|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
21-270 |
3.90e-102 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 297.36 E-value: 3.90e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQLQ 100
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTT 178
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARerIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 179 GLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHrndaevirasrkgkitLE 258
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL----------------LE 224
|
250
....*....|..
gi 1721664488 259 DVFIGLTGTAIR 270
Cdd:COG1131 225 DVFLELTGEEAR 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
20-262 |
1.46e-79 |
|
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: 240.14 E-value: 1.46e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQL 99
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 QSTSFQSELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPT 177
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKkrIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 178 TGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRNDaevirasrkgkiTL 257
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE------------NL 228
|
....*
gi 1721664488 258 EDVFI 262
Cdd:COG4555 229 EDAFV 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-234 |
1.25e-76 |
|
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: 232.01 E-value: 1.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGS--FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQ 98
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQSTSFQSELTVTEIIRLYAAVYGLSLS--DSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEP 176
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSeiKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 177 TTGLDPQSRRQLWERMESLRnAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQ 234
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
29-257 |
1.79e-74 |
|
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: 229.20 E-value: 1.79e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 29 TYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQLQSTSFQSEL 108
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 109 TVTEIIRLYAAVYGLS--LSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRR 186
Cdd:TIGR01188 82 TGRENLEMMGRLYGLPkdEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 187 QLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIvdRHRNDAEVIRASRKGKITL 257
Cdd:TIGR01188 162 AIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL--KRRLGKDTLESRPRDIQSL 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
21-227 |
1.16e-73 |
|
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: 222.66 E-value: 1.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQLQ 100
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIRLyaavyglslsdseieallqnikletasskrfgqlSGGQQQRVSLAIATMHKPKLVLLDEPTTGL 180
Cdd:cd03230 81 EPSLYENLTVRENLKL----------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1721664488 181 DPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRI 227
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
21-233 |
6.33e-71 |
|
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: 217.24 E-value: 6.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQLQ 100
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIRLYAAVYGLSLS--DSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTT 178
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAerRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 179 GLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSP 233
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-270 |
6.78e-63 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 200.03 E-value: 6.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 17 TETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMG 96
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 IQLQSTSFQSELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLD 174
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARalVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 175 EPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDR--------------- 239
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESeigcdvieiygpdpv 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 240 ----------------------HRNDAEVIRASRKGK---------ITLEDVFIGLTGTAIR 270
Cdd:PRK13537 244 alrdelaplaerteisgetlfcYVRDPEPLHARLKGRaglrylhrpANLEDVFLRLTGREMQ 305
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-240 |
1.06e-60 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 195.43 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 4 TMPATNSATSSASTETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYN 83
Cdd:PRK13536 25 GISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 84 LKEKPLHAKANMGIQLQSTSFQSELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLA 161
Cdd:PRK13536 105 VPARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEavIPSLLEFARLESKADARVSDLSGGMKRRLTLA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 162 IATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRH 240
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| nodI |
TIGR01288 |
ATP-binding ABC transporter family nodulation protein NodI; This protein is required for ... |
17-240 |
2.32e-60 |
|
ATP-binding ABC transporter family nodulation protein NodI; This protein is required for normal nodulation by nitrogen-fixing root nodule bacteria such as Mesorhizobium loti. It is a member of the family of ABC transporter ATP binding proteins and works with NodJ to export a nodulation signal molecule. This model does not recognize the highly divergent NodI from Azorhizobium caulinodans. [Cellular processes, Other, Transport and binding proteins, Other]
Pssm-ID: 130355 [Multi-domain] Cd Length: 303 Bit Score: 193.22 E-value: 2.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 17 TETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMG 96
Cdd:TIGR01288 1 SNVAIDLVGVSKSYGDKVVVNDLSFTIARGECFGLLGPNGAGKSTIARMLLGMISPDRGKITVLGEPVPSRARLARVAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 IQLQSTSFQSELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLD 174
Cdd:TIGR01288 81 VVPQFDNLDPEFTVRENLLVFGRYFGMSTREIEavIPSLLEFARLESKADVRVALLSGGMKRRLTLARALINDPQLLILD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 175 EPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRH 240
Cdd:TIGR01288 161 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLESGRKIAEGRPHALIDEQ 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-228 |
8.82e-60 |
|
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: 188.73 E-value: 8.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMG 96
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 IQLQSTSFQSELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLD 174
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTarLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 175 EPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
17-249 |
2.29e-56 |
|
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: 181.39 E-value: 2.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 17 TETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMG 96
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 IqlqSTSFQ-----SELTVTE-----------------IIRLYAAVYGLSLSDSEIEALLQNIKLETASSKRFGQLSGGQ 154
Cdd:COG0411 81 I---ARTFQnprlfPELTVLEnvlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 155 QQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLR-NAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSP 233
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
250
....*....|....*.
gi 1721664488 234 QAIvdrhRNDAEVIRA 249
Cdd:COG0411 238 AEV----RADPRVIEA 249
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
21-228 |
9.44e-56 |
|
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: 178.24 E-value: 9.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAkanMGIQLQ 100
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR---IGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIRLYAAVYGLSLSD--SEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTT 178
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEarRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721664488 179 GLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
20-207 |
2.90e-55 |
|
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: 176.90 E-value: 2.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQL 99
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 QSTSFQSELTVTEIIRLYAAVYGLSLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTG 179
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180
....*....|....*....|....*...
gi 1721664488 180 LDPQSRRQLWERMESLRNAGHAILLTTH 207
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-249 |
6.47e-55 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 179.15 E-value: 6.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkeKPLHAKA------ 93
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-----EPLDPEDrrrigy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 94 ---------NMgiqlqstsfqselTVTEIIRLYAAVYGLSLSDS--EIEALLQNIKLETASSKRFGQLSGGQQQRVSLAI 162
Cdd:COG4152 76 lpeerglypKM-------------KVGEQLVYLARLKGLSKAEAkrRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 163 ATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRN 242
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
....*..
gi 1721664488 243 DAEVIRA 249
Cdd:COG4152 223 NTLRLEA 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-246 |
1.90e-54 |
|
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: 175.70 E-value: 1.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIqlq 100
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQ-----SELTVTEIIRLyAAVYGLSLSDS-------------EIEALLQNIKLETASSKRFGQLSGGQQQRVSLAI 162
Cdd:cd03219 78 GRTFQiprlfPELTVLENVMV-AAQARTGSGLLlararreereareRAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 163 ATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIvdrhRN 242
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV----RN 232
|
....
gi 1721664488 243 DAEV 246
Cdd:cd03219 233 NPRV 236
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
17-239 |
7.65e-54 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 177.98 E-value: 7.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 17 TETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHaKANMG 96
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 iqlqsTSFQSE-----LTVTEIIRlyaavYGLS---LSDSEIEA----LLQNIKLETASSKRFGQLSGGQQQRVSLA--I 162
Cdd:COG3842 81 -----MVFQDYalfphLTVAENVA-----FGLRmrgVPKAEIRArvaeLLELVGLEGLADRYPHQLSGGQQQRVALAraL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 163 ATmhKPKLVLLDEPTTGLDPQSRRQL-WERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDR 239
Cdd:COG3842 151 AP--EPRVLLLDEPLSALDAKLREEMrEELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-227 |
4.00e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 172.58 E-value: 4.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 16 STETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHakanM 95
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR----I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 GIQLQSTSFQSE--LTVTEIIRLYAavYG-------LSLSDSE-IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATM 165
Cdd:COG1121 78 GYVPQRAEVDWDfpITVRDVVLMGR--YGrrglfrrPSRADREaVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 166 HKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRI 227
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-251 |
5.82e-53 |
|
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: 172.29 E-value: 5.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGS----FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkeKPLHAKANMG 96
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDG-----RPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 ----IQL--QS--TSFQSELTVTEIIRLYAAVYGLSLSDSEIEALLQNIKLETASSKRF-GQLSGGQQQRVSLAIATMHK 167
Cdd:COG1124 77 frrrVQMvfQDpyASLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDRYpHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 168 PKLVLLDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRNDA-- 244
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYtr 236
|
....*..
gi 1721664488 245 EVIRASR 251
Cdd:COG1124 237 ELLAASL 243
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
21-229 |
1.94e-52 |
|
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: 169.71 E-value: 1.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKeKPLHAKANMGIQLQ 100
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-KNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIRLYAAVYGLSlsDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGL 180
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIR--KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721664488 181 DPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:cd03268 158 DPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-236 |
6.28e-52 |
|
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: 168.77 E-value: 6.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQL- 99
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 -QSTSFQSELTVTEIIRLYAAVYGLSLSDSEIEALLQNI-KLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPT 177
Cdd:cd03224 81 pEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 178 TGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
20-254 |
3.45e-51 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 167.91 E-value: 3.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKA-NMGIQ 98
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELArRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQSTSFQSELTVTEIIRLYAAVY-----GLSLSDSEI-EALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVL 172
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHlglfgRPSAEDREAvEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 173 LDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHR------NDAE 245
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELleevygVEAR 240
|
....*....
gi 1721664488 246 VIRASRKGK 254
Cdd:COG1120 241 VIEDPVTGR 249
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-225 |
3.65e-51 |
|
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: 166.55 E-value: 3.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 22 QVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHakanMGIQLQS 101
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR----IGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 102 TSFQSE--LTVTEII---RLYAAVYGLSLSDSEIEALLQNIK---LETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLL 173
Cdd:cd03235 77 RSIDRDfpISVRDVVlmgLYGHKGLFRRLSKADKAKVDEALErvgLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 174 DEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHG 225
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
21-241 |
3.75e-51 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 167.12 E-value: 3.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY-GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKA-NMGI- 97
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRrKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 ------QLqstsFqsELTVTEIIrlyaaVYG---LSLSDSEIEA----LLQNIKLETASSKRFGQLSGGQQQRVSLAIAT 164
Cdd:COG1122 81 fqnpddQL----F--APTVEEDV-----AFGpenLGLPREEIRErveeALELVGLEHLADRPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721664488 165 MHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHR 241
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-236 |
6.33e-51 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 174.32 E-value: 6.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 4 TMPATNSATSSASTETVLQVENLRVTY-----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIA 78
Cdd:COG1123 244 GAARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 79 VGGYNLKEKPLHAKANMGIQLQ------STSFQSELTVTEIIRLYAAVYGLsLSDSEIEA----LLQNIKLETASSKRF- 147
Cdd:COG1123 324 FDGKDLTKLSRRSLRELRRRVQmvfqdpYSSLNPRMTVGDIIAEPLRLHGL-LSRAERRErvaeLLERVGLPPDLADRYp 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 148 GQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAIIDHGR 226
Cdd:COG1123 403 HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
250
....*....|
gi 1721664488 227 IIEIDSPQAI 236
Cdd:COG1123 483 IVEDGPTEEV 492
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
21-239 |
1.57e-50 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 169.17 E-value: 1.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKpLHAKA-NMGIql 99
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN-LPPRErRVGF-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 qstSFQS-----ELTVTEIIRlyaavYGLS---LSDSEIEA----LLQNIKLETASsKRF-GQLSGGQQQRVSLAIATMH 166
Cdd:COG1118 80 ---VFQHyalfpHMTVAENIA-----FGLRvrpPSKAEIRArveeLLELVQLEGLA-DRYpSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721664488 167 KPKLVLLDEPTTGLDPQSRRQL--WERmESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDR 239
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELrrWLR-RLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
22-226 |
6.37e-50 |
|
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: 163.41 E-value: 6.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 22 QVENLRVTYGSFT--AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKA-NMGIQ 98
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQSTSFQ-SELTVTEIIrlyaaVYGL---SLSDSEIEA----LLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKL 170
Cdd:cd03225 81 FQNPDDQfFGPTVEEEV-----AFGLenlGLPEEEIEErveeALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 171 VLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGR 226
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
20-237 |
1.31e-49 |
|
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: 163.60 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQ- 98
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 -LQSTSFQSELTVTEIIRlyaAVYGLS--LS----DSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLV 171
Cdd:TIGR04406 81 lPQEASIFRKLTVEENIM---AVLEIRkdLDraerEERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 172 LLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIV 237
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-249 |
9.09e-49 |
|
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: 161.30 E-value: 9.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGI 97
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 -------QLqstsFqSELTVTEIIRLyaAVYGLSlSDSEIEALLQNI-----KLETASSKRFGQLSGGQQQRVSLAIATM 165
Cdd:COG0410 81 gyvpegrRI----F-PSLTVEENLLL--GAYARR-DRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 166 HKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIvdrhRNDAE 245
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL----LADPE 228
|
....
gi 1721664488 246 VIRA 249
Cdd:COG0410 229 VREA 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
21-228 |
1.95e-48 |
|
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: 159.67 E-value: 1.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFsVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQLQ 100
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSL-TLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIRLYAAVYGLSLS--DSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTT 178
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKevKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 179 GLDPQSRrqlwermESLRN------AGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:cd03264 160 GLDPEER-------IRFRNllselgEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-248 |
1.99e-48 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 160.58 E-value: 1.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGI 97
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QL--QSTS-FQsELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVL 172
Cdd:COG1137 81 GYlpQEASiFR-KLTVEDNILAVLELRKLSKKEREerLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 173 LDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVdrhrNDAEVIR 248
Cdd:COG1137 160 LDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEIL----NNPLVRK 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
16-246 |
4.70e-48 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 159.37 E-value: 4.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 16 STETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYN---LKEKPLHA- 91
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KANMGIQLQS----TSfqseLTVTEIIRLYAAVYGlSLSDSEIEAL----LQNIKLETASSKRFGQLSGGQQQRVSLAIA 163
Cdd:COG1127 81 RRRIGMLFQGgalfDS----LTVFENVAFPLREHT-DLSEAEIRELvlekLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 164 TMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIvdRHRN 242
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL--LASD 233
|
....
gi 1721664488 243 DAEV 246
Cdd:COG1127 234 DPWV 237
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-230 |
6.11e-48 |
|
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: 158.82 E-value: 6.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTY----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANM 95
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 G--IQL--Q--STSFQSELTV----TEIIRLYAAVYGLSLSDSEIEALLQNIKLETASSKRF-GQLSGGQQQRVSLAIAT 164
Cdd:cd03257 81 RkeIQMvfQdpMSSLNPRMTIgeqiAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYpHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721664488 165 MHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAIIDHGRIIEI 230
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
21-242 |
1.24e-47 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 161.74 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPlHAKANMGIQLQ 100
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLP-PQKRDYGIVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIrlyaaVYGLSLS-------DSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLL 173
Cdd:TIGR03265 84 SYALFPNLTVADNI-----AYGLKNRgmgraevAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 174 DEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRN 242
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLqRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPAT 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
21-243 |
6.34e-47 |
|
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: 156.24 E-value: 6.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHaKANMGIQLQ 100
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-KRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIrlyaaVYGLSL---SDSEIEA----LLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLL 173
Cdd:cd03300 80 NYALFPHLTVFENI-----AFGLRLkklPKAEIKErvaeALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 174 DEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRND 243
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
21-227 |
6.41e-47 |
|
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: 155.73 E-value: 6.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGS----FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGG---YNLKEKPLHA-- 91
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdiSKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KANMGIQLQSTSFQSELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPK 169
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRerAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 170 LVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAvCDRIAIIDHGRI 227
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-254 |
1.02e-46 |
|
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: 163.15 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTY--GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAA---GNIAVGGYNLKEKPLHAK 92
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 93 AN-MGIQLQSTSFQ-SELTVTEIIRLYAAVYGLSLSD--SEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKP 168
Cdd:COG1123 82 GRrIGMVFQDPMTQlNPVTVGDQIAEALENLGLSRAEarARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 169 KLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRNDAEVI 247
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVP 241
|
....*..
gi 1721664488 248 RASRKGK 254
Cdd:COG1123 242 RLGAARG 248
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-226 |
1.33e-46 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 153.17 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 22 QVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHakanmgiqlqs 101
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 102 tsfqseltvtEIIRLYAAVyglslsdseieallqnikletasskrfGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLD 181
Cdd:cd00267 70 ----------ELRRRIGYV---------------------------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1721664488 182 PQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGR 226
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-263 |
4.26e-46 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 164.91 E-value: 4.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 12 TSSASTETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHA 91
Cdd:NF033858 258 PADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIAT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KANMGIQLQSTSFQSELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPK 169
Cdd:NF033858 338 RRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAarVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 170 LVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAvCDRIAIIDHGRIIEIDSPQAIVDrhrndaevir 248
Cdd:NF033858 418 LLILDEPTSGVDPVARDMFWRLLIELsREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVA---------- 486
|
250
....*....|....*
gi 1721664488 249 asRKGKITLEDVFIG 263
Cdd:NF033858 487 --ARGAATLEEAFIA 499
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
21-231 |
4.54e-46 |
|
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: 153.44 E-value: 4.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHaKANMGIQLQ 100
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIrlyaaVYGLSL---SDSEIEA----LLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLL 173
Cdd:cd03259 80 DYALFPHLTVAENI-----AFGLKLrgvPKAEIRArvreLLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 174 DEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEID 231
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
21-237 |
7.15e-46 |
|
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: 153.85 E-value: 7.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQL- 99
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 -QSTSFQSELTVTEIIRLYAAVYGLSLS--DSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEP 176
Cdd:cd03218 81 pQEASIFRKLTVEENILAVLEIRGLSKKerEEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 177 TTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIV 237
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
21-238 |
2.42e-45 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 152.27 E-value: 2.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYN---LKEKPL-HAKANMG 96
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 IQLQSTSFQSELTVTEIIRLYAAVYGlSLSDSEIEAL----LQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVL 172
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHT-RLSEEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721664488 173 LDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVD 238
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
15-230 |
3.58e-44 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 150.24 E-value: 3.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 15 ASTETVLQVENLRVTY----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkeKPLH 90
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG-----KPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 91 AK-ANMGIqlqstSFQSE-----LTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAI 162
Cdd:COG1116 77 GPgPDRGV-----VFQEPallpwLTVLDNVALGLELRGVPKAERRerARELLELVGLAGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 163 ATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDH--GRIIEI 230
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
21-226 |
4.15e-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: 147.33 E-value: 4.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL----KEKPLHaKANMG 96
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdleDELPPL-RRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 IQLQSTSFQSELTVTEIIRLyaavyglslsdseieallqnikletasskrfgQLSGGQQQRVSLAIATMHKPKLVLLDEP 176
Cdd:cd03229 80 MVFQDFALFPHLTVLENIAL--------------------------------GLSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 177 TTGLDPQSRRQLWERMESLR-NAGHAILLTTHSMEEAEAVCDRIAIIDHGR 226
Cdd:cd03229 128 TSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
21-243 |
1.05e-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: 148.26 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHaKANMGIQLQ 100
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIrlyaaVYGLSL-------SDSEIEA----LLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPK 169
Cdd:cd03296 82 HYALFRHMTVFDNV-----AFGLRVkprserpPEAEIRAkvheLLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 170 LVLLDEPTTGLDPQSRRQL--WERmESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRND 243
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELrrWLR-RLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASP 231
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
21-228 |
1.15e-43 |
|
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: 147.93 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHakaNMGIQLQ 100
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLH---KIGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIRLYAAVygLSLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGL 180
Cdd:TIGR03740 78 SPPLYENLTARENLKVHTTL--LGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1721664488 181 DPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:TIGR03740 156 DPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
21-230 |
3.66e-43 |
|
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: 146.46 E-value: 3.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGS----FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPlhakANMG 96
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG----PDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 IQLQSTSFQSELTVTEIIRLYAAVYGLSLSD--SEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLD 174
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEarERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 175 EPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIID--HGRIIEI 230
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRIVAE 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
22-228 |
5.31e-43 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 144.50 E-value: 5.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 22 QVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKA-NMGIQLQ 100
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELArKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 StsfqseLTVTEIirlyaavygLSLSDseieallqnikletassKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGL 180
Cdd:cd03214 81 A------LELLGL---------AHLAD-----------------RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721664488 181 DPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:cd03214 129 DIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
21-236 |
1.46e-42 |
|
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: 145.02 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLK-----PAAGNIAVGG---YNLKEKPLHAK 92
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGkdiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 93 ANMGIQLQSTS-FqsELTVTEIIRLYAAVYGLSLS---DSEIEALLQNIKL--ETASSKRFGQLSGGQQQRVSLAIATMH 166
Cdd:cd03260 81 RRVGMVFQKPNpF--PGSIYDNVAYGLRLHGIKLKeelDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 167 KPKLVLLDEPTTGLDPQSRRQLWERMESLRNAgHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
21-243 |
3.56e-42 |
|
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: 144.25 E-value: 3.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGS-FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGY---NLKEKPLHA-KANM 95
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinKLKGKALRQlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 GIQLQSTSFQSELTVTEII---RL-----YAAVYGLsLSDSEIE---ALLQNIKLETASSKRFGQLSGGQQQRVSLAIAT 164
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgRLgrrstWRSLFGL-FPKEEKQralAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 165 MHKPKLVLLDEPTTGLDPQSRRQLwerMESLRNA----GHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRH 240
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQV---MDLLKRInreeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
...
gi 1721664488 241 RND 243
Cdd:cd03256 237 LDE 239
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-228 |
4.13e-42 |
|
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: 141.80 E-value: 4.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEK-PLHAKANmGIql 99
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDARRA-GI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 qstsfqseltvteiirlyAAVYglslsdseieallqnikletasskrfgQLSGGQQQRVSLAIATMHKPKLVLLDEPTTG 179
Cdd:cd03216 78 ------------------AMVY---------------------------QLSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721664488 180 LDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:cd03216 113 LTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
21-253 |
2.06e-41 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 142.44 E-value: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY-GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKE-KPLHAKANMGIQ 98
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQSTSFQSELTVTEIIRLYAAVygLSLSDSEIEA----LLQNIKLETAS-SKRF-GQLSGGQQQRVSLAIATMHKPKLVL 172
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKL--LKWPKEKIREradeLLALVGLDPAEfADRYpHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 173 LDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRND--AEVIRA 249
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDfvAEFVGA 238
|
....
gi 1721664488 250 SRKG 253
Cdd:cd03295 239 DRLL 242
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-249 |
8.96e-41 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 141.28 E-value: 8.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 16 STETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANM 95
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 GI--QLQSTSFQSELTVTEiiRLYAAVY---------GL----SLSDSEIEAL------LQNIKLETASSKRFGQLSGGQ 154
Cdd:PRK11300 81 GVvrTFQHVRLFREMTVIE--NLLVAQHqqlktglfsGLlktpAFRRAESEALdraatwLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 155 QQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSP 233
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
250
....*....|....*.
gi 1721664488 234 QAIvdrhRNDAEVIRA 249
Cdd:PRK11300 239 EEI----RNNPDVIKA 250
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
30-228 |
9.51e-41 |
|
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: 140.55 E-value: 9.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 30 YGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYN-LKEKPLHaKANMGIQL-QSTSFQSE 107
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpWKRRKKF-LRRIGVVFgQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 108 LTVTEIIRLYAAVYGLSLSD--SEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSR 185
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARfkKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1721664488 186 RQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:cd03267 190 ENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
18-229 |
1.73e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 139.41 E-value: 1.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTYGS----FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGG---YNLKEKPLH 90
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdiSSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 91 A--KANMGIQLQStsFQ--SELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIAT 164
Cdd:COG1136 82 RlrRRHIGFVFQF--FNllPELTALENVALPLLLAGVSRKERRerARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 165 MHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAvCDRIAIIDHGRIIE 229
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
20-229 |
2.18e-40 |
|
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: 139.64 E-value: 2.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGS----FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYN---LKEKPL-HA 91
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KANMGIQLQSTSFQSELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPK 169
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEerVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 170 LVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVE 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
21-227 |
3.10e-40 |
|
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: 138.43 E-value: 3.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGG--YNLKEKPLHA-KANMGI 97
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQSTSFQSELTVTEIIRLyAAVYGLSLSDSEIEA----LLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLL 173
Cdd:cd03262 81 VFQQFNLFPHLTVLENITL-APIKVKGMSKAEAEEraleLLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 174 DEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRI 227
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-247 |
3.71e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 141.38 E-value: 3.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTY----------GSF-----------TAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIA 78
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 79 VGGYN-LKEKPLHAK---ANMGiqlQSTSFQSELTVTEIIRLYAAVYGlsLSDSEIEALLQNIkletasSKRFG------ 148
Cdd:COG4586 81 VLGYVpFKRRKEFARrigVVFG---QRSQLWWDLPAIDSFRLLKAIYR--IPDAEYKKRLDEL------VELLDlgelld 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 149 ----QLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIID 223
Cdd:COG4586 150 tpvrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVID 229
|
250 260
....*....|....*....|....
gi 1721664488 224 HGRIIEIDSPQAIVDRHRNDAEVI 247
Cdd:COG4586 230 HGRIIYDGSLEELKERFGPYKTIV 253
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
22-228 |
5.13e-40 |
|
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: 137.77 E-value: 5.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 22 QVENLRVTYGSFT-AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKA-----NM 95
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIgyvmqDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 GIQLQSTSFQSELTVTeiIRLYAAVYGlslsdsEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDE 175
Cdd:cd03226 81 DYQLFTDSVREELLLG--LKELDAGNE------QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1721664488 176 PTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
21-227 |
7.55e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 137.25 E-value: 7.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHA--KANMGIQ 98
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQSTSFqsELTVTEIIRLYAAVYGLSLSDSEIEALLQNIKLETAS-SKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPT 177
Cdd:COG4619 81 QEPALW--GGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 178 TGLDPQSRRQLWERMESLRN-AGHAILLTTHSMEEAEAVCDRIAIIDHGRI 227
Cdd:COG4619 159 SALDPENTRRVEELLREYLAeEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
19-228 |
1.80e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 137.50 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 19 TVLQVENLRVTY-GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYN---LKEKPLHA-KA 93
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtaLRGRALRRlRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 94 NMGiqlqsTSFQS-----ELTVTE--------IIRLYAAVYGLsLSDSEIE---ALLQNIKLETASSKRFGQLSGGQQQR 157
Cdd:COG3638 81 RIG-----MIFQQfnlvpRLSVLTnvlagrlgRTSTWRSLLGL-FPPEDREralEALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721664488 158 VSLAIATMHKPKLVLLDEPTTGLDPQSRRQLwerMESLRNA----GHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQV---MDLLRRIaredGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-227 |
1.89e-39 |
|
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: 135.64 E-value: 1.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTYgsftAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGI 97
Cdd:cd03215 2 EPVLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLqstsfqseltVTEIIRLYAAVYGLSLSDseieallqNIkleTASSkrfgQLSGGQQQRVSLAIATMHKPKLVLLDEPT 177
Cdd:cd03215 78 AY----------VPEDRKREGLVLDLSVAE--------NI---ALSS----LLSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721664488 178 TGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRI 227
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
21-242 |
3.70e-39 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 139.44 E-value: 3.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLhAKANMGIqlq 100
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP-KDRNIAM--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 stSFQS-----ELTVTEIIRlyaavYGLSL---SDSEIEALLQNI----KLETASSKRFGQLSGGQQQRVSLAIATMHKP 168
Cdd:COG3839 80 --VFQSyalypHMTVYENIA-----FPLKLrkvPKAEIDRRVREAaellGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721664488 169 KLVLLDEPTTGLDPQSRRQLweRME--SL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRN 242
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVEM--RAEikRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
35-227 |
6.97e-39 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 144.39 E-value: 6.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 35 AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQLQSTSFQSELTVTEII 114
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 115 RLYAAVYGLSLSDS--EIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERM 192
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190
....*....|....*....|....*....|....*
gi 1721664488 193 ESLRnAGHAILLTTHSMEEAEAVCDRIAIIDHGRI 227
Cdd:TIGR01257 1105 LKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-236 |
1.33e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 136.04 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYG-----SFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL---KEKPLHA- 91
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakKKKKLKDl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KANMGI-------QLqstsFqsELTVTEIIrlyaaVYG---LSLSDSEIEA----LLQNIKLETASSKR--FgQLSGGQQ 155
Cdd:TIGR04521 81 RKKVGLvfqfpehQL----F--EETVYKDI-----AFGpknLGLSEEEAEErvkeALELVGLDEEYLERspF-ELSGGQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 156 QRVSLA-IATMhKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSP 233
Cdd:TIGR04521 149 RRVAIAgVLAM-EPEVLILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTP 227
|
...
gi 1721664488 234 QAI 236
Cdd:TIGR04521 228 REV 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
21-231 |
4.33e-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: 133.15 E-value: 4.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPlHAKANMGIQLQ 100
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP-PKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIRlyaavYGLSL---SDSEIEALLQNI----KLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLL 173
Cdd:cd03301 80 NYALYPHMTVYDNIA-----FGLKLrkvPKDEIDERVREVaellQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 174 DEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEID 231
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
18-228 |
6.28e-38 |
|
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: 133.67 E-value: 6.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGN-IAV-----GGYNLKEkplhA 91
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLfgerrGGEDVWE----L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KANMGI---QLQSTsFQSELTVTEIIR--LYAAVyGL--SLSDSEIE---ALLQNIKLETASSKRFGQLSGGQQQRVSLA 161
Cdd:COG1119 77 RKRIGLvspALQLR-FPRDETVLDVVLsgFFDSI-GLyrEPTDEQRErarELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 162 IATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGH-AILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHVEEIPPGITHVLLLKDGRVV 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
20-243 |
1.21e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 132.43 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL--KEKPLHA-KANMG 96
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKlRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 IqlqstSFQS-----ELTVTEIIRLyAAVYGLSLSDSEIEA----LLQNIKLETASSKRFGQLSGGQQQRVslAIA---T 164
Cdd:COG1126 81 M-----VFQQfnlfpHLTVLENVTL-APIKVKKMSKAEAEErameLLERVGLADKADAYPAQLSGGQQQRV--AIAralA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 165 MhKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRND 243
Cdd:COG1126 153 M-EPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-247 |
2.33e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 135.35 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 1 MESTMPATNSATSSASTeTVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVG 80
Cdd:PRK11607 1 MNDAIPRPQAKTRKALT-PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 81 GYNLKEKPLHAKA-NMgiQLQSTSFQSELTVTEIIrlyaaVYGLS---LSDSEI----EALLQNIKLETASSKRFGQLSG 152
Cdd:PRK11607 80 GVDLSHVPPYQRPiNM--MFQSYALFPHMTVEQNI-----AFGLKqdkLPKAEIasrvNEMLGLVHMQEFAKRKPHQLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 153 GQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSR-RQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEID 231
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRdRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
250
....*....|....*...
gi 1721664488 232 SPQAIVDR--HRNDAEVI 247
Cdd:PRK11607 233 EPEEIYEHptTRYSAEFI 250
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-240 |
3.81e-37 |
|
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: 137.97 E-value: 3.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 6 PATNSATSSASTETVLQVENLRVTY-GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL 84
Cdd:COG4988 322 APAGTAPLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 85 KEKPLHAKANmgiQLQSTSFQSEL---TVTEIIRLYAAvyglSLSDSEIEALLQN------IK-----LETASSKRFGQL 150
Cdd:COG4988 402 SDLDPASWRR---QIAWVPQNPYLfagTIRENLRLGRP----DASDEELEAALEAagldefVAalpdgLDTPLGEGGRGL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 151 SGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRnAGHAILLTTHSMEEAEAvCDRIAIIDHGRIIEI 230
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQ 552
|
250
....*....|
gi 1721664488 231 DSPQAIVDRH 240
Cdd:COG4988 553 GTHEELLAKN 562
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-225 |
6.30e-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: 138.99 E-value: 6.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 13 SSASTETVLQVENLRVTYG--SFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLH 90
Cdd:TIGR01257 1930 SGGNKTDILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 91 AKANMGIQLQSTSFQSELTVTEIIRLYAAVYGLSlsDSEIEAL----LQNIKLETASSKRFGQLSGGQQQRVSLAIATMH 166
Cdd:TIGR01257 2010 VHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVP--AEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 167 KPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHG 225
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-261 |
1.18e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 130.66 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 19 TVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANM-GI 97
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRrAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQSTSFQSELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLA------IATMHKPK 169
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDalVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArvlaqlWEPDGPPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 170 LVLLDEPTTGLDPqsRRQLwERMESLRN----AGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPqaivdrhrndAE 245
Cdd:PRK13548 161 WLLLDEPTSALDL--AHQH-HVLRLARQlaheRGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP----------AE 227
|
250
....*....|....*.
gi 1721664488 246 VIRASrkgkiTLEDVF 261
Cdd:PRK13548 228 VLTPE-----TLRRVY 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-228 |
1.40e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 135.54 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 16 STETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLK-EKPLHAkAN 94
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDA-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 95 MGI-------QLqstsFQSeLTVTEIIRLYA-AVYGLSLSDSEIEALLQNIkletasSKRFG----------QLSGGQQQ 156
Cdd:COG3845 80 LGIgmvhqhfML----VPN-LTVAENIVLGLePTKGGRLDRKAARARIREL------SERYGldvdpdakveDLSVGEQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 157 RVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-243 |
2.24e-36 |
|
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: 129.38 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTaVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPlHAKANMGIQLQ 100
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-PEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIrlyaaVYGLSL---SDSEIEALLQNI----KLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLL 173
Cdd:cd03299 79 NYALFPHMTVYKNI-----AYGLKKrkvDKKEIERKVLEIaemlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 174 DEPTTGLDPQSRRQLWERMESLR-NAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRND 243
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNE 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-240 |
3.21e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 130.94 E-value: 3.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTY----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKP---AAGNIAVGGYNLKEkpLHAK 92
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLK--LSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 93 ANMGIQLQSTS--FQSELT-----------VTEIIRLYaavygLSLSDSEIEA----LLQNIKLETASS--KRF-GQLSG 152
Cdd:COG0444 79 ELRKIRGREIQmiFQDPMTslnpvmtvgdqIAEPLRIH-----GGLSKAEAREraieLLERVGLPDPERrlDRYpHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 153 GQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAIIDHGRIIEID 231
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250
....*....|.
gi 1721664488 232 SPQAIVD--RH 240
Cdd:COG0444 234 PVEELFEnpRH 244
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-261 |
3.43e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 129.47 E-value: 3.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANM-GIQL 99
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRrAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 QSTSFQSELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIA-------TMHKPKL 170
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHGSSAAQDRqiVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVlaqlwepVDGGPRW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 171 VLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQaivdrhrndaEVIRAS 250
Cdd:COG4559 162 LFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPE----------EVLTDE 231
|
250
....*....|.
gi 1721664488 251 rkgkiTLEDVF 261
Cdd:COG4559 232 -----LLERVY 237
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
20-238 |
3.80e-36 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 128.96 E-value: 3.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFT-AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGY---NLKEKPLH-AKAN 94
Cdd:TIGR02315 1 MLEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditKLRGKKLRkLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 95 MGIQLQSTSFQSELTVTEII---RL-----YAAVYGLsLSDSEIE---ALLQNIKLETASSKRFGQLSGGQQQRVSLAIA 163
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgRLgykptWRSLLGR-FSEEDKEralSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 164 TMHKPKLVLLDEPTTGLDPQSRRQLwerMESLRN----AGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVD 238
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQV---MDYLKRinkeDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
12-242 |
4.60e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 131.99 E-value: 4.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 12 TSSASTETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHA 91
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 K-ANmgiqlqsTSFQS-----ELTVTEIIrlyaaVYGLSL---SDSEIEAL----LQNIKLETASSKRFGQLSGGQQQRV 158
Cdd:PRK09452 86 RhVN-------TVFQSyalfpHMTVFENV-----AFGLRMqktPAAEITPRvmeaLRMVQLEEFAQRKPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 159 SLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIV 237
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIY 233
|
....*
gi 1721664488 238 DRHRN 242
Cdd:PRK09452 234 EEPKN 238
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
21-244 |
1.31e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.18 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAvhDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKAnmgiqlQ 100
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQ-----SELTVTEIIRLyaavyGLS----LSDSE---IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKP 168
Cdd:COG3840 74 SMLFQennlfPHLTVAQNIGL-----GLRpglkLTAEQraqVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721664488 169 KLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRNDA 244
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPA 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
21-229 |
1.59e-35 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 126.87 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQL- 99
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 -QSTSFQSELTVTEIIRLYAAVYGLSLS--DSEIEALLQniKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEP 176
Cdd:TIGR03410 81 pQGREIFPRLTVEENLLTGLAALPRRSRkiPDEIYELFP--VLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 177 TTGLDPQSRRQLWERMESLRN-AGHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAeGGMAILLVEQYLDFARELADRYYVMERGRVVA 212
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-229 |
1.81e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 126.32 E-value: 1.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTY-GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEkpLHAKA----- 93
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSR--LKRREipylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 94 -NMGIQLQSTSFQSELTVTEIIRLYAAVYGLSLSD--SEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKL 170
Cdd:COG2884 79 rRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEirRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 171 VLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-231 |
2.20e-35 |
|
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: 126.11 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 27 RVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlKEKPLHAkANMGiqlqstsFQS 106
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---RVSSLLG-LGGG-------FNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 107 ELTVTEIIRLYAAVYGLSlsDSEIEALLQNIK----LETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDP 182
Cdd:cd03220 98 ELTGRENIYLNGRLLGLS--RKEIDEKIDEIIefseLGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721664488 183 QSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEID 231
Cdd:cd03220 176 AFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
10-240 |
2.31e-35 |
|
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: 132.97 E-value: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 10 SATSSASTETVLQVENLRVTY--GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEK 87
Cdd:COG4987 323 AEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 88 PLHA-KANMGIQLQSTS-FQSelTVTEIIRLYAAvyglSLSDSEIEALLQNIKLET-ASSKRFG----------QLSGGQ 154
Cdd:COG4987 403 DEDDlRRRIAVVPQRPHlFDT--TLRENLRLARP----DATDEELWAALERVGLGDwLAALPDGldtwlgeggrRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 155 QQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRnAGHAILLTTHSMEEAEAVcDRIAIIDHGRIIEIDSPQ 234
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHE 554
|
....*.
gi 1721664488 235 AIVDRH 240
Cdd:COG4987 555 ELLAQN 560
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-248 |
3.73e-35 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 126.16 E-value: 3.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQL 99
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 --QSTSFQSELTVTE-IIRLYAAVYGLSLSDSEIEA--LLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLD 174
Cdd:PRK10895 83 lpQEASIFRRLSVYDnLMAVLQIRDDLSAEQREDRAneLMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 175 EPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVdrhrNDAEVIR 248
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL----QDEHVKR 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
27-243 |
4.83e-35 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 125.96 E-value: 4.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 27 RVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlKEKPLhakanmgIQLqSTSFQS 106
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVSAL-------LEL-GAGFHP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 107 ELTVTEIIRLYAAVYGLSLsdSEIEALLQNIkLETASSKRF-----GQLSGGQQQRVSLAIATMHKPKLVLLDEPT-TGl 180
Cdd:COG1134 102 ELTGRENIYLNGRLLGLSR--KEIDEKFDEI-VEFAELGDFidqpvKTYSSGMRARLAFAVATAVDPDILLVDEVLaVG- 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721664488 181 DPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRND 243
Cdd:COG1134 178 DAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYEAL 240
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
31-243 |
2.75e-34 |
|
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: 124.68 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 31 GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGG---YNLKEKPLHA--KANMGIQLQSTSFQ 105
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiAAMSRKELRElrRKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 106 SELTVTEIIRLYAAVYGLSLSDSEIEAL--LQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQ 183
Cdd:cd03294 115 PHRTVLENVAFGLEVQGVPRAEREERAAeaLELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 184 SRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRND 243
Cdd:cd03294 195 IRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPAND 255
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
21-226 |
6.22e-34 |
|
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: 120.95 E-value: 6.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFT--AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHA-KANMGI 97
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQSTSFqseltvteiirlyaavyglsLSDSeieaLLQNIkletasskrfgqLSGGQQQRVSLAIATMHKPKLVLLDEPT 177
Cdd:cd03228 81 VPQDPFL--------------------FSGT----IRENI------------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721664488 178 TGLDPQSRRQLWERMESLRNaGHAILLTTHSMEEAEAvCDRIAIIDHGR 226
Cdd:cd03228 125 SALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-229 |
9.26e-34 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 122.43 E-value: 9.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAG--NIAVGGYNLKEKPlHAKA----- 93
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlNIAGNHFDFSKTP-SDKAirelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 94 -NMGIQLQSTSFQSELTVTE-IIRLYAAVYGLSLSDSEIEA--LLQNIKLeTASSKRFG-QLSGGQQQRVSLAIATMHKP 168
Cdd:PRK11124 82 rNVGMVFQQYNLWPHLTVQQnLIEAPCRVLGLSKDQALARAekLLERLRL-KPYADRFPlHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 169 KLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
21-229 |
1.01e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 124.80 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYN---LKEKPL-HAK 92
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 93 ANMG-IqlqstsFQ-----SELTVTEIIRL---YAAVyglslSDSEIEA----LLQNIKLETASSKRFGQLSGGQQQRVS 159
Cdd:COG1135 82 RKIGmI------FQhfnllSSRTVAENVALpleIAGV-----PKAEIRKrvaeLLELVGLSDKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 160 LAIATMHKPKLVLLDEPTTGLDPQS-----------RRQLwermeslrnaGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETtrsildllkdiNREL----------GLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
.
gi 1721664488 229 E 229
Cdd:COG1135 221 E 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
21-229 |
1.03e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 122.43 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGG--YNLKEKPLHAKA----- 93
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDFSQKPSEKAIrllrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 94 NMGIQLQSTSFQSELTVTE-IIRLYAAVYGLSLSDSEIEA--LLQNIKLeTASSKRFG-QLSGGQQQRVSLAIATMHKPK 169
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMEnLIEAPCKVLGLSKEQAREKAmkLLARLRL-TDKADRFPlHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 170 LVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-264 |
1.38e-33 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 129.09 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAK-----AN 94
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAvcpriAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 95 M----GIQLQSTsfqseLTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKP 168
Cdd:NF033858 81 MpqglGKNLYPT-----LSVFENLDFFGRLFGQDAAERRrrIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 169 KLVLLDEPTTGLDPQSRRQLWERMESLR--NAGHAILLTTHSMEEAEAvCDRIAIIDHGRIIEIDSPQAIvdrhrndaev 246
Cdd:NF033858 156 DLLILDEPTTGVDPLSRRQFWELIDRIRaeRPGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAEL---------- 224
|
250
....*....|....*...
gi 1721664488 247 irASRKGKITLEDVFIGL 264
Cdd:NF033858 225 --LARTGADTLEAAFIAL 240
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
36-178 |
1.81e-33 |
|
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: 118.90 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 36 VHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPL-HAKANMGIQLQSTSFQSELTVTEII 114
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 115 RLYAAVYGLS--LSDSEIEALLQNIKLE----TASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTT 178
Cdd:pfam00005 81 RLGLLLKGLSkrEKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
30-239 |
1.85e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 30 YGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLK-----EKPLHAKANMGIQlQSTSF 104
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkvdERLIRQEAGMVFQ-QFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 105 qSELTVTE-----IIRlyaaVYGLSLSDSEIEA--LLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPT 177
Cdd:PRK09493 90 -PHLTALEnvmfgPLR----VRGASKEEAEKQAreLLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 178 TGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDR 239
Cdd:PRK09493 165 SALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
51-236 |
3.66e-33 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 122.99 E-value: 3.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 51 LLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHaKANMGIQLQSTSFQSELTVTEIIrlyaaVYGLSLS---- 126
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH-LRHINMVFQSYALFPHMTVEENV-----AFGLKMRkvpr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 127 ---DSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAI 202
Cdd:TIGR01187 75 aeiKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIqEQLGITF 154
|
170 180 190
....*....|....*....|....*....|....
gi 1721664488 203 LLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
38-236 |
5.40e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 121.86 E-value: 5.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGY---------NLKEkpLHAKANMGIQLQSTSFqSEL 108
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpetgnkNLKK--LRKKVSLVFQFPEAQL-FEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 109 TVTEIIRLYAAVYGLSLSDSEIEAL--LQNIKL-ETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSR 185
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEKALkwLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 186 RQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK13641 182 KEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-258 |
6.74e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.13 E-value: 6.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 17 TETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKtSSL-SAIEGLLKPAAGNIAVGGYNLKEK-PLHAKAN 94
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGK-STLmKILSGVYQPDSGEILLDGEPVRFRsPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 95 mGIQL--QSTSFQSELTVTEIIRL-----------YAAVYglslsdSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLA 161
Cdd:COG1129 80 -GIAIihQELNLVPNLSVAENIFLgreprrgglidWRAMR------RRARELLARLGLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 162 IATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII------EIDSPQ- 234
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVgtgpvaELTEDEl 232
|
250 260
....*....|....*....|....*.
gi 1721664488 235 --AIVDRHRNDAEVIRASRKGKITLE 258
Cdd:COG1129 233 vrLMVGRELEDLFPKRAAAPGEVVLE 258
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-233 |
1.77e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.54 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFT-----AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPL---HAK 92
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklsDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 93 ANMGIQLQSTSFQ-SELTVTEIIrlyaaVYG---LSLSDSEI-----EAL-LQNIKLETASSKRFGQLSGGQQQRVSLAI 162
Cdd:PRK13637 83 KKVGLVFQYPEYQlFEETIEKDI-----AFGpinLGLSEEEIenrvkRAMnIVGLDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 163 ATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSP 233
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
20-226 |
1.84e-32 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 118.50 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTY-GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKA----N 94
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPllrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 95 MGIQLQSTSFQSELTVTEIIRLYAAVYGLS--LSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVL 172
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKerEIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 173 LDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGR 226
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
22-232 |
3.32e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 121.06 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 22 QVENLRVTY----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYN---LKEKPL-HAKA 93
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltaLSEKELrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 94 NMGIQLQSTSFQSELTVTEIIRLYAAVYGlsLSDSEIEA----LLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPK 169
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAG--TPKAEIKArvteLLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 170 LVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDS 232
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
24-260 |
3.72e-32 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 119.81 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 24 ENLRVTY-GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHA-KANMGIQLQS 101
Cdd:COG1125 5 ENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElRRRIGYVIQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 102 TSFQSELTVTEII----RLyaavygLSLSDSEIEA----LLQNIKLETAS-SKRF-GQLSGGQQQRVSLAIATMHKPKLV 171
Cdd:COG1125 85 IGLFPHMTVAENIatvpRL------LGWDKERIRArvdeLLELVGLDPEEyRDRYpHELSGGQQQRVGVARALAADPPIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 172 LLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRND--AEVIR 248
Cdd:COG1125 159 LMDEPFGALDPITREQLQDELLRLqRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDfvADFVG 238
|
250
....*....|....*.
gi 1721664488 249 ASRKGK----ITLEDV 260
Cdd:COG1125 239 ADRGLRrlslLRVEDL 254
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-248 |
3.80e-32 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 124.56 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFT--AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHA-KANMGI 97
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQS------------TSFQSELTVTEIIRLyAAVYGLslsDSEIEALLQniKLETASSKRFGQLSGGQQQRVSLAIATM 165
Cdd:COG2274 554 VLQDvflfsgtireniTLGDPDATDEEIIEA-ARLAGL---HDFIEALPM--GYDTVVGEGGSNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 166 HKPKLVLLDEPTTGLDPQSRRQLWERMESLRnAGHAILLTTHSMEEAEAvCDRIAIIDHGRIIEIDSPQAIVDRHRNDAE 245
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYAE 705
|
...
gi 1721664488 246 VIR 248
Cdd:COG2274 706 LVQ 708
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-247 |
1.35e-31 |
|
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: 119.45 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 25 NLRVTYGSFTAvhDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEK------PLHAKAnMGIQ 98
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrkgiflPPEKRR-IGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQSTSFQSELTVTEIIRlyaavYGLSLSDSEI-----EALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLL 173
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLR-----YGMKRARPSErrisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 174 DEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDR------HRNDAEV 246
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASpdlpwlAREDQGS 235
|
.
gi 1721664488 247 I 247
Cdd:TIGR02142 236 L 236
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-231 |
1.50e-31 |
|
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: 115.86 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 31 GSFTAvhDVSFsVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGG--YNLKEKPLH---AKANMGIQLQSTSFQ 105
Cdd:cd03297 11 PDFTL--KIDF-DLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvLFDSRKKINlppQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 106 SELTVTEIIrlyaaVYGLS-LSDSEI----EALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGL 180
Cdd:cd03297 88 PHLNVRENL-----AFGLKrKRNREDrisvDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 181 DPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEID 231
Cdd:cd03297 163 DRALRLQLLPELKQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
31-243 |
5.13e-31 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 118.42 E-value: 5.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 31 GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLK-----EKPLHAKANMGIQLQSTSFQ 105
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMkqspvELREVRRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 106 SELTVTEIIRLYAAVYGLSLSDSEIEAL--LQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQ 183
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALelLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 184 SRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRND 243
Cdd:TIGR01186 164 IRDSMQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANE 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-235 |
1.21e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 113.35 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKP---AAGNIAVGGYNLKEKPLHAKaNMGI 97
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQR-RIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQSTSFQSELTVTEIIRL-YAAVYGLSLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEP 176
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFaLPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721664488 177 TTGLDP----QSRRQLWERmesLRNAGHAILLTTHSMEEAEAvcdriaiidHGRIIEIDSPQA 235
Cdd:COG4136 161 FSKLDAalraQFREFVFEQ---IRQRGIPALLVTHDEEDAPA---------AGRVLDLGNWQH 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
21-236 |
1.33e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 117.11 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEkpLHAK-ANMGIQL 99
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARdRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 QSTSFQSELTVTEIIrlyaaVYGLSL-----------SDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKP 168
Cdd:PRK10851 81 QHYALFRHMTVFDNI-----AFGLTVlprrerpnaaaIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 169 KLVLLDEPTTGLDPQSRRQL--WERM--ESLRNAGhaiLLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELrrWLRQlhEELKFTS---VFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-247 |
1.70e-30 |
|
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: 116.74 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 25 NLRVTYGSFTAvhDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGG---------YNLkekPLHaKANM 95
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargIFL---PPH-RRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 GIQLQSTSFQSELTVTEIIRlyaavYGLSLSDS--------------EIEALLQnikletassKRFGQLSGGQQQRVSLA 161
Cdd:COG4148 80 GYVFQEARLFPHLSVRGNLL-----YGRKRAPRaerrisfdevvellGIGHLLD---------RRPATLSGGERQRVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 162 IATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGH-AILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDR- 239
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDiPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRp 225
|
250
....*....|....
gi 1721664488 240 ------HRNDAEVI 247
Cdd:COG4148 226 dllplaGGEEAGSV 239
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
14-235 |
2.34e-30 |
|
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: 113.30 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 14 SASTETVLQVENLRVTY----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLK---E 86
Cdd:COG4181 2 SSSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 87 KPLHA--KANMGIQLQStsFQ--SELTVTEIIRLYAAVYGLSLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAI 162
Cdd:COG4181 82 DARARlrARHVGFVFQS--FQllPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 163 ATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAvCDRIAIIDHGRIIEIDSPQA 235
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
21-236 |
9.71e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.43 E-value: 9.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKaNMGIQLQ 100
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR-DICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIRlyaavYGL---SLSDSEI-----EALlQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVL 172
Cdd:PRK11432 86 SYALFPHMSLGENVG-----YGLkmlGVPKEERkqrvkEAL-ELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721664488 173 LDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-236 |
1.05e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.41 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 19 TVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkeKPLHAKANMGIQ 98
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD-----KPISMLSSRQLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQSTSFQSELTVTEIIRLYAAV-YGLS--------LSDSE---IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMH 166
Cdd:PRK11231 76 RRLALLPQHHLTPEGITVRELVaYGRSpwlslwgrLSAEDnarVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 167 KPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-271 |
2.40e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 111.62 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTYGSFT--AVHDVSFSVLGGEIFGLLGPNGAGKtSSLSAI-EGLLKPAAGNIAVGGYNL-KEKPLHAKA 93
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGK-STISKIlTGLLKPQSGEIKIDGITIsKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 94 NMGIQLQSTSFQ-SELTVTEIIrlyaaVYGLS---LSDSE----IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATM 165
Cdd:PRK13632 84 KIGIIFQNPDNQfIGATVEDDI-----AFGLEnkkVPPKKmkdiIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 166 HKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLT-THSMEEAeAVCDRIAIIDHGRIIEIDSPQAIVdrhrNDA 244
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGKPKEIL----NNK 233
|
250 260
....*....|....*....|....*..
gi 1721664488 245 EVIRasrkgKITLEDVFIGLTGTAIRS 271
Cdd:PRK13632 234 EILE-----KAKIDSPFIYKLSKKLKG 255
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-237 |
5.68e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 113.40 E-value: 5.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkeKPLHAK--ANMGIQ 98
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG-----DDVEALsaRAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 L----QSTSFQSELTVTEIIRL----YAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKP 168
Cdd:PRK09536 79 VasvpQDTSLSFEFDVRQVVEMgrtpHRSRFDTWTETDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 169 KLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIV 237
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-236 |
6.24e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 110.88 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 17 TETVLQVENLRVTY--GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKP---LHA 91
Cdd:PRK13635 2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KANMGIQLQSTSFQSElTVTEIIrlyaaVYGLS---LSDSE----IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIAT 164
Cdd:PRK13635 82 QVGMVFQNPDNQFVGA-TVQDDV-----AFGLEnigVPREEmverVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721664488 165 MHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLT-THSMEEAeAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-207 |
7.76e-29 |
|
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: 108.60 E-value: 7.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQLQ 100
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIRLYAAVYGLSlsDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGL 180
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGA--QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180
....*....|....*....|....*..
gi 1721664488 181 DPQSRRQLWERMESLRNAGHAILLTTH 207
Cdd:TIGR01189 159 DKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
9-229 |
8.03e-29 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 111.74 E-value: 8.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 9 NSATSSASTETVLQVENLRVTY----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLkpaAGNIAVGG--- 81
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL---AANGRIGGsat 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 82 ------YNLKEKPLH----AKANMGIQLQSTSFQSELTV----TEIIRLYAavyGLSLSDSEIEA--LLQNIKLETASsK 145
Cdd:PRK09473 78 fngreiLNLPEKELNklraEQISMIFQDPMTSLNPYMRVgeqlMEVLMLHK---GMSKAEAFEESvrMLDAVKMPEAR-K 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 146 RFG----QLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIA 220
Cdd:PRK09473 154 RMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVL 233
|
....*....
gi 1721664488 221 IIDHGRIIE 229
Cdd:PRK09473 234 VMYAGRTME 242
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
17-236 |
9.33e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 109.87 E-value: 9.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 17 TETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIE--GLLKP---AAGNIAVGGYNLKEK---- 87
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIYSPrtdt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 88 -PLHAKANMGIQlQSTSFqsELTVTEIIrlyaaVYGLSLS--------DSEIEALLQNIKLETASSKRFGQ----LSGGQ 154
Cdd:PRK14239 82 vDLRKEIGMVFQ-QPNPF--PMSIYENV-----VYGLRLKgikdkqvlDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 155 QQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAgHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQ 234
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTK 232
|
..
gi 1721664488 235 AI 236
Cdd:PRK14239 233 QM 234
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-236 |
1.98e-28 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 109.06 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY--GSFTAVHDVSFSVLGGEIFGLLGPNGAGKtSSLS-AIEGLLKPAAGNIAVGGYN-LKEKPLHA-KANM 95
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGK-STLAkLLNGLLLPTSGKVTVDGLDtLDEENLWEiRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 GI-------QLQSTsfqselTVTEIIrlyaaVYGLS---LSDSEIEALLQNikletaSSKRFG----------QLSGGQQ 155
Cdd:TIGR04520 80 GMvfqnpdnQFVGA------TVEDDV-----AFGLEnlgVPREEMRKRVDE------ALKLVGmedfrdrephLLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 156 QRVSLA--IAtMhKPKLVLLDEPTTGLDPQSRRQLWERMESLRN-AGHAILLTTHSMEEAeAVCDRIAIIDHGRIIEIDS 232
Cdd:TIGR04520 143 QRVAIAgvLA-M-RPDIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGT 219
|
....
gi 1721664488 233 PQAI 236
Cdd:TIGR04520 220 PREI 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-227 |
2.13e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 107.88 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY-GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEkpLHAKA------ 93
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSD--LRGRAipylrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 94 NMGIQLQSTSFQSELTVTEIIRLYAAVYGLSLSD--SEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLV 171
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREirKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 172 LLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRI 227
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-235 |
2.32e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.80 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 11 ATSSASTETVLQVENLRVTygsfTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEK-PL 89
Cdd:COG1129 247 KRAAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRsPR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 90 HAKANmGIQL-----QSTSFQSELTVTE--------------IIRLYAAVyglSLSDSEIEALlqNIKleTASSKRF-GQ 149
Cdd:COG1129 323 DAIRA-GIAYvpedrKGEGLVLDLSIREnitlasldrlsrggLLDRRRER---ALAEEYIKRL--RIK--TPSPEQPvGN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 150 LSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII- 228
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVg 474
|
....*..
gi 1721664488 229 EIDSPQA 235
Cdd:COG1129 475 ELDREEA 481
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-208 |
2.53e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 107.27 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPL--------HA 91
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeachylgHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KAnmgiqlqstsFQSELTVTEIIRLYAAVYGlsLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLA--IATmHKPk 169
Cdd:PRK13539 82 NA----------MKPALTVAENLEFWAAFLG--GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALArlLVS-NRP- 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 1721664488 170 LVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHS 208
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-229 |
2.77e-28 |
|
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: 108.74 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 19 TVLQVENLRVTY--GSF-------TAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL-KEKP 88
Cdd:TIGR02769 1 SLLEVRDVTHTYrtGGLfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 89 LHAKA-----NMGIQLQSTSFQSELTVTEIIRLYAAVYgLSLSDSE----IEALLQNIKLETASSKRF-GQLSGGQQQRV 158
Cdd:TIGR02769 81 KQRRAfrrdvQLVFQDSPSAVNPRMTVRQIIGEPLRHL-TSLDESEqkarIAELLDMVGLRSEDADKLpRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 159 SLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-229 |
3.59e-28 |
|
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: 106.84 E-value: 3.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGL--LKPAAGNIAVGGYNLKEKPLHAKANMGIQ 98
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LqstSFQSEltvteiirlyAAVYGLSLSDseieaLLQNIKLetasskrfgQLSGGQQQRVSLAIATMHKPKLVLLDEPTT 178
Cdd:cd03217 81 L---AFQYP----------PEIPGVKNAD-----FLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 179 GLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAV-CDRIAIIDHGRIIE 229
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-229 |
4.38e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.08 E-value: 4.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 19 TVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGgynlkekplhAKANMGI- 97
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----------ETVKIGYf 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 -QLQSTsFQSELTVTEIIRLYAAvyglSLSDSEIEALLQnikletasskRF-----------GQLSGGQQQRVSLAIATM 165
Cdd:COG0488 384 dQHQEE-LDPDKTVLDELRDGAP----GGTEQEVRGYLG----------RFlfsgddafkpvGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721664488 166 HKPKLVLLDEPTTGLDPQSRRQLwerMESLRN-AGhAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEAL---EEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-212 |
5.51e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 108.03 E-value: 5.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 19 TVLQVENLRVTYGSF----TAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkeKPLHAK-A 93
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-----VPVTGPgA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 94 NMGIQLQSTSFQSELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLV 171
Cdd:COG4525 77 DRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRarAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1721664488 172 LLDEPTTGLDPQSRrqlwERMESL-----RNAGHAILLTTHSMEEA 212
Cdd:COG4525 157 LMDEPFGALDALTR----EQMQELlldvwQRTGKGVFLITHSVEEA 198
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-219 |
8.97e-28 |
|
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: 111.22 E-value: 8.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 2 ESTMPATNSATSSASTETVLQVENLRVTY-GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVG 80
Cdd:TIGR02857 303 AAPRPLAGKAPVTAAPASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 81 GYNLKEKPLHAKANMGIQLQSTSFQSELTVTEIIRLYAAVyglsLSDSEIEALLQNI-----------KLETASSKRFGQ 149
Cdd:TIGR02857 383 GVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPD----ASDAEIREALERAgldefvaalpqGLDTPIGEGGAG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 150 LSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNaGHAILLTTHSMEEAEAvCDRI 219
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAAL-ADRI 526
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-250 |
1.09e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.47 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFT-AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKP---LHAKANM 95
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKkslLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 GIQLQSTSFQ-SELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLA-IATMhKPKLV 171
Cdd:PRK13639 81 GIVFQNPDDQlFAPTVEEDVAFGPLNLGLSKEEVEkrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAgILAM-KPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 172 LLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVdrhrNDAEVIRAS 250
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF----SDIETIRKA 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
22-261 |
1.28e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 106.71 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 22 QVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKA-NMGIQLQ 100
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAkRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIRlyaavYG--------LSLSDSE-IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLV 171
Cdd:COG4604 83 ENHINSRLTVRELVA-----FGrfpyskgrLTAEDREiIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 172 LLDEPTTGLDPQSRRQLwerMESLRNA----GHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPqaivdrhrndAEVI 247
Cdd:COG4604 158 LLDEPLNNLDMKHSVQM---MKLLRRLadelGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP----------EEII 224
|
250
....*....|....
gi 1721664488 248 RASrkgkiTLEDVF 261
Cdd:COG4604 225 TPE-----VLSDIY 233
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-219 |
3.27e-27 |
|
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: 104.50 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQLQ 100
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIRLYAAVYglslSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGL 180
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADH----SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1721664488 181 DPQSRRQLWERMESLRNAGHAILLTTH-SMEEAEAVCDRI 219
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTHqDLGLSEAGAREL 196
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
20-242 |
4.06e-27 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 105.45 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGL--LKP---AAGNIAVGG---YNLKEKPLHA 91
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndLVPgvrIEGKVLFDGqdiYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KANMGIQLQS-TSFqsELTVTEIIrlyaaVYGLSLS--------DSEIEALLQNIKLETASSKRFGQ----LSGGQQQRV 158
Cdd:TIGR00972 81 RRRVGMVFQKpNPF--PMSIYDNI-----AYGPRLHgikdkkelDEIVEESLKKAALWDEVKDRLHDsalgLSGGQQQRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 159 SLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAgHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVD 238
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFT 232
|
....
gi 1721664488 239 RHRN 242
Cdd:TIGR00972 233 NPKE 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-247 |
5.42e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.96 E-value: 5.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVT-YGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMG 96
Cdd:COG3845 255 EVVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 IqlqstSFQSE----------LTVTE--IIRLY---AAVYGLSLSDSEIEALLQ------NIKLETASSkRFGQLSGGQQ 155
Cdd:COG3845 335 V-----AYIPEdrlgrglvpdMSVAEnlILGRYrrpPFSRGGFLDRKAIRAFAEelieefDVRTPGPDT-PARSLSGGNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 156 QRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIeidspqA 235
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV------G 482
|
250
....*....|..
gi 1721664488 236 IVDRHRNDAEVI 247
Cdd:COG3845 483 EVPAAEATREEI 494
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-229 |
8.43e-27 |
|
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: 108.62 E-value: 8.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 16 STETVLQVENLRVTYGS----FTAVHDVSFSVLGGEIFGLLGPNGAGKT-SSLSAIeGLLKPAA----GNIAVGGYNLke 86
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPAahpsGSILFDGQDL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 87 kpLHAKANmgiQLQ-------STSFQSELT-----------VTEIIRLYAavyGLSLSD--SEIEALLQNIKLETASsKR 146
Cdd:COG4172 79 --LGLSER---ELRrirgnriAMIFQEPMTslnplhtigkqIAEVLRLHR---GLSGAAarARALELLERVGIPDPE-RR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 147 FG----QLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAI 221
Cdd:COG4172 150 LDayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAV 229
|
....*...
gi 1721664488 222 IDHGRIIE 229
Cdd:COG4172 230 MRQGEIVE 237
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-243 |
1.17e-26 |
|
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: 108.23 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 15 ASTETVLQVENLRVTY-----------GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLkPAAGNIAVGGYN 83
Cdd:COG4172 270 PDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 84 ---LKEKPLHA-KANMGIQLQS--TSFQSELTVTEIIRLYAAVYGLSLSDSEIEA----LLQNIKLETASSKRF-GQLSG 152
Cdd:COG4172 349 ldgLSRRALRPlRRRMQVVFQDpfGSLSPRMTVGQIIAEGLRVHGPGLSAAERRArvaeALEEVGLDPAARHRYpHEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 153 GQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEID 231
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQG 508
|
250
....*....|..
gi 1721664488 232 SPQAIVDRHRND 243
Cdd:COG4172 509 PTEQVFDAPQHP 520
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
35-228 |
1.44e-26 |
|
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: 103.05 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 35 AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKE-KPLHAKANMGIQLQSTSFQSElTVTEI 113
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFYG-TLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 114 IRLyaavyGLSLSDSE----------IEALLQNIK--LETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLD 181
Cdd:cd03245 98 ITL-----GAPLADDErilraaelagVTDFVNKHPngLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1721664488 182 PQSRRQLWERMESLRnAGHAILLTTHSMeEAEAVCDRIAIIDHGRII 228
Cdd:cd03245 173 MNSEERLKERLRQLL-GDKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
19-229 |
1.93e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 103.68 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 19 TVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLK-EKPLHAKANMGI 97
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtARSLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQSTS---FQS-----ELTVTE-IIRLYAAVYGLSLSDSEIEA--LLQNIKL---ETASSKRfgqLSGGQQQRVSLAIA 163
Cdd:PRK11264 82 QLRQHVgfvFQNfnlfpHRTVLEnIIEGPVIVKGEPKEEATARAreLLAKVGLagkETSYPRR---LSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 164 TMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-228 |
2.12e-26 |
|
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: 101.86 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVT------YGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAA--GNIAVGGYNLKEKPLha 91
Cdd:cd03213 3 TLSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSF-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KANMGIQLQSTSFQSELTVTEIIRlYAAvyglslsdseieallqNIKletasskrfgQLSGGQQQRVSLAIATMHKPKLV 171
Cdd:cd03213 81 RKIIGYVPQDDILHPTLTVRETLM-FAA----------------KLR----------GLSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 172 LLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHS-MEEAEAVCDRIAIIDHGRII 228
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
21-254 |
2.33e-26 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 107.64 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY-GSFT-AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKE-KPLHAKANMGI 97
Cdd:TIGR03375 464 IEFRNVSFAYpGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQiDPADLRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQSTS-FQSelTVTEIIRLYAAvyglSLSDSEI-EAL-------LQNIK---LETASSKRFGQLSGGQQQRVSLAIATM 165
Cdd:TIGR03375 544 VPQDPRlFYG--TLRDNIALGAP----YADDEEIlRAAelagvteFVRRHpdgLDMQIGERGRSLSGGQRQAVALARALL 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 166 HKPKLVLLDEPTTGLDPQSRRQLWERMESLRnAGHAILLTTHSMEEAEAVcDRIAIIDHGRIIeIDSPQaivdrhrndAE 245
Cdd:TIGR03375 618 RDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLV-DRIIVMDNGRIV-ADGPK---------DQ 685
|
....*....
gi 1721664488 246 VIRASRKGK 254
Cdd:TIGR03375 686 VLEALRKGR 694
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-228 |
2.61e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.63 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFT-----AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANM 95
Cdd:COG1101 2 LELKNLSKTFNPGTvnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 gIqlqSTSFQ-------SELTVTEIIRLYAA---VYGLS--LSDSEIE------ALLqNIKLETASSKRFGQLSGGQQQR 157
Cdd:COG1101 82 -I---GRVFQdpmmgtaPSMTIEENLALAYRrgkRRGLRrgLTKKRRElfrellATL-GLGLENRLDTKVGLLSGGQRQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 158 VSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGH-AILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-240 |
2.92e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.17 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 1 MESTMPATNSATSSASTETVLQVENLRVTY-GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAV 79
Cdd:COG1132 320 EPPEIPDPPGAVPLPPVRGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 80 GGYNLKEKPLHA-KANMGIQLQSTS-FQseLTVTEIIRlyaavYG-LSLSDSEIEA------LLQNIK-----LETASSK 145
Cdd:COG1132 400 DGVDIRDLTLESlRRQIGVVPQDTFlFS--GTIRENIR-----YGrPDATDEEVEEaakaaqAHEFIEalpdgYDTVVGE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 146 RFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRnAGHAILLTTHSMEEAEAvCDRIAIIDHG 225
Cdd:COG1132 473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDG 550
|
250
....*....|....*
gi 1721664488 226 RIIEIDSPQAIVDRH 240
Cdd:COG1132 551 RIVEQGTHEELLARG 565
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
17-236 |
3.10e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.12 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 17 TETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL---KEKPLHAKA 93
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvRDKDGQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 94 NMGIQLQ------STSFQ-----SELTVTE-IIRLYAAVYGLSLSDSEIEALLQNIKL---ETASSKRFGQLSGGQQQRV 158
Cdd:PRK10619 82 ADKNQLRllrtrlTMVFQhfnlwSHMTVLEnVMEAPIQVLGLSKQEARERAVKYLAKVgidERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 159 SLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-233 |
3.86e-26 |
|
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: 101.80 E-value: 3.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY--GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHA-KANMGI 97
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQ-STSFQSEltvteiIRLYAAVYGLSlSDSEIEALLQNIKLETASSKRFGQL-----------SGGQQQRVSLAIATM 165
Cdd:cd03244 83 IPQdPVLFSGT------IRSNLDPFGEY-SDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 166 HKPKLVLLDEPTTGLDPQSRRQLwerMESLRN--AGHAILLTTHSMeeaEAV--CDRIAIIDHGRIIEIDSP 233
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALI---QKTIREafKDCTVLTIAHRL---DTIidSDRILVLDKGRVVEFDSP 221
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
23-219 |
3.88e-26 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 101.54 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 23 VENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNlkEKPLHAKANMGIQLQST 102
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQE--TPPLNSKKASKFRREKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 103 S--FQS-----ELTVTEIIRLyaAVYGLSLSDSEIEAL----LQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLV 171
Cdd:TIGR03608 79 GylFQNfalieNETVEENLDL--GLKYKKLSKKEKREKkkeaLEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1721664488 172 LLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEaVCDRI 219
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK-QADRV 203
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
21-212 |
5.80e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.47 E-value: 5.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkeKPLHAK-ANMGIQL 99
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEGPgAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 QSTSFQSELTVTEIIRLYAAVYGLSLSDSEIEA--LLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPT 177
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAhqMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1721664488 178 TGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEA 212
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEA 192
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-227 |
6.29e-26 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 99.98 E-value: 6.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTA--VHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKE-KPLHAKANMGI 97
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQStsfqseltvteiIRLyaavyglsLSDSeieaLLQNIkletasskrfgqLSGGQQQRVSLAIATMHKPKLVLLDEPT 177
Cdd:cd03246 81 LPQD------------DEL--------FSGS----IAENI------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721664488 178 TGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAvCDRIAIIDHGRI 227
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-230 |
6.74e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.02 E-value: 6.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 1 MESTMPATNSATSSASTETVLQVENlrVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVG 80
Cdd:PRK09700 246 LQNRFNAMKENVSNLAHETVFEVRN--VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLN 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 81 GYNLKEK-PLHA-KANMGIQLQS---TSFQSELTVTEIIRL--------YAAVYGLSLSDSE---IEALLQNIKLETAS- 143
Cdd:PRK09700 324 GKDISPRsPLDAvKKGMAYITESrrdNGFFPNFSIAQNMAIsrslkdggYKGAMGLFHEVDEqrtAENQRELLALKCHSv 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 144 SKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIID 223
Cdd:PRK09700 404 NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFC 483
|
....*..
gi 1721664488 224 HGRIIEI 230
Cdd:PRK09700 484 EGRLTQI 490
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
23-228 |
9.57e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.53 E-value: 9.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 23 VENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkekplhaKANMGIQLQST 102
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----------GLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 103 SFQSELTVTE-----------IIRLYAAVY------------------------GLSLsDSEIEALLQNIKLETAS-SKR 146
Cdd:COG0488 71 PLDDDLTVLDtvldgdaelraLEAELEELEaklaepdedlerlaelqeefealgGWEA-EARAEEILSGLGFPEEDlDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 147 FGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRqlW-ERMesLRNAGHAILLTTHSMEEAEAVCDRIAIIDHG 225
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WlEEF--LKNYPGTVLVVSHDRYFLDRVATRILELDRG 225
|
...
gi 1721664488 226 RII 228
Cdd:COG0488 226 KLT 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
35-236 |
1.08e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.41 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 35 AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVG------GYNLKE-KPLHAKanMGIQLQSTSFQ-S 106
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitaGKKNKKlKPLRKK--VGIVFQFPEHQlF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 107 ELTVTEIIRLYAAVYGLSLSDSEIEA--LLQNIKL-ETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQ 183
Cdd:PRK13634 100 EETVEKDICFGPMNFGVSEEDAKQKAreMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 184 SRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK13634 180 GRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-236 |
1.11e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 101.65 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 11 ATSSASTETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGL--LKPAA---GNIAVGG---Y 82
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGediY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 83 NLKEKPLHAKANMGIqlqstSFQS----ELTVTEIIrlyaaVYGLSL----SDSEIE----------ALLQNIK--LET- 141
Cdd:COG1117 82 DPDVDVVELRRRVGM-----VFQKpnpfPKSIYDNV-----AYGLRLhgikSKSELDeiveeslrkaALWDEVKdrLKKs 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 142 ASSkrfgqLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAgHAILLTTHSMEEAEAVCDRIAI 221
Cdd:COG1117 152 ALG-----LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAF 225
|
250
....*....|....*
gi 1721664488 222 IDHGRIIEIDSPQAI 236
Cdd:COG1117 226 FYLGELVEFGPTEQI 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-237 |
1.21e-25 |
|
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: 105.27 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTY-----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAG--NIAVG---------G 81
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGdewvdmtkpG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 82 YNLKEKplhAKANMGIQLQSTSFQSELTV----TEIIRL--------YAAVYGL---SLSDSEIEALLQnikletassKR 146
Cdd:TIGR03269 357 PDGRGR---AKRYIGILHQEYDLYPHRTVldnlTEAIGLelpdelarMKAVITLkmvGFDEEKAEEILD---------KY 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 147 FGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWER-MESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHG 225
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSiLKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDG 504
|
250
....*....|..
gi 1721664488 226 RIIEIDSPQAIV 237
Cdd:TIGR03269 505 KIVKIGDPEEIV 516
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-225 |
1.26e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 105.25 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 17 TETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGG--YNLKEKPLHAKAN 94
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 95 MGIQLQSTSFQSELTVTE---IIRLYA-AVYGLSLSD-----SEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATM 165
Cdd:PRK09700 82 IGIIYQELSVIDELTVLEnlyIGRHLTkKVCGVNIIDwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 166 HKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHG 225
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
21-226 |
1.58e-25 |
|
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: 98.29 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlKEKPLHakanmgiqlq 100
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---TVKIGY---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 stsfqseltvteiirlyaavyglslsdseieallqnikletasskrFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGL 180
Cdd:cd03221 68 ----------------------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1721664488 181 DPQSRRQLwERMesLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGR 226
Cdd:cd03221 102 DLESIEAL-EEA--LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
30-212 |
1.78e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.62 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 30 YGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkekplHAKANMGIQLQSTSFQSELT 109
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG--------GARVAYVPQRSEVPDSLPLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 110 VTEIIRL-----YAAVYGLSLSD-SEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQ 183
Cdd:NF040873 74 VRDLVAMgrwarRGLWRRLTRDDrAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180
....*....|....*....|....*....
gi 1721664488 184 SRRQLWERMESLRNAGHAILLTTHSMEEA 212
Cdd:NF040873 154 SRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
35-212 |
2.48e-25 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 99.03 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 35 AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL---KEKPLHAKANMGIQLQSTSFQseltvt 111
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDPDDQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 112 eiirLYAAVYG---------LSLSDSEIEAL----LQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTT 178
Cdd:TIGR01166 81 ----LFAADVDqdvafgplnLGLSEAEVERRvreaLTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|....
gi 1721664488 179 GLDPQSRRQLWERMESLRNAGHAILLTTHSMEEA 212
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-228 |
2.87e-25 |
|
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: 99.49 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSvlGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKAnMGIQLQ 100
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-VSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSELTVTEIIRLyAAVYGLSLSDSE---IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPT 177
Cdd:cd03298 78 ENNLFAHLTVEQNVGL-GLSPGLKLTAEDrqaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 178 TGLDPQSRRQLWERM-ESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:cd03298 157 AALDPALRAEMLDLVlDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-230 |
3.02e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 100.30 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGL--LKPAA---GNIAVGG---YNLKEKPLHAK 92
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRLFGrniYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 93 ANMGIQLQSTSFQSELTVTEIIRLYAAVYGLSLSDSEI----EALLQNIKLETASSKRF----GQLSGGQQQRVSLAIAT 164
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELdervEWALKKAALWDEVKDRLndypSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 165 MHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAgHAILLTTHSMEEAEAVCDRIAIIDHGRIIEI 230
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEV 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
38-243 |
3.11e-25 |
|
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: 99.85 E-value: 3.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKplhAKANMgIQLQSTSFQSELTVTEIIRLY 117
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEP---GPDRM-VVFQNYSLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 118 AAVYGLSLSDSEIEAL----LQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWER-M 192
Cdd:TIGR01184 79 VDRVLPDLSKSERRAIveehIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEElM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1721664488 193 ESLRNAGHAILLTTHSMEEAEAVCDRIAIIDH------GRIIEIDSPQAivdRHRND 243
Cdd:TIGR01184 159 QIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNgpaaniGQILEVPFPRP---RDRLE 212
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
11-244 |
3.22e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 100.63 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 11 ATSSASTETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGL--LKPAA---GNIAVGGYNLK 85
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTFHGKNLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 86 EK---PLHAKANMGIQLQSTS-FQSelTVTEIIRLYAAVYGLSLS-DSEIEALLQNIKLETASSKRFGQ----LSGGQQQ 156
Cdd:PRK14243 81 APdvdPVEVRRRIGMVFQKPNpFPK--SIYDNIAYGARINGYKGDmDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 157 RVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAgHAILLTTHSMEEAEAVCDRIAIID---------HGRI 227
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYL 237
|
250
....*....|....*..
gi 1721664488 228 IEIDSPQAIVDRHRNDA 244
Cdd:PRK14243 238 VEFDRTEKIFNSPQQQA 254
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-241 |
6.93e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 103.07 E-value: 6.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQL- 99
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 -QSTSFQSELTVTEIIRL-----YAAVYGLSLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLL 173
Cdd:PRK11288 85 yQELHLVPEMTVAENLYLgqlphKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 174 DEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHR 241
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDRDQ 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-243 |
8.51e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 99.70 E-value: 8.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLL---KPAAGNIAVGGYNLKEKPLHA--- 91
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRLArdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 ---KANMGIQLQSTSFQSELTVTEIIRLYA----------AVYGLSLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRV 158
Cdd:PRK09984 82 rksRANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 159 SLAIATMHKPKLVLLDEPTTGLDPQSRRQLwerMESLR----NAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQ 234
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIV---MDTLRdinqNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
....*....
gi 1721664488 235 AIvDRHRND 243
Cdd:PRK09984 239 QF-DNERFD 246
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
35-236 |
1.45e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.42 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 35 AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL------KE-KPLHAKANMGIQLQSTSFQSE 107
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstskqKEiKPVRKKVGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 108 lTVTEIIRLYAAVYGLSLSDSEIEALLqniKLETAS-SKRFGQ-----LSGGQQQRVSLAIATMHKPKLVLLDEPTTGLD 181
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAE---KLEMVGlADEFWEkspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1721664488 182 PQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-237 |
1.90e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 98.03 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLH--AKANMGI 97
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQSTSFQSELTVTEIIRLYAAVYGLSLSDSEIEALLQNI-KLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEP 176
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 177 TTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIV 237
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-237 |
2.22e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.52 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFT-AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKE--KPLHAKANMG 96
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 IQLQS--TSFQSElTVTEiiRLYAAVYGLSLSDSEIEAL----LQNIKLETASSKRFGQLSGGQQQRVSLA-IATMhKPK 169
Cdd:PRK13644 81 IVFQNpeTQFVGR-TVEE--DLAFGPENLCLPPIEIRKRvdraLAEIGLEKYRHRSPKTLSGGQGQCVALAgILTM-EPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 170 LVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVcDRIAIIDHGRIIEIDSPQAIV 237
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDA-DRIIVMDRGKIVLEGEPENVL 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-239 |
2.67e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.65 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 17 TETVLQVENLRVTYGSFT---AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEK---PLH 90
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnvwDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 91 AKANMGIQLQSTSFQSElTVTEIIRLYAAVYGLSLSD--SEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKP 168
Cdd:PRK13650 81 HKIGMVFQNPDNQFVGA-TVEDDVAFGLENKGIPHEEmkERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 169 KLVLLDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAeAVCDRIAIIDHGRIIEIDSPQAIVDR 239
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
14-241 |
3.72e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 99.04 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 14 SASTETVLQVENLRVTY----GSFT-------AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGY 82
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgGLFGrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 83 NL------KEKPLHAKANMGIQLQSTSFQSELTVTEIIRLYAAVYGLsLSDSE----IEALLQNIKLETASSKRF-GQLS 151
Cdd:COG4608 81 DItglsgrELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGL-ASKAErrerVAELLELVGLRPEHADRYpHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 152 GGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAIIDHGRIIEI 230
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEI 239
|
250
....*....|.
gi 1721664488 231 DSPQAIVDRHR 241
Cdd:COG4608 240 APRDELYARPL 250
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-226 |
4.57e-24 |
|
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: 96.73 E-value: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTygsFT----------AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAV----GGYN 83
Cdd:COG4778 2 TTLLEVENLSKT---FTlhlqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 84 LkekplhAKAnmgiqlqstsfqselTVTEIIRLYAAVYG-----------LSLSDSEIEALL-QNIKLETASSK------ 145
Cdd:COG4778 79 L------AQA---------------SPREILALRRRTIGyvsqflrviprVSALDVVAEPLLeRGVDREEARARarella 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 146 RFG------QL-----SGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEA 214
Cdd:COG4778 138 RLNlperlwDLppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREA 217
|
250
....*....|..
gi 1721664488 215 VCDRIAIIDHGR 226
Cdd:COG4778 218 VADRVVDVTPFS 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
38-228 |
5.13e-24 |
|
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: 96.57 E-value: 5.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAA---GNIAVGGynlkeKPLHA---KANMGIQLQSTSFQSELTVT 111
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNG-----QPRKPdqfQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 112 EIIRLYAAVYGLSLSDSEIEA------LLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSR 185
Cdd:cd03234 100 ETLTYTAILRLPRKSSDAIRKkrvedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1721664488 186 RQLWERMESLRNAGHAILLTTHS-MEEAEAVCDRIAIIDHGRII 228
Cdd:cd03234 180 LNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
12-228 |
7.16e-24 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 98.65 E-value: 7.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 12 TSSASTETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKT-SSLSAieGLLKPAAGNIAVGGYNLKEKPLH 90
Cdd:NF000106 5 TISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**rGALPA--HV*GPDAGRRPWRF*TWCANRRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 91 AKANMGIQLQSTSFQSE-LTVTEIIRLYAAVYGLSLSDSEIEA--LLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHK 167
Cdd:NF000106 83 LRRTIG*HRPVR*GRREsFSGRENLYMIGR*LDLSRKDARARAdeLLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 168 PKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-228 |
7.22e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 100.00 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 17 TETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSslsaiegLLKPAAGNIAVGGYN----LKEKPLHAK 92
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKST-------LMKVLSGVYPHGTYEgeiiFEGEELQAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 93 -------ANMGIQLQSTSFQSELTVTEIIRL-----------YAAVYglslsdSEIEALLQNIKLETASSKRFGQLSGGQ 154
Cdd:PRK13549 75 nirdterAGIAIIHQELALVKELSVLENIFLgneitpggimdYDAMY------LRAQKLLAQLKLDINPATPVGNLGLGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 155 QQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-229 |
7.22e-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: 94.69 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYG--SFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEkplhakanmgiq 98
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQSTSFQSELTVTEIIRLYAAvyglslsdseieALLQNIKLetasskrfgQLSGGQQQRVSLAIATMHKPKLVLLDEPTT 178
Cdd:cd03247 69 LEKALSSLISVLNQRPYLFDT------------TLRNNLGR---------RFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 179 GLDPQSRRQLWERM-ESLRNagHAILLTTHSMEEAEAVcDRIAIIDHGRIIE 229
Cdd:cd03247 128 GLDPITERQLLSLIfEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
33-236 |
1.09e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.16 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 33 FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL----KEKPL-HAKANMGIQLQSTSFQ-S 106
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIrPVRKRIGMVFQFPESQlF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 107 ELTVTEIIRLYAAVYGLSLSDSEIEA--LLQNIKLE--TASSKRFgQLSGGQQQRVSL-AIATMHkPKLVLLDEPTTGLD 181
Cdd:PRK13646 100 EDTVEREIIFGPKNFKMNLDEVKNYAhrLLMDLGFSrdVMSQSPF-QMSGGQMRKIAIvSILAMN-PDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 182 PQSRRQLWERMESLR-NAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK13646 178 PQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
40-227 |
1.28e-23 |
|
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: 95.31 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 40 SFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKAnMGIQLQSTSFQSELTVTEIIRLyAA 119
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP-VSMLFQENNLFAHLTVRQNIGL-GL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 120 VYGLSLSDSE---IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL- 195
Cdd:TIGR01277 96 HPGLKLNAEQqekVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLc 175
|
170 180 190
....*....|....*....|....*....|..
gi 1721664488 196 RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRI 227
Cdd:TIGR01277 176 SERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
34-236 |
1.58e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 96.31 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 34 TAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLK--EKPLHAKANMGIQLQSTSFQSELTVT 111
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeENLWDIRNKAGMVFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 112 EiirlYAAVYG---LSLSDSEIEALLQNI--KLETASSKRFGQ--LSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQS 184
Cdd:PRK13633 104 E----EDVAFGpenLGIPPEEIRERVDESlkKVGMYEYRRHAPhlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1721664488 185 RRQLWERMESL-RNAGHAILLTTHSMEEAeAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK13633 180 RREVVNTIKELnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
18-228 |
2.20e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.07 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTYGSFT-AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL---KEKPLHAKA 93
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 94 NMGIQLQSTSFQ-SELTVTEIIRLyaAVYGLSLSDSEIEALLQNIKLETASS----KRFGQLSGGQQQRVSLAIATMHKP 168
Cdd:PRK13636 83 SVGMVFQDPDNQlFSASVYQDVSF--GAVNLKLPEDEVRKRVDNALKRTGIEhlkdKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 169 KLVLLDEPTTGLDPQSRRQLWERM-ESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLvEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-229 |
3.85e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 98.38 E-value: 3.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 1 MESTMPATNSATSSASTETVLQVE--NLRV-TYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLkPAAGNI 77
Cdd:PRK11174 328 LETPLAHPQQGEKELASNDPVTIEaeDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 78 AVGGYNLKEkplhakanmgiqLQSTSFQSEL------------TVTEIIRLYAAvyglSLSDSEIEALLQNIK------- 138
Cdd:PRK11174 407 KINGIELRE------------LDPESWRKHLswvgqnpqlphgTLRDNVLLGNP----DASDEQLQQALENAWvseflpl 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 139 ----LETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLwerMESLRNA--GHAILLTTHSMEEA 212
Cdd:PRK11174 471 lpqgLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV---MQALNAAsrRQTTLMVTHQLEDL 547
|
250
....*....|....*..
gi 1721664488 213 EAvCDRIAIIDHGRIIE 229
Cdd:PRK11174 548 AQ-WDQIWVMQDGQIVQ 563
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-229 |
3.91e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.14 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 25 NLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL-KEKPLHAKA-----NMGIQ 98
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaKLNRAQRKAfrrdiQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQSTSFQSELTVTEIIR-----LyaavygLSLSDSE----IEALLQNIKL-ETASSKRFGQLSGGQQQRVSLAIATMHKP 168
Cdd:PRK10419 97 DSISAVNPRKTVREIIReplrhL------LSLDKAErlarASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 169 KLVLLDEPTTGLDPQSRRQLWERMESLRN-AGHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:PRK10419 171 KLLILDEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-233 |
3.99e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 94.74 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 19 TVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGgynlkEKPLHAkANMGIQ 98
Cdd:PRK11247 11 TPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAE-AREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQstsFQSEltvteiiRL--YAAV---YGLSLS----DSEIEALlQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPK 169
Cdd:PRK11247 85 LM---FQDA-------RLlpWKKVidnVGLGLKgqwrDAALQAL-AAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 170 LVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRI---IEIDSP 233
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldLTVDLP 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-236 |
8.51e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.43 E-value: 8.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 24 ENLRVTYGSFT-----AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKE-------KPLHA 91
Cdd:PRK13649 6 QNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdiKQIRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KANMGIQLQSTSFQSElTVTEIIRLYAAVYGLSLSDSEIEALlQNIKLETASSKRFGQ----LSGGQQQRVSLAIATMHK 167
Cdd:PRK13649 86 KVGLVFQFPESQLFEE-TVLKDVAFGPQNFGVSQEEAEALAR-EKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAME 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 168 PKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
14-236 |
1.01e-22 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 93.71 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 14 SASTETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKP----- 88
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 89 LHA---------KANMGIQLQSTSFQSELTVTE-IIRlyAAVYGLSLSDSEI----EALLQNIKLETASSKRFGQLSGGQ 154
Cdd:COG4598 82 LVPadrrqlqriRTRLGMVFQSFNLWSHMTVLEnVIE--APVHVLGRPKAEAieraEALLAKVGLADKRDAYPAHLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 155 QQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQ 234
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA 239
|
..
gi 1721664488 235 AI 236
Cdd:COG4598 240 EV 241
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-229 |
1.18e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.21 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGL--LKPAAGNIAVGGYNLKEKPLHAKANMGIQ 98
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LqstSFQS-----ELTVTEIIRL-YAAVYGLSLS----DSEIEALLQNIKLETASSKRF---GqLSGGQQQRVSLAIATM 165
Cdd:COG0396 81 L---AFQYpveipGVSVSNFLRTaLNARRGEELSarefLKLLKEKMKELGLDEDFLDRYvneG-FSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721664488 166 HKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHS---MEEAEAvcDRIAIIDHGRIIE 229
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYqriLDYIKP--DFVHVLVDGRIVK 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
40-247 |
1.47e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.72 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 40 SFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPlHAKANMGIQLQSTSFQSELTVTEIIRLYAA 119
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-PSRRPVSMLFQENNLFSHLTVAQNIGLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 120 VyGLSLSDSE---IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL- 195
Cdd:PRK10771 98 P-GLKLNAAQrekLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVc 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 196 RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRNDAEVI 247
Cdd:PRK10771 177 QERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-254 |
1.70e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 96.23 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLrvtygSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEK-PLHAKANmG 96
Cdd:PRK10762 255 EVRLKVDNL-----SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRsPQDGLAN-G 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 IqlqstSFQSE----------LTVTEIIRLYAAVY----GLSLS-DSEIEAL-----LQNIKleTAS-SKRFGQLSGGQQ 155
Cdd:PRK10762 329 I-----VYISEdrkrdglvlgMSVKENMSLTALRYfsraGGSLKhADEQQAVsdfirLFNIK--TPSmEQAIGLLSGGNQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 156 QRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII-EIDSPQ 234
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISgEFTREQ 481
|
250 260
....*....|....*....|
gi 1721664488 235 AivdrhrnDAEVIRASRKGK 254
Cdd:PRK10762 482 A-------TQEKLMAAAVGK 494
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-207 |
1.70e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 91.79 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIavggyNLKEKPLHAkanmgiql 99
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV-----LWQGEPIRR-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 QSTSFQ-------------SELTVTEIIRLYAAVYGLsLSDSEIEALLQNIKLetassKRF-----GQLSGGQQQRVSLA 161
Cdd:PRK13538 68 QRDEYHqdllylghqpgikTELTALENLRFYQRLHGP-GDDEALWEALAQVGL-----AGFedvpvRQLSAGQQRRVALA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1721664488 162 IATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTH 207
Cdd:PRK13538 142 RLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-227 |
2.33e-22 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 95.97 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY-GSFTAV-HDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKekplhakanmgiQ 98
Cdd:COG4618 331 LSVENLTVVPpGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS------------Q 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQSTSF---------QSEL---TVTEII-RLYAAvyglslsDSE--IEALlqniKL--------------ETASSKRFGQ 149
Cdd:COG4618 399 WDREELgrhigylpqDVELfdgTIAENIaRFGDA-------DPEkvVAAA----KLagvhemilrlpdgyDTRIGEGGAR 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 150 LSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMeEAEAVCDRIAIIDHGRI 227
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVLRDGRV 544
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-240 |
2.43e-22 |
|
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: 92.29 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGS--FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHA-KANMGI 97
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQSTSFQSElTVTEIIRlyaavYGLS-LSDSEIEALLQN------IK-----LETASSKRFGQLSGGQQQRVSLAIATM 165
Cdd:cd03251 81 VSQDVFLFND-TVAENIA-----YGRPgATREEVEEAARAanahefIMelpegYDTVIGERGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 166 HKPKLVLLDEPTTGLDPQSRRQLWERMESLRnAGHAILLTTH---SMEEAeavcDRIAIIDHGRIIEIDSPQAIVDRH 240
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHrlsTIENA----DRIVVLEDGKIVERGTHEELLAQG 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-228 |
5.08e-22 |
|
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: 94.89 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAA--GNIAVGGYNLKEKPLHAKANMGI 97
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QL--QSTSFQSELTVTEIIRLYAAVY--GLSLSDSEI----EALLQNIKLETASSKR-FGQLSGGQQQRVSLAIATMHKP 168
Cdd:TIGR02633 81 VIihQELTLVPELSVAENIFLGNEITlpGGRMAYNAMylraKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 169 KLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-224 |
9.99e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 90.94 E-value: 9.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 19 TVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIavggynlkEKPlhAKANMGIQ 98
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRN--GKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQSTSFQSE--LTVTEIIRLYAAVyglslSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEP 176
Cdd:PRK09544 73 PQKLYLDTTlpLTVNRFLRLRPGT-----KKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721664488 177 TTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAIIDH 224
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-239 |
1.36e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.95 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTYGSFT-AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLH-AKANM 95
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 GIQLQSTSFQS-ELTVTEIIRLYAAVYGLSLS--DSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVL 172
Cdd:PRK13647 82 GLVFQDPDDQVfSSTVWDDVAFGPVNMGLDKDevERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721664488 173 LDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDR 239
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
39-228 |
1.43e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 90.28 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 39 VSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLkPAAGNIAVGGYNLKEKPLHAKAN---MGIQLQSTSFQseLTVTEIIR 115
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARhraYLSQQQSPPFA--MPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 116 LY-AAVYGLSLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAiATMHK--------PKLVLLDEPTTGLDPQSRR 186
Cdd:COG4138 92 LHqPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLA-AVLLQvwptinpeGQLLLLDEPMNSLDVAQQA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1721664488 187 QLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:COG4138 171 ALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-233 |
1.44e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.02 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKtSSLSAIEGLL-KPAAGNIAVGGYNLKEKPLHAKANM 95
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGK-STLMNILGCLdKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 -----GIQLQSTSFQSELTV---TEIIRLYAAVyGLSLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHK 167
Cdd:PRK10535 84 rrehfGFIFQRYHLLSHLTAaqnVEVPAVYAGL-ERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 168 PKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAeAVCDRIAIIDHGRIIEiDSP 233
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVA-AQAERVIEIRDGEIVR-NPP 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-239 |
1.50e-21 |
|
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: 90.24 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 24 ENLRVTYG--SFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKE-KPLHAKANMGIQLQ 100
Cdd:cd03252 4 EHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STSFQSElTVTEIIRL-------YAAVYGLSLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLL 173
Cdd:cd03252 84 ENVLFNR-SIRDNIALadpgmsmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 174 DEPTTGLDPQSRRQLWERMESLrNAGHAILLTTHSMEEAEAVcDRIAIIDHGRIIEIDSPQAIVDR 239
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-222 |
1.52e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 91.10 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY-GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQL 99
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 QSTSFQSELTVTEIIRL--YAAVYGLSLSDSE----IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLL 173
Cdd:PRK15056 87 EEVDWSFPVLVEDVVMMgrYGHMGWLRRAKKRdrqiVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721664488 174 DEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAII 222
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-230 |
2.08e-21 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 92.87 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLrvTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGI 97
Cdd:PRK10982 248 EVILEVRNL--TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGF 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QL-----QSTSFQSELTVT-----EIIRLYAAVYGLsLSDSEIEALLQ----NIKLETASSK-RFGQLSGGQQQRVSLAI 162
Cdd:PRK10982 326 ALvteerRSTGIYAYLDIGfnsliSNIRNYKNKVGL-LDNSRMKSDTQwvidSMRVKTPGHRtQIGSLSGGNQQKVIIGR 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 163 ATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEI 230
Cdd:PRK10982 405 WLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-249 |
2.72e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.81 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 5 MPATNSATSSastetVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL 84
Cdd:PRK15439 1 MQTSDTTAPP-----LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 85 -KEKPLHAKAnMGIQL--QSTSFQSELTVTEIIrlyaaVYGL---SLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRV 158
Cdd:PRK15439 76 aRLTPAKAHQ-LGIYLvpQEPLLFPNLSVKENI-----LFGLpkrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 159 SLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII---EIDSpqa 235
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIAlsgKTAD--- 226
|
250
....*....|....
gi 1721664488 236 ivdrhRNDAEVIRA 249
Cdd:PRK15439 227 -----LSTDDIIQA 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
35-240 |
3.04e-21 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 89.21 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 35 AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANM-GIQLQSTSFQSElTVTEI 113
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMiGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 114 IRLyaavYGLSLSDSEIEALLQNIK-----------LETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDP 182
Cdd:cd03254 97 IRL----GRPNATDEEVIEAAKEAGahdfimklpngYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 183 QSRRQLWERMESLRNAGHAILLTTH--SMEEAeavcDRIAIIDHGRIIEIDSPQAIVDRH 240
Cdd:cd03254 173 ETEKLIQEALEKLMKGRTSIIIAHRlsTIKNA----DKILVLDDGKIIEEGTHDELLAKK 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-236 |
5.56e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 90.29 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 16 STETVLQVENLRVTYGS-----FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLH 90
Cdd:PRK13631 17 SDDIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 91 AKAN-----------------MGIQLQSTSFQ-SELTVTEIIRLYAAVYGLSLSDSEIEA--LLQNIKLETASSKR--FG 148
Cdd:PRK13631 97 HELItnpyskkiknfkelrrrVSMVFQFPEYQlFKDTIEKDIMFGPVALGVKKSEAKKLAkfYLNKMGLDDSYLERspFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 149 qLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:PRK13631 177 -LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
....*...
gi 1721664488 229 EIDSPQAI 236
Cdd:PRK13631 256 KTGTPYEI 263
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
35-243 |
7.05e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.86 E-value: 7.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 35 AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLK-----EKPLHAKANMGIQLQSTSFQSELT 109
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdaELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 110 VTEIIRLYAAVYGLSLSDSEIEAL--LQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQ 187
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALdaLRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 188 LWERMESLRnAGH--AILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRND 243
Cdd:PRK10070 203 MQDELVKLQ-AKHqrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAND 259
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-207 |
7.07e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 87.70 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQL 99
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 QSTSFQSELTVTEiirlyAAVYGLSLSDS--EIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPT 177
Cdd:PRK13540 81 HRSGINPYLTLRE-----NCLYDIHFSPGavGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|
gi 1721664488 178 TGLDPQSRRQLWERMESLRNAGHAILLTTH 207
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
35-227 |
8.28e-21 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 87.85 E-value: 8.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 35 AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL-----KEKPLHAKANMGIQLQSTSFQSELT 109
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVtnlsySQKIILRRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 110 VTEIIRLYAAVYGLSLSD--SEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQ 187
Cdd:NF038007 100 IFDNVALPLKYRGVAKKEriERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1721664488 188 LWERMESLRNAGHAILLTTHSmEEAEAVCDRIAIIDHGRI 227
Cdd:NF038007 180 VLQQLKYINQKGTTIIMVTHS-DEASTYGNRIINMKDGKL 218
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
31-243 |
9.92e-21 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 90.16 E-value: 9.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 31 GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLkekpLHAKANMGIQLQSTS----FQS 106
Cdd:COG4175 38 GQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDI----TKLSKKELRELRRKKmsmvFQH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 107 -----ELTVTEiirlyAAVYGLSL---SDSEIEAL----LQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLD 174
Cdd:COG4175 114 fallpHRTVLE-----NVAFGLEIqgvPKAERRERareaLELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMD 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 175 EPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRND 243
Cdd:COG4175 189 EAFSALDPLIRREMQDELLELqAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPAND 258
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-249 |
1.13e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 88.22 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVtYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPA----AGNIAVGGynlkeKPLHAKANM 95
Cdd:PRK10418 4 QIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDG-----KPVAPCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 GI------QLQSTSFQSELTVTEIIRLYAAVYGLSLSDSEIEALLQNIKLETASS--KRFG-QLSGGQQQRVSLAIATMH 166
Cdd:PRK10418 78 GRkiatimQNPRSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLENAARvlKLYPfEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 167 KPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVdrHRNDAE 245
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF--NAPKHA 235
|
....
gi 1721664488 246 VIRA 249
Cdd:PRK10418 236 VTRS 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-236 |
1.28e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 14 SASTETVLQVENLRVTY-----------GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLkPAAGNIAVGG- 81
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGq 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 82 --YNLKEK---PLHAKANMGIQLQSTSFQSELTVTEIIRLYAAVYGLSLSDSEIE----ALLQNIKLETASSKRF-GQLS 151
Cdd:PRK15134 348 plHNLNRRqllPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQREqqviAVMEEVGLDPETRHRYpAEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 152 GGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGH-AILLTTHSMEEAEAVCDRIAIIDHGRIIEI 230
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQ 507
|
....*.
gi 1721664488 231 DSPQAI 236
Cdd:PRK15134 508 GDCERV 513
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-246 |
1.48e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 88.23 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHD---VSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLK-EKPLHAKANM 95
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 GIQLQSTSFQ-SELTVTEIIRLYAAVYGLSLSD--SEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVL 172
Cdd:PRK13642 84 GMVFQNPDNQfVGATVEDDVAFGMENQGIPREEmiKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721664488 173 LDEPTTGLDPQSRRQLWERMESLRNAGHAILLT-THSMEEAeAVCDRIAIIDHGRIIEIDSPQAIVDRHRNDAEV 246
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
18-235 |
1.81e-20 |
|
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: 87.58 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIavgGYNLKEKPLH------- 90
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTA---TYIMRSGAELelyqlse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 91 ------AKANMGIQLQSTSFQSELTVT-------EIIRLYAAVYG-------LSLSDSEIEAllqnikleTASSKRFGQL 150
Cdd:TIGR02323 78 aerrrlMRTEWGFVHQNPRDGLRMRVSaganigeRLMAIGARHYGnirataqDWLEEVEIDP--------TRIDDLPRAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 151 SGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLvRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
250
....*....|...
gi 1721664488 230 -------IDSPQA 235
Cdd:TIGR02323 230 sgltdqvLDDPQH 242
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-227 |
2.16e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.99 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTYGSFTA---VHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPA-AGNIAVGGYNLK-EKPLHAK 92
Cdd:PRK13549 257 EVILEVRNLTAWDPVNPHikrVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKiRNPQQAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 93 ANmGIQLQSTSFQ-----SELTVTEIIRL--YAAVYGLSLSDSE-----IEALLQNIKLETASSK-RFGQLSGGQQQRVS 159
Cdd:PRK13549 337 AQ-GIAMVPEDRKrdgivPVMGVGKNITLaaLDRFTGGSRIDDAaelktILESIQRLKVKTASPElAIARLSGGNQQKAV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 160 LAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRI 227
Cdd:PRK13549 416 LAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-236 |
4.36e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.16 E-value: 4.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 16 STETVLQVENLRVTY--GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGN---IAVGGYNLKEKPL- 89
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 90 HAKANMGIQLQSTSFQ-SELTVTEIIrlyaaVYGL---SLSDSEIEALLQNI-----KLETASSKRfGQLSGGQQQRVSL 160
Cdd:PRK13640 81 DIREKVGIVFQNPDNQfVGATVGDDV-----AFGLenrAVPRPEMIKIVRDVladvgMLDYIDSEP-ANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721664488 161 AIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEaVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-243 |
5.14e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.51 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 19 TVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGL--LKPAA---GNIAVGGYNLKEKP---LH 90
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEArvsGEVYLDGQDIFKMDvieLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 91 AKANMGIQLQSTSfqSELTVTEIIRLYAAVYGLSLSDSEIEA----LLQNIKLETASSKRF----GQLSGGQQQRVSLAI 162
Cdd:PRK14247 82 RRVQMVFQIPNPI--PNLSIFENVALGLKLNRLVKSKKELQErvrwALEKAQLWDEVKDRLdapaGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 163 ATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAgHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRN 242
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
.
gi 1721664488 243 D 243
Cdd:PRK14247 239 E 239
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
20-236 |
6.23e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.78 E-value: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTY-GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLH-AKANMGI 97
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIReVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQSTSFQS-ELTVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLD 174
Cdd:PRK13652 83 VFQNPDDQIfSPTVEQDIAFGPINLGLDEETVAhrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721664488 175 EPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
38-229 |
8.02e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.63 E-value: 8.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKE---KPLHAKANMGIQ---LQSTSFQSE---- 107
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhHYLHRQVALVGQepvLFSGSVRENiayg 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 108 LTVTEIIRLYAAVYgLSLSDSEIEALLQNIklETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQ 187
Cdd:TIGR00958 579 LTDTPDEEIMAAAK-AANAHDFIMEFPNGY--DTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL 655
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1721664488 188 LWERMESlrnAGHAILLTTHSMEEAEAvCDRIAIIDHGRIIE 229
Cdd:TIGR00958 656 LQESRSR---ASRTVLLIAHRLSTVER-ADQILVLKKGSVVE 693
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
15-234 |
9.44e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 85.75 E-value: 9.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 15 ASTETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIavgGYNLKEKPLHAKAN 94
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV---HYRMRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 95 MGIQLQSTSFQSE-------------LTVT------EiiRLYAA---VYGlslsdsEIEAL----LQNIKLETAsskRF- 147
Cdd:PRK11701 78 LSEAERRRLLRTEwgfvhqhprdglrMQVSaggnigE--RLMAVgarHYG------DIRATagdwLERVEIDAA---RId 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 148 ---GQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIID 223
Cdd:PRK11701 147 dlpTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMK 226
|
250
....*....|....*...
gi 1721664488 224 HGRIIE-------IDSPQ 234
Cdd:PRK11701 227 QGRVVEsgltdqvLDDPQ 244
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-227 |
1.02e-19 |
|
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: 84.83 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTYGSFTAV---HDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL---KEKPLHA 91
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDTlvlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsqyEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KANMGIQ---LQSTSFQSELTvteiirlyaavYGL-SLSDSEIEALLQ------NIKL-----ETASSKRFGQLSGGQQQ 156
Cdd:cd03248 89 KVSLVGQepvLFARSLQDNIA-----------YGLqSCSFECVKEAAQkahahsFISElasgyDTEVGEKGSQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 157 RVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLwERMESLRNAGHAILLTTHSMEEAEAVcDRIAIIDHGRI 227
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQV-QQALYDWPERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-236 |
1.18e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.22 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 23 VENLRVTYG-----SFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGY----NLKE----KPL 89
Cdd:PRK13645 9 LDNVSYTYAkktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipaNLKKikevKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 90 haKANMGIQLQSTSFQselTVTEIIRLYAAVYGLSLSDSEIEA------LLQNIKLETASSKRFG-QLSGGQQQRVSLAI 162
Cdd:PRK13645 89 --RKEIGLVFQFPEYQ---LFQETIEKDIAFGPVNLGENKQEAykkvpeLLKLVQLPEDYVKRSPfELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721664488 163 ATMHKPKLVLLDEPTTGLDPQSRR---QLWERMEslRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLN--KEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
38-229 |
2.45e-19 |
|
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: 84.13 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHA-KANMGI-----QLQSTsfqselTVT 111
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlRSQIGLvsqepVLFDG------TIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 112 EIIRlyaavYGL-SLSDSEIE--ALLQNI---------KLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTG 179
Cdd:cd03249 95 ENIR-----YGKpDATDEEVEeaAKKANIhdfimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721664488 180 LDPQSRRQLWERMESLRnAGHAILLTTHSMEEAEAvCDRIAIIDHGRIIE 229
Cdd:cd03249 170 LDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVE 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-233 |
2.61e-19 |
|
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: 83.62 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSF--TAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHA-KANMGI 97
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQSTSFQSeltvtEIIRLYAAVYGlSLSDSEIEALLQnIKlETASSkrfgqLSGGQQQRVSLAIATMHKPKLVLLDEPT 177
Cdd:cd03369 87 IPQDPTLFS-----GTIRSNLDPFD-EYSDEEIYGALR-VS-EGGLN-----LSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 178 TGLDPQSRRQLWERMESLRNaGHAILLTTHSMEEAeAVCDRIAIIDHGRIIEIDSP 233
Cdd:cd03369 154 ASIDYATDALIQKTIREEFT-NSTILTIAHRLRTI-IDYDKILVMDAGEVKEYDHP 207
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-250 |
3.94e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.55 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 23 VENLRVTY---GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKekplhakanmGIQL 99
Cdd:PRK13657 335 VEFDDVSFsydNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR----------TVTR 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 QS------TSFQSEL----TVTEIIRLYAAvyglSLSDSEIEALL-----------QNIKLETASSKRFGQLSGGQQQRV 158
Cdd:PRK13657 405 ASlrrniaVVFQDAGlfnrSIEDNIRVGRP----DATDEEMRAAAeraqahdfierKPDGYDTVVGERGRQLSGGERQRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 159 SLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNaGHAILLTTH---SMEEAeavcDRIAIIDHGRIIEIDSPQA 235
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHrlsTVRNA----DRILVFDNGRVVESGSFDE 555
|
250
....*....|....*
gi 1721664488 236 IVDRHRNDAEVIRAS 250
Cdd:PRK13657 556 LVARGGRFAALLRAQ 570
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
33-228 |
4.08e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.75 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 33 FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAvggYNLKEKPLHAKANMG------IQLQSTSFQS 106
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIE---WIFKDEKNKKKTKEKekvlekLVIQKTRFKK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 107 ELTVTEIIRLYAAVY-------------------GLSLSDSEIEAL---LQNIKL----ETASSKRFGQLSGGQQQRVSL 160
Cdd:PRK13651 97 IKKIKEIRRRVGVVFqfaeyqlfeqtiekdiifgPVSMGVSKEEAKkraAKYIELvgldESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 161 A-IATMhKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:PRK13651 177 AgILAM-EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
31-227 |
7.09e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.62 E-value: 7.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 31 GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL-----KEKPLhAKANMGIQLQSTSFQ 105
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlknREVPF-LRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 106 SELTVTEIIRLYAAVYGLSLSD--SEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQ 183
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASGDDirRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1721664488 184 SRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRI 227
Cdd:PRK10908 172 LSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-237 |
8.15e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.50 E-value: 8.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 17 TETV--LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKA- 93
Cdd:PRK10253 2 TESVarLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 94 NMGIQLQSTSFQSELTVTEIIRL----YAAVYGLSLSDSE--IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHK 167
Cdd:PRK10253 82 RIGLLAQNATTPGDITVQELVARgrypHQPLFTRWRKEDEeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 168 PKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIV 237
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
21-229 |
8.53e-19 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 85.54 E-value: 8.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYG--SFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLhakANMGIQ 98
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTL---ASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQSTSFQSEL---TVTEIIRlYAAvyGLSLSDSEIEALLQ--NIK---------LETASSKRFGQLSGGQQQRVSLAIAT 164
Cdd:TIGR02203 408 VALVSQDVVLfndTIANNIA-YGR--TEQADRAEIERALAaaYAQdfvdklplgLDTPIGENGVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721664488 165 MHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNaGHAILLTTHSMEEAEAVcDRIAIIDHGRIIE 229
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLSTIEKA-DRIVVMDDGRIVE 547
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-212 |
1.35e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.17 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 16 STETVLQVENLRVTYG----SFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHA 91
Cdd:PRK11629 1 MNKILLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KAN-----MGIQLQSTSFQSELTVTEIIRLYAAVYGLSLSDSEIEAL--LQNIKLETASSKRFGQLSGGQQQRVSLAIAT 164
Cdd:PRK11629 81 KAElrnqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALemLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721664488 165 MHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEA 212
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLA 209
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
5-227 |
1.39e-18 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 85.09 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 5 MPATNSATSSASTETVLQVENlrVTY----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVG 80
Cdd:TIGR01842 301 YPSRDPAMPLPEPEGHLSVEN--VTIvppgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 81 GYNLKE------KPLHAKANMGIQLQSTS-------FQSELTVTEII---RLyAAVYGLSLS-----DSEIEAllqnikl 139
Cdd:TIGR01842 379 GADLKQwdretfGKHIGYLPQDVELFPGTvaeniarFGENADPEKIIeaaKL-AGVHELILRlpdgyDTVIGP------- 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 140 etasskRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVcDRI 219
Cdd:TIGR01842 451 ------GGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCV-DKI 523
|
....*...
gi 1721664488 220 AIIDHGRI 227
Cdd:TIGR01842 524 LVLQDGRI 531
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-240 |
1.67e-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: 81.89 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYG-SFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHA-KANMGIQ 98
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQSTSFQSElTVTEIIRlyaavYG-LSLSDSEIE--ALLQNI---------KLETASSKRFGQLSGGQQQRVSLAIATMH 166
Cdd:cd03253 81 PQDTVLFND-TIGYNIR-----YGrPDATDEEVIeaAKAAQIhdkimrfpdGYDTIVGERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 167 KPKLVLLDEPTTGLDPQSRRQLWERMESLRnAGHAILLTTHSMEEAeAVCDRIAIIDHGRIIEIDSPQAIVDRH 240
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAKG 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-243 |
1.80e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.40 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 16 STETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL-------KEKP 88
Cdd:PRK14246 6 SAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifQIDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 89 LHAKANMGIQLQSTSFQSELTVTEIIRLYAAVYGLSlSDSEI----EALLQNIKLETASSKRF----GQLSGGQQQRVSL 160
Cdd:PRK14246 86 IKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIK-EKREIkkivEECLRKVGLWKEVYDRLnspaSQLSGGQQQRLTI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 161 AIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAgHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRH 240
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
...
gi 1721664488 241 RND 243
Cdd:PRK14246 244 KNE 246
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-229 |
3.62e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 81.23 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 16 STETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGllKPA----AGNIAVGGYNLKEKPLHA 91
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KANMGIQLqstSFQSELTVT-----EIIRLYAAVYGLSLSDSEIEAL----LQNIKLETAS-SKRF-------GqLSGGQ 154
Cdd:CHL00131 81 RAHLGIFL---AFQYPIEIPgvsnaDFLRLAYNSKRKFQGLPELDPLefleIINEKLKLVGmDPSFlsrnvneG-FSGGE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 155 QQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVC-DRIAIIDHGRIIE 229
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIK 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-226 |
4.32e-18 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 80.21 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGS-----FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkekplhakaNM 95
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 GIQLQSTSFQSElTVTEIIrLYAAVYglslsDSE-----IEA--LLQNIKL-----ETasskRFGQ----LSGGQQQRVS 159
Cdd:cd03250 69 AYVSQEPWIQNG-TIRENI-LFGKPF-----DEEryekvIKAcaLEPDLEIlpdgdLT----EIGEkginLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 160 LAIATMHKPKLVLLDEPTTGLDPQSRRQLWER--MESLRNaGHAILLTTHSMEEAEAvCDRIAIIDHGR 226
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFENciLGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-229 |
7.22e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.95 E-value: 7.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY--GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLK---EKPLhaKANM 95
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdysEAAL--RQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 GIQLQSTSFQSElTVTEIIRLYAAvyglSLSDSEIEALLQNIKLETASSKRFG----------QLSGGQQQRVSLAIATM 165
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLAAP----NASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 166 HKPKLVLLDEPTTGLDPQSRRQLwerMESLRN--AGHAILLTTHSMEEAEAVcDRIAIIDHGRIIE 229
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQI---LELLAEhaQNKTVLMITHRLTGLEQF-DRICVMDNGQIIE 553
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-246 |
8.70e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.58 E-value: 8.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 14 SASTETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL----KEKPL 89
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 90 HAKANMGIQLQSTSFQSELTVTEIIrlyaaVYGLSLSDSEIEALLQN---IKLET-----ASSKRFGQLSGGQQQRVSLA 161
Cdd:PRK11831 81 TVRKRMSMLFQSGALFTDMNVFDNV-----AYPLREHTQLPAPLLHStvmMKLEAvglrgAAKLMPSELSGGMARRAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 162 IATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIvdRH 240
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL--QA 233
|
....*.
gi 1721664488 241 RNDAEV 246
Cdd:PRK11831 234 NPDPRV 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-251 |
9.35e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.54 E-value: 9.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGL--LKPAAGNI--------------------- 77
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 78 --AVGGYNLKE---------KPLHA--KANMGIQLQST-SFQSELTVTE-IIRlyaavyglSLSDSEIEA---------L 133
Cdd:TIGR03269 81 pcPVCGGTLEPeevdfwnlsDKLRRriRKRIAIMLQRTfALYGDDTVLDnVLE--------ALEEIGYEGkeavgravdL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 134 LQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERM-ESLRNAGHAILLTTHSMEEA 212
Cdd:TIGR03269 153 IEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASGISMVLTSHWPEVI 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 1721664488 213 EAVCDRIAIIDHGRIIEIDSPQAIVDRHRNDAEVIRASR 251
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKEC 271
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-229 |
1.28e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 80.94 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGS----FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLL----KPAAGNIAVGGYNL------- 84
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLqriseke 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 85 KEKPLHAKANMGIQLQSTSFQSELTV----TEIIRLYAAVYGLSLSDSEIEaLLQNIKLETASSK---RFGQLSGGQQQR 157
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVgfqiMEAIKVHQGGNKKTRRQRAID-LLNQVGIPDPASRldvYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721664488 158 VSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-208 |
1.92e-17 |
|
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: 81.64 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 11 ATSSASTETVLQVENLRVTY-GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKP- 88
Cdd:TIGR02868 325 AGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDq 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 89 -LHAKANMGIQLQSTSFQSelTVTEIIRLYAAvyglSLSDSEIEALLQNIKLE-----------TASSKRFGQLSGGQQQ 156
Cdd:TIGR02868 405 dEVRRRVSVCAQDAHLFDT--TVRENLRLARP----DATDEELWAALERVGLAdwlralpdgldTVLGEGGARLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 157 RVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLwerMESLRNA--GHAILLTTHS 208
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADEL---LEDLLAAlsGRTVVLITHH 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-228 |
2.07e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.59 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 17 TETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEK-PLHAK-AN 94
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgPKSSQeAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 95 MGIQLQSTSFQSELTVTEII---RLYAAVYGLSLSD---SEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKP 168
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIflgREFVNRFGRIDWKkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 169 KLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
48-239 |
2.21e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.67 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 48 IFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkeKPLH--AKANMGIQLQ-STSFQ---SELTVTEIIRLYA-AV 120
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-----KPLDysKRGLLALRQQvATVFQdpeQQIFYTDIDSDIAfSL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 121 YGLSLSDSEIEALLQNiKLETASSKRFGQ-----LSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL 195
Cdd:PRK13638 104 RNLGVPEAEITRRVDE-ALTLVDAQHFRHqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRI 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1721664488 196 RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDR 239
Cdd:PRK13638 183 VAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-218 |
3.07e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.28 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 16 STETVLQVENLRVTYGS----FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHA 91
Cdd:PRK10584 2 PAENIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KA-----NMGIQLQSTSFQSELTVTEIIRLYAAVYGLSLSDSEIEA--LLQNIKLETASSKRFGQLSGGQQQRVSLAIAT 164
Cdd:PRK10584 82 RAklrakHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAkaLLEQLGLGKRLDHLPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1721664488 165 MHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAeAVCDR 218
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLA-ARCDR 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
26-233 |
4.62e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 79.69 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 26 LRVTYGSFTAVH---DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPlHAKANMGIQLQST 102
Cdd:PRK11000 6 LRNVTKAYGDVViskDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP-PAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 103 SFQSELTVTEIIRlyaavYGLSLS---DSEIEALLQNI----KLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDE 175
Cdd:PRK11000 85 ALYPHLSVAENMS-----FGLKLAgakKEEINQRVNQVaevlQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 176 PTTGLDPQSRRQLweRMESLR---NAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSP 233
Cdd:PRK11000 160 PLSNLDAALRVQM--RIEISRlhkRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-239 |
6.01e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 6.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 19 TVLQVENLrvtygSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGI- 97
Cdd:PRK15439 267 PVLTVEDL-----TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLv 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQSTSFQSELTVTEIIR--LYAAVY---GLSLSDSEIEALLQ------NIKLETASsKRFGQLSGGQQQRVSLAIATMH 166
Cdd:PRK15439 342 YLPEDRQSSGLYLDAPLAwnVCALTHnrrGFWIKPARENAVLEryrralNIKFNHAE-QAARTLSGGNQQKVLIAKCLEA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 167 KPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI-VDR 239
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAInVDT 494
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-227 |
7.37e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.87 E-value: 7.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENL---RVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPA-AGNIAVGGYNLKEKPLHAKA 93
Cdd:TIGR02633 255 DVILEARNLtcwDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 94 NMGIQL-----QSTSFQSELTVTEIIRLYA--AVYGLSLSDSE-----IEALLQNIKLETASSK-RFGQLSGGQQQRVSL 160
Cdd:TIGR02633 335 RAGIAMvpedrKRHGIVPILGVGKNITLSVlkSFCFKMRIDAAaelqiIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVL 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721664488 161 AIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRI 227
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
37-238 |
8.25e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.71 E-value: 8.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 37 HDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPA---AGNIAVGGYNLKEKPLHAKAnmGIQLQSTSFQSELTVTEI 113
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIS--AYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 114 IRLYAAV-YGLSLSDSE----IEALLQNIKLETASSKRFGQ------LSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDP 182
Cdd:TIGR00955 120 LMFQAHLrMPRRVTKKEkrerVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 183 QSRRQLWERMESLRNAGHAILLTTHSmEEAEAVC--DRIAIIDHGRIIEIDSPQAIVD 238
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGKTIICTIHQ-PSSELFElfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-236 |
2.21e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENL------------RVTYgSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL- 84
Cdd:PRK10261 311 EPILQVRNLvtrfplrsgllnRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRId 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 85 -----KEKPLHAKANMGIQLQSTSFQSELTVTEIIRLYAAVYGLSLSD---SEIEALLQNIKLETASSKRF-GQLSGGQQ 155
Cdd:PRK10261 390 tlspgKLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKaaaARVAWLLERVGLLPEHAWRYpHEFSGGQR 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 156 QRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQ 234
Cdd:PRK10261 470 QRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRR 549
|
..
gi 1721664488 235 AI 236
Cdd:PRK10261 550 AV 551
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
14-236 |
2.94e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.05 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 14 SASTETVLQVENLRVTYG-------------SFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVG 80
Cdd:PRK15079 2 TEGKKVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 81 GYNL---KEKPLHAKAN---MGIQLQSTSFQSELTVTEIIRLYAAVYGLSLSDSEIE----ALLQNIKLETASSKRF-GQ 149
Cdd:PRK15079 82 GKDLlgmKDDEWRAVRSdiqMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKdrvkAMMLKVGLLPNLINRYpHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 150 LSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
....*...
gi 1721664488 229 EIDSPQAI 236
Cdd:PRK15079 242 ELGTYDEV 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-236 |
3.53e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.97 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 17 TETVLQVENLRVTY----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLH-- 90
Cdd:PRK10261 9 ARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 91 ---------------AKANMGIQLQSTSFQSELTV----TEIIRLYAavyGLSLSDSEIEA--LLQNIKL---ETASSKR 146
Cdd:PRK10261 89 elseqsaaqmrhvrgADMAMIFQEPMTSLNPVFTVgeqiAESIRLHQ---GASREEAMVEAkrMLDQVRIpeaQTILSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 147 FGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHG 225
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
|
250
....*....|.
gi 1721664488 226 RIIEIDSPQAI 236
Cdd:PRK10261 246 EAVETGSVEQI 256
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
39-207 |
3.87e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.74 E-value: 3.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 39 VSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLkPAAGNIAVGGYNLKEKPLHAKANMG---IQLQSTSFQseLTVTEIIR 115
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRaylSQQQTPPFA--MPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 116 LY-AAVYGLSLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMH-----KP--KLVLLDEPTTGLDPQSRRQ 187
Cdd:PRK03695 92 LHqPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLDVAQQAA 171
|
170 180
....*....|....*....|
gi 1721664488 188 LWERMESLRNAGHAILLTTH 207
Cdd:PRK03695 172 LDRLLSELCQQGIAVVMSSH 191
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-236 |
7.36e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.05 E-value: 7.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 16 STETVLQVENLRVTYGS----FTAVHDVSFSVLGGEIFGLLGPNGAGKT-SSLSAIEGLLKPAA----GNIAVGGYNLke 86
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 87 kpLHA-----------KANMGIQLQSTSFQSELTVTEiiRLYAAvygLSL--------SDSEIEALLQNIKLETASsKRF 147
Cdd:PRK15134 79 --LHAseqtlrgvrgnKIAMIFQEPMVSLNPLHTLEK--QLYEV---LSLhrgmrreaARGEILNCLDRVGIRQAA-KRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 148 G----QLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAII 222
Cdd:PRK15134 151 TdyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVM 230
|
250
....*....|....
gi 1721664488 223 DHGRIIEIDSPQAI 236
Cdd:PRK15134 231 QNGRCVEQNRAATL 244
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-185 |
7.38e-16 |
|
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: 74.75 E-value: 7.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 29 TYGSFT-AVHDVSFSvlGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPlhakanmgiqlQSTSFQSE 107
Cdd:cd03237 9 TLGEFTlEVEGGSIS--ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP-----------QYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 108 LTVTEIIR-LYAAVYGLSLSDSEIealLQNIKLETASSKRFGQLSGGQQQRVSLAiATMHKP-KLVLLDEPTTGLDPQSR 185
Cdd:cd03237 76 GTVRDLLSsITKDFYTHPYFKTEI---AKPLQIEQILDREVPELSGGELQRVAIA-ACLSKDaDIYLLDEPSAYLDVEQR 151
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
10-181 |
1.95e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.62 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 10 SATSSASTETVLQVENLRVTYGSFtavhdvSFSVLGGEIF-----GLLGPNGAGKTSSLSAIEGLLKPAAGNIavgGYNL 84
Cdd:PRK13409 330 PPRDESERETLVEYPDLTKKLGDF------SLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPEL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 85 K--EKPlhakanmgiqlQSTSFQSELTVTEIIRLYAAVYGLSLSDSEIealLQNIKLETASSKRFGQLSGGQQQRVSLAI 162
Cdd:PRK13409 401 KisYKP-----------QYIKPDYDGTVEDLLRSITDDLGSSYYKSEI---IKPLQLERLLDKNVKDLSGGELQRVAIAA 466
|
170
....*....|....*....
gi 1721664488 163 ATMHKPKLVLLDEPTTGLD 181
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLD 485
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-205 |
1.99e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 75.74 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVG-----GY-NLKEKPLHAKA 93
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGetvklAYvDQSRDALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 94 NM------G---IQLQSTSFQSeltvteiiRLYAAVYGLSLSDSEieallqnikletassKRFGQLSGGQQQRVSLAIAT 164
Cdd:TIGR03719 402 TVweeisgGldiIKLGKREIPS--------RAYVGRFNFKGSDQQ---------------KKVGQLSGGERNRVHLAKTL 458
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1721664488 165 MHKPKLVLLDEPTTGLDPQSRRQLWERMESLrnAGHAILLT 205
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVIS 497
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
15-238 |
2.99e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 73.63 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 15 ASTETVLQVENLRVTYGSFTA--VHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNI-----AVGGYNLKEK 87
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 88 PLHakanMGIQLQSTSFQselTVTEIIRlYAAVYGL---SLSDSEI-----EALLQNIKLETASSKRfGQLSGGQQQRVS 159
Cdd:PRK13648 82 RKH----IGIVFQNPDNQ---FVGSIVK-YDVAFGLenhAVPYDEMhrrvsEALKQVDMLERADYEP-NALSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 160 LAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGH-AILLTTHSMEEAeAVCDRIAIIDHGRIIEIDSPQAIVD 238
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-255 |
5.83e-15 |
|
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: 72.96 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY--GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKpAAGNIAVGGYNLKEKPLHA-KANMGI 97
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKwRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQSTsfqseLTVTEIIRLYAAVYGlSLSDSEIEALLQNIKLETASSKRFGQL-----------SGGQQQRVSLAIATMH 166
Cdd:cd03289 82 IPQKV-----FIFSGTFRKNLDPYG-KWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 167 KPKLVLLDEPTTGLDPQSrRQLWERMESLRNAGHAILLTTHSMeEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHRNDAEV 246
Cdd:cd03289 156 KAKILLLDEPSAHLDPIT-YQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQA 233
|
....*....
gi 1721664488 247 IRASRKGKI 255
Cdd:cd03289 234 ISPSDRLKL 242
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
21-239 |
8.00e-15 |
|
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: 74.01 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYG-SFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQL 99
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 QSTSFQSELTVTEIIrLYAAVYGLSLSD-------SEIEALLQNIKL--ETASSKRFGQLSGGQQQRVSLAIATMHKPKL 170
Cdd:TIGR01193 554 PQEPYIFSGSILENL-LLGAKENVSQDEiwaaceiAEIKDDIENMPLgyQTELSEEGSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 171 VLLDEPTTGLDPQSRRQLWERMESLRNagHAILLTTHSMEEAEAVcDRIAIIDHGRIIEIDSPQAIVDR 239
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLDR 698
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-229 |
8.91e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.44 E-value: 8.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 25 NLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAG-----NIAVGG---YNLKEKpLHAKANMG 96
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGrsiFNYRDV-LEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 IQLQSTSfqsELTVTEIIRLYAAVYGLSLSDSE-----IEALLQNIKLETASSKRFG----QLSGGQQQRVSLAIATMHK 167
Cdd:PRK14271 105 MLFQRPN---PFPMSIMDNVLAGVRAHKLVPRKefrgvAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 168 PKLVLLDEPTTGLDPQSRRQLWERMESLRNAgHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-208 |
1.38e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 70.29 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 34 TAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLK--EKPL--HAKANMGIQLqstsfqsELT 109
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINniAKPYctYIGHNLGLKL-------EMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 110 VTEIIRLYAAVYGlslSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLW 189
Cdd:PRK13541 87 VFENLKFWSEIYN---SAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
170
....*....|....*....
gi 1721664488 190 ERMESLRNAGHAILLTTHS 208
Cdd:PRK13541 164 NLIVMKANSGGIVLLSSHL 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
48-228 |
1.45e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.60 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 48 IFGLlgpNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL--KEK----PLHaKANMGIQLQSTSFQSELTVTEIIRlyaavY 121
Cdd:PRK11144 29 IFGR---SGAGKTSLINAISGLTRPQKGRIVLNGRVLfdAEKgiclPPE-KRRIGYVFQDARLFPHYKVRGNLR-----Y 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 122 GLSLSDSE----------IEALLqnikletassKRF-GQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWE 190
Cdd:PRK11144 100 GMAKSMVAqfdkivallgIEPLL----------DRYpGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1721664488 191 RMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:PRK11144 170 YLERLaREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-220 |
1.93e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.22 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTS------SLSAIEGLLKpAAGNIAVGGYNLKEK------- 87
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTflkclnRMNELESEVR-VEGRVEFFNQNIYERrvnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 88 --------------PLHAKANMGIQLQSTSFQSELTVTEIIRlyAAVYGLSLSDsEIEALLQNIKLEtasskrfgqLSGG 153
Cdd:PRK14258 87 rrqvsmvhpkpnlfPMSVYDNVAYGVKIVGWRPKLEIDDIVE--SALKDADLWD-EIKHKIHKSALD---------LSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 154 QQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLR-NAGHAILLTTHSMEEAEAVCDRIA 220
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-266 |
2.11e-14 |
|
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: 73.06 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 28 VTYGSFT-------AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGY-------------NLKEK 87
Cdd:TIGR00957 639 VHNATFTwardlppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvayvpqqawiqndSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 88 PLhakanMGIQLQSTSFQSELTVTEIirlyaavyglsLSDSEIeallqnikLETASSKRFGQ----LSGGQQQRVSLAIA 163
Cdd:TIGR00957 719 IL-----FGKALNEKYYQQVLEACAL-----------LPDLEI--------LPSGDRTEIGEkgvnLSGGQKQRVSLARA 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 164 TMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRN--AGHAILLTTHSMEEAEAVcDRIAIIDHGRIIEIDSPQAIVDRHR 241
Cdd:TIGR00957 775 VYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
250 260
....*....|....*....|....*..
gi 1721664488 242 NDAEVIR--ASRKGKITLEDVFIGLTG 266
Cdd:TIGR00957 854 AFAEFLRtyAPDEQQGHLEDSWTALVS 880
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-229 |
2.14e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.97 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTY----GSF-----TAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKP 88
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 89 LHAKAN---MGIQLQSTSFQSELTVTEI----IRLYAAVYGLSLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLA 161
Cdd:PRK15112 82 YSYRSQrirMIFQDPSTSLNPRQRISQIldfpLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 162 IATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNA-GHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
40-236 |
5.31e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.20 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 40 SFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNiavggynlKEKPLHAKANMGI-QLQ---STSFQ-------SE- 107
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE--------RQSQFSHITRLSFeQLQklvSDEWQrnntdmlSPg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 108 -----LTVTEIIRL----------YAAVYGlslsdseIEALLqnikletasSKRFGQLSGGQQQRVSLAIATMHKPKLVL 172
Cdd:PRK10938 95 eddtgRTTAEIIQDevkdparceqLAQQFG-------ITALL---------DRRFKYLSTGETRKTLLCQALMSEPDLLI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 173 LDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAI 236
Cdd:PRK10938 159 LDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-235 |
5.32e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 37 HDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQLQSTSFQSE-----LTVT 111
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKAEgiipvHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 112 EII----RLYAAVYGL--------SLSDSEIEALlqNIKleTASSKR-FGQLSGGQQQRVSLAIATMHKPKLVLLDEPTT 178
Cdd:PRK11288 350 DNInisaRRHHLRAGClinnrweaENADRFIRSL--NIK--TPSREQlIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 179 GLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII-EIDSPQA 235
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAgELAREQA 483
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-225 |
7.45e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.97 E-value: 7.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKAnmgiQL 99
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR----QQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 QSTSFQSEL----TVTEIIRLYAAVYGLSLSDSEIEALLQNIKL-ETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLD 174
Cdd:PRK10247 83 VSYCAQTPTlfgdTVYDNLIFPWQIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 175 EPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHG 225
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
21-239 |
8.52e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 70.26 E-value: 8.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY-GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNL-KEKPlhakANMGIQ 98
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnELEP----ADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LqstSFQS-----ELTVTEIIrlyaaVYGLS---LSDSEIEALLQN----IKLETASSKRFGQLSGGQQQRVSLAIATMH 166
Cdd:PRK11650 80 M---VFQNyalypHMSVRENM-----AYGLKirgMPKAEIEERVAEaariLELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 167 KPKLVLLDEPTTGLDPQSRRQLweRMESLRNagHAILLT-----THSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDR 239
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKLRVQM--RLEIQRL--HRRLKTtslyvTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
38-232 |
1.70e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLK--PAAGNIAVggynlkekplhakanmgiqlQSTSFQSELTVTEIIr 115
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV--------------------PDNQFGREASLIDAI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 116 lyaavyGLSLSDSEIEALLQNIKLETASS--KRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERME 193
Cdd:COG2401 107 ------GRKGDFKDAVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1721664488 194 SL-RNAGHAILLTTHSMEEAEAVC-DRIAIIDHGRIIEIDS 232
Cdd:COG2401 181 KLaRRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEEKR 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-188 |
1.75e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.84 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 6 PATNSATSSASTETVLQVENLRV-TYGSFTAVHDVSFSVLGGEifGLL--GPNGAGKTSSLSAIEGLLKPAAGNIAVggy 82
Cdd:COG4178 348 LPEAASRIETSEDGALALEDLTLrTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIAR--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 83 nlkekPlhakanmgiQLQSTSFQSEltvteiiRLY--------AAVY---GLSLSDSEIEALLQNIKLETASSkRFGQ-- 149
Cdd:COG4178 423 -----P---------AGARVLFLPQ-------RPYlplgtlreALLYpatAEAFSDAELREALEAVGLGHLAE-RLDEea 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1721664488 150 -----LSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQL 188
Cdd:COG4178 481 dwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL 524
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-181 |
4.93e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.61 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 19 TVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGgynlkekplhAKANMGIQ 98
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG----------ETVKLAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQS-TSFQSELTVTEII----------------RLYAAVYGLSLSDSEieallqnikletassKRFGQLSGGQQQRVSLA 161
Cdd:PRK11819 393 DQSrDALDPNKTVWEEIsggldiikvgnreipsRAYVGRFNFKGGDQQ---------------KKVGVLSGGERNRLHLA 457
|
170 180
....*....|....*....|
gi 1721664488 162 IATMHKPKLVLLDEPTTGLD 181
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLD 477
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
37-207 |
1.02e-12 |
|
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: 64.96 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 37 HDVSFSVLGGEIFGLLGPNGAGKTSSLSAI-----EGLLKpaaGNIAVGGYNLKEKPLHAkanMGIQLQSTSFQSELTVT 111
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVIT---GEILINGRPLDKNFQRS---TGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 112 EIIRLYAAVYGLSLSdseieallqnikletasskrfgqlsggQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWER 191
Cdd:cd03232 98 EALRFSALLRGLSVE---------------------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRF 150
|
170
....*....|....*.
gi 1721664488 192 MESLRNAGHAILLTTH 207
Cdd:cd03232 151 LKKLADSGQAILCTIH 166
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-237 |
1.68e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.58 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 15 ASTETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKAN 94
Cdd:PRK10575 6 NHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 95 MGIQLQSTSFQSE-LTVTEIIRL-----YAAVYGLSLSDSE-IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHK 167
Cdd:PRK10575 86 KVAYLPQQLPAAEgMTVRELVAIgrypwHGALGRFGAADREkVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721664488 168 PKLVLLDEPTTGLDPQSRRQ---LWERMESLRnaGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIV 237
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDvlaLVHRLSQER--GLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-241 |
2.53e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.76 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 16 STETVLQVENLRVTY----GSFT------AVHDVSFSVLGGEIFGLLGPNGAGKTS---SLSAIEgllKPAAGNIAVGGY 82
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkrGLFKperlvkALDGVSFTLERGKTLAVVGESGCGKSTlarLLTMIE---TPTGGELYYQGQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 83 NLKEKPLHAKANMGIQLQSTsFQSEL-------TVTEIIRLYAAVyGLSLSDSE----IEALLQNIKLETASSKRFGQL- 150
Cdd:PRK11308 78 DLLKADPEAQKLLRQKIQIV-FQNPYgslnprkKVGQILEEPLLI-NTSLSAAErrekALAMMAKVGLRPEHYDRYPHMf 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 151 SGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLqQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 235
|
250
....*....|..
gi 1721664488 230 IDSPQAIVDRHR 241
Cdd:PRK11308 236 KGTKEQIFNNPR 247
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-233 |
4.87e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.46 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLL--KPAAGNIAV-GGYNLKEKPLHA-KANM 95
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgGGAPRGARVtGDVTLNGEPLAAiDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 96 GIQLQSTSFQSE-----LTVTEIIRL----YAAVYG-LSLSDSEI-EALLQNIKLETASSKRFGQLSGGQQQRVSLAIA- 163
Cdd:PRK13547 81 LARLRAVLPQAAqpafaFSAREIVLLgrypHARRAGaLTHRDGEIaWQALALAGATALVGRDVTTLSGGELARVQFARVl 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721664488 164 --------TMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSP 233
Cdd:PRK13547 161 aqlwpphdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-229 |
5.35e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.20 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKtSSLSAIEGLLKPAA---GNIAVGGYNLKEKPLHAKANMG 96
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGK-STLMKVLSGVYPHGsyeGEILFDGEVCRFKDIRDSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 IQL--QSTSFQSELTVTEIIRL--YAAVYGL---SLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPK 169
Cdd:NF040905 80 IVIihQELALIPYLSIAENIFLgnERAKRGVidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 170 LVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-210 |
5.64e-12 |
|
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: 65.02 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRvtygsftAVHDVSFSvLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGN-----------------IAVGGY- 82
Cdd:COG3593 6 IKIKNFR-------SIKDLSIE-LSDDLTVLVGENNSGKSSILEALRLLLGPSSSRkfdeedfylgddpdlpeIEIELTf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 83 -----NLKEKPLHAKANMGIQLQSTSFQSEL-----TVTEIIRLYAAVYG------LSLSDSEIEALLQNIKL--ETASS 144
Cdd:COG3593 78 gsllsRLLRLLLKEEDKEELEEALEELNEELkealkALNELLSEYLKELLdgldleLELSLDELEDLLKSLSLriEDGKE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721664488 145 KRFGQLSGGQQQRVSLAIATM-------HKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSME 210
Cdd:COG3593 158 LPLDRLGSGFQRLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPH 230
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
10-185 |
7.14e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.19 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 10 SATSSASTETVLQVENLRVTYGSFtavhdvSFSVLGGEIF-----GLLGPNGAGKTSSLSAIEGLLKPAAGNIAvGGYNL 84
Cdd:COG1245 331 APRREKEEETLVEYPDLTKSYGGF------SLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 85 KEKPlhakanmgiqlQSTSFQSELTVTEIIRlyaAVYGLSLSDSEIEA-LLQNIKLETASSKRFGQLSGGQQQRVSLAIA 163
Cdd:COG1245 404 SYKP-----------QYISPDYDGTVEEFLR---SANTDDFGSSYYKTeIIKPLGLEKLLDKNVKDLSGGELQRVAIAAC 469
|
170 180
....*....|....*....|..
gi 1721664488 164 TMHKPKLVLLDEPTTGLDPQSR 185
Cdd:COG1245 470 LSRDADLYLLDEPSAHLDVEQR 491
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
9-239 |
1.03e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 9 NSATSSASTETVLQVENLRVTY--GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLke 86
Cdd:PLN03232 1223 NRPVSGWPSRGSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV-- 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 87 kplhakANMGI----QLQSTSFQSELTVTEIIRLYAAVYGlSLSDSEIEALLQNIKLETASSKR-FG----------QLS 151
Cdd:PLN03232 1301 ------AKFGLtdlrRVLSIIPQSPVLFSGTVRFNIDPFS-EHNDADLWEALERAHIKDVIDRNpFGldaevseggeNFS 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 152 GGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQS----RRQLWERMESLrnaghAILLTTHSMEEAeAVCDRIAIIDHGRI 227
Cdd:PLN03232 1374 VGQRQLLSLARALLRRSKILVLDEATASVDVRTdsliQRTIREEFKSC-----TMLVIAHRLNTI-IDCDKILVLSSGQV 1447
|
250
....*....|..
gi 1721664488 228 IEIDSPQAIVDR 239
Cdd:PLN03232 1448 LEYDSPQELLSR 1459
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-239 |
1.27e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 63.77 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKP----AAGNIAVGGYNL-KEKPLHA 91
Cdd:COG4170 4 LDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLlKLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 92 KANMGIQLqSTSFQSELTvteiirlyaavyglSLSDSEI--EALLQNIKLETASSK---RFG------------------ 148
Cdd:COG4170 84 RKIIGREI-AMIFQEPSS--------------CLDPSAKigDQLIEAIPSWTFKGKwwqRFKwrkkraiellhrvgikdh 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 149 ---------QLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDR 218
Cdd:COG4170 149 kdimnsyphELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADT 228
|
250 260
....*....|....*....|.
gi 1721664488 219 IAIIDHGRIIEIDSPQAIVDR 239
Cdd:COG4170 229 ITVLYCGQTVESGPTEQILKS 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
35-228 |
1.31e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 35 AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQLQSTSFQSELTVTEII 114
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 115 RLYAAVY---GLSLSDS----EIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQ 187
Cdd:PRK10982 93 NMWLGRYptkGMFVDQDkmyrDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNH 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1721664488 188 LWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:PRK10982 173 LFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
46-207 |
1.32e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 46 GEIFGLLGPNGAGKTSSLSAIEGLLKPA--AGNIAVGGYNLKEKPLHakaNMGIQLQSTSFQSELTVTEIIrLYAAVYGL 123
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILK---RTGFVTQDDILYPHLTVRETL-VFCSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 124 --SLSDSE----IEALLQNIKLETASSKRFGQ-----LSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERM 192
Cdd:PLN03211 170 pkSLTKQEkilvAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170
....*....|....*
gi 1721664488 193 ESLRNAGHAILLTTH 207
Cdd:PLN03211 250 GSLAQKGKTIVTSMH 264
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-224 |
1.96e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 61.02 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTA-VHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIavggynlkEKPLHAKANMgiqL 99
Cdd:cd03223 1 IELENLSLATPDGRVlLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEDLLF---L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 QSTSFQSELTVTEIIrLYAavyglslSDSEieallqnikletasskrfgqLSGGQQQRVSLAIATMHKPKLVLLDEPTTG 179
Cdd:cd03223 70 PQRPYLPLGTLREQL-IYP-------WDDV--------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1721664488 180 LDPQSRRQLwerMESLRNAGHAILLTTHSmEEAEAVCDRIAIIDH 224
Cdd:cd03223 122 LDEESEDRL---YQLLKELGITVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-255 |
2.26e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.78 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY--GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKpAAGNIAVGGYNLKEKPLHA-KANMGI 97
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTwRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQ-----STSFQSELTVTEiirlyaavyglSLSDSEIEALLQNIKLETASSKRFGQ-----------LSGGQQQRVSLA 161
Cdd:TIGR01271 1297 IPQkvfifSGTFRKNLDPYE-----------QWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLA 1365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 162 IATMHKPKLVLLDEPTTGLDPQSrRQLWERMESLRNAGHAILLTTHSMeEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHR 241
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVT-LQIIRKTLKQSFSNCTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLLNETS 1443
|
250
....*....|....
gi 1721664488 242 NDAEVIRASRKGKI 255
Cdd:TIGR01271 1444 LFKQAMSAADRLKL 1457
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
33-228 |
3.11e-11 |
|
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: 61.12 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 33 FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAA---GNIAVGGYNLKEKPLHAKANMGIQLQSTSFQSELT 109
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 110 VTEIIRlyaavYGLSLSDSEIeallqnikletasskrFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLW 189
Cdd:cd03233 100 VRETLD-----FALRCKGNEF----------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1721664488 190 ERMESLRNAGHAILLTTHSM--EEAEAVCDRIAIIDHGRII 228
Cdd:cd03233 159 KCIRTMADVLKTTTFVSLYQasDEIYDLFDKVLVLYEGRQI 199
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
35-241 |
3.58e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.99 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 35 AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkekplhAKANMGIqlqSTSFQSELTVTEII 114
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---------SAALIAI---SSGLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 115 RLYAAVYGlsLSDSEIEALLQNIkLETASSKRF-----GQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLW 189
Cdd:PRK13545 107 ELKGLMMG--LTKEKIKEIIPEI-IEFADIGKFiyqpvKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 190 ERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEIDSPQAIVDRHR 241
Cdd:PRK13545 184 DKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYD 235
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-229 |
5.38e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 62.34 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTY-GSFT-AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLhakANMGIQ 98
Cdd:PRK11176 342 IEFRNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTL---ASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 99 LQSTSFQSEL---TVTEIIrLYAAvyGLSLSDSEIE-------ALLQNIKLETASSKRFGQ----LSGGQQQRVSLAIAT 164
Cdd:PRK11176 419 VALVSQNVHLfndTIANNI-AYAR--TEQYSREQIEeaarmayAMDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721664488 165 MHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNaGHAILLTTHSMEEAEAVcDRIAIIDHGRIIE 229
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTIEKA-DEILVVEDGEIVE 558
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-228 |
7.89e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 18 ETVLQVENLRVTYGSFT---AVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLL--KPAAGNIAVGGynlkeKPLHAK 92
Cdd:NF040905 255 EVVFEVKNWTVYHPLHPerkVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDG-----KEVDVS 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 93 anmgiqlqstsfqselTVTEIIR---LYAA----VYGLSLsdseIEALLQNIKL----------------ETASSKRF-- 147
Cdd:NF040905 330 ----------------TVSDAIDaglAYVTedrkGYGLNL----IDDIKRNITLanlgkvsrrgvideneEIKVAEEYrk 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 148 -------------GQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEA 214
Cdd:NF040905 390 kmniktpsvfqkvGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLG 469
|
250
....*....|....
gi 1721664488 215 VCDRIAIIDHGRII 228
Cdd:NF040905 470 MCDRIYVMNEGRIT 483
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
35-219 |
1.01e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.86 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 35 AVHDVSFS-----VLG--------GEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLK--EKPLHakanMGIQL 99
Cdd:PRK13543 13 AAHALAFSrneepVFGpldfhvdaGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATrgDRSRF----MAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 QSTSFQSELTVTEIIRLYAAVYGLSLSDSEIEALLQnIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTG 179
Cdd:PRK13543 89 HLPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAI-VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1721664488 180 LDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRI 219
Cdd:PRK13543 168 LDLEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRM 207
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-249 |
1.23e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.97 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTY----GSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKP----AAGNIAVGGYNL-----KE 86
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLlrlspRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 87 KPLHAKANMGIQLQSTsfQSELTVTEII--RLYAAVYGLSLSDS-----------EIEALLQ-NIKLETASSKRFG-QLS 151
Cdd:PRK15093 83 RRKLVGHNVSMIFQEP--QSCLDPSERVgrQLMQNIPGWTYKGRwwqrfgwrkrrAIELLHRvGIKDHKDAMRSFPyELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 152 GGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIEI 230
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260
....*....|....*....|.
gi 1721664488 231 DSPQAIVD--RHRNDAEVIRA 249
Cdd:PRK15093 241 APSKELVTtpHHPYTQALIRA 261
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-198 |
1.61e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIavggyNLKEkplhaKANMGIQLQ 100
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSE-----NANIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 101 STS--FQSELTVTEIIRLYA-------AVYG----LSLSDSEIEallqnikletassKRFGQLSGGQQQRVSLAIATMHK 167
Cdd:PRK15064 390 DHAydFENDLTLFDWMSQWRqegddeqAVRGtlgrLLFSQDDIK-------------KSVKVLSGGEKGRMLFGKLMMQK 456
|
170 180 190
....*....|....*....|....*....|.
gi 1721664488 168 PKLVLLDEPTTGLDPQSrrqlwerMESLRNA 198
Cdd:PRK15064 457 PNVLVMDEPTNHMDMES-------IESLNMA 480
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-209 |
1.94e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.20 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGSFTAVH---DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVG-GYNLK----------- 85
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKdinlkwwrski 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 86 ----EKPL----HAKANMGIQLQS---------------TSFQSELTVTEIIRLYAAVY-----------GL-------- 123
Cdd:PTZ00265 463 gvvsQDPLlfsnSIKNNIKYSLYSlkdlealsnyynedgNDSQENKNKRNSCRAKCAGDlndmsnttdsnELiemrknyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 124 SLSDSEIEALLQNI-----------KLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERM 192
Cdd:PTZ00265 543 TIKDSEVVDVSKKVlihdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250
....*....|....*...
gi 1721664488 193 ESLR-NAGHAILLTTHSM 209
Cdd:PTZ00265 623 NNLKgNENRITIIIAHRL 640
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
46-207 |
2.02e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 46 GEIFGLLGPNGAGKTSSLSAIEGLLkpaAGNIAVGGYNLKEkplhakanmGIQLQStSFQ-------------SELTVTE 112
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERV---TTGVITGGDRLVN---------GRPLDS-SFQrsigyvqqqdlhlPTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 113 IIRLYAAV-YGLSLSDSE----IEALLQNIKLETASSKRFGQ----LSGGQQQRVSLAIATMHKPKLVL-LDEPTTGLDP 182
Cdd:TIGR00956 856 SLRFSAYLrQPKSVSKSEkmeyVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS 935
|
170 180
....*....|....*....|....*
gi 1721664488 183 QSRRQLWERMESLRNAGHAILLTTH 207
Cdd:TIGR00956 936 QTAWSICKLMRKLADHGQAILCTIH 960
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
38-228 |
2.74e-10 |
|
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: 60.33 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGniavggynlkEKPLHAKANMGIQLQSTSFQSELTVTEIIRL- 116
Cdd:TIGR03719 23 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----------EARPQPGIKVGYLPQEPQLDPTKTVRENVEEg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 117 ----------YAAVYG-LSLSDSEIEAL------LQNI-----------KLETAS--------SKRFGQLSGGQQQRVSL 160
Cdd:TIGR03719 93 vaeikdaldrFNEISAkYAEPDADFDKLaaeqaeLQEIidaadawdldsQLEIAMdalrcppwDADVTKLSGGERRRVAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 161 AIATMHKPKLVLLDEPTTGLDPQSRRQLwERMesLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRII 228
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDAESVAWL-ERH--LQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGI 237
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
34-229 |
2.90e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.11 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 34 TAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHA-KANMGIQLQsTSFQSELTVTE 112
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRLAVVSQ-TPFLFSDTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 113 IIRLYAAvyglSLSDSEIE--ALLQNIK---------LETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLD 181
Cdd:PRK10789 408 NIALGRP----DATQQEIEhvARLASVHddilrlpqgYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1721664488 182 PQSRRQLwerMESLRNAGH--AILLTTHSMeEAEAVCDRIAIIDHGRIIE 229
Cdd:PRK10789 484 GRTEHQI---LHNLRQWGEgrTVIISAHRL-SALTEASEILVMQHGHIAQ 529
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
38-225 |
3.04e-10 |
|
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: 59.49 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkekplhakanmgiqlqSTSFQSEL------TVT 111
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------------RISFSSQFswimpgTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 112 EIIrlyaaVYGLSLSDSEIEALLQNIKLETASSKRFGQ-----------LSGGQQQRVSLAIATMHKPKLVLLDEPTTGL 180
Cdd:cd03291 116 ENI-----IFGVSYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1721664488 181 DPQSRRQLWERMESLRNAGHAILLTTHSMEEAEaVCDRIAIIDHG 225
Cdd:cd03291 191 DVFTEKEIFESCVCKLMANKTRILVTSKMEHLK-KADKILILHEG 234
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-190 |
4.32e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVG-----GYNLKEKPLHAKAN 94
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgiklGYFAQHQLEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 95 MGiQLQSTSFQSELTVTEIIRLYAAVYGLslsdseieallQNIKLeTASSKRFgqlSGGQQQRVSLAIATMHKPKLVLLD 174
Cdd:PRK10636 392 ES-PLQHLARLAPQELEQKLRDYLGGFGF-----------QGDKV-TEETRRF---SGGEKARLVLALIVWQRPNLLLLD 455
|
170
....*....|....*.
gi 1721664488 175 EPTTGLDPQSRRQLWE 190
Cdd:PRK10636 456 EPTNHLDLDMRQALTE 471
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
147-210 |
5.91e-10 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 58.56 E-value: 5.91e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 147 FGQLSGGQQqRVSLAIATMH----KPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSME 210
Cdd:pfam13304 234 AFELSDGTK-RLLALLAALLsalpKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
36-207 |
8.37e-10 |
|
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: 58.99 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 36 VHDVSFSVLGGEIFGLLGPNGAGKtSSLSAIEG---------LLKPAAGNIavggYNLKEKPLHAKANMGIQL----QST 102
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGK-SSLFRILGelwpvyggrLTKPAKGKL----FYVPQRPYMTLGTLRDQIiypdSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 103 SFQSEltvteiirlyaavyglSLSDSEIEALLQNIKLETASSKRFG---------QLSGGQQQRVSLAIATMHKPKLVLL 173
Cdd:TIGR00954 543 DMKRR----------------GLSDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....
gi 1721664488 174 DEPTTGLDPQSRRQLWermESLRNAGHAILLTTH 207
Cdd:TIGR00954 607 DECTSAVSVDVEGYMY---RLCREFGITLFSVSH 637
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
37-229 |
8.63e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 58.68 E-value: 8.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 37 HDVSFSVLGGEIFGLLGPNGAGKtsslSAIEGLL----KPAAGNIAVGGYNLKEKPLHA-KANMGIQLQSTS-FQSelTV 110
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGK----STLARLLfrfyDVTSGRILIDGQDIRDVTQASlRAAIGIVPQDTVlFND--TI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 111 TEIIRlyaavYG-LSLSDSEIE--ALLQNI---------KLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTT 178
Cdd:COG5265 449 AYNIA-----YGrPDASEEEVEaaARAAQIhdfieslpdGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 179 GLDPQSRRqlwERMESLRNA--GHAILLTTHSMEE-AEAvcDRIAIIDHGRIIE 229
Cdd:COG5265 524 ALDSRTER---AIQAALREVarGRTTLVIAHRLSTiVDA--DEILVLEAGRIVE 572
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
32-229 |
1.26e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.52 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 32 SFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkekplhakaNMGIQLQSTSFQSELTVT 111
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------------EVSVIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 112 EIIRLYAAVYGlsLSDSEIEALLQNIkLETASSKRF-----GQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRR 186
Cdd:PRK13546 104 ENIEFKMLCMG--FKRKEIKAMTPKI-IEFSELGEFiyqpvKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1721664488 187 QLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHGRIIE 229
Cdd:PRK13546 181 KCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
150-217 |
1.72e-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: 55.79 E-value: 1.72e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721664488 150 LSGGQQQRVSLA--IATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHS---MEEAEAVCD 217
Cdd:cd03238 88 LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNldvLSSADWIID 160
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
38-237 |
2.73e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.65 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPLHakaNMGIQLQSTSfQSELTVTEIIRLY 117
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLH---DLRFKITIIP-QDPVLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 118 AAVYGlSLSDSEIEALL-----------QNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRR 186
Cdd:TIGR00957 1380 LDPFS-QYSDEEVWWALelahlktfvsaLPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1721664488 187 QLWERMESlRNAGHAILLTTHSMeeaEAVCD--RIAIIDHGRIIEIDSPQAIV 237
Cdd:TIGR00957 1459 LIQSTIRT-QFEDCTVLTIAHRL---NTIMDytRVIVLDKGEVAEFGAPSNLL 1507
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
37-234 |
4.87e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 37 HDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPL-HAKANMGIQLQSTSfqseltvteiir 115
Cdd:PLN03130 1256 HGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLmDLRKVLGIIPQAPV------------ 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 116 LYAAVYGLSL------SDSEI-EAL----LQNI------KLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTT 178
Cdd:PLN03130 1324 LFSGTVRFNLdpfnehNDADLwESLerahLKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 179 GLDPQS----RRQLWERMESLrnaghAILLTTHSMEEAeAVCDRIAIIDHGRIIEIDSPQ 234
Cdd:PLN03130 1404 AVDVRTdaliQKTIREEFKSC-----TMLIIAHRLNTI-IDCDRILVLDAGRVVEFDTPE 1457
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-231 |
5.55e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 10 SATSSASTETVLQVENLRVTYG--SFtAVHDVSFSVLGGEIFGLLGPNGAGKtSSLSAI-EGLLKPAAGNIAVGGynlke 86
Cdd:PRK10522 312 PRPQAFPDWQTLELRNVTFAYQdnGF-SVGPINLTIKRGELLFLIGGNGSGK-STLAMLlTGLYQPQSGEILLDG----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 87 KPLHAKanmgiqlqstsfqselTVTEIIRLYAAVY-------------GLSLSDSEIEALLQNIKLE---TASSKRFG-- 148
Cdd:PRK10522 385 KPVTAE----------------QPEDYRKLFSAVFtdfhlfdqllgpeGKPANPALVEKWLERLKMAhklELEDGRISnl 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 149 QLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLW-ERMESLRNAGHAILLTTHS---MEEAeavcDRIAIIDH 224
Cdd:PRK10522 449 KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYqVLLPLLQEMGKTIFAISHDdhyFIHA----DRLLEMRN 524
|
....*..
gi 1721664488 225 GRIIEID 231
Cdd:PRK10522 525 GQLSELT 531
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
38-225 |
7.07e-09 |
|
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: 56.46 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGynlkekplhakanmgiqlqSTSFQSEL------TVT 111
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------------RISFSPQTswimpgTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 112 EIIrlyaaVYGLSLSDSEIEALLQNIKLETASSKrFGQ------------LSGGQQQRVSLAIATMHKPKLVLLDEPTTG 179
Cdd:TIGR01271 505 DNI-----IFGLSYDEYRYTSVIKACQLEEDIAL-FPEkdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1721664488 180 LDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVcDRIAIIDHG 225
Cdd:TIGR01271 579 LDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKA-DKILLLHEG 623
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
38-207 |
1.17e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKP------AAGNIAVGgYNLKEKPLHAkanmgiqlqstsfqsELTVT 111
Cdd:PRK11819 25 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEfegearPAPGIKVG-YLPQEPQLDP---------------EKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 112 EIIRL-----------YAAVYG-LSLSDSEIEAL------LQNI-----------KLETA--------SSKRFGQLSGGQ 154
Cdd:PRK11819 89 ENVEEgvaevkaaldrFNEIYAaYAEPDADFDALaaeqgeLQEIidaadawdldsQLEIAmdalrcppWDAKVTKLSGGE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 155 QQRVSLAIATMHKPKLVLLDEPTTGLDPQSrrQLW-ERMesLRNAGHAILLTTH 207
Cdd:PRK11819 169 RRRVALCRLLLEKPDMLLLDEPTNHLDAES--VAWlEQF--LHDYPGTVVAVTH 218
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
146-230 |
1.21e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.54 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 146 RFGQ----LSGGQQQRVSLAiATMHKPK----LVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMeeaeavcD 217
Cdd:cd03271 162 KLGQpattLSGGEAQRIKLA-KELSKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL-------D 233
|
90
....*....|...
gi 1721664488 218 RIAIIDHgrIIEI 230
Cdd:cd03271 234 VIKCADW--IIDL 244
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
150-219 |
1.43e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 55.61 E-value: 1.43e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721664488 150 LSGGQQQRVSLA---IATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEaVCDRI 219
Cdd:PRK00635 810 LSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYV 881
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
46-224 |
6.44e-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: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 46 GEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNI-----------AVGGYNLK---EKPLHAKANMGIQLQStsfqseltVT 111
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQnyfTKLLEGDVKVIVKPQY--------VD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 112 EIIRLYAAVYGLSLSDSE----IEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQ 187
Cdd:cd03236 98 LIPKAVKGKVGELLKKKDergkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1721664488 188 LWERMESLRNAGHAILLTTHSMeeaeAVCDRIAIIDH 224
Cdd:cd03236 178 AARLIRELAEDDNYVLVVEHDL----AVLDYLSDYIH 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
38-181 |
6.91e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSVLGGEI------FGL--------LGPNGAGKTSSLSAIEGLLKPAAGNI--------------AVGGYNLKEKPL 89
Cdd:PLN03073 513 DASFGYPGGPLlfknlnFGIdldsriamVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDLSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 90 --HAKANMGIQLQStsfqseltvteiIRLYAAVYGLSlsdseieallQNIKLETASSkrfgqLSGGQQQRVSLAIATMHK 167
Cdd:PLN03073 593 lyMMRCFPGVPEQK------------LRAHLGSFGVT----------GNLALQPMYT-----LSGGQKSRVAFAKITFKK 645
|
170
....*....|....
gi 1721664488 168 PKLVLLDEPTTGLD 181
Cdd:PLN03073 646 PHILLLDEPSNHLD 659
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
46-181 |
7.95e-08 |
|
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: 52.86 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 46 GEIFGLLGPNGAGKTSSLSAIEGLLKPaagniavggynlkekplhakaNMGIqlqstsFQSELTVTEIIRLYAAV----Y 121
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKP---------------------NLGD------YDEEPSWDEVLKRFRGTelqdY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 122 GLSLSDSEIEA--------------------LLQNI-------------KLETASSKRFGQLSGGQQQRVSLAIATMHKP 168
Cdd:COG1245 152 FKKLANGEIKVahkpqyvdlipkvfkgtvreLLEKVdergkldelaeklGLENILDRDISELSGGELQRVAIAAALLRDA 231
|
170
....*....|...
gi 1721664488 169 KLVLLDEPTTGLD 181
Cdd:COG1245 232 DFYFFDEPSSYLD 244
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
38-207 |
7.99e-08 |
|
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: 50.82 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSvlGGEIFGLLGPNGAGKTSSLSAIEgllkpaagnIAVGGynlKEKPLHAKANMGIQLQSTSFQSELTVTeiirly 117
Cdd:cd03227 15 DVTFG--EGSLTIITGPNGSGKSTILDAIG---------LALGG---AQSATRRRSGVKAGCIVAAVSAELIFT------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 118 aavyglslsdseieallqnikletasskrFGQLSGGQQQRVSLA----IATMHKPKLVLLDEPTTGLDPQSRRQLWERME 193
Cdd:cd03227 75 -----------------------------RLQLSGGEKELSALAlilaLASLKPRPLYILDEIDRGLDPRDGQALAEAIL 125
|
170
....*....|....
gi 1721664488 194 SLRNAGHAILLTTH 207
Cdd:cd03227 126 EHLVKGAQVIVITH 139
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-223 |
1.27e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 50.26 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 29 TYGSFTAVHDVSfSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPlhakanmgiqlqstsfqsel 108
Cdd:cd03222 9 RYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP-------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 109 tvteiirlyaavyglslsdseieallQNIKletasskrfgqLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQL 188
Cdd:cd03222 68 --------------------------QYID-----------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA 110
|
170 180 190
....*....|....*....|....*....|....*.
gi 1721664488 189 WERMESL-RNAGHAILLTTHSMEEAEAVCDRIAIID 223
Cdd:cd03222 111 ARAIRRLsEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
109-225 |
1.36e-07 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 51.10 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 109 TVTEI---IRLYAAVYGLSlsdsEIEALLQNIKLETAS-SKRFGQLSGGQQQRVSLAiaTMHKPKLV----LLDEPTTGL 180
Cdd:cd03270 97 TVTEIydyLRLLFARVGIR----ERLGFLVDVGLGYLTlSRSAPTLSGGEAQRIRLA--TQIGSGLTgvlyVLDEPSIGL 170
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1721664488 181 DPQSRRQLWERMESLRNAGHAILLTTHSmEEAEAVCDRiaIIDHG 225
Cdd:cd03270 171 HPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADH--VIDIG 212
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-229 |
1.49e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.95 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 20 VLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGL--LKPAAGNIAVGGYNLKEKPLHAKANMGI 97
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLqstSFQSEL------------TVTEIIRLYAAVYGLSLSDSE--IEALLQNIKLET---ASSKRFGqLSGGQQQRVSL 160
Cdd:PRK09580 81 FM---AFQYPVeipgvsnqfflqTALNAVRSYRGQEPLDRFDFQdlMEEKIALLKMPEdllTRSVNVG-FSGGEKKRNDI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 161 AIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAV-CDRIAIIDHGRIIE 229
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIkPDYVHVLYQGRIVK 226
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
146-209 |
1.50e-07 |
|
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: 52.32 E-value: 1.50e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 146 RFGQ----LSGGQQQRVSLAIATMHK---PKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSM 209
Cdd:TIGR00630 822 RLGQpattLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-210 |
2.03e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.41 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRVTYGS-FTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGniAVGGYNLKEKPLHAKANMGIQL 99
Cdd:cd03290 1 VQVTNGYFSWGSgLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--KVHWSNKNESEPSFEATRSRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 100 QSTSFQSE------LTVTEIIrLYAAVYGLSLSDSEIEA--LLQNIKL-----ETASSKRFGQLSGGQQQRVSLAIATMH 166
Cdd:cd03290 79 YSVAYAAQkpwllnATVEENI-TFGSPFNKQRYKAVTDAcsLQPDIDLlpfgdQTEIGERGINLSGGQRQRICVARALYQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1721664488 167 KPKLVLLDEPTTGLDPQSRRQLWER--MESLRNAGHAILLTTHSME 210
Cdd:cd03290 158 NTNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-181 |
3.02e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 46 GEIFGLLGPNGAGKTSSLSAIEGLLKPaagniavggynlkekplhakaNMGiqlqstSFQSELTVTEIIRLYAAV----Y 121
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIP---------------------NLG------DYEEEPSWDEVLKRFRGTelqnY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 122 GLSLSDSEIEA--------------------LLQNI-------------KLETASSKRFGQLSGGQQQRVSLAIATMHKP 168
Cdd:PRK13409 152 FKKLYNGEIKVvhkpqyvdlipkvfkgkvreLLKKVdergkldevverlGLENILDRDISELSGGELQRVAIAAALLRDA 231
|
170
....*....|...
gi 1721664488 169 KLVLLDEPTTGLD 181
Cdd:PRK13409 232 DFYFFDEPTSYLD 244
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
132-225 |
3.12e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 132 ALLQNIKLETASSKR-FGQLSGGQQQRVSLA-------IATMHkpklvLLDEPTTGLDPQSRRQLWERMESLRNAGHAIL 203
Cdd:PRK00635 458 SILIDLGLPYLTPERaLATLSGGEQERTALAkhlgaelIGITY-----ILDEPSIGLHPQDTHKLINVIKKLRDQGNTVL 532
|
90 100
....*....|....*....|..
gi 1721664488 204 LTTHSmEEAEAVCDRiaIIDHG 225
Cdd:PRK00635 533 LVEHD-EQMISLADR--IIDIG 551
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
21-226 |
4.20e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.14 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRvtygSFTAVHDVSFsvlGGEIFGLLGPNGAGKTSSLSAIEGLLKPaagniavggynlkEKPLHAKANMG---- 96
Cdd:cd03240 4 LSIRNIR----SFHERSEIEF---FSPLTLIVGQNGAGKTTIIEALKYALTG-------------ELPPNSKGGAHdpkl 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 97 IQLQSTSFQSELTVTEII-RLYAAVyglslsdSEIEALLQNIKLETASSKRF-----GQLSGGQQQRVSLAIAT------ 164
Cdd:cd03240 64 IREGEVRAQVKLAFENANgKKYTIT-------RSLAILENVIFCHQGESNWPlldmrGRCSGGEKVLASLIIRLalaetf 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721664488 165 MHKPKLVLLDEPTTGLDPQSRR-QLWERMESLRNAGH-AILLTTHSmEEAEAVCD---RIAIIDHGR 226
Cdd:cd03240 137 GSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQKNfQLIVITHD-EELVDAADhiyRVEKDGRQK 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-80 |
7.54e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 7.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 11 ATSSASTETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVG 80
Cdd:PRK11147 310 EEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG 379
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
70-225 |
7.72e-07 |
|
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: 50.01 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 70 LKPAAGNIAVGGynlkeKPLHAKANMGIQlQSTSFQSELTVTEIIRLYAAvyglsLSDSEIEA---LLQNIKLETAS-SK 145
Cdd:TIGR00630 416 LKPEALAVTVGG-----KSIADVSELSIR-EAHEFFNQLTLTPEEKKIAE-----EVLKEIRErlgFLIDVGLDYLSlSR 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 146 RFGQLSGGQQQRVSLA--IATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSmEEAEAVCDRiaIID 223
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLAtqIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADY--VID 561
|
..
gi 1721664488 224 HG 225
Cdd:TIGR00630 562 IG 563
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
150-233 |
8.75e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 150 LSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTthsmeeaeaVCDRIAIIDHG-RII 228
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT---------IAHRIASIKRSdKIV 1429
|
....*
gi 1721664488 229 EIDSP 233
Cdd:PTZ00265 1430 VFNNP 1434
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
38-229 |
1.47e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.20 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKP-----LHAKANMGIqLQSTSFQSEltvte 112
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVPqvswiFNATVRENI-LFGSDFESE----- 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 113 iiRLYAAVyglslsdsEIEALLQNIKL-----ETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQ 187
Cdd:PLN03232 709 --RYWRAI--------DVTALQHDLDLlpgrdLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1721664488 188 LWERMESLRNAGHAILLTTHSMEEAEAVcDRIAIIDHGRIIE 229
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKE 819
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-227 |
1.55e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 28 VTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGN-IAVGG---------YNLKEKplhakanmgI 97
Cdd:PRK10938 268 VSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNdLTLFGrrrgsgetiWDIKKH---------I 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 98 QLQSTSFQSELTVTEIIR------------LYAAVyglslSD------SEIEALLqNIKLETASSKrFGQLSGGQQQRVS 159
Cdd:PRK10938 339 GYVSSSLHLDYRVSTSVRnvilsgffdsigIYQAV-----SDrqqklaQQWLDIL-GIDKRTADAP-FHSLSWGQQRLAL 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721664488 160 LAIATMHKPKLVLLDEPTTGLDPQSrRQLWER-MESLRNAGHAILL-TTHSMEEA-EAVCDRIAIIDHGRI 227
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLN-RQLVRRfVDVLISEGETQLLfVSHHAEDApACITHRLEFVPDGDI 481
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
46-207 |
1.62e-06 |
|
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: 46.60 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 46 GEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIavggynlkekplhakanmgiqlqstsfqseltvteiirlyaavygLSL 125
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV---------------------------------------------IYI 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 126 SDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWERMES------LRNAG 199
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrlllllKSEKN 116
|
....*...
gi 1721664488 200 HAILLTTH 207
Cdd:smart00382 117 LTVILTTN 124
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-181 |
2.80e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 5 MPA---TNSATSSASTETVLQVENLRVTYGSFTAVHDVSFSVLGGEIFGLLGPNGAGKTS-----SLSAIEGLlkPAAGN 76
Cdd:PLN03073 159 MPGvyvNHDGNGGGPAIKDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTflrymAMHAIDGI--PKNCQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 77 I----------------AVGGYNLKEKPLHAKANMGIQLQSTSFQSELTVTEIIRLYAAVYGLSLSD--SEIEALLQNIK 138
Cdd:PLN03073 237 IlhveqevvgddttalqCVLNTDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQrlEEIYKRLELID 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 139 LETASS-----------------KRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLD 181
Cdd:PLN03073 317 AYTAEAraasilaglsftpemqvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
26-225 |
3.88e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 46.49 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 26 LRVTY-GSFTAVHDVSFSVLGG-EIFGLLGPNGAGKTSSLSAIEGLL--KPAAGNiavggynlKEKPLHAKANMGIQLQS 101
Cdd:cd03279 6 LELKNfGPFREEQVIDFTGLDNnGLFLICGPTGAGKSTILDAITYALygKTPRYG--------RQENLRSVFAPGEDTAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 102 TSFQSELT--VTEIIRlyaaVYGLSLSDSEIEALLQNIKLETASSKRFGQLSGGQQQRVSLAIA--------TMHKPKL- 170
Cdd:cd03279 78 VSFTFQLGgkKYRVER----SRGLDYDQFTRIVLLPQGEFDRFLARPVSTLSGGETFLASLSLAlalsevlqNRGGARLe 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721664488 171 -VLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAIIDHG 225
Cdd:cd03279 154 aLFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLEVIKTP 209
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
146-210 |
3.95e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.71 E-value: 3.95e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 146 RFGQ----LSGGQQQRVSLA-----IATmhKPKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSME 210
Cdd:COG0178 819 KLGQpattLSGGEAQRVKLAselskRST--GKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLD 890
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-228 |
1.04e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 32 SFTAVHDVSFSVLGGEIFGLLGPNGAGKTSSLSAI----EGLLKPAAGNIAVGGYNLKEKPLHAKANMGIQLQSTSFQSE 107
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 108 LTVTE--------------------------IIRLYAAVYGLSlsdseieallqnIKLETASSKRFGQ-LSGGQQQRVSL 160
Cdd:TIGR00956 153 LTVGEtldfaarcktpqnrpdgvsreeyakhIADVYMATYGLS------------HTRNTKVGNDFVRgVSGGERKRVSI 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 161 AIATMHKPKLVLLDEPTTGLDPQSRrqlWERMESLRNAGHaILLTTHSM------EEAEAVCDRIAIIDHGRII 228
Cdd:TIGR00956 221 AEASLGGAKIQCWDNATRGLDSATA---LEFIRALKTSAN-ILDTTPLVaiyqcsQDAYELFDKVIVLYEGYQI 290
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
38-229 |
1.39e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 38 DVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGGYNLKEKPlhakanmgiqlqSTSFQSELTVTEIIrLY 117
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVP------------QVSWIFNATVRDNI-LF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 118 AAVYGLSLSDSEIE--ALLQNIKL-----ETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWE 190
Cdd:PLN03130 702 GSPFDPERYERAIDvtALQHDLDLlpggdLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD 781
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1721664488 191 R--MESLRNAGHaiLLTTHSMEEAEAVcDRIAIIDHGRIIE 229
Cdd:PLN03130 782 KciKDELRGKTR--VLVTNQLHFLSQV-DRIILVHEGMIKE 819
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
39-239 |
1.74e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.93 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 39 VSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIAVGG-----YNLKEkpLHAKANM---------GIQLQSTSF 104
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGreigaYGLRE--LRRQFSMipqdpvlfdGTVRQNVDP 1406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 105 QSELTVTEIirlYAAVYGLSL-----SDSE-IEALLqnikLETASSkrfgqLSGGQQQRVSLAIATMHK-PKLVLLDEPT 177
Cdd:PTZ00243 1407 FLEASSAEV---WAALELVGLrervaSESEgIDSRV----LEGGSN-----YSVGQRQLMCMARALLKKgSGFILMDEAT 1474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721664488 178 TGLDPQSRRQLWERMESLRNAgHAILLTTHSMEEAeAVCDRIAIIDHGRIIEIDSPQAIVDR 239
Cdd:PTZ00243 1475 ANIDPALDRQIQATVMSAFSA-YTVITIAHRLHTV-AQYDKIIVMDHGAVAEMGSPRELVMN 1534
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
51-181 |
1.87e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 51 LLGPNGAGKTSSLSAIEG--LL---------------------KPAAGN----IAVGgynLKEKPLHAKANMGIQLQSTS 103
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGevLLddgriiyeqdlivarlqqdppRNVEGTvydfVAEG---IEEQAEYLKRYHDISHLVET 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 104 FQSELTVTEIIRLYAAV--YGLSLSDSEIEALLQNIKLEtaSSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLD 181
Cdd:PRK11147 111 DPSEKNLNELAKLQEQLdhHNLWQLENRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
140-190 |
3.50e-05 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 41.45 E-value: 3.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721664488 140 ETASSKRFGQLSGGQQQR-VSLAIA------------TMHKPKLVLLDEPTTGLDPQSRRQLWE 190
Cdd:pfam13558 23 EVETYRRSGGLSGGEKQLlAYLPLAaalaaqygsaegRPPAPRLVFLDEAFAKLDEENIRTALE 86
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
36-227 |
8.02e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 36 VHDVSFSVLGGEIFGLLGPNGAGKTSSLSAIEGLLKPAAGNIavggynLKEKPLHAKANMGIQLQSTSFQSELTVTE--I 113
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV------WAERSIAYVPQQAWIMNATVRGNILFFDEedA 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 114 IRLYAAVyglslSDSEIEALLQNIK--LETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLWER 191
Cdd:PTZ00243 750 ARLADAV-----RVSQLEADLAQLGggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEE 824
|
170 180 190
....*....|....*....|....*....|....*.
gi 1721664488 192 MESLRNAGHAILLTTHSMeEAEAVCDRIAIIDHGRI 227
Cdd:PTZ00243 825 CFLGALAGKTRVLATHQV-HVVPRADYVVALGDGRV 859
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
21-196 |
2.62e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 21 LQVENLRvtygSFTAVHDVSFSvlgGEIFGLLGPNGAGKTSSLSAIEGLL----------------KPAAG-----NIAV 79
Cdd:COG0419 5 LRLENFR----SYRDTETIDFD---DGLNLIVGPNGAGKSTILEAIRYALygkarsrsklrsdlinVGSEEasvelEFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 80 GGYNLKEKPLHAKANMGIQLQSTSFQS---ELTVTEIIRLYAAVYGlSLSDSEIEALLQNIKLETASSKRF--------- 147
Cdd:COG0419 78 GGKRYRIERRQGEFAEFLEAKPSERKEalkRLLGLEIYEELKERLK-ELEEALESALEELAELQKLKQEILaqlsgldpi 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721664488 148 GQLSGGQQQRvsLAIATMHKpklVLLDepTTGLDPQSRRQLWERMESLR 196
Cdd:COG0419 157 ETLSGGERLR--LALADLLS---LILD--FGSLDEERLERLLDALEELA 198
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
46-207 |
3.81e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 46 GEIFGLLGPNGAGKTSSLSAIEGLlKPAA---GNIAVGGYNLKEKPLhAKANmGIQLQSTSFQSELTVTEIIrLYAAVYG 122
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGR-KTGGyieGDIRISGFPKKQETF-ARIS-GYCEQNDIHSPQVTVRESL-IYSAFLR 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 123 LSLSDSEIEAL-----------LQNIKLETASSKRFGQLSGGQQQRVSLAIATMHKPKLVLLDEPTTGLDPQSRRQLwer 191
Cdd:PLN03140 982 LPKEVSKEEKMmfvdevmelveLDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV--- 1058
|
170
....*....|....*....
gi 1721664488 192 MESLRN---AGHAILLTTH 207
Cdd:PLN03140 1059 MRTVRNtvdTGRTVVCTIH 1077
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
146-210 |
3.84e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 3.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721664488 146 RFGQ----LSGGQQQRVSLAiATMHKPK----LVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSME 210
Cdd:PRK00349 823 KLGQpattLSGGEAQRVKLA-KELSKRStgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLD 894
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
168-207 |
2.13e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 2.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1721664488 168 PKLVLLDEPTTGLDPQSRRQLWERMESLRNAGHAILLTTH 207
Cdd:PRK00635 1721 PTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDH 1760
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
103-221 |
5.73e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 38.03 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721664488 103 SFQSELTVTEIIRL-------YAAVYGLSLSDSEIEALLQNIKLETASSKR--FGQLSGGQQQRVSLAIA--------TM 165
Cdd:TIGR00618 895 KFLHEITLYANVRLanqsegrFHGRYADSHVNARKYQGLALLVADAYTGSVrpSATLSGGETFLASLSLAlaladllsTS 974
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721664488 166 HKPKLVLL--DEPTTGLDPQSRRQLWERMESLRNAGHAILLTTHSMEEAEAVCDRIAI 221
Cdd:TIGR00618 975 GGTVLDSLfiDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPHRILV 1032
|
|
| |
