79
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGriflDGEdITHLPMH-KRAR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 80 KNVSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKV 159
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446051965 160 IFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLI 227
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHLKER-GIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-238 |
4.46e-33 |
|
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: 129.36 E-value: 4.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVVPQDLALYPTLTAYDNLS 102
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 103 FYADLYGlkgnrkKSRIKEALQF-AQLEDWA--HKRIDT---FSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNH 176
Cdd:TIGR01257 1026 FYAQLKG------RSWEEAQLEMeAMLEDTGlhHKRNEEaqdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446051965 177 IFNCIrhLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKYGEN-YLEIV 238
Cdd:TIGR01257 1100 IWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGfYLTLV 1160
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-224 |
6.96e-33 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 121.42 E-value: 6.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnyDLYTERNKIKK---NVSVVPQDLALYPTLTAYD 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSG-------GVILEGKQITEpgpDRMVVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 100 NLSFYAD--LYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHI 177
Cdd:TIGR01184 74 NIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446051965 178 FNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDK------GEILDIDTPK 224
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNgpaaniGQILEVPFPR 206
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-219 |
1.32e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 120.89 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCN--YDLYTERN-----KIKK 80
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDFSQKPSekairLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 81 NVSVVPQDLALYPTLTAYDNLsFYADLYGLKGNRKKSRIK--EALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPK 158
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENL-IEAPCKVLGLSKEQAREKamKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLvEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILD 219
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-217 |
2.40e-32 |
|
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: 119.56 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 14 KKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnydlyternKIKKNVSVVPQ-DLA-- 90
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG--------------TVTVRGRVSSLlGLGgg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 91 LYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPT-VGi 169
Cdd:cd03220 95 FNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLaVG- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446051965 170 DPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-237 |
3.65e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.51 E-value: 3.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 3 DINTMISIRYIKKSYGD---YTViKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyTERN--K 77
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaatYAL-KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL-SEETvwD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 78 IKKNVSVVPQ--DLALYPTlTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLN 155
Cdd:PRK13635 79 VRRQVGMVFQnpDNQFVGA-TVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 156 KPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMlCHRVAIYDKGEILDIDTPKNlITKYGENYL 235
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEE-IFKSGHMLQ 235
|
..
gi 446051965 236 EI 237
Cdd:PRK13635 236 EI 237
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
8-237 |
3.66e-32 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 122.54 E-value: 3.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLiSILSTLTLPDEG-----YGTVCnydlyTERNKIKKNV 82
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGrrpwrF*TWC-----ANRRALRRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SV-VPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIF 161
Cdd:NF000106 88 G*hRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 162 LDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKYGENYLEI 237
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQI 242
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-226 |
6.41e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 122.25 E-value: 6.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyTERNKIKKNVSVVP 86
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 87 QDLALYPTLTAYDNLSFyadlyGLKGNRK-----KSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIF 161
Cdd:PRK11607 98 QSYALFPHMTVEQNIAF-----GLKQDKLpkaeiASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 162 LDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-228 |
8.40e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 118.66 E-value: 8.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGY----GTVCNYDLYTERNkIKKNV 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdGLKVNDPKVDERL-IRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVVPQDLALYPTLTAYDNLSFYA-DLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIF 161
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446051965 162 LDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-231 |
9.21e-32 |
|
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: 118.65 E-value: 9.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILS---------TLTLPDEGYGTVcnyDLYter 75
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgdlpptygnDVRLFGERRGGE---DVW--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 76 nKIKKNVSVVPQDLALY--PTLTAYDN-LS-FYA--DLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINL 149
Cdd:COG1119 75 -ELRKRIGLVSPALQLRfpRDETVLDVvLSgFFDsiGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 150 VIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEE--AEMlcHRVAIYDKGEIL------DID 221
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEipPGI--THVLLLKDGRVVaagpkeEVL 231
|
250
....*....|
gi 446051965 222 TPKNLITKYG 231
Cdd:COG1119 232 TSENLSEAFG 241
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-230 |
1.16e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 115.56 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 14 KKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnydlyternKIKKNVSVVPQdLAL-- 91
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG--------------RVEVNGRVSAL-LELga 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 92 --YPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPT-VG 168
Cdd:COG1134 98 gfHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLaVG 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446051965 169 iDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKY 230
Cdd:COG1134 178 -DAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAY 237
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-245 |
1.26e-30 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 121.77 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 17 YGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL--YTERNKIKKNVSVVPQDLA--LY 92
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadARHRRAVCPRIAYMPQGLGknLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 93 PTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQ 172
Cdd:NF033858 91 PTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 173 SRNHIFNCIRHLVEEL-GITVIYTTHHMEEAEMLCHRVAIyDKGEILDIDTPKNLITKYGENYLEIV-ISNIPEE 245
Cdd:NF033858 171 SRRQFWELIDRIRAERpGMSVLVATAYMEEAERFDWLVAM-DAGRVLATGTPAELLARTGADTLEAAfIALLPEE 244
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-226 |
1.48e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 115.08 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEgyGTVCnYD------LYTERnKIK 79
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRS--GSIR-FDgeditgLPPHR-IAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 80 KNVSVVPQDLALYPTLTAYDNLsfyadLYGLKGNRKKSRIKEALQ-----FAQLEDWAHKRIDTFSGG---MkrrinLVI 151
Cdd:COG0410 78 LGIGYVPEGRRIFPSLTVEENL-----LLGAYARRDRAEVRADLErvyelFPRLKERRRQRAGTLSGGeqqM-----LAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446051965 152 G--LLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:COG0410 148 GraLMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-211 |
1.76e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.12 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGY----GTVCNYDlyTERNKIKK 80
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEilldGEPVRFR--SPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 81 NVSVVPQDLALYPTLTAYDNLsFYADLYGLKG--NRKKSRiKEALQ-FAQLE---DwAHKRIDTFSGGMKRrinLV-I-- 151
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENI-FLGREPRRGGliDWRAMR-RRARElLARLGldiD-PDTPVGDLSVAQQQ---LVeIar 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 152 GLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAI 211
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTV 212
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-193 |
3.22e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 114.80 E-value: 3.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK-IKKNVSVV 85
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSReLAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 86 PQDLALYPTLTAYDNLSF----YAdlyglKGN---RKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRR--INLVIGllNK 156
Cdd:COG4604 81 RQENHINSRLTVRELVAFgrfpYS-----KGRltaEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRafIAMVLA--QD 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 446051965 157 PKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVI 193
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVV 190
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-217 |
5.98e-30 |
|
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: 111.37 E-value: 5.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCN--YDLYTERNKIKKNVSVV 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 86 PQdlalyptltaydnlsfyadlyglkgnrkksrikealqfaqledwahkridtFSGGMKRRINLVIGLLNKPKVIFLDEP 165
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446051965 166 TVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-218 |
8.56e-30 |
|
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: 112.75 E-value: 8.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLtLPDEG--YGTVCNYDLYTERNKIKKNVSVVPQDLALYPTLTAYD 99
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEGGGttSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 100 NLSFYADLYGLKGNRKKSRIKEALQFAQ----LEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRN 175
Cdd:cd03234 101 TLTYTAILRLPRKSSDAIRKKRVEDVLLrdlaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446051965 176 HIFNCIRHLVEElGITVIyTTHHMEEAEM--LCHRVAIYDKGEIL 218
Cdd:cd03234 181 NLVSTLSQLARR-NRIVI-LTIHQPRSDLfrLFDRILLLSSGEIV 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-227 |
1.06e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 113.06 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 13 IKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYD--LYTERNKIKKNVSVVPQDLA 90
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisLLPLHARARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 91 LYPTLTAYDNLSFYADL-YGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGI 169
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446051965 170 DPQSRNHIFNCIRHLvEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLI 227
Cdd:PRK10895 169 DPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-226 |
2.21e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 112.16 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTviKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyTERNKIKKNVSVVP 86
Cdd:COG3840 1 MLRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 87 QDLALYPTLTAYDNLSFyadlyGLKGNRK-----KSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIF 161
Cdd:COG3840 78 QENNLFPHLTVAQNIGL-----GLRPGLKltaeqRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446051965 162 LDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI---------LDIDTPKNL 226
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIaadgptaalLDGEPPPAL 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-235 |
2.24e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 115.90 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-----ERNKIKKNVSVVPQDLALYPTLTA 97
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaeLREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 98 YDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHI 177
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446051965 178 FNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKYGENYL 235
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
7-223 |
2.38e-29 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 114.81 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRyIKKSYGDYTVikNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKI-----KKN 81
Cdd:COG4148 2 MLEVD-FRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIflpphRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVVPQDLALYPTLTAYDNLsfyadLYGLKGNRKKSRikeALQFAQLEDW---AH---KRIDTFSGGMKRRInlVIG--L 153
Cdd:COG4148 79 IGYVFQEARLFPHLSVRGNL-----LYGRKRAPRAER---RISFDEVVELlgiGHlldRRPATLSGGERQRV--AIGraL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 154 LNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTP 223
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPL 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-197 |
2.42e-29 |
|
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: 110.72 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 21 TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVcnydLY----TERNKIKKNVSVVPQDLALYPTLT 96
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEV----LIngrpLDKRSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 97 AYDNLSFYADLYGLkgnrkksrikealqfaqledwahkridtfSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNH 176
Cdd:cd03213 99 VRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180
....*....|....*....|.
gi 446051965 177 IFNCIRHLVEElGITVIYTTH 197
Cdd:cd03213 150 VMSLLRRLADT-GRTIICSIH 169
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-216 |
3.12e-29 |
|
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: 109.78 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGD--YTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIKKNVSV 84
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 85 VPQDLALYPTlTAYDNLsfyadlyglkgnrkksrikealqfaqledwahkridtFSGGMKRRINLVIGLLNKPKVIFLDE 164
Cdd:cd03228 81 VPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446051965 165 PTVGIDPQSRNHIFNCIRHLVEelGITVIYTTHHMEEAEMlCHRVAIYDKGE 216
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
21-231 |
4.16e-29 |
|
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: 116.79 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 21 TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIKKNVSVVPQDLALYPTlTAYD 99
Cdd:COG4987 349 PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAVVPQRPHLFDT-TLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 100 NLSFyadlyglkGNRKKS--RIKEALQFAQLEDWAH---KRIDT--------FSGGMKRRINLVIGLLNKPKVIFLDEPT 166
Cdd:COG4987 428 NLRL--------ARPDATdeELWAALERVGLGDWLAalpDGLDTwlgeggrrLSGGERRRLALARALLRDAPILLLDEPT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 167 VGIDPQSRNHIFNCIRHLVEelGITVIYTTHHMEEAEmLCHRVAIYDKGEILDIDTPKNLITKYG 231
Cdd:COG4987 500 EGLDAATEQALLADLLEALA--GRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-226 |
6.49e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 113.97 E-value: 6.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILStltlpdeGYGTVCNYDLYT--ER-NKI---KKN 81
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIA-------GLEDITSGDLFIgeKRmNDVppaERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRInlVIG--LLNKPKV 159
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRV--AIGrtLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446051965 160 IFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-217 |
7.55e-29 |
|
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: 110.19 E-value: 7.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSY-GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK----IKKNV 82
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFL 162
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 163 DEPTVGIDPQSRNHIFNCIRHlVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-228 |
8.83e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 111.71 E-value: 8.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYT-VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGY----GTVCNYDlYTERNKIKKN 81
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEvlikGEPIKYD-KKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVV---PQDLALYPTLTayDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPK 158
Cdd:PRK13639 80 VGIVfqnPDDQLFAPTVE--EDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
12-224 |
1.46e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.29 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 12 YIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK---IKKNVSVVPQd 88
Cdd:PRK13637 12 YMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdIRKKVGLVFQ- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 89 lalYPTL-----TAYDNLSFYADLYGLKGNRKKSRIKEALQFAQL--EDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIF 161
Cdd:PRK13637 91 ---YPEYqlfeeTIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446051965 162 LDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPK 224
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR 230
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-236 |
2.06e-28 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 112.13 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRyIKKSYGDYTVikNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKI-----KKNV 82
Cdd:TIGR02142 1 LSAR-FSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppeKRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVVPQDLALYPTLTAYDNLsfyadLYGLKGNRKKSR-IKEA--LQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKV 159
Cdd:TIGR02142 78 GYVFQEARLFPHLSVRGNL-----RYGMKRARPSERrISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446051965 160 IFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKYGENYLE 236
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-229 |
2.27e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.56 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 21 TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERN--KIKKNVSVVPQ--DLALYPTLT 96
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMVFQnpDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 97 AYDnLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNH 176
Cdd:PRK13633 104 EED-VAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446051965 177 IFNCIRHLVEELGITVIYTTHHMEEAeMLCHRVAIYDKGEILDIDTPKNLITK 229
Cdd:PRK13633 183 VVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
7-219 |
3.07e-28 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 109.53 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCN-----YDLYT----ERNK 77
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaeLELYQlseaERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 78 IKKN----VSVVPQDlALYPTLTAYDNLSfyADLYGLkGNRKKSRIKEALQfaqleDWAHK------RID----TFSGGM 143
Cdd:TIGR02323 83 LMRTewgfVHQNPRD-GLRMRVSAGANIG--ERLMAI-GARHYGNIRATAQ-----DWLEEveidptRIDdlprAFSGGM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 144 KRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILD 219
Cdd:TIGR02323 154 QQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-217 |
6.70e-28 |
|
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: 107.34 E-value: 6.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYikksYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL-YTERnkiKKNVSVVP 86
Cdd:cd03226 5 ISFSY----KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkAKER---RKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 87 QDL--ALYpTLTAYDNLSFYADLYGlKGNRKKSRIKEALQFAQLEDWaHKRidTFSGGMKRRINLVIGLLNKPKVIFLDE 164
Cdd:cd03226 78 QDVdyQLF-TDSVREELLLGLKELD-AGNEQAETVLKDLDLYALKER-HPL--SLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446051965 165 PTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-211 |
7.44e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.81 E-value: 7.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG----YGTVcnYDLYTERNKIKKNV 82
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGeiliDGKP--VRIRSPRDAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVVPQDLALYPTLTAYDNLSFYA-DLYGLKGNRKKSRiKEALQFAQ---LE-DWaHKRIDTFSGGMKRRINLVIGLLNKP 157
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLePTKGGRLDRKAAR-ARIRELSErygLDvDP-DAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446051965 158 KVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAI 211
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTV 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-227 |
1.29e-27 |
|
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: 112.20 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYG--DYTVIK---NLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT------ 73
Cdd:TIGR03269 277 EPIIKVRNVSKRYIsvDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVdmtkpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 74 --ERNKIKKNVSVVPQDLALYPTLTAYDNLSfyaDLYGLKGNRKKSRIKE--ALQFAQLEDWAHKRI-----DTFSGGMK 144
Cdd:TIGR03269 357 pdGRGRAKRYIGILHQEYDLYPHRTVLDNLT---EAIGLELPDELARMKAviTLKMVGFDEEKAEEIldkypDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 145 RRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPK 224
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
...
gi 446051965 225 NLI 227
Cdd:TIGR03269 514 EIV 516
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-231 |
1.81e-27 |
|
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: 112.16 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYikksYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK-IKKNVSVVP 86
Cdd:COG4988 342 VSFSY----PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAsWRRQIAWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 87 QDLALYPTlTAYDNLSFYADlyglkgNRKKSRIKEALQFAQLEDWAHKR---IDT--------FSGGMKRRINLVIGLLN 155
Cdd:COG4988 418 QNPYLFAG-TIRENLRLGRP------DASDEELEAALEAAGLDEFVAALpdgLDTplgeggrgLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 156 KPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEelGITVIYTTHHMEEAEmLCHRVAIYDKGEILDIDTPKNLITKYG 231
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-229 |
2.83e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 108.73 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSY----GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT----ERNKI 78
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsekELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 KKNVSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPK 158
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDT-------PKNLITK 229
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTvsevfshPKHPLTR 238
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-226 |
4.47e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 106.37 E-value: 4.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTER---------N 76
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkgliR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 77 KIKKNVSVVPQDLALYPTLTAYDNLsfyadLYG---LKGNRKKSRIKEALQ------FAQLEDWAHKRIdtfSGGMKRRI 147
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENI-----IEGpviVKGEPKEEATARAREllakvgLAGKETSYPRRL---SGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 148 NLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIyTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-203 |
1.33e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.10 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLIS-ILSTLTlPD---EG----YGTVCNyDLYTERnki 78
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLS-PAfsaSGevllNGRRLT-ALPAEQ--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 kKNVSVVPQDLALYPTLTAYDNLSFyaDL-YGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKP 157
Cdd:COG4136 76 -RRIGILFQDDLLFPHLSVGENLAF--ALpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446051965 158 KVIFLDEPTVGIDPQSRNHifncIRHLV----EELGITVIYTTHHMEEAE 203
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQ----FREFVfeqiRQRGIPALLVTHDEEDAP 198
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-217 |
1.62e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 105.01 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG---Y----GTVCnyDLYT----ER 75
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGevhYrmrdGQLR--DLYAlseaER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 76 NKI-KKNVSVVPQDLA--LYPTLTAYDNLSfyADLYGLkGNRKKSRIKE-ALQFAQLEDWAHKRID----TFSGGMKRRI 147
Cdd:PRK11701 84 RRLlRTEWGFVHQHPRdgLRMQVSAGGNIG--ERLMAV-GARHYGDIRAtAGDWLERVEIDAARIDdlptTFSGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446051965 148 NLVIGLLNKPKVIFLDEPTVGID--PQSRnhIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDvsVQAR--LLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-229 |
2.03e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.31 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDYT-VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERN---KIKK 80
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 81 NVSVVPQ--DLALYpTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPK 158
Cdd:PRK13636 83 SVGMVFQdpDNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITK 229
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-218 |
3.45e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 104.32 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 4 INTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDE---------GYGTVCNYDLYTE 74
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 75 RNKIKKNVSVVPQDLALYPTLTAYDNL--------SFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRR 146
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVligalgstPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446051965 147 INLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEIL 218
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-229 |
3.63e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.88 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDY--TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK----I 78
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKtvwdI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 KKNVSVVPQDL-ALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKP 157
Cdd:PRK13640 83 REKVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446051965 158 KVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMlCHRVAIYDKGEILDIDTPKNLITK 229
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-217 |
4.52e-26 |
|
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: 105.14 E-value: 4.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSY----GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLtLPDEGY--GTV--CNYDLYT----E 74
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGL-LPPPGItsGEIlfDGEDLLKlsekE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 75 RNKIK-KNVSVVPQD--LALYPTLTAYDNLsfyADLY----GLKGNRKKSRIKEALQFAQLEDwAHKRID----TFSGGM 143
Cdd:COG0444 80 LRKIRgREIQMIFQDpmTSLNPVMTVGDQI---AEPLrihgGLSKAEARERAIELLERVGLPD-PERRLDryphELSGGM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 144 KRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAI-YdKGEI 217
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVmY-AGRI 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-175 |
4.78e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.46 E-value: 4.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEgyGTVcnydlyternKIKKNVSV 84
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDS--GTV----------KLGETVKI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 85 --VPQDLA-LYPTLTAYDNLSFYADlyglKGNRKKSRikealqfAQLEDW------AHKRIDTFSGGMKRRINLVIGLLN 155
Cdd:COG0488 381 gyFDQHQEeLDPDKTVLDELRDGAP----GGTEQEVR-------GYLGRFlfsgddAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180
....*....|....*....|
gi 446051965 156 KPKVIFLDEPTVGIDPQSRN 175
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLE 469
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-202 |
7.51e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.54 E-value: 7.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 16 SYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnydlyTERNKIKKNVSVVPQDLALYPTL 95
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG----------TVRRAGGARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 96 --TAYD--NLSFYADLYGLKGNRKKSR--IKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGI 169
Cdd:NF040873 71 plTVRDlvAMGRWARRGLWRRLTRDDRaaVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|...
gi 446051965 170 DPQSRNHIFNCIRHLVEElGITVIYTTHHMEEA 202
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELV 182
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-228 |
7.85e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.17 E-value: 7.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL--YTERnKIKKNVS 83
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsmLSSR-QLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQDLaLYP------TLTAYDNlSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKP 157
Cdd:PRK11231 80 LLPQHH-LTPegitvrELVAYGR-SPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446051965 158 KVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-244 |
1.26e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.14 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYT-VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL--YTERNKIKKNVS 83
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQDLAL-YPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFL 162
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 163 DEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMlCHRVAIYDKGEILDIDTPKNLITKYGENYLEIVISNI 242
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSL 238
|
..
gi 446051965 243 PE 244
Cdd:PRK13644 239 IE 240
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-206 |
1.43e-25 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 102.50 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnydlyTERNKIKKNVSVV 85
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKRNGKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 86 PQDLALYPTLTaydnLSFyADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEP 165
Cdd:PRK09544 73 PQKLYLDTTLP----LTV-NRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446051965 166 TVGIDPQSRNHIFNCIRHLVEELGITVIYTTH--HMEEA---EMLC 206
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLRRELDCAVLMVSHdlHLVMAktdEVLC 193
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-228 |
1.70e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 101.88 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL--YTERNKIKKNV 82
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVVPQDLALYPTLTAYDNLS---FYADlyglkGNRKKSRIKEALQ-FAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPK 158
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAmggFFAE-----RDQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-224 |
3.02e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 101.68 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKknvsVV 85
Cdd:PRK11247 11 TPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR----LM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 86 PQDLALYPTLTAYDNLSFyadlyGLKGN-RKKSRikEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDE 164
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGL-----GLKGQwRDAAL--QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446051965 165 PTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI---LDIDTPK 224
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldLTVDLPR 222
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-243 |
3.52e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 101.81 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSY---------GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLY---- 72
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 73 TERNKIKKNVSVVPQDL--ALYPTLTAYDNLSF-YADLYGLKGNRKKSRIKEALQFAQLE-DWAHKRIDTFSGGMKRRIN 148
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDSpsAVNPRMTVRQIIGEpLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 149 LVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILD-IDTPKNLI 227
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEeCDVAQLLS 240
|
250
....*....|....*...
gi 446051965 228 TKY--GENYLEIVISNIP 243
Cdd:TIGR02769 241 FKHpaGRNLQSAVLPEHP 258
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
7-229 |
8.30e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.03 E-value: 8.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSY-GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyTERN--KIKKNVS 83
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-TKENirEVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VV---PQDLALYPTLTayDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVI 160
Cdd:PRK13652 82 LVfqnPDDQIFSPTVE--QDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 161 FLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITK 229
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-223 |
1.17e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 101.84 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSY-GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTL---ISILSTLTlpdEGY----GTVCNyDLY-TERNk 77
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLlrmVAGLERIT---SGEiwigGRVVN-ELEpADRD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 78 ikknVSVVPQDLALYPTLTAYDNLSfyadlYGLKgNRK------KSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVI 151
Cdd:PRK11650 78 ----IAMVFQNYALYPHMSVRENMA-----YGLK-IRGmpkaeiEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446051965 152 GLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTP 223
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTP 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-229 |
1.57e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 103.71 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 16 SY-GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG----YGT-VCNYDLYTERNKIkknvSVVPQDL 89
Cdd:COG1132 348 SYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGriliDGVdIRDLTLESLRRQI----GVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 90 ALYpTLTAYDNLSFyadlyglkGNRKKSR--IKEALQFAQLEDWAHK---RIDT--------FSGGMKRRINLVIGLLNK 156
Cdd:COG1132 424 FLF-SGTIRENIRY--------GRPDATDeeVEEAAKAAQAHEFIEAlpdGYDTvvgergvnLSGGQRQRIAIARALLKD 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446051965 157 PKVIFLDEPTVGIDPQSRNHIFNCIRHLVEelGITVIYTTHHMEEAEMlCHRVAIYDKGEILDIDTPKNLITK 229
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-217 |
1.96e-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: 97.38 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYG--DYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVV 85
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 86 PQDLALYPTlTAYDNLsfyadlyglkGNRkksrikealqfaqledwahkridtFSGGMKRRINLVIGLLNKPKVIFLDEP 165
Cdd:cd03247 81 NQRPYLFDT-TLRNNL----------GRR------------------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446051965 166 TVGIDPQSRNHIFNCIRHLVEELgiTVIYTTHHMEEAEMLcHRVAIYDKGEI 217
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-232 |
6.28e-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: 101.42 E-value: 6.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLT--LPDEG-------YGTVCNY--------- 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGriiyhvaLCEKCGYverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 70 --------------DLY----TERNKIKKNVSVVPQ-DLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLED 130
Cdd:TIGR03269 81 pcpvcggtlepeevDFWnlsdKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 131 WAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVA 210
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260
....*....|....*....|..
gi 446051965 211 IYDKGEILDIDTPKNLITKYGE 232
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAVFME 262
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-229 |
6.79e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 97.68 E-value: 6.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLT--LPD---EGYGTVCNYDLY-TERNKIKKN 81
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelYPEarvSGEVYLDGQDIFkMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKK--SRIKEALQFAQLEDWAHKRID----TFSGGMKRRINLVIGLLN 155
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKElqERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446051965 156 KPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELgiTVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITK 229
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-217 |
1.03e-23 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 96.41 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 26 LSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDlYTERNKIKKNVSVVPQDLALYPTLTAYDNLSFyA 105
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD-VTAAPPADRPVSMLFQENNLFAHLTVEQNVGL-G 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 106 DLYGLKGN-RKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHL 184
Cdd:cd03298 95 LSPGLKLTaEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|...
gi 446051965 185 VEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-290 |
1.12e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 101.28 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 21 TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPD-EGYGTVCNYDLYTERNKIKKNVSVVPQDLALYPTLTAYD 99
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 100 NLSFYADLY---GLKGNRKKSRIKEALQFAQLEDWAHKRIDT------FSGGMKRRINLVIGLLNKPKVIFLDEPTVGID 170
Cdd:TIGR00955 119 HLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 171 PQSRNHIFNCIRHLVEElGITVIyTTHHMEEAEMLC--HRVAIYDKGEILDIDTPKNLI---TKYG----ENYleivisN 241
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQK-GKTII-CTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAVpffSDLGhpcpENY------N 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446051965 242 iPEEFIhkTKMIVDVKSCTLVDKKVIIQCVDSFNVT---REVMKLIQKYNLK 290
Cdd:TIGR00955 271 -PADFY--VQVLAVIPGSENESRERIEKICDSFAVSdigRDMLVNTNLWSGK 319
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-217 |
1.20e-23 |
|
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: 96.50 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIKKNVSVVPQDLAL-YPTLtaYD 99
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLfYGTL--RD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 100 NLSFyADLYGlkgnrKKSRIKEALQFAQLEDWAHK-----------RIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVG 168
Cdd:cd03245 97 NITL-GAPLA-----DDERILRAAELAGVTDFVNKhpngldlqigeRGRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446051965 169 IDPQSRNHIFNCIRHLVEelGITVIYTTHHMEEAEmLCHRVAIYDKGEI 217
Cdd:cd03245 171 MDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-176 |
1.21e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 13 IKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEgyGTVcnydlyternKIKKNVSV--VPQDLA 90
Cdd:COG0488 4 LSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDS--GEV----------SIPKGLRIgyLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 91 LYPTLTAYDN-LSFYADLYGLKgnRKKSRIKEAL---------------QFAQLEDWA-------------------HKR 135
Cdd:COG0488 72 LDDDLTVLDTvLDGDAELRALE--AELEELEAKLaepdedlerlaelqeEFEALGGWEaearaeeilsglgfpeedlDRP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446051965 136 IDTFSGGMKRRINLVIGLLNKPKVIFLDEPTvgidpqsrNH 176
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPT--------NH 182
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-232 |
1.36e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.49 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 1 MTDINTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGyGTVCNYDLYTERN--KI 78
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG-QIIIDGDLLTEENvwDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 KKNVSVVPQDlalyPT-----LTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGL 153
Cdd:PRK13650 80 RHKIGMVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 154 LNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEmLCHRVAIYDKGEILDIDTPKNLITKYGE 232
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGND 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-228 |
1.83e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.15 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLY-TERNKIKKNVSVV 85
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 86 PQDLAL--------------YPTLTAYDNLsfyadlyglkGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVI 151
Cdd:PRK09536 83 PQDTSLsfefdvrqvvemgrTPHRSRFDTW----------TETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446051965 152 GLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-202 |
1.92e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.85 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSYGDY----TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT---ERnki 78
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpgaDR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 kknvSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPK 158
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEA 202
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-219 |
2.87e-23 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 95.58 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGD----YTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT----ERN 76
Cdd:COG4181 6 APIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 77 KIK-KNVSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRikEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLN 155
Cdd:COG4181 86 RLRaRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARAR--ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446051965 156 KPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMlCHRVAIYDKGEILD 219
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-232 |
4.69e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.92 E-value: 4.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTV-----IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyTERNKIK-- 79
Cdd:COG1101 1 MLELKNLSKTFNPGTVnekraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 80 KNVSVVPQDLAL--YPTLTAYDNLSFyADL----YGLK---GNRKKSRIKEALqfAQ----LEDWAHKRIDTFSGGMKRR 146
Cdd:COG1101 80 KYIGRVFQDPMMgtAPSMTIEENLAL-AYRrgkrRGLRrglTKKRRELFRELL--ATlglgLENRLDTKVGLLSGGQRQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 147 INLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI-LDID---- 221
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIiLDVSgeek 236
|
250
....*....|....
gi 446051965 222 ---TPKNLITKYGE 232
Cdd:COG1101 237 kklTVEDLLELFEE 250
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-269 |
5.19e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 95.83 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 1 MTDINTMISIRYIKKSYGDYT--VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG----YGTVCNYDLYTE 74
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGeikiDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 75 rnkIKKNVSVVPQDlalyPT-----LTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINL 149
Cdd:PRK13632 81 ---IRKKIGIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 150 VIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAeMLCHRVAIYDKGEILDIDTPKNLITK 229
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNN 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446051965 230 ygENYLEIVISNIPeeFIHK-TKMIVDVKScTLVDKKVIIQ 269
Cdd:PRK13632 233 --KEILEKAKIDSP--FIYKlSKKLKGIDP-TYNEEELIEQ 268
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-205 |
8.19e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.79 E-value: 8.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 18 GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG-------------YGTVCNYdlyternkikknvsV 84
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtikldggdiddpdVAEACHY--------------L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 85 VPQDlALYPTLTAYDNLSFYADLYGlkgnRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDE 164
Cdd:PRK13539 79 GHRN-AMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446051965 165 PTVGIDPQSRNHIFNCIR-HLveELGITVIYTTHH---MEEAEML 205
Cdd:PRK13539 154 PTAALDAAAVALFAELIRaHL--AQGGIVIAATHIplgLPGAREL 196
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-228 |
1.13e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.45 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLY-TERNKIKKNVSV 84
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 85 VPQdlalYPTLTAydnlSFYAD------LYGLKGNRKKSR--IKEALQFAQLEDWAHKRIDTFSGGMKRRINL--VIGLL 154
Cdd:PRK13548 81 LPQ----HSSLSF----PFTVEevvamgRAPHGLSRAEDDalVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLarVLAQL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446051965 155 ----NKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-201 |
1.28e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 1 MTDINTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKI-K 79
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 80 KNVSVVPQDLALYPTlTAYDNLSFYADLYGLKGNRKKSRiKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKV 159
Cdd:PRK10247 81 QQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFL-DDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446051965 160 IFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEE 201
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-218 |
1.64e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.42 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 4 INTMISIRYIKKSYGDYT-VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK-IKKN 81
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVVPQDlalyP-----TLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNK 156
Cdd:PRK13647 81 VGLVFQD----PddqvfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446051965 157 PKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEIL 218
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-198 |
2.97e-22 |
|
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: 92.04 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 18 GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVVPQDLALYPTLTA 97
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 98 YDNLSFYADLYGLKGNrkksRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHI 177
Cdd:TIGR01189 91 LENLHFWAAIHGGAQR----TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170 180
....*....|....*....|.
gi 446051965 178 FNCIRHLVEELGITVIyTTHH 198
Cdd:TIGR01189 167 AGLLRAHLARGGIVLL-TTHQ 186
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-216 |
3.09e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.56 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 1 MTDINTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLT-----LPDEGYGTVCNYDLYTER 75
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNIYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 76 ---NKIKKNVSVVPQDLALYPtLTAYDNLSFYADLYGLKGNRK-----KSRIKEALQFAQLEDWAHKRIDTFSGGMKRRI 147
Cdd:PRK14258 81 vnlNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEiddivESALKDADLWDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 148 NLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGE 216
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-198 |
4.11e-22 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 91.79 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 18 GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIKKNVSVVPQDLALYPTLTA 97
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 98 YDNLSFYADLYGlkgnrkKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHI 177
Cdd:cd03231 91 LENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|.
gi 446051965 178 FNCIRHLVEELGItVIYTTHH 198
Cdd:cd03231 165 AEAMAGHCARGGM-VVLTTHQ 184
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-222 |
5.16e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 94.00 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygTVcNYDLYTERNK---------- 77
Cdd:PRK13651 8 IVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTG--TI-EWIFKDEKNKkktkekekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 78 ------------------IKKNVSVVPQdLALYPTL--TAYDNLSFYADLYGLKGNRKKSRIKEALQFAQL-EDWAHKRI 136
Cdd:PRK13651 85 eklviqktrfkkikkikeIRRRVGVVFQ-FAEYQLFeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 137 DTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGE 216
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
....*..
gi 446051965 217 IL-DIDT 222
Cdd:PRK13651 243 IIkDGDT 249
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-229 |
7.56e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.42 E-value: 7.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 19 DYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTlpdEGYGTVCNYD---LYTERN-------KIKKNVSVVPQD 88
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLI---EIYDSKIKVDgkvLYFGKDifqidaiKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 89 LALYPTLTAYDNLSFYADLYGLKGNRKKSRI-KEALQFAQLEDWAHKRIDT----FSGGMKRRINLVIGLLNKPKVIFLD 163
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIKEKREIKKIvEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446051965 164 EPTVGIDPQSRNHIFNCIRHLVEElgITVIYTTHHMEEAEMLCHRVAIYDKGEILD-------IDTPKNLITK 229
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEwgssneiFTSPKNELTE 249
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-198 |
8.58e-22 |
|
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: 95.51 E-value: 8.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 18 GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTER-NKIKKNVSVVPQDLALYPTlT 96
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqDEVRRRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 97 AYDNLSFyadlygLKGNRKKSRIKEALQFAQLEDWAHKRID-----------TFSGGMKRRINLVIGLLNKPKVIFLDEP 165
Cdd:TIGR02868 425 VRENLRL------ARPDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....*...
gi 446051965 166 TVGIDPQSRnhifnciRHLVEEL-----GITVIYTTHH 198
Cdd:TIGR02868 499 TEHLDAETA-------DELLEDLlaalsGRTVVLITHH 529
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-217 |
9.00e-22 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 90.18 E-value: 9.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCN--YDLYTERNKIKKNVSVVPQD---LALYPTLT 96
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpVTRRSPRDAIRAGIAYVPEDrkrEGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 97 AYDNLSFYADLYGlkGNRKKsrikealqfaqledwahkridtfsggmkrrinLVIG--LLNKPKVIFLDEPTVGIDPQSR 174
Cdd:cd03215 95 VAENIALSSLLSG--GNQQK--------------------------------VVLArwLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446051965 175 NHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:cd03215 141 AEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-226 |
1.27e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.95 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK------- 77
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 78 -------IKKNVSVVPQDLALYPTLTAYDN-LSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDT-FSGGMKRRIN 148
Cdd:PRK10619 83 dknqlrlLRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446051965 149 LVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-223 |
3.93e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.84 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 17 YGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG----YGTVCNYdlyTERN--KIKKNVSVVPQDLA 90
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGavlwQGKPLDY---SKRGllALRQQVATVFQDPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 91 LYPTLTAYD-NLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGI 169
Cdd:PRK13638 88 QQIFYTDIDsDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446051965 170 DPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTP 223
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
17-217 |
4.83e-21 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 89.15 E-value: 4.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 17 YGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDlYTERNKIKKNVSVVPQDLALYPTLT 96
Cdd:TIGR01277 8 YEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS-HTGLAPYQRPVSMLFQENNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 97 AYDNLSFYADLyGLKGN-RKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRN 175
Cdd:TIGR01277 87 VRQNIGLGLHP-GLKLNaEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446051965 176 HIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:TIGR01277 166 EMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-244 |
9.20e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 89.40 E-value: 9.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyterNKIKKNV---- 82
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL----AAWSPWElarr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 -SVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINL--VI-----GLL 154
Cdd:COG4559 77 rAVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLarVLaqlwePVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 155 NKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITK----- 229
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDeller 235
|
250
....*....|....*.
gi 446051965 230 -YGenyLEIVISNIPE 244
Cdd:COG4559 236 vYG---ADLRVLAHPE 248
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-198 |
1.21e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 87.94 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 18 GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnyDLYTERNKIKKNVSVVPQDL-------A 90
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAG-------EVLWQGEPIRRQRDEYHQDLlylghqpG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 91 LYPTLTAYDNLSFYADLYGLKGNRkksRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGID 170
Cdd:PRK13538 85 IKTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190
....*....|....*....|....*....|
gi 446051965 171 PQSRNHIfncIRHLVE--ELGITVIYTTHH 198
Cdd:PRK13538 162 KQGVARL---EALLAQhaEQGGMVILTTHQ 188
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-202 |
1.68e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.60 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLY---TERnkikknvS 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAER-------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLD 163
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 446051965 164 EPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEA 202
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-217 |
1.89e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.27 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG----YGTVCNYdlYTERNKIKKNV 82
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGtleiGGNPCAR--LTPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVVPQDLALYPTLTAYDNLsfyadLYGL-KGNRKKSRIKEALQfaQLEdwAHKRIDTFSGGM----KRRINLVIGLLNKP 157
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENI-----LFGLpKRQASMQKMKQLLA--ALG--CQLDLDSSAGSLevadRQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 158 KVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-223 |
2.94e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.91 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKIK------KN 81
Cdd:PRK13645 12 VSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKevkrlrKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVVPQ--DLALYPTlTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQL-EDWAHKRIDTFSGGMKRRINLVIGLLNKPK 158
Cdd:PRK13645 92 IGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTP 223
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-217 |
4.55e-20 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 85.35 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYikkSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIKKNVSVVP 86
Cdd:cd03246 6 VSFRY---PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 87 QDLALYP-TLTayDNLsfyadlyglkgnrkksrikealqfaqledwahkridtFSGGMKRRINLVIGLLNKPKVIFLDEP 165
Cdd:cd03246 83 QDDELFSgSIA--ENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446051965 166 TVGIDPQSRNHIFNCIRHLvEELGITVIYTTHHMEEAEMlCHRVAIYDKGEI 217
Cdd:cd03246 124 NSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-228 |
5.11e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.96 E-value: 5.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 25 NLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERN-----KIKKNVSVVPQdlalYPTLTAYD 99
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlkKLRKKVSLVFQ----FPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 100 N-----LSFYADLYGLKGNRKKSRIKEALQFAQL-EDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQS 173
Cdd:PRK13641 101 NtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 174 RNHIFNCIRHLvEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:PRK13641 181 RKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
22-203 |
8.24e-20 |
|
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: 89.65 E-value: 8.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIKKNVSVVPQDLALYPTlTAYDN 100
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 101 LSFYadlyglKGNRKKSRIKEALQFAQLEDWA-------HKRIDT----FSGGMKRRINLVIGLLNKPKVIFLDEPTVGI 169
Cdd:TIGR02857 416 IRLA------RPDASDAEIREALERAGLDEFVaalpqglDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190
....*....|....*....|....*....|....*..
gi 446051965 170 DPQSRNHIFNCIRHLVEelGITVIYTTH---HMEEAE 203
Cdd:TIGR02857 490 DAETEAEVLEALRALAQ--GRTVLLVTHrlaLAALAD 524
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-223 |
8.47e-20 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 86.01 E-value: 8.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYikkSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIKKNVSVVP 86
Cdd:cd03244 8 VSLRY---RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 87 QDlalyPTL---TAYDNLsfyaDLYGLKGNrkkSRIKEALQFAQLEDWahkrIDTFSGGMKRRI-----NLVIG------ 152
Cdd:cd03244 85 QD----PVLfsgTIRSNL----DPFGEYSD---EELWQALERVGLKEF----VESLPGGLDTVVeeggeNLSVGqrqllc 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 153 ----LLNKPKVIFLDEPTVGIDPQSRNHIFNCIRhlvEEL-GITVIYTTHHMeEAEMLCHRVAIYDKGEILDIDTP 223
Cdd:cd03244 150 laraLLRKSKILVLDEATASVDPETDALIQKTIR---EAFkDCTVLTIAHRL-DTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-235 |
8.81e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 86.82 E-value: 8.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 4 INTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPD-----EGYGTVCNYDLYTERN-- 76
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 77 -KIKKNVSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKK--SRIKEALQFAQLEDWAHKRIDTF----SGGMKRRINL 149
Cdd:PRK14267 81 iEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALWDEVKDRLNDYpsnlSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 150 VIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELgiTVIYTTHHMEEAEMLCHRVAIYDKGEILDI-------DT 222
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVgptrkvfEN 238
|
250
....*....|...
gi 446051965 223 PKNLITkygENYL 235
Cdd:PRK14267 239 PEHELT---EKYV 248
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-226 |
9.15e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 86.75 E-value: 9.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 1 MTDinTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILS---------TLTlpdegyGTVC--NY 69
Cdd:PRK14239 1 MTE--PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmndlnpevTIT------GSIVynGH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 70 DLYTERN---KIKKNVSVVPQDLALYPtLTAYDNLsfyadLYGL--KGNRKKSRIKEALQ--------FAQLEDWAHKRI 136
Cdd:PRK14239 73 NIYSPRTdtvDLRKEIGMVFQQPNPFP-MSIYENV-----VYGLrlKGIKDKQVLDEAVEkslkgasiWDEVKDRLHDSA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 137 DTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELgiTVIYTTHHMEEAEMLCHRVAIYDKGE 216
Cdd:PRK14239 147 LGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGD 224
|
250
....*....|
gi 446051965 217 ILDIDTPKNL 226
Cdd:PRK14239 225 LIEYNDTKQM 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-217 |
9.48e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 9.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCN--YDLYTERNKIKKNVSVVPQD---LALYPTLT 96
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDAIRAGIAYVPEDrkgEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 97 AYDNLSfyadLYGLKGNRKKSRIKEALQFAQLEDWAHK----------RIDTFSGGMKRRInlVIG--LLNKPKVIFLDE 164
Cdd:COG1129 347 IRENIT----LASLDRLSRGGLLDRRRERALAEEYIKRlriktpspeqPVGNLSGGNQQKV--VLAkwLATDPKVLILDE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446051965 165 PTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:COG1129 421 PTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-218 |
1.63e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.01 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 4 INTMISIRYIKKSY----GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKI- 78
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 ----KKNVSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLL 154
Cdd:PRK10535 81 aqlrREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446051965 155 NKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDkGEIL 218
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQAERVIEIRD-GEIV 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-216 |
2.68e-19 |
|
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: 87.96 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLtLPDEGYgtvcNYDLYTERNKIK------- 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGTW----DGEIYWSGSPLKasnirdt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 80 --KNVSVVPQDLALYPTLTAYDNLsFYADLYGLKGNRKKS-----RIKEALQFAQLEDWAHKR-IDTFSGGMKRRINLVI 151
Cdd:TIGR02633 76 erAGIVIIHQELTLVPELSVAENI-FLGNEITLPGGRMAYnamylRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 152 GLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLvEELGITVIYTTHHMEEAEMLCHRVAIYDKGE 216
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-229 |
3.09e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.84 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTE-RNK----IKKNVSVVPQ--DLALYPTL 95
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkKNKklkpLRKKVGIVFQfpEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 96 TAYDnLSFYADLYGLKGNRKKSRIKEALQFAQL-EDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSR 174
Cdd:PRK13634 103 VEKD-ICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 175 NHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITK 229
Cdd:PRK13634 182 KEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-218 |
3.19e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 85.17 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 1 MTDINTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEgyGTVcnydLYTERNKIKK 80
Cdd:COG4674 4 DTMHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDS--GSV----LFGGTDLTGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 81 NVSVVP--------QDLALYPTLTAYDNL--------SFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMK 144
Cdd:COG4674 78 DEHEIArlgigrkfQKPTVFEELTVFENLelalkgdrGVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 145 RRinLVIGLL--NKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIytTHHMEEAEMLCHRVAIYDKGEIL 218
Cdd:COG4674 158 QW--LEIGMLlaQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVV--EHDMEFVRQIARKVTVLHQGSVL 229
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-213 |
3.27e-19 |
|
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: 84.77 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 13 IKKSYGDYTviknLSI---DIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnyDLYTERNKikknVSVVPQDL 89
Cdd:cd03237 6 MKKTLGEFT----LEVeggSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-------DIEIELDT----VSYKPQYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 90 ALYPTLTAYDNLS-----FYADLYglkgnrKKSRIKEALQFAQLEDwahKRIDTFSGGMKRRINLVIGLLNKPKVIFLDE 164
Cdd:cd03237 71 KADYEGTVRDLLSsitkdFYTHPY------FKTEIAKPLQIEQILD---REVPELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446051965 165 PTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYD 213
Cdd:cd03237 142 PSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-215 |
7.10e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 7.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCN--YDLYTERNKIKKNVSV 84
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 85 VPQDLALYPTLTAYDNLsFYADLYGLKG------NRKKSRIKEALQFAQLEdwAHKRIDTFSGGM----KRRINLVIGLL 154
Cdd:PRK09700 85 IYQELSVIDELTVLENL-YIGRHLTKKVcgvniiDWREMRVRAAMMLLRVG--LKVDLDEKVANLsishKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446051965 155 NKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKG 215
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-217 |
1.26e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.00 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSY-GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK----IKKN 81
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIF 161
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 162 LDEPTVGIDPQSRNHIFncirHLVEE---LGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:PRK10908 161 ADEPTGNLDDALSEGIL----RLFEEfnrVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-231 |
1.45e-18 |
|
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: 83.05 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL-YTERNKIKKNVSVVPQDLALYPTlTAYDN 100
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrDYTLASLRRQIGLVSQDVFLFND-TVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 101 LSFYADLYGLKGNRKKSRIKEALQF-AQLEDWAHKRID----TFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRN 175
Cdd:cd03251 96 IAYGRPGATREEVEEAARAANAHEFiMELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDEATSALDTESER 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 176 HIFNCIRHLVEelGITVIYTTHHM---EEAemlcHRVAIYDKGEILDIDTPKNLITKYG 231
Cdd:cd03251 176 LVQAALERLMK--NRTTFVIAHRLstiENA----DRIVVLEDGKIVERGTHEELLAQGG 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
1.46e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 83.16 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 1 MTDINTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTL--TLPD---EG---------YGTv 66
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGeilldgediYDP- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 67 cNYDLYTERnkikKNVSVVPQDLALYPTlTAYDNLSfyadlYGLK--GNRKKSRIKE----ALQFAQLEDWAHKRIDT-- 138
Cdd:COG1117 84 -DVDVVELR----RRVGMVFQKPNPFPK-SIYDNVA-----YGLRlhGIKSKSELDEiveeSLRKAALWDEVKDRLKKsa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 139 --FSGGMKRRinLVI--GLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELgiTVIYTTHHMEEAEMLCHRVAIYDK 214
Cdd:COG1117 153 lgLSGGQQQR--LCIarALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYL 228
|
250
....*....|....*
gi 446051965 215 GEILDIDTPKNLITK 229
Cdd:COG1117 229 GELVEFGPTEQIFTN 243
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-201 |
1.47e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 83.66 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG--------YGTVCNYDLYTERN 76
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGeilfdgenIPAMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 77 KIkknvSVVPQDLALYPTLTAYDNLSFYAdlyglkgnRKKSRIKEA---------LQFAQLEDWAHKRIDTFSGGMKRRI 147
Cdd:PRK11831 85 RM----SMLFQSGALFTDMNVFDNVAYPL--------REHTQLPAPllhstvmmkLEAVGLRGAAKLMPSELSGGMARRA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446051965 148 NLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEE 201
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPE 206
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-228 |
2.01e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.11 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 1 MTDINTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK-IK 79
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 80 KNVSVVPQDLALYPTLTAYDNLSF----YADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLN 155
Cdd:PRK10253 81 RRIGLLAQNATTPGDITVQELVARgrypHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446051965 156 KPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEA-EMLCHRVAIYDkGEILDIDTPKNLIT 228
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALRE-GKIVAQGAPKEIVT 233
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-208 |
2.55e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.13 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGD----YTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT----ERNKI 78
Cdd:PRK10584 6 IVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 K-KNVSVVPQDLALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKP 157
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446051965 158 KVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMlCHR 208
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDR 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-231 |
3.09e-18 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 82.15 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIKKNVSVVPQDLALYpTLTAYDN 100
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 101 LSFYADLYGLKgnrkksRIKEALQFAQledwAHKRI-------DT--------FSGGMKRRINLVIGLLNKPKVIFLDEP 165
Cdd:cd03252 96 IALADPGMSME------RVIEAAKLAG----AHDFIselpegyDTivgeqgagLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 166 TVGIDPQSRNHIFNCIRHLVEelGITVIYTTHHMeEAEMLCHRVAIYDKGEILDIDTPKNLITKYG 231
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA--GRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-226 |
4.40e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.47 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 25 NLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-----ERNKIKKNVSVVPQ--DLALYPTlTA 97
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkEIKPVRKKVGVVFQfpESQLFEE-TV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 98 YDNLSFYADLYGLKGNRKKSRIKEALQFAQL--EDWAHKRIDtFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRN 175
Cdd:PRK13643 103 LKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLadEFWEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446051965 176 HIFNCIRHlVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL 226
Cdd:PRK13643 182 EMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-215 |
4.49e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 13 IKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGY----GTVCNYDlyTERNKIKKNVSVVPQD 88
Cdd:PRK11288 10 IGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSilidGQEMRFA--STTAALAAGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 89 LALYPTLTAYDNLsFYADLYGLKG--NRKKSRIKEALQFAQLEDwahkRID------TFSGGMKRRINLVIGLLNKPKVI 160
Cdd:PRK11288 88 LHLVPEMTVAENL-YLGQLPHKGGivNRRLLNYEAREQLEHLGV----DIDpdtplkYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 161 FLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKG 215
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-237 |
5.79e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.11 E-value: 5.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYgTVCNYDLYTERN--KIKKNVSVVPQ--DLALYPTLTAY 98
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGE-IFYNNQAITDDNfeKLRKHIGIVFQnpDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 99 DnLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIF 178
Cdd:PRK13648 104 D-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 179 NCIRHLVEELGITVIYTTHHMEEAeMLCHRVAIYDKGEILDIDTPKNlITKYGENYLEI 237
Cdd:PRK13648 183 DLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTE-IFDHAEELTRI 239
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-231 |
6.23e-18 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 81.12 E-value: 6.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGD-YTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL--YTErNKIKKNVSV 84
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIreVTL-DSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 85 VPQDLALYPTlTAYDNLsfyadLYGlKGNRKKSRIKEALQFAQLedwaHKRIDTF---------------SGGMKRRINL 149
Cdd:cd03253 80 VPQDTVLFND-TIGYNI-----RYG-RPDATDEEVIEAAKAAQI----HDKIMRFpdgydtivgerglklSGGEKQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 150 VIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEelGITVIYTTHHMEEAeMLCHRVAIYDKGEILDIDTPKNLITK 229
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAK 225
|
..
gi 446051965 230 YG 231
Cdd:cd03253 226 GG 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-219 |
6.27e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.66 E-value: 6.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSYGDY---------TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygTVCNYD-----L 71
Cdd:PRK10419 2 TLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQG--NVSWRGeplakL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 72 YTERNK-IKKNVSVVPQDL--ALYPTLTAYDNLSF-YADLYGLKGNRKKSRIKEALQFAQLED-WAHKRIDTFSGGMKRR 146
Cdd:PRK10419 80 NRAQRKaFRRDIQMVFQDSisAVNPRKTVREIIREpLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446051965 147 INLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILD 219
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
8-229 |
6.61e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.13 E-value: 6.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDegYGTVCNYDL-YTERNK------IKK 80
Cdd:PRK13646 8 VSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPT--TGTVTVDDItITHKTKdkyirpVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 81 NVSVVPQdlalYPTLTAYDNLSFYADLYGLKG------NRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLL 154
Cdd:PRK13646 86 RIGMVFQ----FPESQLFEDTVEREIIFGPKNfkmnldEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 155 NKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITK 229
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
11-237 |
1.25e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 81.29 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 11 RYIKKSygDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERN-KIKKNVSVVPQDL 89
Cdd:PRK13642 13 KYEKES--DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 90 -ALYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVG 168
Cdd:PRK13642 91 dNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 169 IDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMlCHRVAIYDKGEILDIDTPKNLITKyGENYLEI 237
Cdd:PRK13642 171 LDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFAT-SEDMVEI 237
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-229 |
1.34e-17 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 80.11 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTtlISILSTLTLPDEGYGTVCNYDLYTERN-----KIKKNVSVVPQD--LALYPTL 95
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKS--LTCLAILGLLPPGLTQTSGEILLDGRPllplsIRGRHIATIMQNprTAFNPLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 96 TAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWA---HKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQ 172
Cdd:TIGR02770 80 TMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446051965 173 SRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEIL-------DIDTPKNLITK 229
Cdd:TIGR02770 160 NQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVergtvkeIFYNPKHETTR 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-217 |
1.42e-17 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 79.82 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 19 DYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK-IKKNVSVVPQDlalyPTLTA 97
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKyLHSKVSLVGQE----PVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 98 ---YDNLSfyadlYGLkGNRKKSRIKEALQFAQLEDWA---HKRIDT--------FSGGMKRRINLVIGLLNKPKVIFLD 163
Cdd:cd03248 102 rslQDNIA-----YGL-QSCSFECVKEAAQKAHAHSFIselASGYDTevgekgsqLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446051965 164 EPTVGIDPQSRNHIFNCIRHLVEELGITVIytTHHMEEAEMlCHRVAIYDKGEI 217
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERRTVLVI--AHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-231 |
1.80e-17 |
|
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: 79.58 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSY-GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIKKNVSVV 85
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 86 PQDLALYPTlTAYDNLSFYADlyglkgNRKKSRIKEALQFAQLEDWAHKRID-----------TFSGGMKRRINLVIGLL 154
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRP------NATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 155 NKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEelGITVIYTTHHM---EEAEmlchRVAIYDKGEILDIDTPKNLITKYG 231
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLstiKNAD----KILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
22-223 |
2.14e-17 |
|
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: 78.99 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIKKNVSVVPQDlalyPTL---TA 97
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIPQD----PTLfsgTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 98 YDNLSFYaDLYGLKGNRKKSRIKEALqfaqledwahkriDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHI 177
Cdd:cd03369 99 RSNLDPF-DEYSDEEIYGALRVSEGG-------------LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446051965 178 FNCIRhlvEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTP 223
Cdd:cd03369 165 QKTIR---EEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-202 |
3.07e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.83 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 17 YGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGY---GTVCNYD--LYTER---NKIKKNVSVVPQD 88
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFrveGKVTFHGknLYAPDvdpVEVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 89 LALYPTlTAYDNLSFYADLYGLKGNRKKsRIKEALQFAQLEDWAHKRIDT----FSGGMKRRINLVIGLLNKPKVIFLDE 164
Cdd:PRK14243 100 PNPFPK-SIYDNIAYGARINGYKGDMDE-LVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 446051965 165 PTVGIDPQSRNHIFNCIRHLVEELgiTVIYTTHHMEEA 202
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQA 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-217 |
8.74e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 8.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 24 KNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL--YTERNKIKKNVSVVPQD-----LALYPTLT 96
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPEDrqssgLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 97 ------AYDNLSFYADlyGLKGNRKKSRIKEAL--QFAQLEdwahKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVG 168
Cdd:PRK15439 360 wnvcalTHNRRGFWIK--PARENAVLERYRRALniKFNHAE----QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446051965 169 IDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-234 |
9.74e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.64 E-value: 9.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYT--VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL--YTERNkIKKNVS 83
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIadYSEAA-LRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQDLALYPTlTAYDNLSFYADlyglkgNRKKSRIKEALQFAQLEDWA--HKRIDTF--------SGGMKRRINLVIGL 153
Cdd:PRK11160 418 VVSQRVHLFSA-TLRDNLLLAAP------NASDEALIEVLQQVGLEKLLedDKGLNAWlgeggrqlSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 154 LNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEelGITVIYTTH------HMEeaemlchRVAIYDKGEILDIDTPKNLI 227
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHrltgleQFD-------RICVMDNGQIIEQGTHQELL 561
|
....*..
gi 446051965 228 TKYGENY 234
Cdd:PRK11160 562 AQQGRYY 568
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-197 |
9.89e-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: 75.56 E-value: 9.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnydlyternkikknvsvvpq 87
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 dlalypTLTAYDNLSFYadlyglkgnrkksrikealQFAQLedwahkridtfSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:cd03221 56 ------IVTWGSTVKIG-------------------YFEQL-----------SGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190
....*....|....*....|....*....|
gi 446051965 168 GIDPQSRNHIfncIRHLVEELGiTVIYTTH 197
Cdd:cd03221 100 HLDLESIEAL---EEALKEYPG-TVILVSH 125
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
13-217 |
1.07e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.53 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 13 IKKSYGDYTVIKNLSIDiRKGeIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKI-----KKNVSVVPQ 87
Cdd:PRK11144 6 FKQQLGDLCLTVNLTLP-AQG-ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRIGYVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 DLALYPTLTAYDNLsfyadLYGLKGNRKKsrikealQFA---QLEDWAH--KRID-TFSGGMKRRInlVIG--LLNKPKV 159
Cdd:PRK11144 84 DARLFPHYKVRGNL-----RYGMAKSMVA-------QFDkivALLGIEPllDRYPgSLSGGEKQRV--AIGraLLTAPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446051965 160 IFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-231 |
1.20e-16 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 80.15 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYG--DYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL--YTERNkIKKNVS 83
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLadYTLAS-LRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQDLALYPTlTAYDNLSfyadlYGLKGNRKKSRIKEALQFAQLEDWAHKR---IDT--------FSGGMKRRINLVIG 152
Cdd:TIGR02203 410 LVSQDVVLFND-TIANNIA-----YGRTEQADRAEIERALAAAYAQDFVDKLplgLDTpigengvlLSGGQRQRLAIARA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 153 LLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEelGITVIYTTHHM---EEAEmlchRVAIYDKGEILDIDTPKNLITK 229
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLstiEKAD----RIVVMDDGRIVERGTHNELLAR 557
|
..
gi 446051965 230 YG 231
Cdd:TIGR02203 558 NG 559
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-213 |
1.32e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.55 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG----YGTVCNYDLYTERNKIKKN-VSVVPQDLALYPTLT 96
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdvifNGQPMSKLSSAAKAELRNQkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 97 AYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNH 176
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 446051965 177 IFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYD 213
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRD 220
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
22-209 |
1.67e-16 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 77.05 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKI---------KKNVSVVPQDLALY 92
Cdd:TIGR02324 23 VLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGAWVDLAQAsprevlevrRKTIGYVSQFLRVI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 93 PTLTAYDNLSFYADLYGLkgNRKKSRIKEALQFAQLED----WaHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVG 168
Cdd:TIGR02324 103 PRVSALEVVAEPLLERGV--PREAARARARELLARLNIperlW-HLPPATFSGGEQQRVNIARGFIADYPILLLDEPTAS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446051965 169 IDPQSRnhifNCIRHLVEEL---GITVIYTTHHMEEAEMLCHRV 209
Cdd:TIGR02324 180 LDAANR----QVVVELIAEAkarGAALIGIFHDEEVRELVADRV 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
8-234 |
1.75e-16 |
|
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: 77.19 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSygDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGT-----VCNYDLYTERNKIkknv 82
Cdd:cd03249 6 VSFRYPSRP--DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldgvdIRDLNLRWLRSQI---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVVPQDLALYPTlTAYDNLsfyadLYGlKGNRKKSRIKEALQFAQledwAHKRIDTF---------------SGGMKRRI 147
Cdd:cd03249 80 GLVSQEPVLFDG-TIAENI-----RYG-KPDATDEEVEEAAKKAN----IHDFIMSLpdgydtlvgergsqlSGGQKQRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 148 NLVIGLLNKPKVIFLDEPTVGIDPQSrnhifnciRHLVEE------LGITVIYTTHHM---EEAEmlchRVAIYDKGEIL 218
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAES--------EKLVQEaldramKGRTTIVIAHRLstiRNAD----LIAVLQNGQVV 216
|
250
....*....|....*.
gi 446051965 219 DIDTPKNLITKYGENY 234
Cdd:cd03249 217 EQGTHDELMAQKGVYA 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-223 |
2.06e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.34 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygTVCNYDLYTER---NKI-KKN 81
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGG--TILLRGQHIEGlpgHQIaRMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVVPQDLALYPTLTAYDNL----------SFYADLYGLKGNRKKSRikEALQFAQ-------LEDWAHKRIDTFSGGMK 144
Cdd:PRK11300 82 VVRTFQHVRLFREMTVIENLlvaqhqqlktGLFSGLLKTPAFRRAES--EALDRAAtwlervgLLEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 145 RRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTP 223
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-219 |
2.14e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.36 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 13 IKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTliSILSTLTL-PDEGYGTVCNYDLYTERNK----IKKNVSVVPQ 87
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKST--TGLALLRLiNSQGEIWFDGQPLHNLNRRqllpVRHRIQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 D--LALYPTLTAydnLSFYADlyGLKGNRK-------KSRIKEALQFAQLE-DWAHKRIDTFSGGMKRRINLVIGLLNKP 157
Cdd:PRK15134 370 DpnSSLNPRLNV---LQIIEE--GLRVHQPtlsaaqrEQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446051965 158 KVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILD 219
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-246 |
4.93e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 76.71 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 25 NLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLY-TERNK----IKKNVSVVPQdlalYPTL---- 95
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITsTSKNKdikqIRKKVGLVFQ----FPESqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 96 -TAYDNLSFYADLYGLKGNRKKSRIKEALQFAQL-EDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQS 173
Cdd:PRK13649 101 eTVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 174 RNHIFNCIRHLvEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNL----------------ITKYGENYLE- 236
Cdd:PRK13649 181 RKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIfqdvdfleekqlgvpkITKFAQRLADr 259
|
250
....*....|....
gi 446051965 237 -IVISNIP---EEF 246
Cdd:PRK13649 260 gISFSSLPitiEEF 273
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-227 |
5.76e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.36 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 21 TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNK-IKKNVSVVPQDLALYPTLT--- 96
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKaFARKVAYLPQQLPAAEGMTvre 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 97 --AYDNLSFYADLyGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSR 174
Cdd:PRK10575 105 lvAIGRYPWHGAL-GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446051965 175 NHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLI 227
Cdd:PRK10575 184 VDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
12-232 |
1.73e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 76.85 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 12 YIKKSYGDY-TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEgyGTVcnydlyternKIKKNVSVVPQDLA 90
Cdd:PRK13545 28 FFRSKDGEYhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNK--GTV----------DIKGSAALIAISSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 91 LYPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGID 170
Cdd:PRK13545 96 LNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446051965 171 PQSRNhifNCIRHLVE--ELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKYGE 232
Cdd:PRK13545 176 QTFTK---KCLDKMNEfkEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-220 |
2.63e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.43 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT----ERNKIKKNVSVVPQD--LALYPTLT 96
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQDpyASLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 97 AYDNLSFYADLYGL-KGNRKKSRIKEALQFAQLE-DWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSR 174
Cdd:PRK10261 420 VGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446051965 175 NHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDI 220
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-219 |
4.29e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 73.67 E-value: 4.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 4 INTMISIRYIKKSYGDYT---------VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL--- 71
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 72 -YTERNKikkNVSVVPQD--LALYPTLTAYDNLSFYADL-YGLKGNRKKSRIKEAL-QFAQLEDWAHKRIDTFSGGMKRR 146
Cdd:PRK15112 81 dYSYRSQ---RIRMIFQDpsTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLrQVGLLPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446051965 147 INLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILD 219
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-254 |
4.45e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.50 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDegYGTVCNYDLYT-------------E 74
Cdd:PRK13631 27 LYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSK--YGTIQVGDIYIgdkknnhelitnpY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 75 RNKIK------KNVSVVPQ--DLALYPTlTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQL-EDWAHKRIDTFSGGMKR 145
Cdd:PRK13631 105 SKKIKnfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 146 RINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKN 225
Cdd:PRK13631 184 RVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYE 262
|
250 260
....*....|....*....|....*....
gi 446051965 226 LITKygenyleivisnipEEFIHKTKMIV 254
Cdd:PRK13631 263 IFTD--------------QHIINSTSIQV 277
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-217 |
4.73e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.08 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 27 SIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDlYTERNKIKKNVSVVPQDLALYPTLTAYDNLSFYAD 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 107 LyGLKGNrkksrikeALQFAQLEDWAHK-RIDTF--------SGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHI 177
Cdd:PRK10771 98 P-GLKLN--------AAQREKLHAIARQmGIEDLlarlpgqlSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446051965 178 FNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-198 |
5.32e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.23 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 21 TVIKNLSIDIRKGEiiGLL--GPNGAGKTTLISILS--------TLTLPDEGygtvcnydlyternkikkNVSVVPQ--- 87
Cdd:COG4178 377 PLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAglwpygsgRIARPAGA------------------RVLFLPQrpy 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 -------DLALYP-TLTAYDNlsfyadlyglkgnrkkSRIKEALQFAQLEDWAHkRIDT-------FSGGMKRRINLVIG 152
Cdd:COG4178 437 lplgtlrEALLYPaTAEAFSD----------------AELREALEAVGLGHLAE-RLDEeadwdqvLSLGEQQRLAFARL 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446051965 153 LLNKPKVIFLDEPTVGIDPQSRNHIFnciRHLVEEL-GITVIYTTHH 198
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALY---QLLREELpGTTVISVGHR 543
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-231 |
6.19e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 75.14 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIKKNVSVVPQDLALYpTLTAYDN 100
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLF-SGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 101 LsfyadLYGLkgnrkKSRIKEALQFAQLEDWAHKRIDTF---------------SGGMKRRINLVIGLLNKPKVIFLDEP 165
Cdd:TIGR00958 575 I-----AYGL-----TDTPDEEIMAAAKAANAHDFIMEFpngydtevgekgsqlSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 166 TVGIDPQsrnhifncIRHLVEEL----GITVIYTTHHMEEAEMlCHRVAIYDKGEILDIDTPKNLITKYG 231
Cdd:TIGR00958 645 TSALDAE--------CEQLLQESrsraSRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-193 |
9.13e-15 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 71.52 E-value: 9.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 10 IRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLisiLSTLTLPDEGYGTV------CNYDLYTERNKIKKNVS 83
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTL---LKALANRTEGNVSVegdihyNGIPYKEFAEKYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQDLALYPTLTAYDNLSFYADLyglKGNrkksrikealQFaqledwahkrIDTFSGGMKRRINLVIGLLNKPKVIFLD 163
Cdd:cd03233 87 YVSEEDVHFPTLTVRETLDFALRC---KGN----------EF----------VRGISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190
....*....|....*....|....*....|
gi 446051965 164 EPTVGIDPQSRNHIFNCIRHLVEELGITVI 193
Cdd:cd03233 144 NSTRGLDSSTALEILKCIRTMADVLKTTTF 173
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-218 |
1.34e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 20 YTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyteRNKIKKN-VSVVPQDLAL---YPTL 95
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNlVAYVPQSEEVdwsFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 96 TA-YDNLSFYADLYGLKGNRKKSR--IKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQ 172
Cdd:PRK15056 97 VEdVVMMGRYGHMGWLRRAKKRDRqiVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446051965 173 SRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLC-HRVAIydKGEIL 218
Cdd:PRK15056 177 TEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCdYTVMV--KGTVL 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-170 |
1.93e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.43 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG---YG-TVcnydlyternkikk 80
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGtieIGeTV-------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 81 NVSVVPQDL-ALYPTLTAYDNLSFYADLYGLkGNRK-KSR-------IKEALQfaqledwaHKRIDTFSGGMKRRINLVI 151
Cdd:TIGR03719 386 KLAYVDQSRdALDPNKTVWEEISGGLDIIKL-GKREiPSRayvgrfnFKGSDQ--------QKKVGQLSGGERNRVHLAK 456
|
170
....*....|....*....
gi 446051965 152 GLLNKPKVIFLDEPTVGID 170
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLD 475
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-197 |
2.34e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.30 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSYGDYTviknLSID---IRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnyDLYTErnkIKknV 82
Cdd:PRK13409 339 TLVEYPDLTKKLGDFS----LEVEggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG-------EVDPE---LK--I 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVVPQDLALYPTLTAYDNLSFYADLYGlkGNRKKSRIKEALQFAQLEDwahKRIDTFSGGMKRRINLVIGLLNKPKVIFL 162
Cdd:PRK13409 403 SYKPQYIKPDYDGTVEDLLRSITDDLG--SSYYKSEIIKPLQLERLLD---KNVKDLSGGELQRVAIAACLSRDADLYLL 477
|
170 180 190
....*....|....*....|....*....|....*
gi 446051965 163 DEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTH 197
Cdd:PRK13409 478 DEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDH 512
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-231 |
2.49e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 73.62 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 2 TDINTMISIRYIKKSYG-DYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIK 79
Cdd:TIGR01193 468 NNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 80 KNVSVVPQDLALYpTLTAYDNLsfyadLYGLKGNRKKSRIKEALQFAQLED-------WAHKRID----TFSGGMKRRIN 148
Cdd:TIGR01193 548 QFINYLPQEPYIF-SGSILENL-----LLGAKENVSQDEIWAACEIAEIKDdienmplGYQTELSeegsSISGGQKQRIA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 149 LVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElgiTVIYTTHHMEEAEMlCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLD 697
|
...
gi 446051965 229 KYG 231
Cdd:TIGR01193 698 RNG 700
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-198 |
3.43e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.98 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnyDLYTERNKIKKNVSVVP 86
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKG-------EILFERQSIKKDLCTYQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 87 QDL-------ALYPTLTAYDNLsfYADLYGLKGNRKksrIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKV 159
Cdd:PRK13540 74 KQLcfvghrsGINPYLTLRENC--LYDIHFSPGAVG---ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 446051965 160 IFLDEPTVGIDPQSRNHIFNCIRHLVEELGiTVIYTTHH 198
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKGG-AVLLTSHQ 186
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-234 |
1.03e-13 |
|
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: 71.90 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGY-----GTVCNYDLYTERNKIkknvSVVPQDLALYP-TL 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEiiidgLNIAKIGLHDLRFKI----TIIPQDPVLFSgSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 96 TA-YDNLSFYADlyglkgnrkkSRIKEALQFAQLEDWAHKRID-----------TFSGGMKRRINLVIGLLNKPKVIFLD 163
Cdd:TIGR00957 1377 RMnLDPFSQYSD----------EEVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446051965 164 EPTVGIDPQSRNHIFNCIRHLVEElgITVIYTTHHMEEAeMLCHRVAIYDKGEILDIDTPKNLITKYGENY 234
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTI-MDYTRVIVLDKGEVAEFGAPSNLLQQRGIFY 1514
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-216 |
1.37e-13 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 68.26 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 9 SIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLIS-ILSTLTLPDegyGTVCnydlyternkIKKNVSVVPQ 87
Cdd:cd03250 7 SFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLS---GSVS----------VPGSIAYVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 dlalYPTL---TAYDNLSFYADLYglkgnrkKSRIKEALQFAQLEdwahKRIDTF---------------SGGMKRRINL 149
Cdd:cd03250 74 ----EPWIqngTIRENILFGKPFD-------EERYEKVIKACALE----PDLEILpdgdlteigekginlSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446051965 150 VIGLLNKPKVIFLDEPTVGIDPQSRNHIF-NCIRHLVEElGITVIYTTHHMEEAEmLCHRVAIYDKGE 216
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLN-NKTRILVTHQLQLLP-HADQIVVLDNGR 204
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-206 |
1.37e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 11 RYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLtLPdegYGTvcnYD-----------LYTERNKIK 79
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YP---HGT---YEgeiifegeelqASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 80 KNVSVVPQDLALYPTLTAYDNLsFYADLYGLKG----NRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLN 155
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENI-FLGNEITPGGimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446051965 156 KPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLC 206
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAIS 210
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-197 |
1.86e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 67.65 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 12 YIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILStltlpDEGYGTVCNYDLYTERNKIKKN----VSVVPQ 87
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA-----GRKTAGVITGEILINGRPLDKNfqrsTGYVEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 88 DLALYPTLTAYDNLSFYADLYGLkgnrkksrikealqfaQLEDwahkridtfsggmKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:cd03232 87 QDVHSPNLTVREALRFSALLRGL----------------SVEQ-------------RKRLTIGVELAAKPSILFLDEPTS 137
|
170 180 190
....*....|....*....|....*....|
gi 446051965 168 GIDPQSRNHIFNCIRHLVEElGITVIYTTH 197
Cdd:cd03232 138 GLDSQAAYNIVRFLKKLADS-GQAILCTIH 166
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-197 |
2.05e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.95 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 16 SYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIKKNVSVVPqdlALYPT 94
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMAYLGHLP---GLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 95 LTAYDNLSFyadLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSR 174
Cdd:PRK13543 97 LSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
|
170 180
....*....|....*....|...
gi 446051965 175 NHIFNCIRHLVEELGITVIyTTH 197
Cdd:PRK13543 174 TLVNRMISAHLRGGGAALV-TTH 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-244 |
2.26e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.78 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIKKNVSVVPQDLALYPTLTAY-- 98
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLFSGTVRFni 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 99 DNLSFYADLyGLKGNRKKSRIKEALQFAQ--LEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNH 176
Cdd:PLN03232 1331 DPFSEHNDA-DLWEALERAHIKDVIDRNPfgLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446051965 177 IFNCIRhlvEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKYGENYLEIVISNIPE 244
Cdd:PLN03232 1410 IQRTIR---EEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPA 1474
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-198 |
2.40e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 66.79 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 21 TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLtlpdegygtvcnYDLYTERNKI--KKNVSVVPQDlalyPTLTAy 98
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL------------WPWGSGRIGMpeGEDLLFLPQR----PYLPL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 99 dnlsfyadlyglkGNrkksrIKEALQFAqledWAhkriDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIF 178
Cdd:cd03223 78 -------------GT-----LREQLIYP----WD----DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170 180
....*....|....*....|
gi 446051965 179 NcirhLVEELGITVIYTTHH 198
Cdd:cd03223 132 Q----LLKELGITVISVGHR 147
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
14-230 |
4.01e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 68.30 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 14 KKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnydlyternKIKKN--VSVVPQDLAL 91
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG--------------KVDRNgeVSVIAISAGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 92 YPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEP-TVGid 170
Cdd:PRK13546 97 SGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVG-- 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446051965 171 pqSRNHIFNCIRHLVE--ELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKY 230
Cdd:PRK13546 175 --DQTFAQKCLDKIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-226 |
4.41e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.29 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 21 TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL--YTERNKIKKNVSVVPQD---LALYPTL 95
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItgLSPRERRRLGVAYIPEDrlgRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 96 TAYDNLSFyaDLYGLKGNRKKSRIKealqFAQLEDWAHKRIDTF--------------SGGmkrriN---LVIG--LLNK 156
Cdd:COG3845 352 SVAENLIL--GRYRRPPFSRGGFLD----RKAIRAFAEELIEEFdvrtpgpdtparslSGG-----NqqkVILAreLSRD 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446051965 157 PKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVA-IYDkGEILDIDTPKNL 226
Cdd:COG3845 421 PKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAvMYE-GRIVGEVPAAEA 489
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-197 |
4.62e-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: 69.43 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 2 TDINTMISIRYIKKSYGDYTviknLSID---IRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcNYDLyternKI 78
Cdd:COG1245 336 KEEETLVEYPDLTKSYGGFS----LEVEggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG-----EVDE-----DL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 KknVSVVPQDLALYPTLTAYDNL-SFYADLYGlkGNRKKSRIKEALqfaQLEDWAHKRIDTFSGGMKRRINLVIGLLNKP 157
Cdd:COG1245 402 K--ISYKPQYISPDYDGTVEEFLrSANTDDFG--SSYYKTEIIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDA 474
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446051965 158 KVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTH 197
Cdd:COG1245 475 DLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDH 514
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
13-216 |
6.09e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.99 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 13 IKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG----YGTVCNYDlyTERNKIKKNVSVVPQD 88
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGsilfQGKEIDFK--SSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 89 LALYPTLTAYDNLsfYADLYGLKG----NRKKSRIKEALqFAQLE---DwAHKRIDTFSGGMKRRINLVIGLLNKPKVIF 161
Cdd:PRK10982 82 LNLVLQRSVMDNM--WLGRYPTKGmfvdQDKMYRDTKAI-FDELDidiD-PRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 162 LDEPTVGIDPQSRNHIFNCIRHLvEELGITVIYTTHHMEEAEMLCHRVAIYDKGE 216
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-209 |
1.57e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 65.92 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSY-----GDYT--VIKNLSIDIRKGEIIGLLGPNGAGKTTLI-SILSTLtLPDEG-------YGTVcny 69
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLkCIYGNY-LPDSGsilvrhdGGWV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 70 DLYT--ERNKI---KKNVSVVPQDLALYPTLTAYDnlsFYAD-LYGLKGNRKKSRIKEALQFAQLedwahkRID------ 137
Cdd:COG4778 78 DLAQasPREILalrRRTIGYVSQFLRVIPRVSALD---VVAEpLLERGVDREEARARARELLARL------NLPerlwdl 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446051965 138 ---TFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRnhifNCIRHLVEEL---GITVIYTTHHMEEAEMLCHRV 209
Cdd:COG4778 149 ppaTFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANR----AVVVELIEEAkarGTAIIGIFHDEEVREAVADRV 222
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-166 |
2.35e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEgyGTVcnydlyternKIKKNVSV 84
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDS--GTI----------KIGETVKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 85 --VPQ--DlALYPTLTAYDNLSFYADLYGLkGNRK-KSR-------IKEALQfaqledwaHKRIDTFSGGMKRRINLVIG 152
Cdd:PRK11819 390 ayVDQsrD-ALDPNKTVWEEISGGLDIIKV-GNREiPSRayvgrfnFKGGDQ--------QKKVGVLSGGERNRLHLAKT 459
|
170
....*....|....
gi 446051965 153 LLNKPKVIFLDEPT 166
Cdd:PRK11819 460 LKQGGNVLLLDEPT 473
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-219 |
3.00e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.89 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 21 TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGY---GTVC--NYDLYTERN--KIKKNVSVVPQDLALYP 93
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysGDVLlgGRSIFNYRDvlEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 94 tLTAYDNLsfyadLYGLKGNR----------KKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLD 163
Cdd:PRK14271 115 -MSIMDNV-----LAGVRAHKlvprkefrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 164 EPTVGIDPQSRNHIFNCIRHLVEELgiTVIYTTHHMEEAEMLCHRVAIYDKGEILD 219
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-217 |
4.46e-12 |
|
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: 66.25 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 14 KKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLisilsTLTL----PDEGYGTVCNYDLYT----ERNKIKKNVSVV 85
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTL-----GLALlrliPSEGEIRFDGQDLDGlsrrALRPLRRRMQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 86 PQD--LALYPTLTAYD----NLSFYADlyGLKGNRKKSRIKEALQFAQL-EDWAHKRIDTFSGGMKRRINLVIGLLNKPK 158
Cdd:COG4172 368 FQDpfGSLSPRMTVGQiiaeGLRVHGP--GLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:COG4172 446 LLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-200 |
4.57e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 21 TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISIL--STLTLPDEGYGTVcnydlytERNKIKKNVSVVPQDLALYPTLTAy 98
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDV-------PDNQFGREASLIDAIGRKGDFKDA- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 99 dnlsfyadlyglkgnrkksriKEALQFAQLED-WAHKR-IDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQ---- 172
Cdd:COG2401 116 ---------------------VELLNAVGLSDaVLWLRrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtakr 174
|
170 180
....*....|....*....|....*....
gi 446051965 173 -SRNhifncIRHLVEELGITVIYTTHHME 200
Cdd:COG2401 175 vARN-----LQKLARRAGITLVVATHHYD 198
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-217 |
5.39e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTlTLPDEGYGTVC----NYDLYTERNKIKKNVSVVPQDL---ALYP- 93
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRWEGEIFidgkPVKIRNPQQAIAQGIAMVPEDRkrdGIVPv 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 94 -------TLTAYDNLSfyadlyglkgnrKKSRIKEALQFAQLEDWAHK----------RIDTFSGGMKRRINLVIGLLNK 156
Cdd:PRK13549 356 mgvgkniTLAALDRFT------------GGSRIDDAAELKTILESIQRlkvktaspelAIARLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446051965 157 PKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-240 |
6.36e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.30 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIKKNVSVVPQDLALYpTLTAYDN 100
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQAPVLF-SGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 101 LSFY-----ADLYglkgnrkksrikEALQFAQLEDWAHKRI-----------DTFSGGMKRRINLVIGLLNKPKVIFLDE 164
Cdd:PLN03130 1333 LDPFnehndADLW------------ESLERAHLKDVIRRNSlgldaevseagENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 165 PTVGIDPQSRNHIFNCIRhlvEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKYGENYLEIVIS 240
Cdd:PLN03130 1401 ATAAVDVRTDALIQKTIR---EEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS 1473
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-217 |
8.64e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 65.62 E-value: 8.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTlTLPDEGYGTVC----NYDLYTERNKIKKNVSVVPQDL---ALYPTL 95
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFEGNVFingkPVDIRNPAQAIRAGIAMVPEDRkrhGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 96 TAYDNLSfyadLYGLKGNRKKSRIKEALQFaQLEDWAHKR-----------IDTFSGGMKRRINLVIGLLNKPKVIFLDE 164
Cdd:TIGR02633 355 GVGKNIT----LSVLKSFCFKMRIDAAAEL-QIIGSAIQRlkvktaspflpIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446051965 165 PTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-209 |
1.09e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.75 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 18 GDYTVIKNLSIDIRKGEIIGLLGPNGAGKT----TLISILST---------------LTLPDegygtvcnydlyTERNKI 78
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAAngriggsatfngreiLNLPE------------KELNKL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 K-KNVSVVPQD--LALYPTLTAYDNLSFYADLYglKGNRKKSRIKEALQF--AQLEDWAHKRIDT----FSGGMKRRINL 149
Cdd:PRK09473 95 RaEQISMIFQDpmTSLNPYMRVGEQLMEVLMLH--KGMSKAEAFEESVRMldAVKMPEARKRMKMypheFSGGMRQRVMI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 150 VIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRV 209
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKV 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-245 |
1.17e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 19 DYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL--YTERNKIKKNVSVVPQ---DLALYP 93
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITEsrrDNGFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 94 TLTAYDNLSF--------YADLYGLKGNRKKSRIKEAlqfaQLEDWAHK------RIDTFSGGMKRRINLVIGLLNKPKV 159
Cdd:PRK09700 355 NFSIAQNMAIsrslkdggYKGAMGLFHEVDEQRTAEN----QRELLALKchsvnqNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 160 IFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKYgenylEIVI 239
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE-----EIMA 504
|
....*.
gi 446051965 240 SNIPEE 245
Cdd:PRK09700 505 WALPQE 510
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-228 |
1.18e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 19 DYTVIKNLSIDIRKGEIIGLLGPNGAGKT-TLISILSTLTLPDEGY---------GTVCNYDLYTERNKIKKNVSVVPQD 88
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVVYpsgdirfhgESLLHASEQTLRGVRGNKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 89 --LALYPTLTA----YDNLSFYadlyglKGNRKKSRIKEAL---------QFAQ-LEDWAHKridtFSGGMKRRINLVIG 152
Cdd:PRK15134 101 pmVSLNPLHTLekqlYEVLSLH------RGMRREAARGEILncldrvgirQAAKrLTDYPHQ----LSGGERQRVMIAMA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 153 LLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
15-213 |
2.28e-11 |
|
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: 61.43 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 15 KSYGDYTVIKNLSiDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYgtvCNYDLYTernkikknVSVVPQdlalypt 94
Cdd:cd03222 8 KRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN---DEWDGIT--------PVYKPQ------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 95 ltaydnlsfYADLyglkgnrkksrikealqfaqledwahkridtfSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSR 174
Cdd:cd03222 69 ---------YIDL--------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQR 107
|
170 180 190
....*....|....*....|....*....|....*....
gi 446051965 175 NHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYD 213
Cdd:cd03222 108 LNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-197 |
2.28e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.19 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 4 INTMISIRyikKSY-GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTL-------TLPDEGYgtvcnydlyter 75
Cdd:TIGR03719 4 IYTMNRVS---KVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkdfngeARPQPGI------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 76 nkikkNVSVVPQDLALYPTLTAYDN-----------LSFYADLYGLKGN---------RKKSRIKEALQFAQLEDWAHK- 134
Cdd:TIGR03719 69 -----KVGYLPQEPQLDPTKTVRENveegvaeikdaLDRFNEISAKYAEpdadfdklaAEQAELQEIIDAADAWDLDSQl 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446051965 135 --------------RIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSrnhIFNCIRHLVEELGiTVIYTTH 197
Cdd:TIGR03719 144 eiamdalrcppwdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPG-TVVAVTH 216
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
8-229 |
2.42e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 62.95 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKksyGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLtLPDEGYGTV--CNYDLYTERnKIKKNVSVV 85
Cdd:cd03289 8 LTAKYTE---GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIdgVSWNSVPLQ-KWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 86 PQDLALYpTLTAYDNLsfyaDLYGLKGNRKKSRIKEAL-------QFA-----QLEDWAHkridTFSGGMKRRINLVIGL 153
Cdd:cd03289 83 PQKVFIF-SGTFRKNL----DPYGKWSDEEIWKVAEEVglksvieQFPgqldfVLVDGGC----VLSHGHKQLMCLARSV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 154 LNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEelGITVIYTTHHMeEAEMLCHRVAIYDKGEILDIDTPKNLITK 229
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-244 |
3.06e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.11 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTtlISILSTLTLPDEGYGTV-CNYDLYTERNK--IKKNVSVVPQ-------DLA-- 90
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKS--VTALALMRLLEQAGGLVqCDKMLLRRRSRqvIELSEQSAAQmrhvrgaDMAmi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 91 -------LYPTLTAYDNLSFYADLY-GLKGNRKKSRIKEALQFAQLEDwAHKRIDTF----SGGMKRRINLVIGLLNKPK 158
Cdd:PRK10261 110 fqepmtsLNPVFTVGEQIAESIRLHqGASREEAMVEAKRMLDQVRIPE-AQTILSRYphqlSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLITKYGENYLEIV 238
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRAL 268
|
....*.
gi 446051965 239 ISNIPE 244
Cdd:PRK10261 269 LAAVPQ 274
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
27-211 |
4.30e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.83 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 27 SIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGY----GTvcnyDLYT----ERNKIKKNVSVVPQD--LALYPTLT 96
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEilfdGQ----DITGlsgrELRPLRRRMQMVFQDpyASLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 97 AYDNLSFYADLYGLK-GNRKKSRIKEALQFAQL-EDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPT----VGID 170
Cdd:COG4608 114 VGDIIAEPLRIHGLAsKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVsaldVSIQ 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446051965 171 PQsrnhIFNCIRHLVEELGITVIYTTH------HMeeaemlCHRVAI 211
Cdd:COG4608 194 AQ----VLNLLEDLQDELGLTYLFISHdlsvvrHI------SDRVAV 230
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-198 |
4.40e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.75 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 21 TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERnKIKKNVSVVPQDLALYPTLTAYDN 100
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTK-QILKRTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 101 LSFYADLYGLKGNRKKSRIKEA------LQFAQLEDW--AHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQ 172
Cdd:PLN03211 161 LVFCSLLRLPKSLTKQEKILVAesviseLGLTKCENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180
....*....|....*....|....*.
gi 446051965 173 SRNHIFNCIRHLVEElGITVIYTTHH 198
Cdd:PLN03211 241 AAYRLVLTLGSLAQK-GKTIVTSMHQ 265
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-239 |
1.03e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.72 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 26 LSIDIRKGEIIGLLGPNGAGKTTLISILSTLTlpdEGYGTVCNYDlyternkikKNVSVVPQ-DLALYptlTAY----DN 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL---PGSGSIQFAG---------QPLEAWSAaELARH---RAYlsqqQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 101 LSF------YADLYGLKGNRK---KSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLL-----NKP--KVIFLDE 164
Cdd:PRK03695 80 PPFampvfqYLTLHQPDKTRTeavASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 165 PTVGIDPQSRNHIFNCIRHLVeELGITVI-------YTTHHMEEAEMLCHRVAIYdKGEILDIDTPKNLITKYGENYLEI 237
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELC-QQGIAVVmsshdlnHTLRHADRVWLLKQGKLLA-SGRRDEVLTPENLAQVFGVNFRRL 237
|
..
gi 446051965 238 VI 239
Cdd:PRK03695 238 DV 239
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-170 |
1.74e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.52 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYT-ERNKIKKNVSVVPQDLALYpTLTAYDNL 101
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLF-NRSIEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 102 SFyadlyGlKGNRKKSRIKEALQFAQLEDWAHKRIDTF-----------SGGMKRRINLVIGLLNKPKVIFLDEPTVGID 170
Cdd:PRK13657 430 RV-----G-RPDATDEEMRAAAERAQAHDFIERKPDGYdtvvgergrqlSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-217 |
2.37e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 27 SIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCN--YDLYTERNKIKKNVSVVPQD---LALYPTLTAYDNL 101
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGIMLCPEDrkaEGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 102 SFYADLYGLKG----NRKKSRIKEALQFAQLE---DWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSR 174
Cdd:PRK11288 353 NISARRHHLRAgcliNNRWEAENADRFIRSLNiktPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAK 432
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446051965 175 NHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:PRK11288 433 HEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-229 |
3.48e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.08 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 13 IKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLtLPDEGYGTV--CNYDLYTERnKIKKNVSVVPQDLA 90
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIdgVSWNSVTLQ-TWRKAFGVIPQKVF 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 91 LYpTLTAYDNLSFY-----------ADLYGLkgnrkKSRIKE---ALQFaQLEDWAHkridTFSGGMKRRINLVIGLLNK 156
Cdd:TIGR01271 1303 IF-SGTFRKNLDPYeqwsdeeiwkvAEEVGL-----KSVIEQfpdKLDF-VLVDGGY----VLSNGHKQLMCLARSILSK 1371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446051965 157 PKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElgITVIYTTHHMeEAEMLCHRVAIYDKGEILDIDTPKNLITK 229
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTLKQSFSN--CTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-217 |
6.81e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.86 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 16 SYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLtLPDEGYGTVCNYDLYT-ERNKIKKNVSVVPQDlalyPT 94
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRElDPESWRKHLSWVGQN----PQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 95 L---TAYDNLsfyadLYGlKGNRKKSRIKEALQFAQLEDWAHKR---IDT--------FSGGMKRRINLVIGLLNKPKVI 160
Cdd:PRK11174 434 LphgTLRDNV-----LLG-NPDASDEQLQQALENAWVSEFLPLLpqgLDTpigdqaagLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446051965 161 FLDEPTVGIDPQSRNHIFNCIRHLVEelGITVIYTTHHMEEAEMlCHRVAIYDKGEI 217
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-228 |
1.49e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.91 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 21 TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILS-TLTLPDEGYGTVCNYDLY--------TERNKIKKNVSVVPQD--- 88
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAPRGARVTGDVTlngeplaaIDAPRLARLRAVLPQAaqp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 89 -----------LALYPtltaydnlsfYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGL---- 153
Cdd:PRK13547 95 afafsareivlLGRYP----------HARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 154 -----LNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-217 |
1.61e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 16 SYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILsTLTLPdEGYGTvcNYDLYTERN-------KIKKNVSVVPQD 88
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-TGDHP-QGYSN--DLTLFGRRRgsgetiwDIKKHIGYVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 89 LAL-YPTLTAYDN--LSFYAD---LYGLKGNRKKSRIKEALQFAQLEDW-AHKRIDTFSGGMKRRINLVIGLLNKPKVIF 161
Cdd:PRK10938 345 LHLdYRVSTSVRNviLSGFFDsigIYQAVSDRQQKLAQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLLI 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446051965 162 LDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEA-EMLCHRVAIYDKGEI 217
Cdd:PRK10938 425 LDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDApACITHRLEFVPDGDI 481
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-231 |
2.21e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 56.77 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 26 LSIDIRKGEIIGLLGPNGAGKTTLISILSTLtLPDEGygtvcnydlyternkikkNVSVVPQDLALYPT-----LTAY-- 98
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQG------------------EILLNGRPLSDWSAaelarHRAYls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 99 --DNLSF------YADLYGLKGNRKKSRIKEALQFA---QLEDWAHKRIDTFSGGMKRRINLVIGLLN-------KPKVI 160
Cdd:COG4138 76 qqQSPPFampvfqYLALHQPAGASSEAVEQLLAQLAealGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 161 FLDEPTVGIDpqsrnhifncIRH------LVEEL---GITVIYTTHHMEEAEMLCHRVAIYDKGEIL------DIDTPKN 225
Cdd:COG4138 156 LLDEPMNSLD----------VAQqaaldrLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVasgetaEVMTPEN 225
|
....*.
gi 446051965 226 LITKYG 231
Cdd:COG4138 226 LSEVFG 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-166 |
2.53e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 16 SYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGY---------------------GTVCNY----- 69
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRiiyeqdlivarlqqdpprnveGTVYDFvaegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 70 ----DLYTERNKIKKNVSVVPQDLALYPTLTAYDNLSfYADLYGLkgnrkKSRIKEALqfAQLEDWAHKRIDTFSGGMKR 145
Cdd:PRK11147 92 eeqaEYLKRYHDISHLVETDPSEKNLNELAKLQEQLD-HHNLWQL-----ENRINEVL--AQLGLDPDAALSSLSGGWLR 163
|
170 180
....*....|....*....|.
gi 446051965 146 RINLVIGLLNKPKVIFLDEPT 166
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPT 184
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-197 |
6.52e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 13 IKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTlpDEGYGTvcnydlYTER--NKIKKNVS------- 83
Cdd:TIGR00956 769 VKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVIT------GGDRlvNGRPLDSSfqrsigy 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQDLALyPTLTAYDNLSFYADLYGLKGNRKKSR---IKEALQFAQLEDWAHKRIDTFSGGM--KRRINLVIG--LLNK 156
Cdd:TIGR00956 841 VQQQDLHL-PTSTVRESLRFSAYLRQPKSVSKSEKmeyVEEVIKLLEMESYADAVVGVPGEGLnvEQRKRLTIGveLVAK 919
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446051965 157 PK-VIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTH 197
Cdd:TIGR00956 920 PKlLLFLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIH 960
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-217 |
6.66e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTlTLPDEGyGTVcnydlyTERNKIKKNVSvvPQD-LA----------- 90
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYG-ALPRTS-GYV------TLDGHEVVTRS--PQDgLAngivyisedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 91 ---LYPTLTAYDNLSFYADLYGlkgNRKKSRIKEALQFAQLEDW----------AHKRIDTFSGGMKRRINLVIGLLNKP 157
Cdd:PRK10762 338 rdgLVLGMSVKENMSLTALRYF---SRAGGSLKHADEQQAVSDFirlfniktpsMEQAIGLLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 158 KVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-217 |
7.57e-09 |
|
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: 56.62 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 21 TVIKNLSIDIRKGEIIGLLGPNGAGKTtlISILSTLTL-PDEG---YGTVC--NYDLYT----ERNKIKKN-VSVVPQD- 88
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKS--VTALSILRLlPDPAahpSGSILfdGQDLLGlserELRRIRGNrIAMIFQEp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 89 -LALYPTLTA----YDNLSFYAdlyGLKGNRKKSRIKEALQFAQLEDwAHKRIDTF----SGGMKRRINLVIGLLNKPKV 159
Cdd:COG4172 102 mTSLNPLHTIgkqiAEVLRLHR---GLSGAAARARALELLERVGIPD-PERRLDAYphqlSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446051965 160 IFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:COG4172 178 LIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-198 |
7.77e-09 |
|
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: 54.25 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLisilstltlpdegygtvCNYDLYTE-RNKIKKNVSVVPQDLALyptltAYDNL 101
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL-----------------VNEGLYASgKARLISFLPKFSRNKLI-----FIDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 102 SFYADL---YgLKGNRKKSrikealqfaqledwahkridTFSGGMKRRINLV--IGLLNKPKVIFLDEPTVGIDPQSRNH 176
Cdd:cd03238 69 QFLIDVglgY-LTLGQKLS--------------------TLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQ 127
|
170 180
....*....|....*....|..
gi 446051965 177 IFNCIRHLVeELGITVIYTTHH 198
Cdd:cd03238 128 LLEVIKGLI-DLGNTVILIEHN 148
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
23-231 |
1.01e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.18 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDL--YTERNkIKKNVSVVPQDLALYPTLTAyDN 100
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdYTLAS-LRNQVALVSQNVHLFNDTIA-NN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 101 LSFYAdlyglkgNRKKSR--IKEALQFAQLEDWAHKR---IDT--------FSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:PRK11176 437 IAYAR-------TEQYSReqIEEAARMAYAMDFINKMdngLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446051965 168 GIDPQSRNHIFNCIRHLVEELgiTVIYTTHHM---EEAEMlchrVAIYDKGEILDIDTPKNLITKYG 231
Cdd:PRK11176 510 ALDTESERAIQAALDELQKNR--TSLVIAHRLstiEKADE----ILVVEDGEIVERGTHAELLAQNG 570
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-197 |
1.37e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 55.57 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 26 LSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEgyGTVC---------NYDLYteRNKIkknvSVVPQDlalyptlt 96
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPES--GEILldgqpvtadNREAY--RQLF----SAVFSD-------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 97 aydnlsFY--ADLYGLKGNRKKSRIKEALQFAQLEdwaHK------RIDT--FSGGMKRRINLVIGLL-NKPkVIFLDEP 165
Cdd:COG4615 415 ------FHlfDRLLGLDGEADPARARELLERLELD---HKvsvedgRFSTtdLSQGQRKRLALLVALLeDRP-ILVFDEW 484
|
170 180 190
....*....|....*....|....*....|....*
gi 446051965 166 TVGIDPQSRnHIFncIRHLVEEL---GITVIYTTH 197
Cdd:COG4615 485 AADQDPEFR-RVF--YTELLPELkarGKTVIAISH 516
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-219 |
1.59e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.32 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTtlISILSTLTLPDEGY----GTVCNYDLYTERNKIK-KNVSVVPQD--LALYPTL 95
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVrqtaGRVLLDGKPVAPCALRgRKIATIMQNprSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 96 TAYDNLSFYADLYGLKGNRkkSRIKEALQFAQLEDwAHKRIDTF----SGGMKRRINLVIGLLNKPKVIFLDEPTVGIDP 171
Cdd:PRK10418 97 TMHTHARETCLALGKPADD--ATLTAALEAVGLEN-AARVLKLYpfemSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446051965 172 QSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILD 219
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-216 |
2.84e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 6 TMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG----YGTVCNYDlyTERNKIKKN 81
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsilyLGKEVTFN--GPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVVPQDLALYPTLTAYDNL----SFYADLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKP 157
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 158 KVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGE 216
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-197 |
3.11e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 54.33 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLY----TERNKIKKNVSVVPQD-LA-LYPTLT 96
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkdDEWRAVRSDIQMIFQDpLAsLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 97 AYDNLS-----FYADLyglKGNRKKSRIKEA-LQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGID 170
Cdd:PRK15079 117 IGEIIAeplrtYHPKL---SRQEVKDRVKAMmLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180
....*....|....*....|....*..
gi 446051965 171 PQSRNHIFNCIRHLVEELGITVIYTTH 197
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAH 220
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-197 |
3.64e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 4 INTMISIRyikKSYG-DYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTL-------TLPDEGYgtvcnydlyter 75
Cdd:PRK11819 6 IYTMNRVS---KVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkefegeARPAPGI------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 76 nkikkNVSVVPQDLALYPTLTAYDN-----------LSFYADLYGLKGN---------RKKSRIKEALQFA-------QL 128
Cdd:PRK11819 71 -----KVGYLPQEPQLDPEKTVRENveegvaevkaaLDRFNEIYAAYAEpdadfdalaAEQGELQEIIDAAdawdldsQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 129 E---------DWAHKrIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSrnhifncI----RHLVEELGiTVIYT 195
Cdd:PRK11819 146 EiamdalrcpPWDAK-VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES-------VawleQFLHDYPG-TVVAV 216
|
..
gi 446051965 196 TH 197
Cdd:PRK11819 217 TH 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
8-215 |
3.83e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.34 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSY-GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLYTERNKI-KKNVSVV 85
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 86 PQDlalyPTLTAYdnlSFYADLyGLKGNRKKSRIKEALQFAQLEDWA-------HKRI----DTFSGGMKRRINLVIGLL 154
Cdd:PRK10790 421 QQD----PVVLAD---TFLANV-TLGRDISEEQVWQALETVQLAELArslpdglYTPLgeqgNNLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446051965 155 NKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIytTHHME---EAE--MLCHRVAIYDKG 215
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVI--AHRLStivEADtiLVLHRGQAVEQG 556
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-173 |
3.95e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 13 IKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEgyGTVcnydLYTErnkiKKNVSVVPQDLALY 92
Cdd:PRK15064 325 LTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDS--GTV----KWSE----NANIGYYAQDHAYD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 93 --PTLTAYDNLSFYADlygLKGNRKKSR-IKEALQFAQleDWAHKRIDTFSGGMKRRinLVIG--LLNKPKVIFLDEPTV 167
Cdd:PRK15064 395 feNDLTLFDWMSQWRQ---EGDDEQAVRgTLGRLLFSQ--DDIKKSVKVLSGGEKGR--MLFGklMMQKPNVLVMDEPTN 467
|
....*.
gi 446051965 168 GIDPQS 173
Cdd:PRK15064 468 HMDMES 473
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-195 |
4.04e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 10 IRYIKKSYGDYTV--IKNLSIDIRKGEIIGLLGPNGAGKTTLI-SILSTLTLPDEGYGTVCNYDLYTErNKIKK----NV 82
Cdd:TIGR00956 62 FRKLKKFRDTKTFdiLKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTDGFHIGVEGVITYDGITP-EEIKKhyrgDV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVVPQDLALYPTLTAYDNLSFYADLYGlKGNR-----KKSRIK-EALQFAQLEDWAHKR--------IDTFSGGMKRRIN 148
Cdd:TIGR00956 141 VYNAETDVHFPHLTVGETLDFAARCKT-PQNRpdgvsREEYAKhIADVYMATYGLSHTRntkvgndfVRGVSGGERKRVS 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446051965 149 LVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYT 195
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
16-198 |
5.66e-08 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 52.65 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 16 SYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTltlpDEGY----GTV-----CNYDLYTErNKIKKNVSVVP 86
Cdd:TIGR01978 9 SVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG----HPSYevtsGTIlfkgqDLLELEPD-ERARAGLFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 87 QDLALYPTLTaydNLSFyadLYGLKGNRKKSRIKEALQFAQLEDWAHKRIDT---------------FSGGMKRRINLVI 151
Cdd:TIGR01978 84 QYPEEIPGVS---NLEF---LRSALNARRSARGEEPLDLLDFEKLLKEKLALldmdeeflnrsvnegFSGGEKKRNEILQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446051965 152 GLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEE-LGITVIytTHH 198
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPdRSFLII--THY 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-170 |
5.73e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 5 NTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEG-----YGTVCNY-------DLY 72
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGeiglaKGIKLGYfaqhqleFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 73 TERNKIKKNVSVVPQDLAlyptltayDNLSFYADLYGLKGNrKKSRIKEalqfaqledwahkridTFSGGMKRRINLVIG 152
Cdd:PRK10636 390 ADESPLQHLARLAPQELE--------QKLRDYLGGFGFQGD-KVTEETR----------------RFSGGEKARLVLALI 444
|
170
....*....|....*...
gi 446051965 153 LLNKPKVIFLDEPTVGID 170
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLD 462
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-218 |
6.13e-08 |
|
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: 52.14 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 18 GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILstltLPDEGYGTVcnydlyteRNKIK-KNVSVvpqdLALYPTLT 96
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI----MGHPKYEVT--------EGEILfKGEDI----TDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 97 AYDN--LSFY--ADLYGLKgnrkksrIKEALQFAQledwahkriDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQ 172
Cdd:cd03217 75 ARLGifLAFQypPEIPGVK-------NADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446051965 173 SRNHIFNCIRHLVEElGITVIYTTHHmeeAEMLCH----RVAIYDKGEIL 218
Cdd:cd03217 139 ALRLVAEVINKLREE-GKSVLIITHY---QRLLDYikpdRVHVLYDGRIV 184
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
66-199 |
8.17e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 66 VCNYDLYTERNKIkknvSVVPQDLALYptltaydNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAH---KRIDT---- 138
Cdd:PTZ00265 1286 ICDYNLKDLRNLF----SIVSQEPMLF-------NMSIYENIKFGKEDATREDVKRACKFAAIDEFIEslpNKYDTnvgp 1354
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446051965 139 ----FSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHM 199
Cdd:PTZ00265 1355 ygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-187 |
8.54e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.37 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 31 RKGEIIGLLGPNGAGKTTLISILSTLTLPDEG-YGTVCNYD------------LYTERNKIKK-NVSVVPQDLALYPTL- 95
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGkFDDPPDWDeildefrgselqNYFTKLLEGDvKVIVKPQYVDLIPKAv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 96 --TAYDNLSFYADlyglkgNRKKSRIKEALQFAQLEDwahKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQS 173
Cdd:cd03236 104 kgKVGELLKKKDE------RGKLDELVDQLELRHVLD---RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170
....*....|....
gi 446051965 174 RNHIFNCIRHLVEE 187
Cdd:cd03236 175 RLNAARLIRELAED 188
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-197 |
9.91e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.21 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILS--------TLTLPDEG------------YGTVCNYDLYTERNKIKKN 81
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGklfyvpqrpymtLGTLRDQIIYPDSSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 82 VSVVPQDLALYPTLTAYDNLsfyadlyglkgnrkksrIKEALQFAQLEDWAhkriDTFSGGMKRRINLVIGLLNKPKVIF 161
Cdd:TIGR00954 547 RGLSDKDLEQILDNVQLTHI-----------------LEREGGWSAVQDWM----DVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*.
gi 446051965 162 LDEPTVGIDPQSRNHIFNcirhLVEELGITVIYTTH 197
Cdd:TIGR00954 606 LDECTSAVSVDVEGYMYR----LCREFGITLFSVSH 637
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-170 |
1.14e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 16 SYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGY---GT---VCNYDLYTErnkikknvsvvpqdl 89
Cdd:PRK11147 328 QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRihcGTkleVAYFDQHRA--------------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 90 ALYPTLTAYDNLsfyADlyGLKGNRKKSRIKEALQFAQLEDWAHKRIDT----FSGGMKRRInLVIGLLNKP-KVIFLDE 164
Cdd:PRK11147 393 ELDPEKTVMDNL---AE--GKQEVMVNGRPRHVLGYLQDFLFHPKRAMTpvkaLSGGERNRL-LLARLFLKPsNLLILDE 466
|
....*.
gi 446051965 165 PTVGID 170
Cdd:PRK11147 467 PTNDLD 472
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
8-197 |
2.07e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.28 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTV-IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnyDLYTErnkikkNVSVVP 86
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSG-------EILLD------GKPVTA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 87 QDLALYPTL--TAYDNLSFYADLYGLKGNRKKSRIKEA-LQFAQLED---WAHKRIDT--FSGGMKRRINLVIGLLNKPK 158
Cdd:PRK10522 390 EQPEDYRKLfsAVFTDFHLFDQLLGPEGKPANPALVEKwLERLKMAHkleLEDGRISNlkLSKGQKKRLALLLALAEERD 469
|
170 180 190
....*....|....*....|....*....|....*....
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTH 197
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISH 508
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
21-197 |
2.19e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.26 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 21 TVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVCNYDLyterNKIKKN-VSVVPQDLALYPTLTAYD 99
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI----NNIAKPyCTYIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 100 NLSFYADLYGlkgnrKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFN 179
Cdd:PRK13541 90 NLKFWSEIYN-----SAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN 164
|
170
....*....|....*...
gi 446051965 180 CIRHLVEELGItVIYTTH 197
Cdd:PRK13541 165 LIVMKANSGGI-VLLSSH 181
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
34-237 |
2.79e-07 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 50.44 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 34 EIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnydlytERNKIKKNVSVVPQDLALYPTLTAYDNLSFYADLYGLKGN 113
Cdd:PRK15177 14 EHIGILAAPGSGKTTLTRLLCGLDAPDEG-----------DFIGLRGDALPLGANSFILPGLTGEENARMMASLYGLDGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 114 RKKSRikeALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVI 193
Cdd:PRK15177 83 EFSHF---CYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALACQLQQKGLIVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446051965 194 ytTHHMEEAEMLCHRVAIYDKGEIL---DIDTPKNLITKYGENYLEI 237
Cdd:PRK15177 160 --THNPRLIKEHCHAFGVLLHGKITmceDLAQATALFEQYQSNQATI 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-187 |
5.02e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 30 IRKGEIIGLLGPNGAGKTTLISILSTLTLPDegygtVCNYD----------------LYTERNKIKKN---VSVVPQDLA 90
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPN-----LGDYEeepswdevlkrfrgteLQNYFKKLYNGeikVVHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 91 LYPTLtaydnlsfyadLYG-----LKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEP 165
Cdd:PRK13409 171 LIPKV-----------FKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180
....*....|....*....|..
gi 446051965 166 TVGIDPQSRNHIFNCIRHLVEE 187
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEG 261
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
13-252 |
6.40e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.19 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 13 IKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTlPDEGYGTVCNY-----DLYT----ERNK-IKKNV 82
Cdd:PRK15093 13 FKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVT-KDNWRVTADRMrfddiDLLRlsprERRKlVGHNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVV---PQDlALYPTLTAYDNLSFYADLYGLKG------NRKKSRIKEALQFAQLEDwaHKRID-----TFSGGMKRRIN 148
Cdd:PRK15093 92 SMIfqePQS-CLDPSERVGRQLMQNIPGWTYKGrwwqrfGWRKRRAIELLHRVGIKD--HKDAMrsfpyELTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 149 LVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
|
250 260
....*....|....*....|....*..
gi 446051965 229 KYGENYLEIVISNIPE---EFIHKTKM 252
Cdd:PRK15093 249 TPHHPYTQALIRAIPDfgsAMPHKSRL 275
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-199 |
6.54e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.10 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 18 GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILstLTLPDEGYGTVcnydlyternKIKKNVSVVPQDlALYPTLTA 97
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDKVEGHV----------HMKGSVAYVPQQ-AWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 98 YDNLsfyadLYG--LKGNRKKSRIKEALQFAQLE--------DWAHKRIDtFSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:TIGR00957 716 RENI-----LFGkaLNEKYYQQVLEACALLPDLEilpsgdrtEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190
....*....|....*....|....*....|....*.
gi 446051965 168 GIDPQSRNHIFNcirHLVEELGI----TVIYTTHHM 199
Cdd:TIGR00957 790 AVDAHVGKHIFE---HVIGPEGVlknkTRILVTHGI 822
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-235 |
7.04e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILstLTLPDEGYGTVC----NYDLYTERNKIKKNVSVVPQD---LALYPTL 95
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETL--FGIREKSAGTITlhgkKINNHNANEAINHGFALVTEErrsTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 96 -----TAYDNLSFYADLYGLKGNRK-KSRIKEALQFAQLEDWAHK-RIDTFSGGMKRRInlVIG--LLNKPKVIFLDEPT 166
Cdd:PRK10982 342 digfnSLISNIRNYKNKVGLLDNSRmKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKV--IIGrwLLTQPEILMLDEPT 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446051965 167 VGIDPQSRNHIFNCIRHLV-EELGITVIytTHHMEEAEMLCHRVAIYDKGEILDI----DTPKNLITKYGENYL 235
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAkKDKGIIII--SSEMPELLGITDRILVMSNGLVAGIvdtkTTTQNEILRLASLHL 491
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-252 |
8.40e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.90 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDI-----------------RKGEIIGLLGPNGAGKTtLI--SILSTLtlPDEGYGTV-----CNYDL----YTE 74
Cdd:COG4170 6 IRNLTIEIdtpqgrvkavdrvsltlNEGEIRGLVGESGSGKS-LIakAICGIT--KDNWHVTAdrfrwNGIDLlklsPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 75 RNKI-KKNVSVVPQDLA--LYPTLTAYDNLSFYADLYGLKG---NRKKSRIKEALQFAQ---LEDwaHKRI-DTF----S 140
Cdd:COG4170 83 RRKIiGREIAMIFQEPSscLDPSAKIGDQLIEAIPSWTFKGkwwQRFKWRKKRAIELLHrvgIKD--HKDImNSYphelT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 141 GGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDI 220
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250 260 270
....*....|....*....|....*....|....*
gi 446051965 221 DTPKNLITKYGENYLEIVISNIP---EEFIHKTKM 252
Cdd:COG4170 241 GPTEQILKSPHHPYTKALLRSMPdfrQPLPHKSRL 275
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-212 |
1.58e-06 |
|
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: 49.91 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnydlyternKIKKN--VSVVPQDLALYPTlTAYD 99
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG--------------KIKHSgrISFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 100 NLsfyadLYGLkgNRKKSRIKEALQFAQLEDWAHKRID-----------TFSGGMKRRINLVIGLLNKPKVIFLDEPTVG 168
Cdd:TIGR01271 506 NI-----IFGL--SYDEYRYTSVIKACQLEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446051965 169 IDPQSRNHIF-NCI-RHLVEELGITVIYTTHHMEEAE--MLCHRVAIY 212
Cdd:TIGR01271 579 LDVVTEKEIFeSCLcKLMSNKTRILVTSKLEHLKKADkiLLLHEGVCY 626
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-244 |
1.60e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.97 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 17 YGD----YTVIKNLSIDIRKGEIIGLLGPNGAGKTtlISILSTLTLPDEGyGTVC-------NYDLYT-----ERNKIKK 80
Cdd:PRK11022 13 FGDesapFRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMGLIDYP-GRVMaeklefnGQDLQRisekeRRNLVGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 81 NVSVVPQD--LALYPTLTAYdnlsfYADLYGLK----GNRK--KSRIKEALQFAQLEDWAhKRIDTF----SGGMKRRIN 148
Cdd:PRK11022 90 EVAMIFQDpmTSLNPCYTVG-----FQIMEAIKvhqgGNKKtrRQRAIDLLNQVGIPDPA-SRLDVYphqlSGGMSQRVM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 149 LVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTHHMEEAEMLCHRVAIYDKGEILDIDTPKNLIT 228
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
250
....*....|....*.
gi 446051965 229 KYGENYLEIVISNIPE 244
Cdd:PRK11022 244 APRHPYTQALLRALPE 259
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-187 |
2.09e-06 |
|
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: 49.01 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 31 RKGEIIGLLGPNGAGKTTLISILSTLTLPDEG-YGTVCNYD----------LYTERNKIKKN---VSVVPQDLALYP--- 93
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGdYDEEPSWDevlkrfrgteLQDYFKKLANGeikVAHKPQYVDLIPkvf 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 94 TLTAydnlsfyADLygLKGNRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQS 173
Cdd:COG1245 177 KGTV-------REL--LEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170
....*....|....
gi 446051965 174 RNHIFNCIRHLVEE 187
Cdd:COG1245 248 RLNVARLIRELAEE 261
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
31-197 |
3.06e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 31 RKGEIIGLLGPNGAGKTTLISIL---------------STLTLPDEGYGTVCNYdlyTERNKIKKnvsvvpqdlalyPTL 95
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLagrktggyiegdiriSGFPKKQETFARISGY---CEQNDIHS------------PQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 96 TAYDNLSFYADLYGLKGNRKKSR---IKEALQFAQLEDWAHK-----RIDTFSGGMKRRINLVIGLLNKPKVIFLDEPTV 167
Cdd:PLN03140 969 TVRESLIYSAFLRLPKEVSKEEKmmfVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190
....*....|....*....|....*....|
gi 446051965 168 GIDPQSRNHIFNCIRHLVEElGITVIYTTH 197
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNTVDT-GRTVVCTIH 1077
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-198 |
4.05e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 46.98 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 18 GDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTltlpDEGY----GTVcnydLY----------TERnkIKKNVS 83
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG----HPKYevtsGSI----LLdgedilelspDER--ARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 84 VVPQdlalYPT-----------LTAY-----DNLSFYADLyglkgnrkkSRIKEALQFAQL-EDWAHKRID-TFSGGMKR 145
Cdd:COG0396 81 LAFQ----YPVeipgvsvsnflRTALnarrgEELSAREFL---------KLLKEKMKELGLdEDFLDRYVNeGFSGGEKK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446051965 146 RINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHH 198
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHY 199
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
8-218 |
4.91e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.78 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 8 ISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILstLTLPDEGYGTVCNYDLYTERNKI---KKNVSV 84
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI--QRHFDVSEGDIRFHDIPLTKLQLdswRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 85 VPQDLALYPTLTAyDNLSFyadlyGlKGNRKKSRIKEALQFAQLedwaHKRI-------DT--------FSGGMKRRINL 149
Cdd:PRK10789 394 VSQTPFLFSDTVA-NNIAL-----G-RPDATQQEIEHVARLASV----HDDIlrlpqgyDTevgergvmLSGGQKQRISI 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 150 VIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEelGITVIYTTHHMEeaemlchrvAIYDKGEIL 218
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLS---------ALTEASEIL 520
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-211 |
5.21e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 11 RYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLtLPDEGY-------GTVCNY-DLyteRNKIKKNV 82
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGSYegeilfdGEVCRFkDI---RDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 83 SVVPQDLALYPTLTAYDNLsFYADLYGLKG----NRKKSRIKEALQFAQLEDWAHKRIDTFSGGMKRRINLVIGLLNKPK 158
Cdd:NF040905 81 VIIHQELALIPYLSIAENI-FLGNERAKRGvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446051965 159 VIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAI 211
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITV 211
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
22-229 |
6.17e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 46.83 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLisILSTLTLPDEGYGT-------VCNYDLYTERNKIkknvSVVPQDLALYPT 94
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIFDGKividgidISKLPLHTLRSRL----SIILQDPILFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 95 LTAYDnlsfyadlygLKGNRK--KSRIKEALQFAQLEDWAhKRI------------DTFSGGMKRRINLVIGLLNKPKVI 160
Cdd:cd03288 110 SIRFN----------LDPECKctDDRLWEALEIAQLKNMV-KSLpggldavvteggENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 161 FLDEPTVGIDPQSRNHIFNCI-RHLVEELGITVIYTTHHMEEAEMlchrVAIYDKGEILDIDTPKNLITK 229
Cdd:cd03288 179 IMDEATASIDMATENILQKVVmTAFADRTVVTIAHRVSTILDADL----VLVLSRGILVECDTPENLLAQ 244
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-217 |
6.17e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTL-ISILStltlpdEGYGTVCNYDLYTERNKIkkNVSVVPQ----DLAlYPT-- 94
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFG------RSYGRNISGTVFKDGKEV--DVSTVSDaidaGLA-YVTed 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 95 -----LTAYDNLSFYADLYGLKGNRKKSRIKEALQFAQLEDWAHK-RIDT---------FSGGMKRRINLVIGLLNKPKV 159
Cdd:NF040905 346 rkgygLNLIDDIKRNITLANLGKVSRRGVIDENEEIKVAEEYRKKmNIKTpsvfqkvgnLSGGNQQKVVLSKWLFTDPDV 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446051965 160 IFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAIYDKGEI 217
Cdd:NF040905 426 LILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
7-54 |
9.86e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 9.86e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446051965 7 MISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILS 54
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLA 48
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-53 |
1.17e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.79 E-value: 1.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446051965 1 MTDINTMISIRYIKKSYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISIL 53
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI 53
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-200 |
5.47e-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: 44.08 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnydlyternKIKKN--VSVVPQDLALYPTlTAYD 99
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG--------------KIKHSgrISFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 100 NLsfyadLYGLkgNRKKSRIKEALQFAQLEDWAHKRID-----------TFSGGMKRRINLVIGLLNKPKVIFLDEPTVG 168
Cdd:cd03291 117 NI-----IFGV--SYDEYRYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190
....*....|....*....|....*....|...
gi 446051965 169 IDPQSRNHIF-NCIRHLVEELgiTVIYTTHHME 200
Cdd:cd03291 190 LDVFTEKEIFeSCVCKLMANK--TRILVTSKME 220
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-233 |
6.35e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.58 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLLGPNGAGKTTLISILSTLTLPDEGYGTVcnydlyternkIKKNVSVVPQDLALYpTLTAYDNLS 102
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIF-NATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 103 FYADLyglkgnrKKSRIKEALQFAQLED-----WAHKRID------TFSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDP 171
Cdd:PLN03232 701 FGSDF-------ESERYWRAIDVTALQHdldllPGRDLTEigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446051965 172 QSRNHIFN-CIRHlvEELGITVIYTTHHME-----EAEMLCHRVAIYDKGEILDIDTPKNLITKYGEN 233
Cdd:PLN03232 774 HVAHQVFDsCMKD--ELKGKTRVLVTNQLHflplmDRIILVSEGMIKEEGTFAELSKSGSLFKKLMEN 839
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
139-197 |
6.47e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.80 E-value: 6.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 139 FSGGMKRRINLVIGLLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEELGITVIYTTH 197
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISH 213
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-170 |
1.24e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 16 SYGDYTVIKNLSIDIRKGEIIGLLGPNGAGKTTLISILS------------TLTLPDEGYG---TV--CNYDLYTERNKI 78
Cdd:PLN03073 186 SVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqILHVEQEVVGddtTAlqCVLNTDIERTQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 79 -KKNVSVVPQDLAL-YPTLTAYDNLSFYADLYGLKGNRKKSRIKEALQF--------------AQLE---DWAHKRIDTF 139
Cdd:PLN03073 266 lEEEAQLVAQQRELeFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELidaytaearaasilAGLSftpEMQVKATKTF 345
|
170 180 190
....*....|....*....|....*....|.
gi 446051965 140 SGGMKRRINLVIGLLNKPKVIFLDEPTVGID 170
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-201 |
1.44e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 32 KGEIIGLLGPNGAGKTTLISILSTLTLPDEGygtvcnydlyternkikKNVSVVPQDLALYptltAYDNLSFYADLYGLK 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG-----------------GVIYIDGEDILEE----VLDQLLLIIVGGKKA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 112 GNRKKSRIKEALQFAQledwahkridtfsggmkrrinlviglLNKPKVIFLDEPTVGIDPQSRNHIFNCIRHLV-----E 186
Cdd:smart00382 60 SGSGELRLRLALALAR--------------------------KLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkS 113
|
170
....*....|....*
gi 446051965 187 ELGITVIYTTHHMEE 201
Cdd:smart00382 114 EKNLTVILTTNDEKD 128
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
23-197 |
3.01e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.91 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGeIIGLLGPNGAGKTTLISILStLTLPDEGYGTVCNYDLYTERNKIKKNV-------SVVPQDLALYPTL 95
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALR-LLLGPSSSRKFDEEDFYLGDDPDLPEIeieltfgSLLSRLLRLLLKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 96 TAYDNLSfyADLYGLKGNRKKS--RIKEALQ--FAQLEDWAHKRID---------------TFSGGMKRRIN-------- 148
Cdd:COG3593 92 EDKEELE--EALEELNEELKEAlkALNELLSeyLKELLDGLDLELElsldeledllkslslRIEDGKELPLDrlgsgfqr 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446051965 149 -LVIGLL---------NKPKVIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTH 197
Cdd:COG3593 170 lILLALLsalaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEK-PNQVIITTH 227
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
23-178 |
5.40e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.75 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 23 IKNLSIDIRKGEIIGLL-GPNGAGKTTLISILST-LTLPDEGYGTVCNYDLYTERNKIKKNVSVVpqdlALYPT--LTAY 98
Cdd:COG3950 14 FEDLEIDFDNPPRLTVLvGENGSGKTTLLEAIALaLSGLLSRLDDVKFRKLLIRNGEFGDSAKLI----LYYGTsrLLLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 99 DNLSFYADLYGLKGNRkKSRIKEALQ----FAQLEDWAHKRIDTFSGGMK----RRINLVIGLLNKpkvIFLDEPTVGID 170
Cdd:COG3950 90 GPLKKLERLKEEYFSR-LDGYDSLLDedsnLREFLEWLREYLEDLENKLSdeldEKLEAVREALNK---LLPDFKDIRID 165
|
....*...
gi 446051965 171 PQSRNHIF 178
Cdd:COG3950 166 RDPGRLVI 173
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
136-212 |
6.41e-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: 39.65 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 136 IDTFSGGMKRRINL--VIGLLNKPK--VIFLDEPTVGIDPQSRNHIFNCIRHLVEElGITVIYTTHHMEEAEMLCHRVAI 211
Cdd:cd03227 75 RLQLSGGEKELSALalILALASLKPrpLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELAELADKLIHI 153
|
.
gi 446051965 212 Y 212
Cdd:cd03227 154 K 154
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
27-59 |
5.85e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.50 E-value: 5.85e-03
10 20 30
....*....|....*....|....*....|...
gi 446051965 27 SIDIRKGEIIGLLGPNGAGKTTLISILSTLTLP 59
Cdd:pfam13555 16 TIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP 48
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-251 |
7.16e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 134 KRIDTFSGGMKRRINL-------VIGLLnkpkvIFLDEPTVGIDPQSRNHIFNCIRHLvEELGITVIYTTHhmeEAEMLc 206
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLatqigsgLTGVL-----YVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEH---DEDTI- 553
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446051965 207 hRVAIYdkgeILDIDtPKNlitkyGENYLEIVISNIPEEFIHKTK 251
Cdd:TIGR00630 554 -RAADY----VIDIG-PGA-----GEHGGEVVASGTPEEILANPD 587
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-213 |
8.61e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 37.84 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 22 VIKNLSIDIRKGEIIGLLGPNGAGKTTLI-SILStltlpdegygtvcNYDLYTERNKIKKNVSVVPQDlALYPTLTAYDN 100
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLqSLLS-------------QFEISEGRVWAERSIAYVPQQ-AWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446051965 101 LSFYADlyglkgnRKKSRIKEALQFAQLE-DWAH-----------KRIDtFSGGMKRRINLVIGLLNKPKVIFLDEPTVG 168
Cdd:PTZ00243 741 ILFFDE-------EDAARLADAVRVSQLEaDLAQlgggleteigeKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446051965 169 IDPQSRNHIfncirhlVEEL------GITVIYTTHHMEEAEMLCHRVAIYD 213
Cdd:PTZ00243 813 LDAHVGERV-------VEECflgalaGKTRVLATHQVHVVPRADYVVALGD 856
|
|
| |
