|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-239 |
1.05e-72 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 221.89 E-value: 1.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 17 AAADVLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG------SVRIGYVP 89
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLpPTSGTVRLFGkpprraRRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 90 QNFVV-TDVPITVRDF--LGFKSGAGF------------EESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNV 154
Cdd:COG1121 82 QRAEVdWDFPITVRDVvlMGRYGRRGLfrrpsradreavDEALERVGL-EDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 155 LLFDEPTATVDIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLALNRTVRFFGASSRFSEPELLMEIFGSGA 234
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSRAYGGPV 239
|
....*
gi 1670356525 235 GLVEH 239
Cdd:COG1121 240 ALLAH 244
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
23-215 |
3.32e-63 |
|
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: 196.60 E-value: 3.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 23 RVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG------SVRIGYVPQNFVV- 94
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkPTSGSIRVFGkplekeRKRIGYVPQRRSId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 95 TDVPITVRDF--LGFKSGAGF------------EESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:cd03235 81 RDFPISVRDVvlMGLYGHKGLfrrlskadkakvDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 161 TATVDIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLALNRTVRFFG 215
Cdd:cd03235 160 FAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
21-242 |
9.12e-48 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 158.28 E-value: 9.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG-----------SVRIGYV 88
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLkPSSGEVLLDGrdlaslsrrelARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 89 PQNFVVTDvPITVRDF--LGFKSGAGF------------EESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNV 154
Cdd:COG1120 81 PQEPPAPF-GLTVRELvaLGRYPHLGLfgrpsaedreavEEALERTGL-EHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 155 LLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR-TVRFFGASSRFSEPELLMEIFGSG 233
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDgRIVAQGPPEEVLTPELLEEVYGVE 238
|
....*....
gi 1670356525 234 AGLVEHKHD 242
Cdd:COG1120 239 ARVIEDPVT 247
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-242 |
5.96e-46 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 153.73 E-value: 5.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 20 DVLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSVRIGYVPQNFVV-TDV 97
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVaPDEGVIKRNGKLRIGYVPQKLYLdTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 PITVRDFLGFKSGAGFEESLAAVGLGSA--VLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYES 175
Cdd:PRK09544 83 PLTVNRFLRLRPGTKKEDILPALKRVQAghLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1670356525 176 LNRLEKETNITVFLITHDLHIVSQYSDAVLALNRTVRFFGASSRFSEPELLMEIFGS-GA---GLVEHKHD 242
Cdd:PRK09544 163 IDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPEVVSLHPEFISMFGPrGAeqlGIYRHHHN 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
23-208 |
2.80e-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: 2.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 23 RVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTV--------EWSGSVR---IGYVPQ 90
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLkPSSGEIlldgkdlaSLSPKELarkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 91 nfvvtdvpitvrdflgfksgagfeeSLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSED 170
Cdd:cd03214 81 -------------------------ALELLGL-AHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 1670356525 171 MLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALN 208
Cdd:cd03214 135 ELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLK 172
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
22-208 |
1.33e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.80 E-value: 1.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV-----------RIGYVP 89
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDpPTSGEIYLDGKPlsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 90 QNFVVtdVPITVRDFLGF--------KSGAGFEESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPT 161
Cdd:COG4619 81 QEPAL--WGGTVRDNLPFpfqlrerkFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1670356525 162 ATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALN 208
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLE 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
22-209 |
9.03e-40 |
|
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: 135.22 E-value: 9.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV----------RIGYVPQ 90
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDSGEIKVLGKDikkepeevkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 91 NFVVTDVpITVRDFLgfksgagfeeslaavglgsavlpkrldVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSED 170
Cdd:cd03230 81 EPSLYEN-LTVRENL---------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190
....*....|....*....|....*....|....*....
gi 1670356525 171 MLYESLNRLEKEtNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:cd03230 133 EFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNN 170
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
22-209 |
1.12e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 137.12 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG-SV---------RIGYVPQ 90
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPTSGEVRVLGeDVardpaevrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 91 NFVVtDVPITVRDFLGFKSG----------AGFEESLAAVGLGSAvLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:COG1131 81 EPAL-YPDLTVRENLRFFARlyglprkearERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1670356525 161 TATVDIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:COG1131 159 TSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDK 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
32-228 |
5.38e-39 |
|
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: 135.15 E-value: 5.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSV-----------RIGYVPQN----FVVT 95
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTsGEVLVDGKDitkknlrelrrKVGLVFQNpddqLFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 96 dvpiTVRDFLGFksgaGFE--------------ESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAwAVLD-RPNVLLFDEP 160
Cdd:COG1122 92 ----TVEEDVAF----GPEnlglpreeirerveEALELVGL-EHLADRPPHELSGGQKQRVAIA-GVLAmEPEVLVLDEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 161 TATVDIGSEDMLYESLNRLEKEtNITVFLITHDLHIVSQYSDAVLALNR-TVRFFGASSR-FSEPELLME 228
Cdd:COG1122 162 TAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDgRIVADGTPREvFSDYELLEE 230
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-207 |
5.54e-39 |
|
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: 135.70 E-value: 5.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVR----LDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSV-----------RI 85
Cdd:COG1124 2 LEVRNLSVSygqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWsGEVTFDGRPvtrrrrkafrrRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 86 GYVPQNfvvtdvPI-------TVRDFLG--------FKSGAGFEESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLD 150
Cdd:COG1124 82 QMVFQD------PYaslhprhTVDRILAeplrihglPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1670356525 151 RPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLAL 207
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
35-209 |
1.72e-38 |
|
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: 133.36 E-value: 1.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG-----------SVRIGYVPQN----FVVTdvp 98
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLgPTSGEVLVDGkdltklslkelRRKVGLVFQNpddqFFGP--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 iTVRDFLGFksgaGFE--------------ESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATV 164
Cdd:cd03225 92 -TVEEEVAF----GLEnlglpeeeieerveEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1670356525 165 DIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:cd03225 166 DPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-209 |
4.80e-38 |
|
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: 138.88 E-value: 4.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 19 ADVLRVAHLGVRLDH--APILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVewSGSV------------- 83
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI--SGEVlldgrdllelsea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 ----RIGYVPQNFVVTDVPITVRDFLGFKSGAGF----------EESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVL 149
Cdd:COG1123 80 lrgrRIGMVFQDPMTQLNPVTVGDQIAEALENLGlsraeararvLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 150 DRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDD 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
32-199 |
7.07e-38 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 130.20 E-value: 7.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG---------SVR--IGYVPQN-FVVTDvp 98
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGvdlrdldleSLRknIAYVPQDpFLFSG-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 iTVRDflgfksgagfeeslaavglgsavlpkrlDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNR 178
Cdd:cd03228 91 -TIRE----------------------------NILSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRA 141
|
170 180
....*....|....*....|.
gi 1670356525 179 LEKETniTVFLITHDLHIVSQ 199
Cdd:cd03228 142 LAKGK--TVIVIAHRLSTIRD 160
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-209 |
2.56e-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: 137.58 E-value: 2.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 3 AAPPPSRSPTREAGAAADV-LRVAHLGVRL-DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEW 79
Cdd:COG4988 317 APEPAAPAGTAPLPAAGPPsIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPYSGSILI 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 80 SG-----------SVRIGYVPQNFVVtdVPITVRDFLGFK----SGAGFEESLAAVGLGSAV--LPKRLDV--------L 134
Cdd:COG4988 397 NGvdlsdldpaswRRQIAWVPQNPYL--FAGTIRENLRLGrpdaSDEELEAALEAAGLDEFVaaLPDGLDTplgeggrgL 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 135 SGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETniTVFLITHDLHIVSQYsDAVLALNR 209
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQA-DRILVLDD 546
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-209 |
7.23e-37 |
|
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: 135.80 E-value: 7.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 6 PPSRSPTREAGAAADVLRVAHLGVR-----LDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEW 79
Cdd:COG1123 245 AARGRAAPAAAAAEPLLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLrPTSGSILF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 80 SGSV--------------RIGYVPQNfvvtdvP-------ITVRD-------FLGFKSGAGFE----ESLAAVGLGSAVL 127
Cdd:COG1123 325 DGKDltklsrrslrelrrRVQMVFQD------PysslnprMTVGDiiaeplrLHGLLSRAERRervaELLERVGLPPDLA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 128 PKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLAL 207
Cdd:COG1123 399 DRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVM 478
|
..
gi 1670356525 208 NR 209
Cdd:COG1123 479 YD 480
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
21-205 |
1.94e-36 |
|
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: 128.39 E-value: 1.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLD----HAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV------------ 83
Cdd:cd03257 1 LLEVKNLSVSFPtgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDGKDllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 --RIGYVPQNfvvtdvPI-------TVRD-------FLGFKSGAGFE-----ESLAAVGLGSAVLPKRLDVLSGGEMQRV 142
Cdd:cd03257 81 rkEIQMVFQD------PMsslnprmTIGEqiaeplrIHGKLSKKEARkeavlLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1670356525 143 LIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVL 205
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-214 |
2.12e-36 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 134.42 E-value: 2.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 5 PPPSRSPTreagaaaDVLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGSV 83
Cdd:COG0488 306 PPPERLGK-------KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGeLEPDSGTVKLGETV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 RIGYVPQNFVVTDVPITVRDFLGFKSGAGFEESLAAVgLGS------AVLpKRLDVLSGGEMQRVLIAWAVLDRPNVLLF 157
Cdd:COG0488 379 KIGYFDQHQEELDPDKTVLDELRDGAPGGTEQEVRGY-LGRflfsgdDAF-KPVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1670356525 158 DEPTATVDIGSEDMLYESLNRLEKetniTVFLITHDLHIVSQYSDAVLAL-NRTVRFF 214
Cdd:COG0488 457 DEPTNHLDIETLEALEEALDDFPG----TVLLVSHDRYFLDRVATRILEFeDGGVREY 510
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
21-234 |
1.12e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 127.10 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRL-DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSV--------------R 84
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTsGEILVDGQDvtalrgralrrlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 85 IGYVPQNF-------VVTDVPI-------TVRDFLGF-----KSGAgfEESLAAVGLGSAVLpKRLDVLSGGEMQRVLIA 145
Cdd:COG3638 82 IGMIFQQFnlvprlsVLTNVLAgrlgrtsTWRSLLGLfppedRERA--LEALERVGLADKAY-QRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 146 WAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR-TVRFFGASSRFSEpE 224
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDgRVVFDGPPAELTD-A 237
|
250
....*....|
gi 1670356525 225 LLMEIFGSGA 234
Cdd:COG3638 238 VLREIYGGEA 247
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
23-209 |
1.18e-34 |
|
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: 121.58 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 23 RVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV-----------RIGYVPQ 90
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLkPTSGEILIDGKDiaklpleelrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 91 nfvvtdvpitvrdflgfksgagfeeslaavglgsavlpkrldvLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSED 170
Cdd:cd00267 81 -------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190
....*....|....*....|....*....|....*....
gi 1670356525 171 MLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:cd00267 118 RLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
21-237 |
1.28e-34 |
|
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: 124.20 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSG--------SVR--IGYVP 89
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGlLKPDSGSILIDGedvrkeprEARrqIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 90 QNFVVTDVpITVRDFLGF----------KSGAGFEESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDE 159
Cdd:COG4555 81 DERGLYDR-LTVRENIRYfaelyglfdeELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 160 PTATVDIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLALNR-TVRFFGASSRFSE-------PELLMEIFG 231
Cdd:COG4555 159 PTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKgKVVAQGSLDELREeigeenlEDAFVALIG 237
|
....*.
gi 1670356525 232 SGAGLV 237
Cdd:COG4555 238 SEEGEA 243
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
32-199 |
2.46e-34 |
|
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: 129.95 E-value: 2.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSG---------SVR--IGYVPQnfvvtDVPI 99
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLyEPTSGRILIDGidlrqidpaSLRrqIGVVLQ-----DVFL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 ---TVRD-FLGFKSGAGFEESLAA---VGLGSAV--LPKRLD--------VLSGGEMQRVLIAWAVLDRPNVLLFDEPTA 162
Cdd:COG2274 561 fsgTIREnITLGDPDATDEEIIEAarlAGLHDFIeaLPMGYDtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
170 180 190
....*....|....*....|....*....|....*..
gi 1670356525 163 TVDIGSEDMLYESLNRLEKetNITVFLITHDLHIVSQ 199
Cdd:COG2274 641 ALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL 675
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-231 |
4.27e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 123.30 E-value: 4.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSG-----------SVRIGYVP 89
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVRLNGrplaawspwelARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 90 Q----NFvvtdvPITVRDF--LG----FKSGAGF----EESLAAVGLGSavLPKRL-DVLSGGEMQRVLIA------W-A 147
Cdd:COG4559 82 QhsslAF-----PFTVEEVvaLGraphGSSAAQDrqivREALALVGLAH--LAGRSyQTLSGGEQQRVQLArvlaqlWeP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 148 VLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKEtNITVFLITHDLHIVSQYSDAVLALNR-TVRFFGASSRFSEPELL 226
Cdd:COG4559 155 VDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQgRLVAQGTPEEVLTDELL 233
|
....*
gi 1670356525 227 MEIFG 231
Cdd:COG4559 234 ERVYG 238
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
22-225 |
1.50e-33 |
|
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: 121.14 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHA-PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG------------SVR--I 85
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVePTSGSVLIDGtdinklkgkalrQLRrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 86 GYVPQNF-------VVTDVPI-------TVRDFLGFKSGAGFEESLAA---VGLGSAVLpKRLDVLSGGEMQRVLIAWAV 148
Cdd:cd03256 81 GMIFQQFnlierlsVLENVLSgrlgrrsTWRSLFGLFPKEEKQRALAAlerVGLLDKAY-QRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1670356525 149 LDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALN--RTVrFFGASSRFSEPEL 225
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKdgRIV-FDGPPAELTDEVL 237
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
30-205 |
2.66e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 119.26 E-value: 2.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 30 RLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSVRIGYVPQNFVVTDV-PITVRDF--- 104
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTsGTVRRAGGARVAYVPQRSEVPDSlPLTVRDLvam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 105 -----------LGFKSGAGFEESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLY 173
Cdd:NF040873 81 grwarrglwrrLTRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180 190
....*....|....*....|....*....|..
gi 1670356525 174 ESLNRlEKETNITVFLITHDLHIVSQYSDAVL 205
Cdd:NF040873 160 ALLAE-EHARGATVVVVTHDLELVRRADPCVL 190
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
22-209 |
6.48e-33 |
|
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: 116.78 E-value: 6.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGSVRIGYVPQnfvvtdvpit 100
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGeLEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 101 vrdflgfksgagfeeslaavglgsavlpkrldvLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLnrle 180
Cdd:cd03221 71 ---------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL---- 113
|
170 180
....*....|....*....|....*....
gi 1670356525 181 KETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:cd03221 114 KEYPGTVILVSHDRYFLDQVATKIIELED 142
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
36-208 |
9.11e-33 |
|
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: 118.13 E-value: 9.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSVR--------IGYVPQNfvvtdvpitVRDFLG 106
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNGKPIkakerrksIGYVMQD---------VDYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 107 FKS-----GAGFEESLAAVGLGSAVLpKRLDV----------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDM 171
Cdd:cd03226 86 TDSvreelLLGLKELDAGNEQAETVL-KDLDLyalkerhplsLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1670356525 172 LYESLNRLEKETNiTVFLITHDLHIVSQYSDAVLALN 208
Cdd:cd03226 165 VGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLA 200
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
22-208 |
1.24e-32 |
|
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: 116.90 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV-------------RIGY 87
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEePDSGSILIDGEDltdledelpplrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 88 VPQNFVVtdVP-ITVRDFLGFksgagfeeslaavglgsavlpkrldVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDI 166
Cdd:cd03229 81 VFQDFAL--FPhLTVLENIAL-------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1670356525 167 GSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALN 208
Cdd:cd03229 134 ITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-238 |
4.99e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.19 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHA--PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV-----------RIG 86
Cdd:PRK13635 5 IIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlPEAGTITVGGMVlseetvwdvrrQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 87 YVPQN----FVVTdvpiTVRDFLGFksgaGFE--------------ESLAAVGLGSAVL--PKRldvLSGGEMQRVLIAW 146
Cdd:PRK13635 85 MVFQNpdnqFVGA----TVQDDVAF----GLEnigvpreemvervdQALRQVGMEDFLNrePHR---LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 147 AVLDRPNVLLFDEPTATVD-IGSEDMLyESLNRLEKETNITVFLITHDLHIVSQySDAVLALNRtvrffgaSSRFSE--P 223
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDpRGRREVL-ETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNK-------GEILEEgtP 224
|
250
....*....|....*
gi 1670356525 224 EllmEIFGSGAGLVE 238
Cdd:PRK13635 225 E---EIFKSGHMLQE 236
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
37-162 |
8.09e-32 |
|
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: 114.28 E-value: 8.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSG-----------SVRIGYVPQNfvVTDVP-ITVRD 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTeGTILLDGqdltdderkslRKEIGYVFQD--PQLFPrLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1670356525 104 FLGF----------KSGAGFEESLAAVGLGSA---VLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTA 162
Cdd:pfam00005 79 NLRLglllkglskrEKDARAEEALEKLGLGDLadrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1-209 |
1.00e-31 |
|
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: 122.18 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 1 MVAAPPPSRSPTREAGAAADV-LRVAHLGVRLDHA--PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGT 76
Cdd:COG4987 312 LLDAPPAVTEPAEPAPAPGGPsLELEDVSFRYPGAgrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLdPQSGS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 77 VEWSG---------SVR--IGYVPQnfvvtDVPI---TVRDFLGF-KSGAGFEE---SLAAVGLGSAV--LPKRLDV--- 133
Cdd:COG4987 392 ITLGGvdlrdldedDLRrrIAVVPQ-----RPHLfdtTLRENLRLaRPDATDEElwaALERVGLGDWLaaLPDGLDTwlg 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 134 -----LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETniTVFLITHDLHIVSQYsDAVLALN 208
Cdd:COG4987 467 eggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERM-DRILVLE 543
|
.
gi 1670356525 209 R 209
Cdd:COG4987 544 D 544
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
35-195 |
1.17e-31 |
|
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: 115.65 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSG------SVRIGYVPQNFVVtdVP-ITVRD--F 104
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTsGEVLVDGepvtgpGPDRGYVFQQDAL--LPwLTVLDnvA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 105 LGFK-SGAGFEES-------LAAVGLGSAV--LPKRLdvlSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYE 174
Cdd:cd03293 96 LGLElQGVPKAEAreraeelLELVGLSGFEnaYPHQL---SGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQE 172
|
170 180
....*....|....*....|.
gi 1670356525 175 SLNRLEKETNITVFLITHDLH 195
Cdd:cd03293 173 ELLDIWRETGKTVLLVTHDID 193
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
17-194 |
2.93e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 115.96 E-value: 2.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 17 AAADVLRVAHLGVRLDHA----PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSV------RI 85
Cdd:COG1116 3 AAAPALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTsGEVLVDGKPvtgpgpDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 86 GYVPQNFVVtdVP-ITVRD--FLGFKsGAGF---------EESLAAVGLGSAV--LPKRldvLSGGEMQRVLIAWAVLDR 151
Cdd:COG1116 83 GVVFQEPAL--LPwLTVLDnvALGLE-LRGVpkaerreraRELLELVGLAGFEdaYPHQ---LSGGMRQRVAIARALAND 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1670356525 152 PNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDL 194
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDV 199
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
22-209 |
7.00e-31 |
|
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: 113.38 E-value: 7.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV---------RIGYVPQN 91
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLErPDSGEILIDGRDvtgvpperrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 92 FVVtdVP-ITVRDFLGF-----KSGAG-----FEESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:cd03259 81 YAL--FPhLTVAENIAFglklrGVPKAeirarVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1670356525 161 TATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE 206
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
32-229 |
7.56e-31 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 114.83 E-value: 7.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSG----------SVR--IGYVPQN----FVV 94
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLlLPTSGKVTVDGldtldeenlwEIRkkVGMVFQNpdnqFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 95 TdvpiTVRDFLGFksgaGFE--------------ESLAAVGLGSAVL--PKRLdvlSGGEMQRVLIAWAVLDRPNVLLFD 158
Cdd:TIGR04520 93 A----TVEDDVAF----GLEnlgvpreemrkrvdEALKLVGMEDFRDrePHLL---SGGQKQRVAIAGVLAMRPDIIILD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1670356525 159 EPTATVD-IGSEDMLyESLNRLEKETNITVFLITHDLHIVSQySDAVLALNR-TVRFFGASSR-FSEPELLMEI 229
Cdd:TIGR04520 162 EATSMLDpKGRKEVL-ETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKgKIVAEGTPREiFSQVELLKEI 233
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
21-231 |
1.04e-30 |
|
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: 113.93 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRL--DHApILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG------------SVR- 84
Cdd:TIGR02315 1 MLEVENLSKVYpnGKQ-ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVePSSGSILLEGtditklrgkklrKLRr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 85 -IGYVPQNF-------VVTDVPI-------TVRDFLGFKSGAGFEESLAA---VGLGSAVLpKRLDVLSGGEMQRVLIAW 146
Cdd:TIGR02315 80 rIGMIFQHYnlierltVLENVLHgrlgykpTWRSLLGRFSEEDKERALSAlerVGLADKAY-QRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 147 AVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR-TVRFFGASSRFSEpEL 225
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAgEIVFDGAPSELDD-EV 237
|
....*.
gi 1670356525 226 LMEIFG 231
Cdd:TIGR02315 238 LRHIYG 243
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
21-193 |
2.56e-30 |
|
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: 111.80 E-value: 2.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV----------RIGYV- 88
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLpPSAGEVLWNGEPirdaredyrrRLAYLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 89 PQNFVVTDvpITVRDFLGF--------KSGAGFEESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:COG4133 82 HADGLKPE--LTVRENLRFwaalyglrADREAIDEALEAVGLA-GLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|...
gi 1670356525 161 TATVDIGSEDMLYESLNRlEKETNITVFLITHD 193
Cdd:COG4133 159 FTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-193 |
3.74e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.09 E-value: 3.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 24 VAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGSVRIGYVPQNfVVTDVPITVR 102
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGeLEPDSGEVSIPKGLRIGYLPQE-PPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 103 DFL--GFKSGAGFEESLAAV----------------------------------------GLGSAVLPKRLDVLSGGEMQ 140
Cdd:COG0488 80 DTVldGDAELRALEAELEELeaklaepdedlerlaelqeefealggweaearaeeilsglGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 141 RVLIAWAVLDRPNVLLFDEPTATVDIgsedmlyESLNRLE---KETNITVFLITHD 193
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDL-------ESIEWLEeflKNYPGTVLVVSHD 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-197 |
5.94e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 117.19 E-value: 5.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 11 PTREAGAAADVLRVAHLGVRLDH--------APILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSG 81
Cdd:COG1132 322 PEIPDPPGAVPLPPVRGEIEFENvsfsypgdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTsGRILIDG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 82 ---------SVR--IGYVPQNFVVTDvpITVRDFLGF-KSGAGFEE---SLAAVGLGSAV--LPKRLD--------VLSG 136
Cdd:COG1132 402 vdirdltleSLRrqIGVVPQDTFLFS--GTIRENIRYgRPDATDEEveeAAKAAQAHEFIeaLPDGYDtvvgergvNLSG 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1670356525 137 GEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETniTVFLITHDLHIV 197
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTI 538
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-209 |
6.70e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 112.17 E-value: 6.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVE--------WSG---SVRIGYV 88
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEVRlngrpladWSPaelARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 89 PQNFVVTdVPITVRDFLGF----------KSGAGFEESLAAVGLgsAVLPKRL-DVLSGGEMQRVLIA------WAVLDR 151
Cdd:PRK13548 82 PQHSSLS-FPFTVEEVVAMgraphglsraEDDALVAAALAQVDL--AHLAGRDyPQLSGGEQQRVQLArvlaqlWEPDGP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1670356525 152 PNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
35-207 |
1.55e-29 |
|
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: 110.27 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGSV---------------RIGYVPQNFVVtdVP 98
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVRVDGTDisklsekelaafrrrHIGFVFQSFNL--LP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 -ITVRD-------FLGFKSG---AGFEESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIG 167
Cdd:cd03255 96 dLTALEnvelpllLAGVPKKerrERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1670356525 168 SEDMLYESLNRLEKETNITVFLITHDLHIVSqYSDAVLAL 207
Cdd:cd03255 175 TGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIEL 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
35-207 |
2.62e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 109.75 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGSV---------------RIGYVPQNFVVtdVP 98
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVLIDGQDisslserelarlrrrHIGFVFQFFNL--LP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 -ITVRD-------FLGFKSGAG---FEESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIG 167
Cdd:COG1136 100 eLTALEnvalpllLAGVSRKERrerARELLERVGLG-DRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1670356525 168 SEDMLYESLNRLEKETNITVFLITHDLHIVSqYSDAVLAL 207
Cdd:COG1136 179 TGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRL 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
17-196 |
8.75e-29 |
|
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: 108.68 E-value: 8.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 17 AAADVLRVAHLGVRLDHA----PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSG---------- 81
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPTSGTVRLAGqdlfaldeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 82 -----SVRIGYVPQNF-----------VVtdVPITVRDFLGFKSGAgfEESLAAVGLGsavlpKRLD----VLSGGEMQR 141
Cdd:COG4181 84 rarlrARHVGFVFQSFqllptltalenVM--LPLELAGRRDARARA--RALLERVGLG-----HRLDhypaQLSGGEQQR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1670356525 142 VLIAWAVLDRPNVLLFDEPTATVD------IgsEDMLYEsLNRlekETNITVFLITHDLHI 196
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDaatgeqI--IDLLFE-LNR---ERGTTLVLVTHDPAL 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-209 |
1.66e-28 |
|
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: 106.15 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHA--PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGS-----------VRIGY 87
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLlRPTSGRVRLDGAdisqwdpnelgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 88 VPQNfvvtdvpitvrDFLgfksgagFEESLAAvglgsavlpkrlDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIG 167
Cdd:cd03246 81 LPQD-----------DEL-------FSGSIAE------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1670356525 168 SEDMLYESLNRLeKETNITVFLITHDLHIVSQySDAVLALNR 209
Cdd:cd03246 131 GERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLED 170
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
22-215 |
2.29e-28 |
|
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: 107.59 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGS--------------VRIG 86
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLrPDSGEVLIDGEdisglseaelyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 87 YVPQN---FvvTDvpITVRDFLGF---KSGAGFEES--------LAAVGLGSAVLpKRLDVLSGGEMQRVLIAWAVLDRP 152
Cdd:cd03261 81 MLFQSgalF--DS--LTVFENVAFplrEHTRLSEEEireivlekLEAVGLRGAED-LYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 153 NVLLFDEPTATVD-IGSeDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLAL-NRTVRFFG 215
Cdd:cd03261 156 ELLLYDEPTAGLDpIAS-GVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLyDGKIVAEG 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-222 |
5.72e-28 |
|
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: 106.36 E-value: 5.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGS----------VR--IGYV 88
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSIRFDGRditglppherARagIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 89 PQN---FvvtdVPITVRDFL----GFKSGAGFEESLAAVglgSAVLPK---RLD----VLSGGEMQRVLIAWAVLDRPNV 154
Cdd:cd03224 81 PEGrriF----PELTVEENLllgaYARRRAKRKARLERV---YELFPRlkeRRKqlagTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1670356525 155 LLFDEPTATVDIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLALNR-TVRFFGASSRFSE 222
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERgRVVLEGTAAELLA 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-197 |
7.65e-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: 110.84 E-value: 7.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 3 AAPPPSRSPTREAGAA-ADVLRVAHLGVRL-DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTV-- 77
Cdd:TIGR02857 302 DAAPRPLAGKAPVTAApASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVdPTEGSIav 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 78 ------EWSGSV---RIGYVPQNFVVtdVPITVRDFLGF----KSGAGFEESLAAVGLGSAV--LPKRLDV--------L 134
Cdd:TIGR02857 382 ngvplaDADADSwrdQIAWVPQHPFL--FAGTIAENIRLarpdASDAEIREALERAGLDEFVaaLPQGLDTpigeggagL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1670356525 135 SGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKetNITVFLITHDLHIV 197
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA 520
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
37-209 |
9.25e-28 |
|
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: 105.53 E-value: 9.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVEW---------SGSVR--IGYVPQNFVVtDVPITVRDFL 105
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvaghdvvrePREVRrrIGIVFQDLSV-DDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 106 ----------GFKSGAGFEESLAAVGLGSAVlPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYES 175
Cdd:cd03265 95 yiharlygvpGAERRERIDELLDFVGLLEAA-DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY 173
|
170 180 190
....*....|....*....|....*....|....
gi 1670356525 176 LNRLEKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:cd03265 174 IEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDH 207
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
32-208 |
1.06e-27 |
|
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: 105.78 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG---------SVR--IGYVPQNFVVTDVpi 99
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYdVSSGSILIDGqdirevtldSLRraIGVVPQDTVLFND-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 TVRDFLGF-KSGAGFEESLAAVGLG-------------SAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVD 165
Cdd:cd03253 90 TIGYNIRYgRPDATDEEVIEAAKAAqihdkimrfpdgyDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1670356525 166 IGSEDMLYESLNRLEKetNITVFLITHDLHIVSQySDAVLALN 208
Cdd:cd03253 170 THTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLK 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-205 |
1.17e-27 |
|
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: 107.83 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLD----HAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVewSGSV------------- 83
Cdd:COG0444 1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGIT--SGEIlfdgedllklsek 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 --------RIGYVPQNfvvtdvP-------ITVRDFL-------GFKSGAGFE----ESLAAVGLGSAvlPKRLDV---- 133
Cdd:COG0444 79 elrkirgrEIQMIFQD------PmtslnpvMTVGDQIaeplrihGGLSKAEAReraiELLERVGLPDP--ERRLDRyphe 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1670356525 134 LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVL 205
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
22-209 |
1.30e-27 |
|
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: 105.06 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGS-------VRIGYVP---- 89
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIlPDSGEVLFDGKpldiaarNRIGYLPeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 90 --QNFVVTDVPITVRDFLGFKSGAGFEES---LAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATV 164
Cdd:cd03269 81 lyPKMKVIDQLVYLAQLKGLKKEEARRRIdewLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1670356525 165 DIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:cd03269 160 DPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
21-215 |
1.48e-27 |
|
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: 105.45 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV--------------RI 85
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLrPDSGEILVDGQDitglsekelyelrrRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 86 GYVPQN---FvvTDvpITVRDFLGF----KSGAGFEE-------SLAAVGLGSAV--LPKRLdvlSGGeMQ-RVLIAWAV 148
Cdd:COG1127 85 GMLFQGgalF--DS--LTVFENVAFplreHTDLSEAEirelvleKLELVGLPGAAdkMPSEL---SGG-MRkRVALARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1670356525 149 LDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSD--AVLAlNRTVRFFG 215
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADrvAVLA-DGKIIAEG 224
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
22-198 |
1.87e-27 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 109.60 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGSVRIGYVPQN----FvvtD 96
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGeLEPDSGTVKWSENANIGYYAQDhaydF---E 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 97 VPITVRDFLG-FKSGAGFEESLAAVgLGSAV-----LPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSed 170
Cdd:PRK15064 397 NDLTLFDWMSqWRQEGDDEQAVRGT-LGRLLfsqddIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES-- 473
|
170 180
....*....|....*....|....*....
gi 1670356525 171 mlYESLNR-LEKETNiTVFLITHDLHIVS 198
Cdd:PRK15064 474 --IESLNMaLEKYEG-TLIFVSHDREFVS 499
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-210 |
2.32e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.90 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 1 MVAAPPPSRSPTREAGAAADVLRVAHLGVRL-DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPH-TGTVE 78
Cdd:COG4178 342 LEAADALPEAASRIETSEDGALALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYgSGRIA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 79 WSGSVRIGYVPQN---FVVT--DV---PITVRDFlgfkSGAGFEESLAAVGLGSavLPKRLD-------VLSGGEMQRVL 143
Cdd:COG4178 422 RPAGARVLFLPQRpylPLGTlrEAllyPATAEAF----SDAELREALEAVGLGH--LAERLDeeadwdqVLSLGEQQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1670356525 144 IAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETniTVFLITHDlHIVSQYSDAVLALNRT 210
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT--TVISVGHR-STLAAFHDRVLELTGD 559
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
22-213 |
1.26e-26 |
|
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: 102.64 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL------VPHTGTVEWSGSV------------ 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipgAPDEGEVLLDGKDiydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 -RIGYVPQNfvVTDVPITVRDFL-------GFKSGAGF----EESLAAVGLGSAVLpKRLDV--LSGGEMQRVLIAWAVL 149
Cdd:cd03260 81 rRVGMVFQK--PNPFPGSIYDNVayglrlhGIKLKEELdervEEALRKAALWDEVK-DRLHAlgLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 150 DRPNVLLFDEPTATVDIGSEDMLYESLNRLEKEtnITVFLITHDLHIVSQYSD--AVLALNRTVRF 213
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADrtAFLLNGRLVEF 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
44-205 |
1.90e-26 |
|
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: 107.18 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 44 VRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEwsGSVRIGYVPQnFVVTDVPITVRDFLGFKSGAGFEESLA---- 118
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGvLKPDEGEVD--EDLKISYKPQ-YISPDYDGTVEEFLRSANTDDFGSSYYktei 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 119 AVGLG-SAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIV 197
Cdd:COG1245 440 IKPLGlEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLI 519
|
....*...
gi 1670356525 198 SQYSDAVL 205
Cdd:COG1245 520 DYISDRLM 527
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
22-215 |
2.14e-26 |
|
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: 101.89 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTlAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGS----------VRIGYVPQ 90
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSsGTIRIDGQdvlkqpqklrRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 91 NFVVTDvPITVRDFLGF----------KSGAGFEESLAAVGLGSaVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:cd03264 80 EFGVYP-NFTVREFLDYiawlkgipskEVKARVDEVLELVNLGD-RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 161 TATVDIGSEDMLYESLNRLEKETniTVFLITHDLHIVSQYSDAVLALNR-TVRFFG 215
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKgKLVFEG 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
35-209 |
7.72e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.51 E-value: 7.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSG-SV-------------RIGYVPQNF------- 92
Cdd:COG2884 16 EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPTSGQVLVNGqDLsrlkrreipylrrRIGVVFQDFrllpdrt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 93 ---------VVTDVPitvRDFLGFKSgagfEESLAAVGLGS--AVLPkrlDVLSGGEMQRVLIAWAVLDRPNVLLFDEPT 161
Cdd:COG2884 96 vyenvalplRVTGKS---RKEIRRRV----REVLDLVGLSDkaKALP---HELSGGEQQRVAIARALVNRPELLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1670356525 162 ATVDigsEDM------LYESLNRLeketNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:COG2884 166 GNLD---PETsweimeLLEEINRR----GTTVLIATHDLELVDRMPKRVLELED 212
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
33-209 |
1.73e-25 |
|
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: 99.63 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 33 HAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGSV--------------RIGYVPQNFVVTD- 96
Cdd:TIGR02673 14 GVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGaLTPSRGQVRIAGEDvnrlrgrqlpllrrRIGVVFQDFRLLPd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 97 --------VPITVRDFLGFKSGAGFEESLAAVGLGSA--VLPkrlDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDi 166
Cdd:TIGR02673 94 rtvyenvaLPLEVRGKKEREIQRRVGAALRQVGLEHKadAFP---EQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLD- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1670356525 167 gseDMLYESLNRLEKETNI---TVFLITHDLHIVSQYSDAVLALNR 209
Cdd:TIGR02673 170 ---PDLSERILDLLKRLNKrgtTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-209 |
2.11e-25 |
|
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: 97.88 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSVRIGYVPQNFVvtdvpiTV 101
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD-----SGEILVDGKEVSFA------SP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 102 RDflgfksgagfeeslaAVGLGSAVLPKrldvLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLeK 181
Cdd:cd03216 70 RD---------------ARRAGIAMVYQ----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL-R 129
|
170 180
....*....|....*....|....*...
gi 1670356525 182 ETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:cd03216 130 AQGVAVIFISHRLDEVFEIADRVTVLRD 157
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
34-224 |
2.29e-25 |
|
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: 99.58 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 34 APILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSG--------------SVRIGYVPQNFVVTDVP 98
Cdd:cd03258 18 VTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTSGSVLVDGtdltllsgkelrkaRRRIGMIFQHFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 iTVRDFLGF----------KSGAGFEESLAAVGLGSAV--LPKRLdvlSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDI 166
Cdd:cd03258 98 -TVFENVALpleiagvpkaEIEERVLELLELVGLEDKAdaYPAQL---SGGQKQRVGIARALANNPKVLLCDEATSALDP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 167 GSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSD--AVLALNRTVRFFGASSRFSEPE 224
Cdd:cd03258 174 ETTQSILALLRDINRELGLTIVLITHEMEVVKRICDrvAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
44-205 |
2.48e-25 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 104.12 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 44 VRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSgsVRIGYVPQnFVVTDVPITVRDFLGF---KSGAGFEESLAA 119
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGvLKPDEGEVDPE--LKISYKPQ-YIKPDYDGTVEDLLRSitdDLGSSYYKSEII 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 120 VGLG-SAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVS 198
Cdd:PRK13409 439 KPLQlERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMID 518
|
....*..
gi 1670356525 199 QYSDAVL 205
Cdd:PRK13409 519 YISDRLM 525
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
22-193 |
2.52e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 102.10 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV---------RIGYVPQN 91
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFEtPDSGRILLDGRDvtglppekrNVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 92 ---FvvtdvP-ITVRDFLGF-----KSGAGF-----EESLAAVGLGSavLPKRL-DVLSGGEMQRVLIAWAVLDRPNVLL 156
Cdd:COG3842 86 yalF-----PhLTVAENVAFglrmrGVPKAEirarvAELLELVGLEG--LADRYpHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1670356525 157 FDEPTATVDIGS-EDMLYEsLNRLEKETNITVFLITHD 193
Cdd:COG3842 159 LDEPLSALDAKLrEEMREE-LRRLQRELGITFIYVTHD 195
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
35-238 |
3.37e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.19 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTG---------TVE--WSGSVRIGYVPQNFVVTDVPITVR 102
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGlLEAESGqiiidgdllTEEnvWDIRHKIGMVFQNPDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 103 DFLGFksgaGFE--------------ESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGS 168
Cdd:PRK13650 101 DDVAF----GLEnkgipheemkervnEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 169 EDMLYESLNRLEKETNITVFLITHDLHIVSqYSDAVLALNRtvrffGASSRFSEPEllmEIFGSGAGLVE 238
Cdd:PRK13650 176 RLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKN-----GQVESTSTPR---ELFSRGNDLLQ 236
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
21-195 |
3.58e-25 |
|
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: 99.39 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT--GTVEWSG------SV-----RIGY 87
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTygNDVRLFGerrggeDVwelrkRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 88 V----PQNFvvtDVPITVRDFL--GFKSGAGF------------EESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVL 149
Cdd:COG1119 83 VspalQLRF---PRDETVLDVVlsGFFDSIGLyreptdeqreraRELLELLGL-AHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1670356525 150 DRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLH 195
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVE 204
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-231 |
4.95e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.84 E-value: 4.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG-----------SVRIGYVP 89
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLtPTAGTVLVAGddvealsaraaSRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 90 Q------NFVVTDV------PITVR-DFLGFKSGAGFEESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLL 156
Cdd:PRK09536 84 QdtslsfEFDVRQVvemgrtPHRSRfDTWTETDRAAVERAMERTGV-AQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 157 FDEPTATVDIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLAL-NRTVRFFGASSRFSEPELLMEIFG 231
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLaDGRVRAAGPPADVLTADTLRAAFD 237
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
22-208 |
5.92e-25 |
|
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: 98.06 E-value: 5.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV---------RIGyvpqn 91
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIkPDSGEITFDGKSyqkniealrRIG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 92 fVVTDVPI-----TVRDFLGFKS-GAGF-----EESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:cd03268 76 -ALIEAPGfypnlTARENLRLLArLLGIrkkriDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1670356525 161 TATVD-IGSEDMLyeSLNRLEKETNITVFLITHDLHIVSQYSDAVLALN 208
Cdd:cd03268 154 TNGLDpDGIKELR--ELILSLRDQGITVLISSHLLSEIQKVADRIGIIN 200
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
34-209 |
8.37e-25 |
|
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: 97.54 E-value: 8.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 34 APILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGSvrIGYVPQN-FVVTDvpiTVRDFLGFksGA 111
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKLSGSVSVPGS--IAYVSQEpWIQNG---TIRENILF--GK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 112 GF-----EESLAAVGLGS--AVLPKRLDV--------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESL 176
Cdd:cd03250 91 PFdeeryEKVIKACALEPdlEILPDGDLTeigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC 170
|
170 180 190
....*....|....*....|....*....|...
gi 1670356525 177 NRLEKETNITVFLITHDLHIVSQySDAVLALNR 209
Cdd:cd03250 171 ILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
34-216 |
9.11e-25 |
|
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: 102.13 E-value: 9.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 34 APILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSVR-----------------IGYVPQNfvVTD 96
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPT-----AGSVRldgadlsqwdreelgrhIGYLPQD--VEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 97 VPITVRD----FlgfkSGAGFEESLAA---VGLGSAV--LPKRLD--------VLSGGEMQRVLIAWAVLDRPNVLLFDE 159
Cdd:COG4618 418 FDGTIAEniarF----GDADPEKVVAAaklAGVHEMIlrLPDGYDtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDE 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1670356525 160 PTATVDIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQySDAVLALNR-TVRFFGA 216
Cdd:COG4618 494 PNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA-VDKLLVLRDgRVQAFGP 549
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-210 |
9.21e-25 |
|
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: 96.07 E-value: 9.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRL-DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPH-TGTVEWSGSVRIGYVPQNFVVTDVpi 99
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWgSGRIGMPEGEDLLFLPQRPYLPLG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 TVRDFLgfksgagfeeslaavglgsaVLPKRlDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRL 179
Cdd:cd03223 79 TLREQL--------------------IYPWD-DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL 137
|
170 180 190
....*....|....*....|....*....|.
gi 1670356525 180 EketnITVFLITHDlHIVSQYSDAVLALNRT 210
Cdd:cd03223 138 G----ITVISVGHR-PSLWKFHDRVLDLDGE 163
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
35-209 |
9.22e-25 |
|
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: 98.07 E-value: 9.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSG---------SVR--IGYVPQN-FVVTDvpiTV 101
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkGQILIDGidirdisrkSLRsmIGVVLQDtFLFSG---TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 102 RDFLGF-KSGAGFEE---SLAAVGLGSAV--LPKRLD--------VLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIG 167
Cdd:cd03254 94 MENIRLgRPNATDEEvieAAKEAGAHDFImkLPNGYDtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1670356525 168 SEDMLYESLNRLEKetNITVFLITHDLHIVsQYSDAVLALNR 209
Cdd:cd03254 174 TEKLIQEALEKLMK--GRTSIIIAHRLSTI-KNADKILVLDD 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
37-209 |
9.81e-25 |
|
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: 98.18 E-value: 9.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGS---------VRIGYVPQNFVVtdVP-ITVRDFL 105
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGfIKPDSGKILLNGKditnlppekRDISYVPQNYAL--FPhMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 106 GF------KSGAGFEESLAAVG--LG-SAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESL 176
Cdd:cd03299 93 AYglkkrkVDKKEIERKVLEIAemLGiDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREEL 172
|
170 180 190
....*....|....*....|....*....|...
gi 1670356525 177 NRLEKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:cd03299 173 KKIRKEFGVTVLHVTHDFEEAWALADKVAIMLN 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-209 |
1.38e-24 |
|
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: 97.51 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSVR----------------- 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT-----SGSVLfdgeditglppheiarl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 85 -IGY------------VPQNFVVTDVPITVRDFLGFKSGAGF-------EESLAAVGLGsavlpKRLDV----LSGGEMQ 140
Cdd:cd03219 76 gIGRtfqiprlfpeltVLENVMVAAQARTGSGLLLARARREEreareraEELLERVGLA-----DLADRpageLSYGQQR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1670356525 141 RVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQ 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
44-205 |
1.59e-24 |
|
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: 97.86 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 44 VRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGsVRIGYVPQnFVVTDVPITVRDFL-----GFKSGAGFEESL 117
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLkPDEGDIEIEL-DTVSYKPQ-YIKADYEGTVRDLLssitkDFYTHPYFKTEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 118 AAVGLGSAVLPKRLDVLSGGEMQRVLIAwAVLDRP-NVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHI 196
Cdd:cd03237 100 AKPLQIEQILDREVPELSGGELQRVAIA-ACLSKDaDIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIM 178
|
....*....
gi 1670356525 197 VSQYSDAVL 205
Cdd:cd03237 179 IDYLADRLI 187
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
32-194 |
2.13e-24 |
|
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: 97.30 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG---------SVR--IGYVPQN-FVVTDvp 98
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYdVDSGRILIDGhdvrdytlaSLRrqIGLVSQDvFLFND-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 iTVRDFLGF-KSGAGFEESLAAVGLGSAV-----LPKRLDV--------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATV 164
Cdd:cd03251 91 -TVAENIAYgRPGATREEVEEAARAANAHefimeLPEGYDTvigergvkLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190
....*....|....*....|....*....|
gi 1670356525 165 DIGSEDMLYESLNRLEKetNITVFLITHDL 194
Cdd:cd03251 170 DTESERLVQAALERLMK--NRTTFVIAHRL 197
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
35-195 |
3.50e-24 |
|
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: 96.03 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG-SVR---------IGYVPQnFVVTDVPITVRD 103
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELrPTSGTAYINGySIRtdrkaarqsLGYCPQ-FDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 104 FL-------GFKSGAGFEESLA---AVGLgSAVLPKRLDVLSGGeMQRVL-IAWAVLDRPNVLLFDEPTATVDIGSEDML 172
Cdd:cd03263 95 HLrfyarlkGLPKSEIKEEVELllrVLGL-TDKANKRARTLSGG-MKRKLsLAIALIGGPSVLLLDEPTSGLDPASRRAI 172
|
170 180
....*....|....*....|...
gi 1670356525 173 YESLNRLEKETniTVFLITHDLH 195
Cdd:cd03263 173 WDLILEVRKGR--SIILTTHSMD 193
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
35-192 |
5.46e-24 |
|
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: 95.73 E-value: 5.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTV--------EWSGSV---RIGYVPQNfvVTDVPITVR 102
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSVlldgtdirQLDPADlrrNIGYVPQD--VTLFYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 103 DFLGFKSG-AGFEESLAAVGLG-----SAVLPKRLDV--------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGS 168
Cdd:cd03245 96 DNITLGAPlADDERILRAAELAgvtdfVNKHPNGLDLqigergrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175
|
170 180
....*....|....*....|....
gi 1670356525 169 EDMLYESLNRLEKETniTVFLITH 192
Cdd:cd03245 176 EERLKERLRQLLGDK--TLIIITH 197
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
22-193 |
5.90e-24 |
|
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: 95.77 E-value: 5.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSVRIGYVPqnfvVTDVPITV 101
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT-----SGEILLDGKD----ITNLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 102 RDF-LGFKSGAGF---------------------------EESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPN 153
Cdd:cd03300 72 RPVnTVFQNYALFphltvfeniafglrlkklpkaeikervAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1670356525 154 VLLFDEPTATVDIG-SEDMLYEsLNRLEKETNITVFLITHD 193
Cdd:cd03300 151 VLLLDEPLGALDLKlRKDMQLE-LKRLQKELGITFVFVTHD 190
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-194 |
6.39e-24 |
|
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: 99.74 E-value: 6.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 3 AAPPPSRSPTREAGAAADV------LRVAHLGVRLDHAPI-LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHT 74
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAAGAVglgkptLELRDLSAGYPGAPPvLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLdPLQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 75 GTVEWSG-----------SVRIGYVPQNFVVTDVpiTVRDFLGFK----SGAGFEESLAAVGLGS--AVLPKRLDV---- 133
Cdd:TIGR02868 390 GEVTLDGvpvssldqdevRRRVSVCAQDAHLFDT--TVRENLRLArpdaTDEELWAALERVGLADwlRALPDGLDTvlge 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 134 ----LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETniTVFLITHDL 194
Cdd:TIGR02868 468 ggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
18-209 |
1.11e-23 |
|
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: 95.88 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 18 AADVLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSVRIGYVPqnfvVTDV 97
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPT-----SGRILFDGRD----ITGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 P---------------------ITVRD-----------------FLGFKSGAGFE--------ESLAAVGLGsAVLPKRL 131
Cdd:COG0411 72 PphriarlgiartfqnprlfpeLTVLEnvlvaaharlgrgllaaLLRLPRARREEreareraeELLERVGLA-DRADEPA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1670356525 132 DVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIG-SEDMLyESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEeTEELA-ELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
21-202 |
1.39e-23 |
|
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: 95.05 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGS----------VR--IGY 87
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRsGSIRFDGEditglpphriARlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 88 VPQN-FVVTDvpITVRDFL-----GFKSGAGFEESLAAVglgSAVLPK---RLD----VLSGGEMQRVLIAWAVLDRPNV 154
Cdd:COG0410 83 VPEGrRIFPS--LTVEENLllgayARRDRAEVRADLERV---YELFPRlkeRRRqragTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1670356525 155 LLFDEPTA-----TVdigseDMLYESLNRLeKETNITVFLITHDLHIVSQYSD 202
Cdd:COG0410 158 LLLDEPSLglaplIV-----EEIFEIIRRL-NREGVTILLVEQNARFALEIAD 204
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
37-209 |
1.50e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 96.33 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGS-------VRIGYVP------QNfvvtdvpITVR 102
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILaPDSGEVLWDGEpldpedrRRIGYLPeerglyPK-------MKVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 103 DFLGF--------KSGA--GFEESLAAVGLGSAvLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDML 172
Cdd:COG4152 90 EQLVYlarlkglsKAEAkrRADEWLERLGLGDR-ANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1670356525 173 YESLNRLeKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:COG4152 169 KDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINK 204
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
35-192 |
2.82e-23 |
|
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: 93.00 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTvewSGSV--------------RIGYVPQNFVVTDVpIT 100
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGV---SGEVlingrpldkrsfrkIIGYVPQDDILHPT-LT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 101 VRDFLGFksgagfeeslaavglgSAvlpkRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLE 180
Cdd:cd03213 99 VRETLMF----------------AA----KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA 158
|
170
....*....|..
gi 1670356525 181 KeTNITVFLITH 192
Cdd:cd03213 159 D-TGRTIICSIH 169
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
36-207 |
4.25e-23 |
|
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: 93.06 E-value: 4.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGSV---------------RIGYVPQNFVVTD--- 96
Cdd:TIGR03608 13 ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLeKFDSGQVYLNGQEtpplnskkaskfrreKLGYLFQNFALIEnet 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 97 -----------VPITVRDFLGFKsgagfEESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVD 165
Cdd:TIGR03608 93 veenldlglkyKKLSKKEKREKK-----KEALEKVGL-NLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1670356525 166 IGSEDMLYESLNRLEKEtNITVFLITHDLHIVSQySDAVLAL 207
Cdd:TIGR03608 167 PKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
39-194 |
7.36e-23 |
|
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: 92.74 E-value: 7.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 39 DVSFHVRRGTTlAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV---------------RIGYVPQNFvvTDVP-ITV 101
Cdd:cd03297 16 KIDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEkPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQQY--ALFPhLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 102 RDFL--GFKSGAG------FEESLAAVGLGSaVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLY 173
Cdd:cd03297 93 RENLafGLKRKRNredrisVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180
....*....|....*....|.
gi 1670356525 174 ESLNRLEKETNITVFLITHDL 194
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDL 192
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-194 |
8.42e-23 |
|
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: 96.81 E-value: 8.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 19 ADVLRVAHLGVRLDHA--------PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG-------- 81
Cdd:COG5265 348 APPLVVGGGEVRFENVsfgydperPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYdVTSGRILIDGqdirdvtq 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 82 -SVR--IGYVPQNFVV-TDvpiTVRDFLGF-KSGAGFEESLAAVGLGS-----AVLPKRLDV--------LSGGEMQRVL 143
Cdd:COG5265 428 aSLRaaIGIVPQDTVLfND---TIAYNIAYgRPDASEEEVEAAARAAQihdfiESLPDGYDTrvgerglkLSGGEKQRVA 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1670356525 144 IAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKetNITVFLITHDL 194
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRL 553
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-209 |
1.21e-22 |
|
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: 92.79 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSG------SVR---IGYVPQN 91
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLeRPDSGTILFGGedatdvPVQernVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 92 FVVTDvPITVRDFLGFksgaGFEESLAAVGLGSAVLPKR----LDV-------------LSGGEMQRVLIAWAVLDRPNV 154
Cdd:cd03296 83 YALFR-HMTVFDNVAF----GLRVKPRSERPPEAEIRAKvhelLKLvqldwladrypaqLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 155 LLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK 212
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-193 |
2.00e-22 |
|
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: 95.39 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSVRIGYVPQNFVVTDVPI 99
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEqPDSGTIEIGETVKLAYVDQSRDALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 TVrdflgfksgagFEE---SLAAVGLGSAVLP----------------KRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:TIGR03719 402 TV-----------WEEisgGLDIIKLGKREIPsrayvgrfnfkgsdqqKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
170 180 190
....*....|....*....|....*....|....*.
gi 1670356525 161 TATVDIgsedmlyESLNRLEK---ETNITVFLITHD 193
Cdd:TIGR03719 471 TNDLDV-------ETLRALEEallNFAGCAVVISHD 499
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
22-194 |
2.73e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 93.67 E-value: 2.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV----------RIGYVPQ 90
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLEtPDSGRIVLNGRDlftnlpprerRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 91 N---FvvtdvP-ITVRD---FlGFKSGAGFEES--------LAAVGLGSavLPKRL-DVLSGGEMQRVLIAWAVLDRPNV 154
Cdd:COG1118 83 HyalF-----PhMTVAEniaF-GLRVRPPSKAEirarveelLELVQLEG--LADRYpSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1670356525 155 LLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDL 194
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQ 194
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-209 |
6.81e-22 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 89.03 E-value: 6.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVrldhAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSG------SVR------IGY 87
Cdd:cd03215 4 VLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPAsGEITLDGkpvtrrSPRdairagIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 88 VPQNfvvtdvpitvRdflgFKSGAGFEESLAAvglgSAVLPkrlDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIG 167
Cdd:cd03215 80 VPED----------R----KREGLVLDLSVAE----NIALS---SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1670356525 168 SEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:cd03215 139 AKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYE 179
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
39-223 |
7.23e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.09 E-value: 7.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 39 DVSFHVRRGTTLAIVGPNGAGKT-TLFrVLLGLVPHTGTVewSGSVR-----IGYVPQN-----------FVVTDvPIT- 100
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqTAF-ALMGLLAANGRI--GGSATfngreILNLPEKelnklraeqisMIFQD-PMTs 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 101 ------VRDFL--------GFKSGAGFEES---LAAVGLGSAvlPKRLDV----LSGGEMQRVLIAWAVLDRPNVLLFDE 159
Cdd:PRK09473 110 lnpymrVGEQLmevlmlhkGMSKAEAFEESvrmLDAVKMPEA--RKRMKMypheFSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 160 PTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLAL--NRTVRFFGASSRFSEP 223
Cdd:PRK09473 188 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMyaGRTMEYGNARDVFYQP 253
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
35-208 |
1.10e-21 |
|
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: 90.08 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV----RIGYVPQNFVVT--------DVPitV 101
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqPTSGEVRVAGLVpwkrRKKFLRRIGVVFgqktqlwwDLP--V 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 102 RDFLGFK------SGAGFEESLA----AVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDM 171
Cdd:cd03267 113 IDSFYLLaaiydlPPARFKKRLDelseLLDLE-ELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190
....*....|....*....|....*....|....*..
gi 1670356525 172 LYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALN 208
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-207 |
1.42e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.39 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSVRIGYVPQNF-----VV 94
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPTSGTLLFEGEDISTLKPEIYrqqvsYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 95 TDVPI----TVRDFLGFK--------SGAGFEESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTA 162
Cdd:PRK10247 87 AQTPTlfgdTVYDNLIFPwqirnqqpDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1670356525 163 TVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQySDAVLAL 207
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
32-208 |
1.69e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.05 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV-----------RIGYVPQN----FVvt 95
Cdd:PRK13632 20 SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSGEIKIDGITiskenlkeirkKIGIIFQNpdnqFI-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 96 dvPITVRDFLGF----------KSGAGFEESLAAVGLGSAvLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVD 165
Cdd:PRK13632 98 --GATVEDDIAFglenkkvppkKMKDIIDDLAKKVGMEDY-LDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1670356525 166 IGSEDMLYESLNRLEKETNITVFLITHDLHIVSQySDAVLALN 208
Cdd:PRK13632 175 PKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFS 216
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
36-194 |
1.72e-21 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 88.95 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSG---------------SVRIGYVPQ------NFV 93
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLdNPTSGEVLFNGqslsklssneraklrNKKLGFIYQfhhllpDFT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 94 VTD---VPITVRDFLGFKSGAGFEESLAAVGLGSAvLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSED 170
Cdd:TIGR02211 100 ALEnvaMPLLIGKKSVKEAKERAYEMLEKVGLEHR-INHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAK 178
|
170 180
....*....|....*....|....
gi 1670356525 171 MLYESLNRLEKETNITVFLITHDL 194
Cdd:TIGR02211 179 IIFDLMLELNRELNTSFLVVTHDL 202
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-192 |
2.13e-21 |
|
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: 88.35 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGlvpHTGTVEWSGSVRIgyvpQNFVVTDVPITV 101
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG---HPKYEVTEGEILF----KGEDITDLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 102 RD----FLGFKS-----GAGFEESLAAVGLGsavlpkrldvLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDML 172
Cdd:cd03217 74 RArlgiFLAFQYppeipGVKNADFLRYVNEG----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180
....*....|....*....|
gi 1670356525 173 YESLNRLEKETNiTVFLITH 192
Cdd:cd03217 144 AEVINKLREEGK-SVLIITH 162
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
37-209 |
2.17e-21 |
|
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: 88.96 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG----------SVRIGYVPQNFVVTDvPITVRDFL 105
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFATVDGfdvvkepaeaRRRLGFVSDSTGLYD-RLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 106 GFKSG----AGFE-----ESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESL 176
Cdd:cd03266 100 EYFAGlyglKGDEltarlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179
|
170 180 190
....*....|....*....|....*....|...
gi 1670356525 177 NRLeKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:cd03266 180 RQL-RALGKCILFSTHIMQEVERLCDRVVVLHR 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
35-209 |
3.09e-21 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 88.32 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSV-----------------RIGYVPQNfvvtdv 97
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS-----SGSIlidgvdiskiglhdlrsRISIIPQD------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 PI----TVR---DFLGFKSGAGFEESLAAVGLGSAV--LPKRLD--------VLSGGEMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:cd03244 87 PVlfsgTIRsnlDPFGEYSDEELWQALERVGLKEFVesLPGGLDtvveeggeNLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1670356525 161 TATVDIGSEDMLYESLNrlEKETNITVFLITHDLHIVSQYsDAVLALNR 209
Cdd:cd03244 167 TASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIIDS-DRILVLDK 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-204 |
3.12e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.00 E-value: 3.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSVR------------IGYVPQNFVVtdVP-ITVR 102
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDsGEILLDGEPVrfrsprdaqaagIAIIHQELNL--VPnLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 103 D--FLG-FKSGAGF----------EESLAAVGLgsavlpkRLDV------LSGGEMQRVLIAWAVLDRPNVLLFDEPTAT 163
Cdd:COG1129 98 EniFLGrEPRRGGLidwramrrraRELLARLGL-------DIDPdtpvgdLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1670356525 164 VDiGSE-DMLYESLNRLeKETNITVFLITHDLHIVSQYSDAV 204
Cdd:COG1129 171 LT-EREvERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRV 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
37-204 |
3.55e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.63 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG-SVR-----------IGYVPQNFvvTDVP-ITVR 102
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYqPDSGEILIDGkPVRirsprdaialgIGMVHQHF--MLVPnLTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 103 D--FLGFKSGAGFEESLAAV-----------GLgsAVLPKRLdV--LSGGEMQRVLIAWAVLDRPNVLLFDEPTA--T-- 163
Cdd:COG3845 99 EniVLGLEPTKGGRLDRKAArarirelseryGL--DVDPDAK-VedLSVGEQQRVEILKALYRGARILILDEPTAvlTpq 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1670356525 164 -VDIgsedmLYESLNRLeKETNITVFLITHDLHIVSQYSDAV 204
Cdd:COG3845 176 eADE-----LFEILRRL-AAEGKSIIFITHKLREVMAIADRV 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
37-229 |
5.35e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.31 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV---------------RIGYV------------ 88
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqPTSGTVTIGERVitagkknkklkplrkKVGIVfqfpehqlfeet 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 89 --------PQNFVVTDVpitvrdflgfKSGAGFEESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:PRK13634 103 vekdicfgPMNFGVSEE----------DAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1670356525 161 TATVD-IGSEDMLyESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR-TVRFFGASSR-FSEPELLMEI 229
Cdd:PRK13634 173 TAGLDpKGRKEMM-EMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKgTVFLQGTPREiFADPDELEAI 243
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
23-231 |
6.58e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.22 E-value: 6.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 23 RVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVP-HTGTV--------EWSGSV---RIGYVPQ 90
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPpDSGEVlvdgldvaTTPSRElakRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 91 -NFVVTDvpITVRDFLGFksG--------------AGFEESLAAVGLGSavLPKR-LDVLSGGEMQRVLIAwAVL--DRP 152
Cdd:COG4604 83 eNHINSR--LTVRELVAF--GrfpyskgrltaedrEIIDEAIAYLDLED--LADRyLDELSGGQRQRAFIA-MVLaqDTD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 153 NVLLfDEPTATVDIG-SEDMLyESLNRLEKETNITVFLITHDLHIVSQYSDAVLAL-NRTVRFFGASSRFSEPELLMEIF 230
Cdd:COG4604 156 YVLL-DEPLNNLDMKhSVQMM-KLLRRLADELGKTVVIVLHDINFASCYADHIVAMkDGRVVAQGTPEEIITPEVLSDIY 233
|
.
gi 1670356525 231 G 231
Cdd:COG4604 234 D 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
36-205 |
1.03e-20 |
|
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: 86.81 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSV-------------RIGYVPQNFV-------- 93
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTIIIDGLKltddkkninelrqKVGMVFQQFNlfphltvl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 94 --VTDVPITVRDFLGFKSGAGFEESLAAVGLG--SAVLPKRLdvlSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDigsE 169
Cdd:cd03262 95 enITLAPIKVKGMSKAEAEERALELLEKVGLAdkADAYPAQL---SGGQQQRVAIARALAMNPKVMLFDEPTSALD---P 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1670356525 170 DMLYESLNRLE--KETNITVFLITHDLHIVSQYSDAVL 205
Cdd:cd03262 169 ELVGEVLDVMKdlAEEGMTMVVVTHEMGFAREVADRVI 206
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
21-161 |
1.22e-20 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 86.97 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSV-------------RIG 86
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTITVDGEDltdskkdinklrrKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 87 YVPQNF-------V---VTDVPITVRdflgfksGAGFEES-------LAAVGLGSavlpkRLDV----LSGGEMQRVLIA 145
Cdd:COG1126 81 MVFQQFnlfphltVlenVTLAPIKVK-------KMSKAEAeeramelLERVGLAD-----KADAypaqLSGGQQQRVAIA 148
|
170
....*....|....*.
gi 1670356525 146 WAVLDRPNVLLFDEPT 161
Cdd:COG1126 149 RALAMEPKVMLFDEPT 164
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-244 |
1.28e-20 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 89.00 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 29 VRLDHAPILEDVSFHVR-RGTTlAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV---------------RIGYVPQN 91
Cdd:COG4148 7 FRLRRGGFTLDVDFTLPgRGVT-ALFGPSGSGKTTLLRAIAGLErPDSGRIRLGGEVlqdsargiflpphrrRIGYVFQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 92 ---FvvtdvP-ITVRDFLGF--------KSGAGFEESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDE 159
Cdd:COG4148 86 arlF-----PhLSVRGNLLYgrkrapraERRISFDEVVELLGIG-HLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 160 PTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALN--RTVRFFGASSRFSEPELLMEIFGSGAG-- 235
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEqgRVVASGPLAEVLSRPDLLPLAGGEEAGsv 239
|
250
....*....|...
gi 1670356525 236 ----LVEHKHDFG 244
Cdd:COG4148 240 leatVAAHDPDYG 252
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
35-229 |
1.29e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.93 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPH--------------TGTVEWSGSVRIGYVPQNFVVTDVPI 99
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDdnpnskitvdgitlTAKTVWDIREKVGIVFQNPDNQFVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 TVRDFLGFksgaGFE--------------ESLAAVGLgsavlpkrLDV-------LSGGEMQRVLIAWAVLDRPNVLLFD 158
Cdd:PRK13640 101 TVGDDVAF----GLEnravprpemikivrDVLADVGM--------LDYidsepanLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1670356525 159 EPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQySDAVLALNRTVRFFGASSR--FSEPELLMEI 229
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVeiFSKVEMLKEI 240
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
37-226 |
1.36e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.96 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV---------------RIGYVPQ--------NF 92
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkPSSGTITIAGYHitpetgnknlkklrkKVSLVFQfpeaqlfeNT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 93 VVTDVPITVRDFlGFKSGAGFEES---LAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSE 169
Cdd:PRK13641 103 VLKDVEFGPKNF-GFSEDEAKEKAlkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1670356525 170 DMLYESLNRLEKETNiTVFLITHDLHIVSQYSDAVLALN--RTVRFFGASSRFSEPELL 226
Cdd:PRK13641 182 KEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEhgKLIKHASPKEIFSDKEWL 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
22-193 |
1.84e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 88.59 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSV---------RIGYVPQN 91
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTsGEILIGGRDvtdlppkdrNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 92 FVVTDvPITVRDFLGFksG---AGF---------EESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDE 159
Cdd:COG3839 84 YALYP-HMTVYENIAF--PlklRKVpkaeidrrvREAAELLGL-EDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1670356525 160 PTATVDIGS-EDMLYEsLNRLEKETNITVFLITHD 193
Cdd:COG3839 160 PLSNLDAKLrVEMRAE-IKRLHRRLGTTTIYVTHD 193
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-204 |
2.41e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 89.36 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHA----PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPH-----TGTVEWSG---------- 81
Cdd:COG4172 6 LLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahpSGSILFDGqdllglsere 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 82 --SVR---IGYVPQNfvvtdvPIT-----------VRDFLGFKSGAGFEES-------LAAVGLGSAvlPKRLDV----L 134
Cdd:COG4172 86 lrRIRgnrIAMIFQE------PMTslnplhtigkqIAEVLRLHRGLSGAAAraralelLERVGIPDP--ERRLDAyphqL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 135 SGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAV 204
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRV 227
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
37-209 |
3.15e-20 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 86.01 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSG------SVR---IGYVPQNFVVTDvPITVRDFLG 106
Cdd:TIGR00968 16 LDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLeQPDSGRIRLNGqdatrvHARdrkIGFVFQHYALFK-HLTVRDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 107 F----------KSGAGFEESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESL 176
Cdd:TIGR00968 95 FgleirkhpkaKIKARVEELLELVQL-EGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKELRSWL 173
|
170 180 190
....*....|....*....|....*....|...
gi 1670356525 177 NRLEKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:TIGR00968 174 RKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSN 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
32-194 |
3.70e-20 |
|
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: 85.82 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTV--------EWSGSV---RIGYVPQN------FV 93
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTsGEIfidgedirEQDPVElrrKIGYVIQQiglfphMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 94 VTDVPITVRDFLGFKSG---AGFEESLAAVGLGSAVLPKRL-DVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSE 169
Cdd:cd03295 92 VEENIALVPKLLKWPKEkirERADELLALVGLDPAEFADRYpHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITR 171
|
170 180
....*....|....*....|....*
gi 1670356525 170 DMLYESLNRLEKETNITVFLITHDL 194
Cdd:cd03295 172 DQLQEEFKRLQQELGKTIVFVTHDI 196
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
41-194 |
3.75e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.58 E-value: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 41 SFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGsvrigyvpQNfvVTDVPI------------------TV 101
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGfLPPDSGRILWNG--------QD--LTALPPaerpvsmlfqennlfphlTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 102 RD--FLGFKSG--------AGFEESLAAVGLGSavLPKRL-DVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIG-SE 169
Cdd:COG3840 89 AQniGLGLRPGlkltaeqrAQVEQALERVGLAG--LLDRLpGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAlRQ 166
|
170 180
....*....|....*....|....*
gi 1670356525 170 DMLYEsLNRLEKETNITVFLITHDL 194
Cdd:COG3840 167 EMLDL-VDELCRERGLTVLMVTHDP 190
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
33-201 |
6.33e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.25 E-value: 6.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 33 HAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGSV---------------RIGYVPQ------ 90
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQPmsklssaakaelrnqKLGFIYQfhhllp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 91 NFVVTD---VPITVRDFLGFKSGAGFEESLAAVGLGSAVlPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIG 167
Cdd:PRK11629 101 DFTALEnvaMPLLIGKKKPAEINSRALEMLAAVGLEHRA-NHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180 190
....*....|....*....|....*....|....
gi 1670356525 168 SEDMLYESLNRLEKETNITVFLITHDLHIVSQYS 201
Cdd:PRK11629 180 NADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
28-192 |
1.06e-19 |
|
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: 87.88 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 28 GVRLDHAPI--------LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVP-HTGTVEWSGSVRIGYVPQNFVVTD-- 96
Cdd:TIGR00954 451 GIKFENIPLvtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPvYGGRLTKPAKGKLFYVPQRPYMTLgt 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 97 ------VPITVRDFL--GFkSGAGFEESLAAVGLGSAVlpKR----------LDVLSGGEMQRVLIAWAVLDRPNVLLFD 158
Cdd:TIGR00954 531 lrdqiiYPDSSEDMKrrGL-SDKDLEQILDNVQLTHIL--EReggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....
gi 1670356525 159 EPTATVDIGSEDMLYeslnRLEKETNITVFLITH 192
Cdd:TIGR00954 608 ECTSAVSVDVEGYMY----RLCREFGITLFSVSH 637
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-220 |
1.07e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.06 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVphTG-------------TVEWSGSV---- 83
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI--TGdksagshiellgrTVQREGRLardi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 -----RIGYVPQNF-------VVTDVPITV-------RDFLGFKSGAGFEESLAA---VGLgSAVLPKRLDVLSGGEMQR 141
Cdd:PRK09984 82 rksraNTGYIFQQFnlvnrlsVLENVLIGAlgstpfwRTCFSWFTREQKQRALQAltrVGM-VHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 142 VLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNRTVRFF-GASSRF 220
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYdGSSQQF 240
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-192 |
1.10e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.24 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 9 RSPTREAGAAADVLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTvewSGSVRigyV 88
Cdd:COG2401 18 SSVLDLSERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV---AGCVD---V 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 89 PQNFVVTDVPItVRDFLGFKSGAGFEESLAAVGLGSAVLPKRL-DVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIG 167
Cdd:COG2401 92 PDNQFGREASL-IDAIGRKGDFKDAVELLNAVGLSDAVLWLRRfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*
gi 1670356525 168 SEDMLYESLNRLEKETNITVFLITH 192
Cdd:COG2401 171 TAKRVARNLQKLARRAGITLVVATH 195
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
37-239 |
1.48e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.51 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTV--------EWSG---SVRIGYVPQNfVVTDVPITVRDFL 105
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEIllngrplsDWSAaelARHRAYLSQQ-QSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 106 GF--KSGAGFEESLAAVG-LGSAV-----LPKRLDVLSGGEMQRVLIAWAVL-----DRPN--VLLFDEPTATVDIGSED 170
Cdd:COG4138 91 ALhqPAGASSEAVEQLLAqLAEALgledkLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 171 MLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLALNR-TVRFFGASSRFSEPELLMEIFGSGAGLVEH 239
Cdd:COG4138 171 ALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQgKLVASGETAEVMTPENLSEVFGVKFRRLEV 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-234 |
1.53e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 11 PTREAGAAADVLRVAHLGVRldhaPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVP-HTGTVEWSG------SV 83
Cdd:COG1129 246 PKRAAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPaDSGEIRLDGkpvrirSP 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 R------IGYVP----QNFVVTDVPItvRD-----FLGFKSGAGF-----EESLAAvglgSAVlpKRLDV---------- 133
Cdd:COG1129 322 RdairagIAYVPedrkGEGLVLDLSI--REnitlaSLDRLSRGGLldrrrERALAE----EYI--KRLRIktpspeqpvg 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 134 -LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKEtNITVFLITHDLHIVSQYSDAVLALN--RT 210
Cdd:COG1129 394 nLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMRegRI 472
|
250 260
....*....|....*....|....
gi 1670356525 211 VRFFGAsSRFSEPELLMEIFGSGA 234
Cdd:COG1129 473 VGELDR-EEATEEAIMAAATGGAA 495
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
23-223 |
1.54e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 84.74 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 23 RVAHLGVRLDHA--PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSG----------------SV 83
Cdd:PRK10419 12 HYAHGGLSGKHQhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQGNVSWRGeplaklnraqrkafrrDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 R------IGYV-PQNFVVTDVPITVRDFLGFKSG---AGFEESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPN 153
Cdd:PRK10419 92 QmvfqdsISAVnPRKTVREIIREPLRHLLSLDKAerlARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1670356525 154 VLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALN-------RTVrffGASSRFSEP 223
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDngqivetQPV---GDKLTFSSP 245
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
36-231 |
2.18e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.27 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG-----------SVRIGYVPQNfVVTDVPITVRD 103
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPAHGHVWLDGehiqhyaskevARRIGLLAQN-ATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 104 FLGF--------------KSGAGFEESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSE 169
Cdd:PRK10253 101 LVARgryphqplftrwrkEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1670356525 170 DMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR-TVRFFGASSRFSEPELLMEIFG 231
Cdd:PRK10253 180 IDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREgKIVAQGAPKEIVTAELIERIYG 242
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
22-193 |
2.63e-19 |
|
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: 83.07 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSVRIGyvpqNFVVTDVP--- 98
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT-----SGRIYIG----GRDVTDLPpkd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 ---------------ITVRDFLGF--KSGAGFEESL------AAVGLG-SAVLPKRLDVLSGGEMQRVLIAWAVLDRPNV 154
Cdd:cd03301 72 rdiamvfqnyalyphMTVYDNIAFglKLRKVPKDEIdervreVAELLQiEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 1670356525 155 LLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHD 193
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
39-207 |
2.66e-19 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 85.55 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 39 DVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV---------------RIGYV-------PQNFVVT 95
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrPDEGEIVLNGRTlfdsrkgiflppekrRIGYVfqearlfPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 96 DVPITVRDFLGFKSGAGFEESLAAVGLGSaVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYES 175
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190
....*....|....*....|....*....|..
gi 1670356525 176 LNRLEKETNITVFLITHDLHIVSQYSDAVLAL 207
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVL 205
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
22-193 |
2.75e-19 |
|
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: 85.47 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGsvRIgyvpqnfvVTDVPIT 100
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLeRQTAGTIYQGG--RD--------ITRLPPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 101 VRDF-LGFKSGAGF---------------------------EESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRP 152
Cdd:TIGR03265 75 KRDYgIVFQSYALFpnltvadniayglknrgmgraevaervAELLDLVGL-PGSERKYPGQLSGGQQQRVALARALATSP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1670356525 153 NVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHD 193
Cdd:TIGR03265 154 GLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHD 194
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-194 |
3.08e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.98 E-value: 3.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG------SVRIGYVPQNFVV 94
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVpYQHGSITLDGkpvegpGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 95 tdVP-ITVRDFLGFK---SGAGFEES-------LAAVGLGSAVlPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTAT 163
Cdd:PRK11248 82 --LPwRNVQDNVAFGlqlAGVEKMQRleiahqmLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|.
gi 1670356525 164 VDIGSEDMLYESLNRLEKETNITVFLITHDL 194
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-205 |
3.17e-19 |
|
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: 86.28 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 7 PSRSPTREAGAAADVLRVAHLGV-----------RLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTG 75
Cdd:COG4172 261 PRGDPRPVPPDAPPLLEARDLKVwfpikrglfrrTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 76 TVEWSG------------SVR--IGYVPQNfvvtdvP-------ITVRDFL--GFK------SGAGFE----ESLAAVGL 122
Cdd:COG4172 341 EIRFDGqdldglsrralrPLRrrMQVVFQD------PfgslsprMTVGQIIaeGLRvhgpglSAAERRarvaEALEEVGL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 123 GSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSD 202
Cdd:COG4172 415 DPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAH 494
|
...
gi 1670356525 203 AVL 205
Cdd:COG4172 495 RVM 497
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
36-192 |
3.37e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.47 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGS----------VRIGYVPQnFVVTDVPITVRDF 104
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLThPDAGSISLCGEpvpsrarharQRVGVVPQ-FDNLDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 105 LG-----FKSGAGFEESLAAVGLGSAVLPKRLDV----LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYES 175
Cdd:PRK13537 101 LLvfgryFGLSAAAARALVPPLLEFAKLENKADAkvgeLSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWER 180
|
170
....*....|....*..
gi 1670356525 176 LNRLEKETNiTVFLITH 192
Cdd:PRK13537 181 LRSLLARGK-TILLTTH 196
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
39-207 |
3.47e-19 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 83.19 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 39 DVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPhTGTVEWSGSVR---------------IGYVPQNFVVTDVPI---- 99
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLP-PGLTQTSGEILldgrpllplsirgrhIATIMQNPRTAFNPLftmg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 -----TVRDFLGFKSGAGFE--ESLAAVGL--GSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSED 170
Cdd:TIGR02770 83 nhaieTLRSLGKLSKQARALilEALEAVGLpdPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQA 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1670356525 171 MLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLAL 207
Cdd:TIGR02770 163 RVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVM 199
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
21-191 |
4.07e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.15 E-value: 4.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSVRIGyvpqNFVVTDVPIT 100
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD-----SGRIFLD----GEDITHLPMH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 101 VRDFLGFksgaGF-------------EESLAAV----GLGSAVLPKRLD-----------------VLSGGEMQRVLIAW 146
Cdd:COG1137 74 KRARLGI----GYlpqeasifrkltvEDNILAVlelrKLSKKEREERLEelleefgithlrkskaySLSGGERRRVEIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1670356525 147 AVLDRPNVLLFDEPTATVD-IGSEDmLYESLNRLeKETNITVfLIT 191
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDpIAVAD-IQKIIRHL-KERGIGV-LIT 192
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
30-208 |
4.32e-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: 82.97 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 30 RLDHaPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSG---------SVR--IGYVPQNFVVTDv 97
Cdd:cd03249 13 RPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFyDPTSGEILLDGvdirdlnlrWLRsqIGLVSQEPVLFD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 pITVRDFLGF-KSGAGFEESLAAVGLGSA-----VLPKRLDV--------LSGGEMQRVLIAWAVLDRPNVLLFDEPTAT 163
Cdd:cd03249 91 -GTIAENIRYgKPDATDEEVEEAAKKANIhdfimSLPDGYDTlvgergsqLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1670356525 164 VDIGSEDMLYESLNRLEKetNITVFLITHDLHIVsQYSDAVLALN 208
Cdd:cd03249 170 LDAESEKLVQEALDRAMK--GRTTIVIAHRLSTI-RNADLIAVLQ 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-224 |
9.82e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 9.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHA----PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVEWSGSVRigYVPQNFVVTDV 97
Cdd:PRK15134 6 LAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIR--FHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 PiTVRDFLGFKSGAGFEE---SL-----------------------AA----------VGLGSAvlPKRLD----VLSGG 137
Cdd:PRK15134 84 Q-TLRGVRGNKIAMIFQEpmvSLnplhtlekqlyevlslhrgmrreAArgeilncldrVGIRQA--AKRLTdyphQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 138 EMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSD--AVLALNRTVRFFG 215
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADrvAVMQNGRCVEQNR 240
|
....*....
gi 1670356525 216 ASSRFSEPE 224
Cdd:PRK15134 241 AATLFSAPT 249
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
21-191 |
1.10e-18 |
|
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: 81.94 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSVRIGyvpqNFVVTDVPIT 100
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPD-----AGKILID----GQDITHLPMH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 101 VRDFLG----------FKsGAGFEESLAAV-----GLGSAVLPKRLDV-----------------LSGGEMQRVLIAWAV 148
Cdd:TIGR04406 72 ERARLGigylpqeasiFR-KLTVEENIMAVleirkDLDRAEREERLEAlleefqishlrdnkamsLSGGERRRVEIARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1670356525 149 LDRPNVLLFDEPTATVD-IGSEDMlyESLNRLEKETNITVfLIT 191
Cdd:TIGR04406 151 ATNPKFILLDEPFAGVDpIAVGDI--KKIIKHLKERGIGV-LIT 191
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
22-231 |
1.26e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.98 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG-----------SVRIGYVP 89
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLtPQSGTVFLGDkpismlssrqlARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 90 QNFVVTDvPITVRDF--------------LGFKSGAGFEESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVL 155
Cdd:PRK11231 83 QHHLTPE-GITVRELvaygrspwlslwgrLSAEDNARVNQAMEQTRI-NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1670356525 156 LFDEPTATVDIGSEDMLYESLNRLEKETNiTVFLITHDLHIVSQYSD--AVLALNRTVRfFGASSRFSEPELLMEIFG 231
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDhlVVLANGHVMA-QGTPEEVMTPGLLRTVFD 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
35-224 |
1.31e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.98 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVL-LGLVPHTGTVEWSGS------------VR-----IGYVPQNF---- 92
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPDSGQLNIAGHqfdfsqkpsekaIRllrqkVGMVFQQYnlwp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 93 ---V---VTDVPITVrdfLGFKSGAGFEEslAAVGLGSAVLPKRLDV----LSGGEMQRVLIAWAVLDRPNVLLFDEPTA 162
Cdd:COG4161 96 hltVmenLIEAPCKV---LGLSKEQAREK--AMKLLARLRLTDKADRfplhLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1670356525 163 TVDIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLAL-NRTVRFFGASSRFSEPE 224
Cdd:COG4161 171 ALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMeKGRIIEQGDASHFTQPQ 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
37-226 |
1.72e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.16 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGS---------VR--IGYVPQNFVVTDVPITVRDF 104
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGiLKPTSGSVLIRGEpitkenireVRkfVGLVFQNPDDQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 105 LGF-KSGAGFEESLAAVGLGSAV----LPKRLDV----LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYES 175
Cdd:PRK13652 100 IAFgPINLGLDEETVAHRVSSALhmlgLEELRDRvphhLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDF 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1670356525 176 LNRLEKETNITVFLITHDLHIVSQYSDAVLALN--RTVRFFGASSRFSEPELL 226
Cdd:PRK13652 180 LNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDkgRIVAYGTVEEIFLQPDLL 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
35-192 |
2.42e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.57 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGS----------VRIGYVPQnFVVTDVPITVRD 103
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTsPDAGKITVLGVpvpararlarARIGVVPQ-FDNLDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 104 FL---GFKSGAGFEESLAAVG--LGSAVLPKRLDV----LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYE 174
Cdd:PRK13536 134 NLlvfGRYFGMSTREIEAVIPslLEFARLESKADArvsdLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWE 213
|
170
....*....|....*...
gi 1670356525 175 SLNRLEKETNiTVFLITH 192
Cdd:PRK13536 214 RLRSLLARGK-TILLTTH 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
35-192 |
3.21e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 81.29 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTV------------EWSGSVRIGYVPQN----FVVTDV 97
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALlIPSEGKVyvdgldtsdeenLWDIRNKAGMVFQNpdnqIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 PITVR---DFLGFKSG---AGFEESLAAVGLGSAvlpKRL--DVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVD-IGS 168
Cdd:PRK13633 104 EEDVAfgpENLGIPPEeirERVDESLKKVGMYEY---RRHapHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpSGR 180
|
170 180
....*....|....*....|....
gi 1670356525 169 EDMLyESLNRLEKETNITVFLITH 192
Cdd:PRK13633 181 REVV-NTIKELNKKYGITIILITH 203
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
36-209 |
3.24e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 82.46 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGsvrigyvpQNFV----VTDVPITVRDF-LGFKSG 110
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPT-----EG--------QIFIdgedVTHRSIQQRDIcMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 111 AGF---------------------------EESLAAVGLgsAVLPKR-LDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTA 162
Cdd:PRK11432 88 ALFphmslgenvgyglkmlgvpkeerkqrvKEALELVDL--AGFEDRyVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1670356525 163 TVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNK 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
44-204 |
4.49e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.93 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 44 VRRGTTLAIVGPNGAGKTTLFRVLLG-LVP----HTGTVEW--------------------SGSVRIGYVPQnfVVTDVP 98
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGeLIPnlgdYEEEPSWdevlkrfrgtelqnyfkklyNGEIKVVHKPQ--YVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 I----TVRDFLGFKSGAG-FEESLAAVGLGSaVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIgsedmlY 173
Cdd:PRK13409 174 KvfkgKVRELLKKVDERGkLDEVVERLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI------R 246
|
170 180 190
....*....|....*....|....*....|....*
gi 1670356525 174 ESLN--RLEKE--TNITVFLITHDLHIVSQYSDAV 204
Cdd:PRK13409 247 QRLNvaRLIRElaEGKYVLVVEHDLAVLDYLADNV 281
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
37-197 |
4.51e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 81.66 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGSV--------------RIGYVPQNF--------- 92
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLeRPTSGSVLVDGVDltalserelraarrKIGMIFQHFnllssrtva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 93 -------VVTDVP---ITVRdflgfksgagFEESLAAVGLG--SAVLPKRLdvlSGGEMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:COG1135 101 envalplEIAGVPkaeIRKR----------VAELLELVGLSdkADAYPSQL---SGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1670356525 161 TATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIV 197
Cdd:COG1135 168 TSALDPETTRSILDLLKDINRELGLTIVLITHEMDVV 204
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
32-226 |
4.93e-18 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 81.29 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSG-SV----------RIGYVPQN---F---- 92
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTsGRILIDGeDIrdldpvelrrRIGYVIQQiglFphmt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 93 VVTDVpITVRDFLGF---KSGAGFEESLAAVGLGSAVLPKRL-DVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGS 168
Cdd:COG1125 93 VAENI-ATVPRLLGWdkeRIRARVDELLELVGLDPEEYRDRYpHELSGGQQQRVGVARALAADPPILLMDEPFGALDPIT 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1670356525 169 EDMLYESLNRLEKETNITVFLITHDL----------------HIVsQYS--DAVLA--LNRTVR-FFGASSRFSEPELL 226
Cdd:COG1125 172 REQLQDELLRLQRELGKTIVFVTHDIdealklgdriavmregRIV-QYDtpEEILAnpANDFVAdFVGADRGLRRLSLL 249
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
35-209 |
5.29e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.85 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGsVRIGYVPQNFVVTDVPI----------TVRD 103
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLyQPTGGQVLLDG-VPLVQYDHHYLHRQVALvgqepvlfsgSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 104 FLGFKSGAGFEESLAAVGLGSAV------LPKRLDV--------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSE 169
Cdd:TIGR00958 574 NIAYGLTDTPDEEIMAAAKAANAhdfimeFPNGYDTevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE 653
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1670356525 170 DMLYESLNRLEKetniTVFLITHDLHIVSQySDAVLALNR 209
Cdd:TIGR00958 654 QLLQESRSRASR----TVLLIAHRLSTVER-ADQILVLKK 688
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
36-196 |
5.39e-18 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 79.68 E-value: 5.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTV-----EWSGSV---------RIGYVPQNFVVTDVpIT 100
Cdd:TIGR02982 20 VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLrSVQEGSLkvlgqELHGASkkqlvqlrrRIGYIFQAHNLLGF-LT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 101 VRD--FLGFKSGAGF---------EESLAAVGLGsavlpKRLDV----LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVD 165
Cdd:TIGR02982 99 ARQnvQMALELQPNLsyqeareraRAMLEAVGLG-----DHLNYyphnLSGGQKQRVAIARALVHHPKLVLADEPTAALD 173
|
170 180 190
....*....|....*....|....*....|.
gi 1670356525 166 IGSEDMLYESLNRLEKETNITVFLITHDLHI 196
Cdd:TIGR02982 174 SKSGRDVVELMQKLAKEQGCTILMVTHDNRI 204
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
30-197 |
5.46e-18 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 80.22 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 30 RLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSG---------SVR--IGYVPQ------- 90
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGhdlaladpaWLRrqVGVVLQenvlfnr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 91 ----NFVVTDVPITVRDFLGFKSGAGFEESLAAVGLG-SAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVD 165
Cdd:cd03252 91 sirdNIALADPGMSMERVIEAAKLAGAHDFISELPEGyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190
....*....|....*....|....*....|..
gi 1670356525 166 IGSEDMLYESLNRLEKetNITVFLITHDLHIV 197
Cdd:cd03252 171 YESEHAIMRNMHDICA--GRTVIIIAHRLSTV 200
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
37-231 |
7.01e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.98 E-value: 7.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTV--------EWSGS---VRIGYVPQN-FVVTDVPitVRDF 104
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIqfagqpleAWSAAelaRHRAYLSQQqTPPFAMP--VFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 105 LGFKSGAG---------FEESLAAVGLGSAvLPKRLDVLSGGEMQRVLIAWAVLD-----RPN--VLLFDEPTATVDIGS 168
Cdd:PRK03695 90 LTLHQPDKtrteavasaLNEVAEALGLDDK-LGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 169 EDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLALNRTVRFfgASSRFSE---PELLMEIFG 231
Cdd:PRK03695 169 QAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL--ASGRRDEvltPENLAQVFG 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-209 |
8.20e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 8.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 11 PTREAGAAADVLRVAHLGVRLDH----APILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVEWSGS---- 82
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 83 -------------------VR---IGYVPQNFVVTDVPI-----TVRDFLGFKSGAGFEESLAA---------VGLGSAV 126
Cdd:PRK10261 82 rrsrqvielseqsaaqmrhVRgadMAMIFQEPMTSLNPVftvgeQIAESIRLHQGASREEAMVEakrmldqvrIPEAQTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 127 LPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLA 206
Cdd:PRK10261 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLV 241
|
...
gi 1670356525 207 LNR 209
Cdd:PRK10261 242 MYQ 244
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
36-192 |
8.83e-18 |
|
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: 79.24 E-value: 8.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVewSGSV--------------RIGYVPQNFVVtdVP-IT 100
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTT--SGQIlfngqprkpdqfqkCVAYVRQDDIL--LPgLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 101 VRDFLGF---------KSGAGFEESLAAVGLGSAVLP----KRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIG 167
Cdd:cd03234 98 VRETLTYtailrlprkSSDAIRKKRVEDVLLRDLALTriggNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180
....*....|....*....|....*
gi 1670356525 168 SEDMLYESLNRLEKEtNITVFLITH 192
Cdd:cd03234 178 TALNLVSTLSQLARR-NRIVILTIH 201
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
37-211 |
8.89e-18 |
|
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: 79.43 E-value: 8.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGSVRIGYVPQNFVVTD----VP-ITVRDFLGF--- 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEGKQITEPGPDRMVVFQnyslLPwLTVRENIALavd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 108 ---------KSGAGFEESLAAVGLGSAVlPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNR 178
Cdd:TIGR01184 81 rvlpdlsksERRAIVEEHIALVGLTEAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190
....*....|....*....|....*....|...
gi 1670356525 179 LEKETNITVFLITHDLhivsqySDAVLALNRTV 211
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDV------DEALLLSDRVV 186
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
32-207 |
9.22e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.81 E-value: 9.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVEWSG---------SVR--IGYVPQNfvvtdvPI- 99
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGielreldpeSWRkhLSWVGQN------PQl 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 ---TVRD--FLGfKSGAGFEESLAAVGLGSA-----VLPKRLDV--------LSGGEMQRVLIAWAVLDRPNVLLFDEPT 161
Cdd:PRK11174 435 phgTLRDnvLLG-NPDASDEQLQQALENAWVseflpLLPQGLDTpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1670356525 162 ATVDIGSEDMLYESLNRLEKETniTVFLITHDLHIVSQYsDAVLAL 207
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVM 556
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
35-209 |
1.01e-17 |
|
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: 78.99 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV--------------RIGYVPQNFVVTdVPI 99
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEElPTSGTIRVNGQDvsdlrgraipylrrKIGVVFQDFRLL-PDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 TVRDFLGFksgagfeeSLAAVGLGSAVLPKR----LDV-------------LSGGEMQRVLIAWAVLDRPNVLLFDEPTA 162
Cdd:cd03292 94 NVYENVAF--------ALEVTGVPPREIRKRvpaaLELvglshkhralpaeLSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1670356525 163 TVDigsEDMLYESLNRLEK--ETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:cd03292 166 NLD---PDTTWEIMNLLKKinKAGTTVVVATHAKELVDTTRHRVIALER 211
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
36-215 |
1.03e-17 |
|
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: 79.11 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSVR------IGYVPQnfvvtdvpITVRD----- 103
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYpPDSGTVTVRGRVSsllglgGGFNPE--------LTGREniyln 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 104 --FLGFK---SGAGFEESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNR 178
Cdd:cd03220 109 grLLGLSrkeIDEKIDEIIEFSELG-DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRE 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 1670356525 179 LeKETNITVFLITHDLHIVSQYSDAVLALNR-TVRFFG 215
Cdd:cd03220 188 L-LKQGKTVILVSHDPSSIKRLCDRALVLEKgKIRFDG 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
36-239 |
1.05e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.83 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTL-------------AIVGPNGAGKTTLFRvLLGL--VPHTGTV--------EWSGSV---RIGYVP 89
Cdd:PRK10575 13 ALRNVSFRVPGRTLLhplsltfpagkvtGLIGHNGSGKSTLLK-MLGRhqPPSEGEIlldaqpleSWSSKAfarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 90 QNFVVTDvPITVRDF--------------LGFKSGAGFEESLAAVGLGSavLPKRL-DVLSGGEMQRVLIAWAVLDRPNV 154
Cdd:PRK10575 92 QQLPAAE-GMTVRELvaigrypwhgalgrFGAADREKVEEAISLVGLKP--LAHRLvDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 155 LLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALnRTVRFF--GASSRFSEPELLMEIFGS 232
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVAL-RGGEMIaqGTPAELMRGETLEQIYGI 247
|
....*..
gi 1670356525 233 GAGLVEH 239
Cdd:PRK10575 248 PMGILPH 254
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
37-229 |
1.11e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 80.09 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG-----------SVR-------------------- 84
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPTSGKIIIDGvditdkkvklsDIRkkvglvfqypeyqlfeetie 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 85 --IGYVPQNFVVTDVPITVRdflgfksgagFEESLAAVGLGSAVLPKRLDV-LSGGEMQRVLIAWAVLDRPNVLLFDEPT 161
Cdd:PRK13637 103 kdIAFGPINLGLSEEEIENR----------VKRAMNIVGLDYEDYKDKSPFeLSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 162 ATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR-TVRFFGASSR-FSEPELLMEI 229
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKgKCELQGTPREvFKEVETLESI 242
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
36-224 |
1.18e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 79.41 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVL-LGLVPHTGTV--------------EWSGSVR-----IGYVPQNF--- 92
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInLLEQPEAGTIrvgditidtarslsQQKGLIRqlrqhVGFVFQNFnlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 93 ----VVTDV---PITVRDFLGFKSGAGFEESLAAVGLGSA--VLPKRLdvlSGGEMQRVLIAWAVLDRPNVLLFDEPTAT 163
Cdd:PRK11264 98 phrtVLENIiegPVIVKGEPKEEATARARELLAKVGLAGKetSYPRRL---SGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 164 VDigsEDMLYESLN--RLEKETNITVFLITHDLHIVSQYSDAVLALN--RTVRFFGASSRFSEPE 224
Cdd:PRK11264 175 LD---PELVGEVLNtiRQLAQEKRTMVIVTHEMSFARDVADRAIFMDqgRIVEQGPAKALFADPQ 236
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
34-208 |
1.26e-17 |
|
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: 81.71 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 34 APILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG---------SVR--IGYVPQNFVVTDVPITV 101
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFqARSGEILLNGfslkdidrhTLRqfINYLPQEPYIFSGSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 102 RDFLGFKSGAGFEESLAAVGLGS-----AVLPKRLDV--------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGS 168
Cdd:TIGR01193 567 NLLLGAKENVSQDEIWAACEIAEikddiENMPLGYQTelseegssISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1670356525 169 EDMLYESLNRLEKETNItvfLITHDLHIVSQySDAVLALN 208
Cdd:TIGR01193 647 EKKIVNNLLNLQDKTII---FVAHRLSVAKQ-SDKIIVLD 682
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
36-215 |
1.27e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.97 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSVR------IGYVPQnfvvtdvpITVRD----- 103
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILePTSGRVEVNGRVSallelgAGFHPE--------LTGREniyln 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 104 --FLGFkSGAGFEESLAAV----GLGSAV-LP-KRldvLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDigsEDMLYES 175
Cdd:COG1134 113 grLLGL-SRKEIDEKFDEIvefaELGDFIdQPvKT---YSSGMRARLAFAVATAVDPDILLVDEVLAVGD---AAFQKKC 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1670356525 176 LNRLE--KETNITVFLITHDLHIVSQYSDAVLALNR-TVRFFG 215
Cdd:COG1134 186 LARIRelRESGRTVIFVSHSMGAVRRLCDRAIWLEKgRLVMDG 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
21-193 |
1.53e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 80.76 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGSVrigyvpqnfvVTDVP- 98
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFeTPDSGRIMLDGQD----------ITHVPa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 -----------------ITVRDFLGF-----KSGAG-----FEESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDR 151
Cdd:PRK09452 84 enrhvntvfqsyalfphMTVFENVAFglrmqKTPAAeitprVMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1670356525 152 PNVLLFDEPTATVDIG-SEDMLYEsLNRLEKETNITVFLITHD 193
Cdd:PRK09452 163 PKVLLLDESLSALDYKlRKQMQNE-LKALQRKLGITFVFVTHD 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
22-209 |
1.91e-17 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 77.84 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRL--DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG-----------SVRIGY 87
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGidistipledlRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 88 VPQNFVVTDVpiTVR---DFLGFKSGAGFEESLAAVGLGSAvlpkrldvLSGGEMQRVLIAWAVLDRPNVLLFDEPTATV 164
Cdd:cd03369 87 IPQDPTLFSG--TIRsnlDPFDEYSDEEIYGALRVSEGGLN--------LSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1670356525 165 DIGSEDMLYESLNrlEKETNITVFLITHDLHIVSQYsDAVLALNR 209
Cdd:cd03369 157 DYATDALIQKTIR--EEFTNSTILTIAHRLRTIIDY-DKILVMDA 198
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-192 |
1.97e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.57 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTvewSGSVR----------------- 84
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVT---SGSILldgedilelspderara 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 85 -IGYVPQNFVvtDVP-ITVRDFL---------GFKSGAGF----EESLAAVGLGSAVLPKRLDV-LSGGEMQRVLIAWAV 148
Cdd:COG0396 78 gIFLAFQYPV--EIPgVSVSNFLrtalnarrgEELSAREFlkllKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQML 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1670356525 149 LDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNiTVFLITH 192
Cdd:COG0396 156 LLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDR-GILIITH 198
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-224 |
2.48e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.55 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 14 EAGAAA-DVLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVP-HTGTVEWSGSVRigYVPQN 91
Cdd:PRK14246 2 EAGKSAeDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKVL--YFGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 92 FVVTDVpITVRDFLG--FKSGAGF----------------------------EESLAAVGLGSAV---LPKRLDVLSGGE 138
Cdd:PRK14246 80 IFQIDA-IKLRKEVGmvFQQPNPFphlsiydniayplkshgikekreikkivEECLRKVGLWKEVydrLNSPASQLSGGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 139 MQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKEtnITVFLITHDLHIVSQYSDAVLAL-NRTVRFFGAS 217
Cdd:PRK14246 159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLyNGELVEWGSS 236
|
....*...
gi 1670356525 218 SR-FSEPE 224
Cdd:PRK14246 237 NEiFTSPK 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
37-226 |
2.53e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.97 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSG-----------SVR--IGYVPQN--------FVV 94
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPTSGEVLIKGepikydkksllEVRktVGIVFQNpddqlfapTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 95 TDV---PITvrdfLGFKS---GAGFEESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGS 168
Cdd:PRK13639 98 EDVafgPLN----LGLSKeevEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 169 EDMLYESLNRLEKEtNITVFLITHDLHIVSQYSDAVLALNRTVRFFGASSR--FSEPELL 226
Cdd:PRK13639 173 ASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKevFSDIETI 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
32-238 |
2.97e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 78.64 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGS---------VR--IGYVPQN----FVVT 95
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIeKVKSGEIFYNNQaitddnfekLRkhIGIVFQNpdnqFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 96 DVPITVrdflGFksgaGFEESLAAVGLGSAVLPKRL-DV------------LSGGEMQRVLIAWAVLDRPNVLLFDEPTA 162
Cdd:PRK13648 100 IVKYDV----AF----GLENHAVPYDEMHRRVSEALkQVdmleradyepnaLSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 163 TVDIGSEDMLYESLNRLEKETNITVFLITHDLhIVSQYSDAVLALNRtvrffGASSRFSEPEllmEIFGSGAGLVE 238
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDL-SEAMEADHVIVMNK-----GTVYKEGTPT---EIFDHAEELTR 238
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-193 |
3.72e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.51 E-value: 3.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 17 AAADVLRVAHLGVRL---DHA-PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVP-------------HTGTVEW 79
Cdd:PRK10584 2 PAENIVEVHHLKKSVgqgEHElSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDgssgevslvgqplHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 80 SGSVR---IGYVPQNFVV---------TDVPITVRDFLGFKSGAGFEESLAAVGLGsavlpKRLD----VLSGGEMQRVL 143
Cdd:PRK10584 82 RAKLRakhVGFVFQSFMLiptlnalenVELPALLRGESSRQSRNGAKALLEQLGLG-----KRLDhlpaQLSGGEQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1670356525 144 IAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHD 193
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-193 |
3.83e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 77.98 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLD----HAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSVRIGYVP-------- 89
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS-----SGEITLDGVPvtgpgadr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 90 ----QNFVVtdVP-ITVRDFLGF----------KSGAGFEESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPNV 154
Cdd:COG4525 79 gvvfQKDAL--LPwLNVLDNVAFglrlrgvpkaERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1670356525 155 LLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHD 193
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
39-194 |
4.62e-17 |
|
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: 78.07 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 39 DVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG---------------SVRIGYVPQNFVVtdVP-ITV 101
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIePTSGKVLIDGqdiaamsrkelrelrRKKISMVFQSFAL--LPhRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 102 RDFLGFksgaGFE--------------ESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVD-- 165
Cdd:cd03294 120 LENVAF----GLEvqgvpraereeraaEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDpl 194
|
170 180
....*....|....*....|....*....
gi 1670356525 166 IGSEdmLYESLNRLEKETNITVFLITHDL 194
Cdd:cd03294 195 IRRE--MQDELLRLQAELQKTIVFITHDL 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
37-228 |
5.42e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.85 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGSV-----------RIGYVPQN-----FVVT---D 96
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREvnaenekwvrsKVGLVFQDpddqvFSSTvwdD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 97 V---PITVRdFLGFKSGAGFEESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLY 173
Cdd:PRK13647 101 VafgPVNMG-LDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1670356525 174 ESLNRLEKETNiTVFLITHDLHIVSQYSDAVLALN--RTVRfFGASSRFSEPELLME 228
Cdd:PRK13647 179 EILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKegRVLA-EGDKSLLTDEDIVEQ 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-209 |
5.95e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.74 E-value: 5.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSVrIGYVPQNFVV--TDV 97
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKP-LDYSKRGLLAlrQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 PITVRD------FLGFKSGAGFeeSLAAVGLGSAVLPKRLD-----------------VLSGGEMQRVLIAWAVLDRPNV 154
Cdd:PRK13638 80 ATVFQDpeqqifYTDIDSDIAF--SLRNLGVPEAEITRRVDealtlvdaqhfrhqpiqCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 155 LLFDEPTATVDIGSEDMLYESLNRLEKETNiTVFLITHDLHIVSQYSDAVLALNR 209
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQ 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
37-209 |
6.23e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 78.59 E-value: 6.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPhTgtvewSGSVRI-GYVPQ--------NF-VVT--------DV 97
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-T-----SGEVRVlGYVPFkrrkefarRIgVVFgqrsqlwwDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 PitVRD-FLGFK-----SGAGFEESLAAvglgsavLPKRLDV----------LSGGEMQRVLIAWAVLDRPNVLLFDEPT 161
Cdd:COG4586 112 P--AIDsFRLLKaiyriPDAEYKKRLDE-------LVELLDLgelldtpvrqLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1670356525 162 ATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
26-209 |
8.27e-17 |
|
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: 76.70 E-value: 8.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 26 HL--GVRLdhaPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG---------LVPHTGtvEW----SGSVR------ 84
Cdd:COG4778 17 HLqgGKRL---PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylpdsgsiLVRHDG--GWvdlaQASPReilalr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 85 ---IGYVPQNFVVtdVP-ITVRDFLgfksgagfEESLAAVGLGSAV-------------LPKRLDVL-----SGGEMQRV 142
Cdd:COG4778 92 rrtIGYVSQFLRV--IPrVSALDVV--------AEPLLERGVDREEarararellarlnLPERLWDLppatfSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1670356525 143 LIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-195 |
1.14e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.61 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 12 TREAGAAADVLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVEWSGSV-------- 83
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEIlldgediy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 -----------RIGYVPQN---FvvtdvPITVRD-------FLGFKSGAGF----EESLAAVGLGSAVlpK-RLD----V 133
Cdd:COG1117 82 dpdvdvvelrrRVGMVFQKpnpF-----PKSIYDnvayglrLHGIKSKSELdeivEESLRKAALWDEV--KdRLKksalG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 134 LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGS----EDMLYEslnrlEKEtNITVFLITHDLH 195
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakiEELILE-----LKK-DYTIVIVTHNMQ 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
36-224 |
1.16e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.59 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVL-LGLVPHTGTVEWSGSV-----------------RIGYVPQNF----- 92
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPRSGTLNIAGNHfdfsktpsdkairelrrNVGMVFQQYnlwph 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 93 --VV---TDVPITVrdfLGFKSGAGFEESLAavglgsavLPKRLDV----------LSGGEMQRVLIAWAVLDRPNVLLF 157
Cdd:PRK11124 97 ltVQqnlIEAPCRV---LGLSKDQALARAEK--------LLERLRLkpyadrfplhLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1670356525 158 DEPTATVDIGSEDMLYESLNRLEkETNITVFLITHDLHIVSQYSDAVLAL-NRTVRFFGASSRFSEPE 224
Cdd:PRK11124 166 DEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMeNGHIVEQGDASCFTQPQ 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-209 |
1.21e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 1 MVAAPPPSRSPTREAGAAADVLRVAHLGVRLDH-APILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVE 78
Cdd:COG3845 237 MVGREVLLRVEKAPAEPGEVVLEVENLSVRDDRgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAsGSIR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 79 WSG------SVR------IGYVP---------------QNFVVTDV---PITVRDFLGFKSGAGFEESLAA---VGLGSA 125
Cdd:COG3845 317 LDGeditglSPRerrrlgVAYIPedrlgrglvpdmsvaENLILGRYrrpPFSRGGFLDRKAIRAFAEELIEefdVRTPGP 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 126 VLPKRLdvLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVL 205
Cdd:COG3845 397 DTPARS--LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIA 473
|
....
gi 1670356525 206 ALNR 209
Cdd:COG3845 474 VMYE 477
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
22-165 |
1.45e-16 |
|
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: 76.04 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSVRIGYVPqnfvVTDVPITV 101
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPD-----SGKILLDGQD----ITKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 102 RDFLG----------FKsGAGFEESLAAV----GLGSAVLPKRLD-----------------VLSGGEMQRVLIAWAVLD 150
Cdd:cd03218 72 RARLGigylpqeasiFR-KLTVEENILAVleirGLSKKEREEKLEelleefhithlrkskasSLSGGERRRVEIARALAT 150
|
170
....*....|....*
gi 1670356525 151 RPNVLLFDEPTATVD 165
Cdd:cd03218 151 NPKFLLLDEPFAGVD 165
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-180 |
1.64e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 78.24 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHL----GVRLdhapILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGSVRIGYVPQNfvvt 95
Cdd:PRK11819 324 VIEAENLsksfGDRL----LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQeQPDSGTIKIGETVKLAYVDQS---- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 96 dvpitvRDFL-GFKSgaGFEE---SLAAVGLGSAVLP----------------KRLDVLSGGEMQRVLIAWAVLDRPNVL 155
Cdd:PRK11819 396 ------RDALdPNKT--VWEEisgGLDIIKVGNREIPsrayvgrfnfkggdqqKKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
170 180
....*....|....*....|....*
gi 1670356525 156 LFDEPTATVDIgsedmlyESLNRLE 180
Cdd:PRK11819 468 LLDEPTNDLDV-------ETLRALE 485
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
37-208 |
1.68e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.05 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEW--------SGSVRIGYVPQNFVVTDVPI-------T 100
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALlLPDTGTIEWifkdeknkKKTKEKEKVLEKLVIQKTRFkkikkikE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 101 VRDFLG----------FKS-------------GAGFEES--LAA-----VGLGSAVLPKRLDVLSGGEMQRVLIAWAVLD 150
Cdd:PRK13651 103 IRRRVGvvfqfaeyqlFEQtiekdiifgpvsmGVSKEEAkkRAAkyielVGLDESYLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1670356525 151 RPNVLLFDEPTATVD-IGSEDMLyESLNRLEKEtNITVFLITHDLHIVSQYSDAVLALN 208
Cdd:PRK13651 183 EPDFLVFDEPTAGLDpQGVKEIL-EIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFK 239
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
35-172 |
1.97e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGS--------VRIGYV-PQNFVVTdvPITVRDF 104
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAaGTIKLDGGdiddpdvaEACHYLgHRNAMKP--ALTVAEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1670356525 105 LGF------KSGAGFEESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDML 172
Cdd:PRK13539 94 LEFwaaflgGEELDIAAALEAVGLA-PLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
37-211 |
1.98e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 77.08 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSV--------------RIGYVPQNfvvtdvP--- 98
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTsGEILFDGQDitglsgrelrplrrRMQMVFQD------Pyas 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 ----ITVRDFLGF-------KSGAGFE----ESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTAT 163
Cdd:COG4608 108 lnprMTVGDIIAEplrihglASKAERRervaELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1670356525 164 VDIgsedmlyeS--------LNRLEKETNITVFLITHDLHIVSQYSD--AVLALNRTV 211
Cdd:COG4608 188 LDV--------SiqaqvlnlLEDLQDELGLTYLFISHDLSVVRHISDrvAVMYLGKIV 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
35-245 |
2.15e-16 |
|
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: 78.41 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGsvRIGYVPQNFVVtdVPITVRDFLGFksGAGF 113
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEGKIKHSG--RISFSPQTSWI--MPGTIKDNIIF--GLSY 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 114 EE-----SLAAVGLGS--AVLPKRLDV--------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYES-LN 177
Cdd:TIGR01271 514 DEyrytsVIKACQLEEdiALFPEKDKTvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLC 593
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1670356525 178 RLekETNITVFLITHDLHIVSQySDAVLALNRTVRFFGASsrFSEPELLMEIFGSGAGLVEHKHDFGA 245
Cdd:TIGR01271 594 KL--MSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGT--FSELQAKRPDFSSLLLGLEAFDNFSA 656
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-209 |
2.48e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.30 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 25 AHLGVRldhaPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG--------------SVRIGYVP 89
Cdd:PRK10908 10 AYLGGR----QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIErPSAGKIWFSGhditrlknrevpflRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 90 QNFVVTdVPITVRDFLGFK---SGAGFEESLAAVglgSAVLPK--RLD-------VLSGGEMQRVLIAWAVLDRPNVLLF 157
Cdd:PRK10908 86 QDHHLL-MDRTVYDNVAIPliiAGASGDDIRRRV---SAALDKvgLLDkaknfpiQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 158 DEPTATVDigseDMLYESLNRLEKETN---ITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:PRK10908 162 DEPTGNLD----DALSEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
37-209 |
3.05e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.97 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEwSGSVRIGYVPQNFVVTDVPITVRDFLGFKSGAGFEE 115
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLkPTTGTVT-VDDITITHKTKDKYIRPVRKRIGMVFQFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 116 S--------------------------LAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSE 169
Cdd:PRK13646 102 TvereiifgpknfkmnldevknyahrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1670356525 170 DMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:PRK13646 182 RQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKE 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
36-193 |
4.41e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.91 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGSVRIGYVPQNFVVTDVPITVRDFLgfksGAGFE 114
Cdd:PRK11147 334 LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNL----AEGKQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 115 ESLAAvGLGSAVL---------PKR----LDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIgsedmlyESLNRLEK 181
Cdd:PRK11147 410 EVMVN-GRPRHVLgylqdflfhPKRamtpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV-------ETLELLEE 481
|
170
....*....|....*
gi 1670356525 182 ---ETNITVFLITHD 193
Cdd:PRK11147 482 lldSYQGTVLLVSHD 496
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-238 |
4.41e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 75.63 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPH---------TGTVEWSG---------- 81
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarvTGDVTLNGeplaaidapr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 82 -SVRIGYVPQN------FVVTDVPITVRDFLGFKSGAGFEE----SLAAVGLGSAVLPKRLDV--LSGGEMQRVLIA--- 145
Cdd:PRK13547 81 lARLRAVLPQAaqpafaFSAREIVLLGRYPHARRAGALTHRdgeiAWQALALAGATALVGRDVttLSGGELARVQFArvl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 146 ---WAVLDR---PNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLAL-NRTVRFFGASS 218
Cdd:PRK13547 161 aqlWPPHDAaqpPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLaDGAIVAHGAPA 240
|
250 260
....*....|....*....|
gi 1670356525 219 RFSEPELLMEIFGSGAGLVE 238
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVD 260
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-176 |
4.47e-16 |
|
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: 74.07 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGS-------------VRIGY 87
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLaGRVLLNGGpldfqrdsiarglLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 88 VPQNFVVTDVPITVRDFLGFKSGAGFEESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIG 167
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEEALARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
....*....
gi 1670356525 168 SEDMLYESL 176
Cdd:cd03231 160 GVARFAEAM 168
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
36-209 |
5.06e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.10 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGtvewsGSVRIGYVPQNFVVTDVPITVRD--FLGFKS---- 109
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSA-----GELLAGTAPLAEAREDTRLMFQDarLLPWKKvidn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 110 -GAGF--------EESLAAVGLGSAV--LPKrldVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNR 178
Cdd:PRK11247 102 vGLGLkgqwrdaaLQALAAVGLADRAneWPA---ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIES 178
|
170 180 190
....*....|....*....|....*....|.
gi 1670356525 179 LEKETNITVFLITHDLhivsqySDAVLALNR 209
Cdd:PRK11247 179 LWQQHGFTVLLVTHDV------SEAVAMADR 203
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-197 |
6.31e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.54 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 13 REAGAAADVLRVAHLgVRLDH--------APILEDVSFHVRRGTTLAIVGPNGAGKTTLFRvLLGLV--PHTGTVEWSG- 81
Cdd:PRK13657 320 RDPPGAIDLGRVKGA-VEFDDvsfsydnsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLIN-LLQRVfdPQSGRILIDGt 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 82 --------SVR--IGYVPQNFVVTDVPITVRDFLGfKSGAGFEESLAAVGLGSA-------------VLPKRLDVLSGGE 138
Cdd:PRK13657 398 dirtvtraSLRrnIAVVFQDAGLFNRSIEDNIRVG-RPDATDEEMRAAAERAQAhdfierkpdgydtVVGERGRQLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1670356525 139 MQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKetNITVFLITHDLHIV 197
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTV 533
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-238 |
6.91e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.94 E-value: 6.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPH--TGTVEWSGSVriGYVPQNFVVTDVpiTVRDFLGFksGAG 112
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIRGSV--AYVPQVSWIFNA--TVRENILF--GSD 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 113 FEESLAAVGLGSAVLPKRLDVL---------------SGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLN 177
Cdd:PLN03232 705 FESERYWRAIDVTALQHDLDLLpgrdlteigergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCM 784
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1670356525 178 RLEKETNITVfLITHDLHIVSQYSDAVLALNRTVRFFGASSRFSEPELLMEIFGSGAGLVE 238
Cdd:PLN03232 785 KDELKGKTRV-LVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMD 844
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-226 |
7.16e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.88 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRL-DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSG-----------SVR--I 85
Cdd:PRK13636 5 ILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRILFDGkpidysrkglmKLResV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 86 GYVPQN--------FVVTDVPITVRDfLGFKSGA---GFEESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNV 154
Cdd:PRK13636 85 GMVFQDpdnqlfsaSVYQDVSFGAVN-LKLPEDEvrkRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 155 LLFDEPTATVD-IGSEDMLyESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR-TVRFFGASSR-FSEPELL 226
Cdd:PRK13636 163 LVLDEPTAGLDpMGVSEIM-KLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEgRVILQGNPKEvFAEKEML 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-248 |
8.31e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.69 E-value: 8.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVEWSGsvRIGYVPQNFVVTDV---- 97
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEG--RVEFFNQNIYERRVnlnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 ---------------PITVRD-------FLGFKSGAGF----EESLAAVGLGSAV---LPKRLDVLSGGEMQRVLIAWAV 148
Cdd:PRK14258 86 lrrqvsmvhpkpnlfPMSVYDnvaygvkIVGWRPKLEIddivESALKDADLWDEIkhkIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 149 LDRPNVLLFDEPTATVDIGSEdMLYESL-NRLEKETNITVFLITHDLHIVSQYSDAvlalnrTVRFFGASSRFSEpelLM 227
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIAS-MKVESLiQSLRLRSELTMVIVSHNLHQVSRLSDF------TAFFKGNENRIGQ---LV 235
|
250 260
....*....|....*....|.
gi 1670356525 228 EiFGSGAGLVEHKHDFGARGF 248
Cdd:PRK14258 236 E-FGLTKKIFNSPHDSRTREY 255
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
46-215 |
1.02e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.30 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 46 RGTTlAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV---------------RIGYVPQN---FvvtdvP-ITVRDFL 105
Cdd:PRK11144 24 QGIT-AIFGRSGAGKTSLINAISGLTrPQKGRIVLNGRVlfdaekgiclppekrRIGYVFQDarlF-----PhYKVRGNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 106 GF----KSGAGFEESLAAVGLGSavLPKRLDV-LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDI--GSEDMLYesLNR 178
Cdd:PRK11144 98 RYgmakSMVAQFDKIVALLGIEP--LLDRYPGsLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprKRELLPY--LER 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1670356525 179 LEKETNITVFLITHDLHIVSQYSDAVLALNR-TVRFFG 215
Cdd:PRK11144 174 LAREINIPILYVSHSLDEILRLADRVVVLEQgKVKAFG 211
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-205 |
1.06e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.13 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAP-------------ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSG----- 81
Cdd:PRK15079 8 LLEVADLKVHFDIKDgkqwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATdGEVAWLGkdllg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 82 -------SVR--IGYVPQNFVVTDVP-ITVRDFLG-----FKSGAGFEE-------SLAAVGLGSAVLPKRLDVLSGGEM 139
Cdd:PRK15079 88 mkddewrAVRsdIQMIFQDPLASLNPrMTIGEIIAeplrtYHPKLSRQEvkdrvkaMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 140 QRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVL 205
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
45-204 |
1.20e-15 |
|
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: 75.59 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 45 RRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVE----W--------------------SGSVRIGYVPQNfvVTDVPI 99
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGeLKPNLGDYDeepsWdevlkrfrgtelqdyfkklaNGEIKVAHKPQY--VDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 ----TVRDFLgfkSGAG----FEESLAAVGLGSaVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIgsedm 171
Cdd:COG1245 175 vfkgTVRELL---EKVDergkLDELAEKLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI----- 245
|
170 180 190
....*....|....*....|....*....|....*...
gi 1670356525 172 lYESLN--RLEKE---TNITVFLITHDLHIVSQYSDAV 204
Cdd:COG1245 246 -YQRLNvaRLIRElaeEGKYVLVVEHDLAILDYLADYV 282
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
44-228 |
1.27e-15 |
|
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: 72.22 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 44 VRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGsVRIGYVPQNFVvtdvpitvrdflgfksgagfeeslaavgl 122
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGqLIPNGDNDEWDG-ITPVYKPQYID----------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 123 gsavlpkrldvLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSD 202
Cdd:cd03222 72 -----------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSD 140
|
170 180
....*....|....*....|....*....
gi 1670356525 203 avlalnRTVRFFGASS---RFSEPELLME 228
Cdd:cd03222 141 ------RIHVFEGEPGvygIASQPKGTRE 163
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
37-213 |
1.46e-15 |
|
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: 75.61 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTV------EW----------SGSVR--IGYVPQNFVV--- 94
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTsGEVnvrvgdEWvdmtkpgpdgRGRAKryIGILHQEYDLyph 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 95 -------TD-VPITVRDFLGFKSG------AGFEESLAavglgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:TIGR03269 380 rtvldnlTEaIGLELPDELARMKAvitlkmVGFDEEKA-----EEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1670356525 161 TATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVlALNRTVRF 213
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRA-ALMRDGKI 506
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-205 |
1.57e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLD----HAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSVRIGYVPQN----- 91
Cdd:PRK10762 249 LDKAPGEVRLKvdnlSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTsGYVTLDGHEVVTRSPQDglang 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 92 -----------------FVVTDVPITVRDFLGFKSGA--GFEESLAA---VGLGSAVLPKR---LDVLSGGEMQRVLIAW 146
Cdd:PRK10762 329 ivyisedrkrdglvlgmSVKENMSLTALRYFSRAGGSlkHADEQQAVsdfIRLFNIKTPSMeqaIGLLSGGNQQKVAIAR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1670356525 147 AVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKEtNITVFLITHDLHIVSQYSDAVL 205
Cdd:PRK10762 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRIL 466
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
32-209 |
1.64e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.74 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGS---------VRIGYVPQNFVVTDvPITV 101
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTsGHIRFHGTdvsrlhardRKVGFVFQHYALFR-HMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 102 RDFLGFksgagfeeslaavglGSAVLPKR---------------LDV-------------LSGGEMQRVLIAWAVLDRPN 153
Cdd:PRK10851 92 FDNIAF---------------GLTVLPRRerpnaaaikakvtqlLEMvqlahladrypaqLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 154 VLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQ 212
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-172 |
1.68e-15 |
|
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: 72.39 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGsvriGYVPQnfvVTDVPIT 100
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLrPDSGEVRWNG----TPLAE---QRDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 101 VRDFLGFKSG----------------------AGFEESLAAVGL-GSAVLPKRldVLSGGEMQRVLIAWAVLDRPNVLLF 157
Cdd:TIGR01189 74 NILYLGHLPGlkpelsalenlhfwaaihggaqRTIEDALAAVGLtGFEDLPAA--QLSAGQQRRLALARLWLSRRPLWIL 151
|
170
....*....|....*
gi 1670356525 158 DEPTATVDIGSEDML 172
Cdd:TIGR01189 152 DEPTTALDKAGVALL 166
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
37-209 |
1.79e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.00 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV---------------RIGYVPQ--------NF 92
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVGDIVvsstskqkeikpvrkKVGVVFQfpesqlfeET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 93 VVTDVPITVRDFLGFKSGAG--FEESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGS-- 168
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEkiAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAri 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1670356525 169 EDM-LYESLNrlekETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:PRK13643 182 EMMqLFESIH----QSGQTVVLVTHLMDDVADYADYVYLLEK 219
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
44-204 |
2.01e-15 |
|
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: 73.17 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 44 VRRGTTLAIVGPNGAGKTTLFRVLLG-LVP----HTGTVEW--------------------SGSVRIGYVPQNfvVTDVP 98
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGkLKPnlgkFDDPPDWdeildefrgselqnyftkllEGDVKVIVKPQY--VDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 I----TVRDFLGFKSGAGFEESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYE 174
Cdd:cd03236 101 KavkgKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAAR 180
|
170 180 190
....*....|....*....|....*....|
gi 1670356525 175 SLNRLEKETNiTVFLITHDLHIVSQYSDAV 204
Cdd:cd03236 181 LIRELAEDDN-YVLVVEHDLAVLDYLSDYI 209
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
36-202 |
3.18e-15 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 74.44 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGSVRIGYVPQN---FVVTD-VPI----------- 99
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPVSGEIGLAKGIKLGYFAQHqleFLRADeSPLqhlarlapqel 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 --TVRDFLGfksGAGFEeslaavglGSAVlPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLn 177
Cdd:PRK10636 407 eqKLRDYLG---GFGFQ--------GDKV-TEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL- 473
|
170 180
....*....|....*....|....*
gi 1670356525 178 rLEKETNITVflITHDLHIVSQYSD 202
Cdd:PRK10636 474 -IDFEGALVV--VSHDRHLLRSTTD 495
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
34-232 |
3.69e-15 |
|
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: 72.97 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 34 APILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGsvRIGYVPQnfVVTDVPITVRDFLGF----- 107
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPSEGKIKHSG--RISFSSQ--FSWIMPGTIKENIIFgvsyd 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 108 ----KS---GAGFEESLAAVG-LGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYES-LNR 178
Cdd:cd03291 126 eyryKSvvkACQLEEDITKFPeKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEScVCK 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1670356525 179 LekETNITVFLITHDLHIVSQySDAVLALNRTVRFFGASsrFSEPELLMEIFGS 232
Cdd:cd03291 206 L--MANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGT--FSELQSLRPDFSS 254
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-207 |
4.08e-15 |
|
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: 74.09 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 1 MVAAPPPSRSPTREAGAAADVLRVAHLG---VRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHtgtv 77
Cdd:TIGR02633 237 MVGREITSLYPHEPHEIGDVILEARNLTcwdVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPG---- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 78 EWSGSV----------------------------RIGYVPQNFVVTDVPITVRDFLGFKSGAGFEESLAAVGLGSavlpK 129
Cdd:TIGR02633 313 KFEGNVfingkpvdirnpaqairagiamvpedrkRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAI----Q 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 130 RLDV-----------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKEtNITVFLITHDLHIVS 198
Cdd:TIGR02633 389 RLKVktaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVL 467
|
....*....
gi 1670356525 199 QYSDAVLAL 207
Cdd:TIGR02633 468 GLSDRVLVI 476
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
35-229 |
4.62e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 72.85 E-value: 4.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSG-------------SVR--IGYVPQ-------- 90
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLhVPTQGSVRVDDtlitstsknkdikQIRkkVGLVFQfpesqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 91 NFVVTDVPITVRDFLGFKSGAG--FEESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGS 168
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEalAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1670356525 169 EDMLYESLNRLEkETNITVFLITHDLHIVSQYSDAVLALN--RTVRFFGASSRFSEPELLMEI 229
Cdd:PRK13649 181 RKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEkgKLVLSGKPKDIFQDVDFLEEK 242
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
37-211 |
4.87e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSG-SVR-------IGYVPQNFVVT-DVPITVRD--F 104
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLAsGKISILGqPTRqalqknlVAYVPQSEEVDwSFPVLVEDvvM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 105 LGFKSGAGF------------EESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDML 172
Cdd:PRK15056 103 MGRYGHMGWlrrakkrdrqivTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 1670356525 173 YESLNRLEKETNiTVFLITHDLHIVSQYSDAVLALNRTV 211
Cdd:PRK15056 182 ISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMVKGTV 219
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
39-209 |
5.66e-15 |
|
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: 72.17 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 39 DVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEW---SGSVRI-----------------GYVPQNfvvtdv 97
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrLAPDHGTATYimrSGAELElyqlseaerrrlmrtewGFVHQN------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 pitVRDFL--GFKSGAGFEESLAAVGLGS---------------AVLPKRLD----VLSGGEMQRVLIAWAVLDRPNVLL 156
Cdd:TIGR02323 95 ---PRDGLrmRVSAGANIGERLMAIGARHygnirataqdwleevEIDPTRIDdlprAFSGGMQQRLQIARNLVTRPRLVF 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1670356525 157 FDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:TIGR02323 172 MDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQ 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
33-207 |
6.41e-15 |
|
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: 71.35 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 33 HAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTG----------------------------TVEWSGSVR 84
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGgqvlldgkpisqyehkylhskvslvgqePVLFARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 85 --IGYVpqnfvVTDVPITVRDFLGFKSGAGFEESLAAVGLGSAVlPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTA 162
Cdd:cd03248 106 dnIAYG-----LQSCSFECVKEAAQKAHAHSFISELASGYDTEV-GEKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1670356525 163 TVDIGSEDMLYESLNrlEKETNITVFLITHDLHIVsQYSDAVLAL 207
Cdd:cd03248 180 ALDAESEQQVQQALY--DWPERRTVLVIAHRLSTV-ERADQILVL 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-205 |
1.03e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.04 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 1 MVAAPPPSRSPTREAGAAADVLRVAHLGVrLD----HAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVP--HT 74
Cdd:PRK13549 239 MVGRELTALYPREPHTIGEVILEVRNLTA-WDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgrWE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 75 GTVEWSG---SVR---------IGYVPQNF----VVTDVP----ITVRDFLGFKSGAGFEESLAAVGLGSAVlpKRLDV- 133
Cdd:PRK13549 318 GEIFIDGkpvKIRnpqqaiaqgIAMVPEDRkrdgIVPVMGvgknITLAALDRFTGGSRIDDAAELKTILESI--QRLKVk 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 134 ----------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKEtNITVFLITHDLHIVSQYSDA 203
Cdd:PRK13549 396 taspelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDR 474
|
..
gi 1670356525 204 VL 205
Cdd:PRK13549 475 VL 476
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-209 |
1.48e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.81 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAP-----ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVeWSGSVRIGYVPQNFVV 94
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkSKYGTI-QVGDIYIGDKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 95 TDVPIT--VRDFLGFKSGAGF-----------------------------EES-------LAAVGLGSAVLPKRLDVLSG 136
Cdd:PRK13631 100 ITNPYSkkIKNFKELRRRVSMvfqfpeyqlfkdtiekdimfgpvalgvkkSEAkklakfyLNKMGLDDSYLERSPFGLSG 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1670356525 137 GEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYEsLNRLEKETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVIVMDK 251
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-193 |
1.65e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.82 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLvpHTGTVEWSGSV---------------RIG 86
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGT--LSPAFSASGEVllngrrltalpaeqrRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 87 YVPQnfvvtDVPI----TVRDFLGFKSGAGF---------EESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPN 153
Cdd:COG4136 80 ILFQ-----DDLLfphlSVGENLAFALPPTIgraqrrarvEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1670356525 154 VLLFDEPTATVDIG-SEDMLYESLNRLeKETNITVFLITHD 193
Cdd:COG4136 154 ALLLDEPFSKLDAAlRAQFREFVFEQI-RQRGIPALLVTHD 193
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-228 |
1.82e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.79 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 8 SRSPTREAGAAADVLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGsVRIG 86
Cdd:PRK11607 6 PRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLDG-VDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 87 YVPQnfvvTDVPITvrdfLGFKSGAGFE----ESLAAVGLGSAVLPK----------------------RLDVLSGGEMQ 140
Cdd:PRK11607 85 HVPP----YQRPIN----MMFQSYALFPhmtvEQNIAFGLKQDKLPKaeiasrvnemlglvhmqefakrKPHQLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 141 RVLIAWAVLDRPNVLLFDEPTATVDIGSED-MLYESLNRLEKeTNITVFLITHDLHIVSQYSDAVLALNRtvrffGASSR 219
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDrMQLEVVDILER-VGVTCVMVTHDQEEAMTMAGRIAIMNR-----GKFVQ 230
|
....*....
gi 1670356525 220 FSEPELLME 228
Cdd:PRK11607 231 IGEPEEIYE 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
39-205 |
1.84e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 39 DVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVEWSGSVRIG-------------YVPQNFVVT----DVPIT- 100
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINalstaqrlarglvYLPEDRQSSglylDAPLAw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 101 -----VRDFLGF-----KSGAGFEESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSED 170
Cdd:PRK15439 361 nvcalTHNRRGFwikpaRENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190
....*....|....*....|....*....|....*
gi 1670356525 171 MLYESLNRLEKEtNITVFLITHDLHIVSQYSDAVL 205
Cdd:PRK15439 441 DIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVL 474
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
17-208 |
1.86e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.79 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 17 AAADVLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGS----------VRI 85
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYkPTGGTILLRGQhieglpghqiARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 86 GYVP--QNFVVTDVPITVRDFL---------GFKSG----AGFEES-----------LAAVGLGSaVLPKRLDVLSGGEM 139
Cdd:PRK11300 81 GVVRtfQHVRLFREMTVIENLLvaqhqqlktGLFSGllktPAFRRAesealdraatwLERVGLLE-HANRQAGNLAYGQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1670356525 140 QRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALN 208
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVN 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
32-225 |
3.84e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.02 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG----------SVR--IGYVPQNFVVTDVP 98
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQKGKVLVSGidtgdfsklqGIRklVGIVFQNPETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 ITVRDFLGF----------KSGAGFEESLAAVGLGSAVL--PKrldVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDI 166
Cdd:PRK13644 93 RTVEEDLAFgpenlclppiEIRKRVDRALAEIGLEKYRHrsPK---TLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1670356525 167 GSEDMLYESLNRLEkETNITVFLITHDLHIVsQYSDAVLALNR-TVRFFGA-SSRFSEPEL 225
Cdd:PRK13644 170 DSGIAVLERIKKLH-EKGKTIVYITHNLEEL-HDADRIIVMDRgKIVLEGEpENVLSDVSL 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
37-229 |
4.71e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 69.74 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPH------------TGTVEWSGSVRIGYVPQNFVVTDVPITVRDF 104
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEfegkvkidgellTAENVWNLRRKIGMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 105 LGF---KSGAGFEESLAAVG---LGSAVL------PKRLdvlSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDML 172
Cdd:PRK13642 103 VAFgmeNQGIPREEMIKRVDealLAVNMLdfktrePARL---SGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1670356525 173 YESLNRLEKETNITVFLITHDLHIVSQySDAVLAL--NRTVRFFGASSRFSEPELLMEI 229
Cdd:PRK13642 180 MRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMkaGEIIKEAAPSELFATSEDMVEI 237
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
36-179 |
5.32e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.85 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPhtGTVEWSGSVRI--------------GYVPQN--FVVTdvpI 99
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSP--KGVKGSGSVLLngmpidakemraisAYVQQDdlFIPT---L 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 TVRDFLGF-----------KSG--AGFEESLAAVGLGSAV-----LPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPT 161
Cdd:TIGR00955 115 TVREHLMFqahlrmprrvtKKEkrERVDEVLQALGLRKCAntrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170
....*....|....*...
gi 1670356525 162 ATVDIGSEDMLYESLNRL 179
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGL 212
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
28-223 |
5.44e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.34 E-value: 5.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 28 GVRLD-HAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPhTGTVEWSGSVRIGYVP---------------QN 91
Cdd:PRK10418 9 NIALQaAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILP-AGVRQTAGRVLLDGKPvapcalrgrkiatimQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 92 FVVTDVPI---------TVRDFLGFKSGAGFEESLAAVGLGSA--VLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:PRK10418 88 PRSAFNPLhtmhthareTCLALGKPADDATLTAALEAVGLENAarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 161 TATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSD--AVLALNRTVRFFGASSRFSEP 223
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADdvAVMSHGRIVEQGDVETLFNAP 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-192 |
5.76e-14 |
|
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: 68.67 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 30 RLDHAPILEDVSFhvRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGsVRIGYVPqnfvVTDVPI--------- 99
Cdd:cd03298 9 SYGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLING-VDVTAAP----PADRPVsmlfqennl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 ----TVRDFLGFKSGAGF----------EESLAAVGLGSavLPKRL-DVLSGGEMQRVLIAWAVL-DRPnVLLFDEPTAT 163
Cdd:cd03298 82 fahlTVEQNVGLGLSPGLkltaedrqaiEVALARVGLAG--LEKRLpGELSGGERQRVALARVLVrDKP-VLLLDEPFAA 158
|
170 180
....*....|....*....|....*....
gi 1670356525 164 VDIGSEDMLYESLNRLEKETNITVFLITH 192
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTH 187
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-194 |
5.89e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.18 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEW---SGSVRI------------ 85
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSArLAPDAGEVHYrmrDGQLRDlyalseaerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 86 -----GYVPQNfvvtdvpitVRDFL--GFKSGAGFEESLAAVG------LGSAVL---------PKRLDVL----SGGEM 139
Cdd:PRK11701 87 lrtewGFVHQH---------PRDGLrmQVSAGGNIGERLMAVGarhygdIRATAGdwlerveidAARIDDLpttfSGGMQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 140 QRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDL 194
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDL 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
35-209 |
8.93e-14 |
|
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: 67.34 E-value: 8.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSG----------SVRIGYVPQNFVVTDVpiTVRD 103
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGvpvsdlekalSSLISVLNQRPYLFDT--TLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 104 FLGFKsgagfeeslaavglgsavlpkrldvLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLnrLEKET 183
Cdd:cd03247 94 NLGRR-------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI--FEVLK 146
|
170 180
....*....|....*....|....*.
gi 1670356525 184 NITVFLITHDLHIVSQYsDAVLALNR 209
Cdd:cd03247 147 DKTLIWITHHLTGIEHM-DKILFLEN 171
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-238 |
1.02e-13 |
|
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: 70.22 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL---VPHTGTVEWSGSV--RIGYV-PQNFVVT 95
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyEPTSGRIIYHVALceKCGYVeRPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 96 DVPIT-------VRDFLGF-----------------KSGAGFEE---------SLAAVGL-GSAVLPKRLDV-------- 133
Cdd:TIGR03269 81 PCPVCggtlepeEVDFWNLsdklrrrirkriaimlqRTFALYGDdtvldnvleALEEIGYeGKEAVGRAVDLiemvqlsh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 134 --------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVL 205
Cdd:TIGR03269 161 rithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270
....*....|....*....|....*....|...
gi 1670356525 206 ALNRtvrffGASSRFSEPELLMEIFGSGAGLVE 238
Cdd:TIGR03269 241 WLEN-----GEIKEEGTPDEVVAVFMEGVSEVE 268
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
40-199 |
1.62e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.00 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 40 VSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTV-----EWSGSVRIGYVP---QNFVVTDVPITVRDFL------ 105
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVmaeklEFNGQDLQRISEkerRNLVGAEVAMIFQDPMtslnpc 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 106 ---GFK---------SGAGFEESLAAVGLGSAV-LP---KRLDV----LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVD 165
Cdd:PRK11022 106 ytvGFQimeaikvhqGGNKKTRRQRAIDLLNQVgIPdpaSRLDVyphqLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
170 180 190
....*....|....*....|....*....|....
gi 1670356525 166 IGSEDMLYESLNRLEKETNITVFLITHDLHIVSQ 199
Cdd:PRK11022 186 VTIQAQIIELLLELQQKENMALVLITHDLALVAE 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
22-209 |
1.63e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.07 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGSV----------------- 83
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLeKPSEGSIVVNGQTinlvrdkdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 -------RIGYVPQNFV----------VTDVPITVrdfLGFKSGAGFEES---LAAVGLGSAVLPKRLDVLSGGEMQRVL 143
Cdd:PRK10619 86 qlrllrtRLTMVFQHFNlwshmtvlenVMEAPIQV---LGLSKQEARERAvkyLAKVGIDERAQGKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1670356525 144 IAWAVLDRPNVLLFDEPTATVDigsEDMLYESLNRLEK--ETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALD---PELVGEVLRIMQQlaEEGKTMVVVTHEMGFARHVSSHVIFLHQ 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-197 |
1.83e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 7 PSRSPTREAGAAADVLRVAHLGV-----------RLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTG 75
Cdd:PRK15134 261 PSGDPVPLPEPASPLLDVEQLQVafpirkgilkrTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 76 TVEWSGSV--------------RIGYVPQNFVVTDVP-ITVRDFL--GFK------SGAGFEE----SLAAVGLGSAVLP 128
Cdd:PRK15134 341 EIWFDGQPlhnlnrrqllpvrhRIQVVFQDPNSSLNPrLNVLQIIeeGLRvhqptlSAAQREQqviaVMEEVGLDPETRH 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1670356525 129 KRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIV 197
Cdd:PRK15134 421 RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVV 489
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-205 |
1.99e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.38 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT--GTVEWSGSVriGYVPQnfVVTDVPITVRDFLGFksGAG 112
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRsdASVVIRGTV--AYVPQ--VSWIFNATVRDNILF--GSP 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 113 FEESLAAVGLGSAVLPKRLDVL---------------SGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLN 177
Cdd:PLN03130 705 FDPERYERAIDVTALQHDLDLLpggdlteigergvniSGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCI 784
|
170 180 190
....*....|....*....|....*....|
gi 1670356525 178 R--LEKETNItvfLITHDLHIVSQYSDAVL 205
Cdd:PLN03130 785 KdeLRGKTRV---LVTNQLHFLSQVDRIIL 811
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
35-209 |
2.56e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 68.81 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGSVRIGYVPQNFVVtDVPITVR----------- 102
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKDFNGEARPQPGIKVGYLPQEPQL-DPTKTVRenveegvaeik 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 103 --------------------DFLgFKSGAGFEESLAAVGLGSavLPKRLDV----------------LSGGEMQRVLIAW 146
Cdd:TIGR03719 98 daldrfneisakyaepdadfDKL-AAEQAELQEIIDAADAWD--LDSQLEIamdalrcppwdadvtkLSGGERRRVALCR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 147 AVLDRPNVLLFDEPTATVDIgsedmlyESLNRLE---KETNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLDA-------ESVAWLErhlQEYPGTVVAVTHDRYFLDNVAGWILELDR 233
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-234 |
3.19e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.17 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVEWSGSVRIgyVPQNFVVTDV-PITVRDFLG-------- 106
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRL--FGRNIYSPDVdPIEVRREVGmvfqypnp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 107 FKSGAGFEESLAAVGLGSAVLPK----------------------RLD----VLSGGEMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLVKSKkeldervewalkkaalwdevkdRLNdypsNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1670356525 161 TATVDIGSEDMLYESLNRLEKEtnITVFLITHDLHIVSQYSD--AVLALNRTVRFFGASSRFSEPE-LLMEIFGSGA 234
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDyvAFLYLGKLIEVGPTRKVFENPEhELTEKYVTGA 251
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
52-209 |
1.11e-12 |
|
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: 66.36 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 52 IVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGS--------VR-IGYVPQNFVVtdVP-ITVRDFLGF---KSGAGFEE-- 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEqPDSGSIMLDGEdvtnvpphLRhINMVFQSYAL--FPhMTVEENVAFglkMRKVPRAEik 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 116 -----SLAAVGLGSAVlPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLI 190
Cdd:TIGR01187 79 prvleALRLVQLEEFA-DRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFV 157
|
170
....*....|....*....
gi 1670356525 191 THDLHIVSQYSDAVLALNR 209
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRK 176
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
30-194 |
1.63e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.11 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 30 RLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTG--------TVEwSGSVRI-------GYVPQNF-- 92
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSgdlivdglKVN-DPKVDErlirqeaGMVFQQFyl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 93 -----VVTDV---PITVRdflgfksGAGFEES-------LAAVGLGSAV--LPKRLdvlSGGEMQRVLIAWAVLDRPNVL 155
Cdd:PRK09493 89 fphltALENVmfgPLRVR-------GASKEEAekqarelLAKVGLAERAhhYPSEL---SGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1670356525 156 LFDEPTATVDigsEDMLYESLNRLEK--ETNITVFLITHDL 194
Cdd:PRK09493 159 LFDEPTSALD---PELRHEVLKVMQDlaEEGMTMVIVTHEI 196
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-198 |
2.04e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.42 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PIL-EDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGSVRIGYVPQNFV----VTDVPI--TVRDFLG 106
Cdd:PLN03073 522 PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQPSSGTVFRSAKVRMAVFSQHHVdgldLSSNPLlyMMRCFPG 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 107 FKSgAGFEESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKetniT 186
Cdd:PLN03073 602 VPE-QKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG----G 676
|
170
....*....|..
gi 1670356525 187 VFLITHDLHIVS 198
Cdd:PLN03073 677 VLMVSHDEHLIS 688
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-199 |
2.07e-12 |
|
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: 66.51 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 9 RSPTREAGAAADVLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSVriGY 87
Cdd:TIGR00957 626 RRTIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVeGHVHMKGSV--AY 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 88 VPQNFVVTDVpiTVRDFLGFksGAGFEES-LAAVGLGSAVLP--------KRLDV------LSGGEMQRVLIAWAVLDRP 152
Cdd:TIGR00957 704 VPQQAWIQND--SLRENILF--GKALNEKyYQQVLEACALLPdleilpsgDRTEIgekgvnLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1670356525 153 NVLLFDEPTATVD-----------IGSEDMLyeslnrlekeTNITVFLITHDLHIVSQ 199
Cdd:TIGR00957 780 DIYLFDDPLSAVDahvgkhifehvIGPEGVL----------KNKTRILVTHGISYLPQ 827
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
37-205 |
2.12e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.76 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRvLLGLV--PHTGTVEWSGsvrigyvpQNFVVTDvPITVRDF-----LGF-- 107
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLAR-LLTMIetPTGGELYYQG--------QDLLKAD-PEAQKLLrqkiqIVFqn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 108 ---------KSGAGFEESL-------------------AAVGLGsavlPKRLD----VLSGGEMQRVLIAWAVLDRPNVL 155
Cdd:PRK11308 101 pygslnprkKVGQILEEPLlintslsaaerrekalammAKVGLR----PEHYDryphMFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1670356525 156 LFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVL 205
Cdd:PRK11308 177 VADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVM 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
39-192 |
3.01e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 39 DVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSV----------RIGYVPQNF-VVTDvpITVRDFL- 105
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASeGEAWLFGQPvdagdiatrrRVGYMSQAFsLYGE--LTVRQNLe 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 106 ---------GFKSGAGFEESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESL 176
Cdd:NF033858 362 lharlfhlpAAEIAARVAEMLERFDLA-DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLL 440
|
170
....*....|....*.
gi 1670356525 177 NRLEKETNITVFLITH 192
Cdd:NF033858 441 IELSREDGVTIFISTH 456
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
30-207 |
3.80e-12 |
|
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: 63.44 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 30 RLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVEwsGSVR----------------IGYVPQNfv 93
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVE--GDIHyngipykefaekypgeIIYVSEE-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 94 vtDV---PITVRDFLGFksgagfeeslAAVGLGSAVLpkRldVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSED 170
Cdd:cd03233 92 --DVhfpTLTVRETLDF----------ALRCKGNEFV--R--GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1670356525 171 MLYESLNRLEKETNITVFLithdlhIVSQYSDAVLAL 207
Cdd:cd03233 156 EILKCIRTMADVLKTTTFV------SLYQASDEIYDL 186
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
134-211 |
4.12e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.82 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 134 LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDA--VLALNRTV 211
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKinVLYCGQTV 238
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
21-202 |
4.39e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.03 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVL--LG-LVPH---TGTVEWSG----SVR------ 84
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNdLNPEvtiTGSIVYNGhniySPRtdtvdl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 85 ---IGYV---PQNFvvtdvPITVRDFL-------GFKSGAGFEESLAAVGLGSAVLPKRLDVL-------SGGEMQRVLI 144
Cdd:PRK14239 85 rkeIGMVfqqPNPF-----PMSIYENVvyglrlkGIKDKQVLDEAVEKSLKGASIWDEVKDRLhdsalglSGGQQQRVCI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1670356525 145 AWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKEtnITVFLITHDLHIVSQYSD 202
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISD 215
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-204 |
5.40e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 63.60 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGS----------VRIGyVP 89
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTrPDSGSVLFGGTdltgldeheiARLG-IG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 90 QNFVVTDV--PITVRD--------------FLGFKSGAG----FEESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVL 149
Cdd:COG4674 89 RKFQKPTVfeELTVFEnlelalkgdrgvfaSLFARLTAEerdrIEEVLETIGL-TDKADRLAGLLSHGQKQWLEIGMLLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 150 DRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETniTVFLITHDLHIVSQYSDAV 204
Cdd:COG4674 168 QDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH--SVVVVEHDMEFVRQIARKV 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
37-204 |
9.27e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 63.67 E-value: 9.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSV--------------------RIGYVPQNF---- 92
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPT-----SGRVlvdgqdltalsekelrkarrQIGMIFQHFnlls 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 93 ---VVTDV--PITVRDFLGFKSGAGFEESLAAVGLGSavlpKRlDV----LSGGEMQRVLIAWAVLDRPNVLLFDEPTAT 163
Cdd:PRK11153 96 srtVFDNValPLELAGTPKAEIKARVTELLELVGLSD----KA-DRypaqLSGGQKQRVAIARALASNPKVLLCDEATSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1670356525 164 VDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAV 204
Cdd:PRK11153 171 LDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRV 211
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-179 |
1.73e-11 |
|
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: 61.49 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 29 VRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVL-----LGLVphTGTVEWSG-------SVRIGYVPQNFVVTD 96
Cdd:cd03232 15 VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVI--TGEILINGrpldknfQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 97 VpITVRDFLGFksgagfeeslaavglgSAVLPKrldvLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESL 176
Cdd:cd03232 93 N-LTVREALRF----------------SALLRG----LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
...
gi 1670356525 177 NRL 179
Cdd:cd03232 152 KKL 154
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-204 |
1.73e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.39 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSVRIGYVPQNFV-VTD---------------VP-I 99
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD-----AGSILIDGQEMRFAsTTAalaagvaiiyqelhlVPeM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 TVRD--FLG-FKSGAGF--EESLAAV------GLGSAVLPK-RLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIG 167
Cdd:PRK11288 95 TVAEnlYLGqLPHKGGIvnRRLLNYEareqleHLGVDIDPDtPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1670356525 168 SEDMLYESLNRLEKETNITVFlITHDLHIVSQYSDAV 204
Cdd:PRK11288 175 EIEQLFRVIRELRAEGRVILY-VSHRMEEIFALCDAI 210
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-162 |
1.91e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.36 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSvrigyvpqnfvvtdvPI 99
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLArPDAGEVLWQGE---------------PI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 -TVRD-------FLGFKSG-----AGFE------------------ESLAAVGL-GSAVLPKRldVLSGGEMQRVLIAWA 147
Cdd:PRK13538 66 rRQRDeyhqdllYLGHQPGiktelTALEnlrfyqrlhgpgddealwEALAQVGLaGFEDVPVR--QLSAGQQRRVALARL 143
|
170
....*....|....*.
gi 1670356525 148 VLDRPNVLLFDEP-TA 162
Cdd:PRK13538 144 WLTRAPLWILDEPfTA 159
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
37-205 |
2.05e-11 |
|
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: 60.80 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLfrVLLGLvphtgtvEWSGSVRIGYVPQNFvvTDVPITVRDFLGFksgagfees 116
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGL-------YASGKARLISFLPKF--SRNKLIFIDQLQF--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 117 LAAVGLGSAVLPKRLDVLSGGEMQRVLIAW--AVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNiTVFLITHDL 194
Cdd:cd03238 71 LIDVGLGYLTLGQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNL 149
|
170
....*....|.
gi 1670356525 195 HiVSQYSDAVL 205
Cdd:cd03238 150 D-VLSSADWII 159
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
36-192 |
2.13e-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: 63.39 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVEWSG----SVRI-------GYVPQN-FVVTDvpiTVRD 103
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGvswnSVTLqtwrkafGVIPQKvFIFSG---TFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 104 FLGFKSGAGFEE---SLAAVGLGSAV--LPKRLD--------VLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDigseD 170
Cdd:TIGR01271 1311 NLDPYEQWSDEEiwkVAEEVGLKSVIeqFPDKLDfvlvdggyVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD----P 1386
|
170 180
....*....|....*....|....
gi 1670356525 171 MLYESLNRLEKET--NITVFLITH 192
Cdd:TIGR01271 1387 VTLQIIRKTLKQSfsNCTVILSEH 1410
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
35-205 |
2.53e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.11 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVP-HTGTVEWSG---------SVR--IGYVPQN-FVVTDvpiTV 101
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDiDEGEILLDGhdlrdytlaSLRnqVALVSQNvHLFND---TI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 102 RDFLGFKSGAGF--EESLAAVGLGSAV-----LPKRLDV--------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDI 166
Cdd:PRK11176 434 ANNIAYARTEQYsrEQIEEAARMAYAMdfinkMDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
170 180 190
....*....|....*....|....*....|....*....
gi 1670356525 167 GSEDMLYESLNRLEKetNITVFLITHDLHIVSQySDAVL 205
Cdd:PRK11176 514 ESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEIL 549
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
37-204 |
3.65e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHtGTveWSGSVRIGYVPQNF-------------------VVTDV 97
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPH-GT--YEGEIIFEGEELQAsnirdteragiaiihqelaLVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 PITVRDFLGFKSGAG-----------FEESLAAVGLGSAVLPKRLDvLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDI 166
Cdd:PRK13549 98 SVLENIFLGNEITPGgimdydamylrAQKLLAQLKLDINPATPVGN-LGLGQQQLVEIAKALNKQARLLILDEPTASLTE 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1670356525 167 GSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAV 204
Cdd:PRK13549 177 SETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTI 213
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
36-245 |
5.27e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.49 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSV----RIGYVPQNFVVTDVpiTVRDFLGFksga 111
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS-----EGRVwaerSIAYVPQQAWIMNA--TVRGNILF---- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 112 gFEESLAAvGLGSAV-----------LPKRLDV--------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVD--IGSED 170
Cdd:PTZ00243 744 -FDEEDAA-RLADAVrvsqleadlaqLGGGLETeigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDahVGERV 821
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 171 MLYESLNRLEKETNItvfLITHDLHIVSQySDAVLALNR-TVRFFGASSRFSEPELLMEIfgsGAGLVEHKHDFGA 245
Cdd:PTZ00243 822 VEECFLGALAGKTRV---LATHQVHVVPR-ADYVVALGDgRVEFSGSSADFMRTSLYATL---AAELKENKDSKEG 890
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-193 |
7.61e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGSVRIGYVPQNFVVtDVPITVR----------- 102
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKEFEGEARPAPGIKVGYLPQEPQL-DPEKTVRenveegvaevk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 103 --------------------DFLgFKSGAGFEESLAAVG---LGSAV--------LP---KRLDVLSGGEMQRVLIAWAV 148
Cdd:PRK11819 100 aaldrfneiyaayaepdadfDAL-AAEQGELQEIIDAADawdLDSQLeiamdalrCPpwdAKVTKLSGGERRRVALCRLL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1670356525 149 LDRPNVLLFDEPTATVDIgsedmlyESLNRLE---KETNITVFLITHD 193
Cdd:PRK11819 179 LEKPDMLLLDEPTNHLDA-------ESVAWLEqflHDYPGTVVAVTHD 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
32-195 |
8.63e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 61.38 E-value: 8.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLlglvphtgTVEW---SGSVRIGYVP-QNF----------VVTD- 96
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL--------TRAWdpqQGEILLNGQPiADYseaalrqaisVVSQr 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 97 VPI---TVRDFLGFKSGAGFEESLAA----VGLGSAV-LPKRLDV--------LSGGEMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:PRK11160 423 VHLfsaTLRDNLLLAAPNASDEALIEvlqqVGLEKLLeDDKGLNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEP 502
|
170 180 190
....*....|....*....|....*....|....*
gi 1670356525 161 TATVDIGSEDMLYESLNRLEKetNITVFLITHDLH 195
Cdd:PRK11160 503 TEGLDAETERQILELLAEHAQ--NKTVLMITHRLT 535
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
134-202 |
9.16e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 60.69 E-value: 9.16e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1670356525 134 LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSD 202
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWAD 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
36-165 |
1.05e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.91 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPH-TGTV------------EWSGSVRIGYVPQN------FVVTD 96
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRdAGNIiiddedisllplHARARRGIGYLPQEasifrrLSVYD 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1670356525 97 ---VPITVRDFLGFKSGAGFEESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVD 165
Cdd:PRK10895 98 nlmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-192 |
1.22e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT---GTVEWSGSVRIGYVPQN------ 91
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKileGDILFKGESILDLEPEErahlgi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 92 FVVTDVPITV-----RDFL--GFKSGAGFE---------------ESLAAVGLGSAVLPKRL-DVLSGGEMQRVLIAWAV 148
Cdd:CHL00131 87 FLAFQYPIEIpgvsnADFLrlAYNSKRKFQglpeldplefleiinEKLKLVGMDPSFLSRNVnEGFSGGEKKRNEILQMA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1670356525 149 LDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNiTVFLITH 192
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITH 209
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-224 |
1.26e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.11 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 9 RSPTREAGAAADVLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVEWSGSV----- 83
Cdd:PRK14271 9 QSGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVllggr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 -------------RIGYV---PQNF---VVTDVPITVR--DFLGFKSGAGFEES-LAAVGLGSAVLPKRLDV---LSGGE 138
Cdd:PRK14271 89 sifnyrdvlefrrRVGMLfqrPNPFpmsIMDNVLAGVRahKLVPRKEFRGVAQArLTEVGLWDAVKDRLSDSpfrLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 139 MQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKEtnITVFLITHDLHIVSQYSD--AVLALNRTVRFFGA 216
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDraALFFDGRLVEEGPT 246
|
....*...
gi 1670356525 217 SSRFSEPE 224
Cdd:PRK14271 247 EQLFSSPK 254
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-209 |
1.35e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.54 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 20 DVLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVEWSGSV---------------- 83
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVyldgqdifkmdvielr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 -RIGYV-------PQNFVVTDVPITVRDFLGFKSGAGFEE----SLAAVGLGSAVlPKRLDV----LSGGEMQRVLIAWA 147
Cdd:PRK14247 82 rRVQMVfqipnpiPNLSIFENVALGLKLNRLVKSKKELQErvrwALEKAQLWDEV-KDRLDApagkLSGGQQQRLCIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1670356525 148 VLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKEtnITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYK 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
30-207 |
1.59e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.80 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 30 RLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG-----------SVRIGYVPQNFV---- 93
Cdd:PRK15112 22 RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIePTSGELLIDDhplhfgdysyrSQRIRMIFQDPStsln 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 94 -------VTDVPITVR-DFLGFKSGAGFEESLAAVGLgsavLPKRLD----VLSGGEMQRVLIAWAVLDRPNVLLFDEPT 161
Cdd:PRK15112 102 prqrisqILDFPLRLNtDLEPEQREKQIIETLRQVGL----LPDHASyyphMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1670356525 162 ATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLAL 207
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVM 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
35-229 |
1.73e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSVRIGYVP---QNFVVTDVP--------ITVR 102
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVpPDSGTLEIGGNPCARLTPakaHQLGIYLVPqepllfpnLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 103 D--FLGFKSGAGFEESLAAV--GLGSAVlpkRLDVLSG----GEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYE 174
Cdd:PRK15439 105 EniLFGLPKRQASMQKMKQLlaALGCQL---DLDSSAGslevADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFS 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 175 SLNRLEKEtNITVFLITHDLHIVSQYSDAVLAL-NRTVRFFGASSRFSEPELLMEI 229
Cdd:PRK15439 182 RIRELLAQ-GVGIVFISHKLPEIRQLADRISVMrDGTIALSGKTADLSTDDIIQAI 236
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
17-165 |
1.80e-10 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 59.43 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 17 AAADVLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGSV------------ 83
Cdd:COG4598 4 TAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLeTPDSGEIRVGGEEirlkpdrdgelv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 ------------RIGYVPQNFV----------VTDVPITVrdfLGFKSGAGFEES---LAAVGLGsavlpKRLDV----L 134
Cdd:COG4598 84 padrrqlqrirtRLGMVFQSFNlwshmtvlenVIEAPVHV---LGRPKAEAIERAealLAKVGLA-----DKRDAypahL 155
|
170 180 190
....*....|....*....|....*....|.
gi 1670356525 135 SGGEMQRVLIAWAVLDRPNVLLFDEPTATVD 165
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
37-204 |
1.86e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.19 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPH---TGTVEWSGSVR------------IGYVPQNFVVtdVP--- 98
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsyEGEILFDGEVCrfkdirdsealgIVIIHQELAL--IPyls 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 ITVRDFLG---FKSG--------AGFEESLAAVGLG--SAVLPKRLDVlsgGEMQRVLIAWAVLDRPNVLLFDEPTATVd 165
Cdd:NF040905 95 IAENIFLGnerAKRGvidwnetnRRARELLAKVGLDesPDTLVTDIGV---GKQQLVEIAKALSKDVKLLILDEPTAAL- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1670356525 166 igSEDmlyESLNRLE-----KETNITVFLITHDLHIVSQYSDAV 204
Cdd:NF040905 171 --NEE---DSAALLDlllelKAQGITSIIISHKLNEIRRVADSI 209
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-160 |
1.95e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 7 PSRSPTREAGAAADVLRvaHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPH------------- 73
Cdd:PRK10938 248 PSARHALPANEPRIVLN--NGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQgysndltlfgrrr 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 74 -TGTVEWSGSVRIGYVPQNFVVT-DVPITVRDFL--GFKSGAGF------------EESLAAVGLGSAVLPKRLDVLSGG 137
Cdd:PRK10938 326 gSGETIWDIKKHIGYVSSSLHLDyRVSTSVRNVIlsGFFDSIGIyqavsdrqqklaQQWLDILGIDKRTADAPFHSLSWG 405
|
170 180
....*....|....*....|...
gi 1670356525 138 EMQRVLIAWAVLDRPNVLLFDEP 160
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEP 428
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
35-195 |
2.24e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.29 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGSVRIGYVPQ------NFVVTDVPI-------- 99
Cdd:PRK15064 15 PLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGdLEPSAGNVSLDPNERLGKLRQdqfafeEFTVLDTVImghtelwe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 100 --TVRDFL----------GFK------------------------SGAGFEESLAAvGLGSAVLPkrldvlsgGEMQRVL 143
Cdd:PRK15064 95 vkQERDRIyalpemseedGMKvadlevkfaemdgytaearagellLGVGIPEEQHY-GLMSEVAP--------GWKLRVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1670356525 144 IAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNrlekETNITVFLITHDLH 195
Cdd:PRK15064 166 LAQALFSNPDILLLDEPTNNLDINTIRWLEDVLN----ERNSTMIIISHDRH 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
32-193 |
2.40e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.66 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 32 DHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSVRIGYVPQNfvvtDVP------------- 98
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDIT-----SGDLFIGEKRMN----DVPpaergvgmvfqsy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 -----ITVRDFLGFK---SGAGFEESLAAVGLGSAVL---------PKrldVLSGGEMQRVLIAWAVLDRPNVLLFDEPT 161
Cdd:PRK11000 85 alyphLSVAENMSFGlklAGAKKEEINQRVNQVAEVLqlahlldrkPK---ALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190
....*....|....*....|....*....|..
gi 1670356525 162 ATVDIGSEDMLYESLNRLEKETNITVFLITHD 193
Cdd:PRK11000 162 SNLDAALRVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
35-194 |
2.45e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.01 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGSvrigyvpqnfvvtDVPITVRDFLG------- 106
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGqIAPDHGEILFDGE-------------NIPAMSRSRLYtvrkrms 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 107 --FKSGAGFEE----------------------------SLAAVGL-GSAVL-PKRldvLSGGEMQRVLIAWAVLDRPNV 154
Cdd:PRK11831 88 mlFQSGALFTDmnvfdnvayplrehtqlpapllhstvmmKLEAVGLrGAAKLmPSE---LSGGMARRAALARAIALEPDL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1670356525 155 LLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDL 194
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-236 |
4.25e-10 |
|
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: 59.57 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 3 AAPPPSRSPTREAGaaadvLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTT----LFRVLLGLvphTGTVE 78
Cdd:TIGR00957 1273 TAPPSGWPPRGRVE-----FRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINESA---EGEII 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 79 WSG--SVRIGYVPQNFVVTDVPI-------TVRDFLGFKSGAGFEESLAAVGLGS-----AVLPKRLDV--------LSG 136
Cdd:TIGR00957 1345 IDGlnIAKIGLHDLRFKITIIPQdpvlfsgSLRMNLDPFSQYSDEEVWWALELAHlktfvSALPDKLDHecaeggenLSV 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 137 GEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLyESLNRLEKETnITVFLITHDLHIVSQYSDAVLALNRTVRFFGA 216
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI-QSTIRTQFED-CTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGA 1502
|
250 260
....*....|....*....|
gi 1670356525 217 SSRFSEPELLMEIFGSGAGL 236
Cdd:TIGR00957 1503 PSNLLQQRGIFYSMAKDAGL 1522
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
39-226 |
4.81e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 39 DVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPH-TGTVEWSG----------SVR--IGYVPQ---------NFVVTD 96
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRaGGEIRLNGkdisprspldAVKkgMAYITEsrrdngffpNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 97 vPITVRDFL---GFKSGAGF----------EESLAAVGLGSAVLPKRLDVLSGGEMQRVLIA-WAVLDrPNVLLFDEPTA 162
Cdd:PRK09700 361 -NMAISRSLkdgGYKGAMGLfhevdeqrtaENQRELLALKCHSVNQNITELSGGNQQKVLISkWLCCC-PEVIIFDEPTR 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 163 TVDIGSEDMLYESLNRLEKEtNITVFLITHDLHIVSQYSD--AVLALNRTVRFFGASSRFSEPELL 226
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDriAVFCEGRLTQILTNRDDMSEEEIM 503
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-232 |
7.78e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 7.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 6 PPSRSPTREAGAAADVlrvaHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVphtgTVEwSGSVRI 85
Cdd:PLN03232 1225 PVSGWPSRGSIKFEDV----HLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIV----ELE-KGRIMI 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 86 -GYVPQNFVVTDV----------PI----TVR---DFLGFKSGAGFEESLAAVGLGSAVL--PKRLD--VLSGGEM---- 139
Cdd:PLN03232 1296 dDCDVAKFGLTDLrrvlsiipqsPVlfsgTVRfniDPFSEHNDADLWEALERAHIKDVIDrnPFGLDaeVSEGGENfsvg 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 140 QRVL--IAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNrlEKETNITVFLITHDLHIVSQySDAVLALNRtvrffGAS 217
Cdd:PLN03232 1376 QRQLlsLARALLRRSKILVLDEATASVDVRTDSLIQRTIR--EEFKSCTMLVIAHRLNTIID-CDKILVLSS-----GQV 1447
|
250
....*....|....*
gi 1670356525 218 SRFSEPELLMEIFGS 232
Cdd:PLN03232 1448 LEYDSPQELLSRDTS 1462
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-224 |
8.94e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 33 HApiLEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSvRIGYVPQ----------NFVVTDV---- 97
Cdd:PRK10261 338 HA--VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVeSQGGEIIFNGQ-RIDTLSPgklqalrrdiQFIFQDPyasl 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 ------------PITVRDFL-GFKSGAGFEESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATV 164
Cdd:PRK10261 415 dprqtvgdsimePLRVHGLLpGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1670356525 165 DIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSD--AVLALNRTVRFFGASSRFSEPE 224
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHrvAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-202 |
1.05e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.10 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRV---LLGLVPhTGTVEWsgsvRIGYVPQNFVVTDV 97
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIP-GFRVEG----KVTFHGKNLYAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 -PITVRDFLGF---------KS-------GA---GF--------EESLAAVGLGSAVLPKRLD---VLSGGEMQRVLIAW 146
Cdd:PRK14243 85 dPVEVRRRIGMvfqkpnpfpKSiydniayGArinGYkgdmdelvERSLRQAALWDEVKDKLKQsglSLSGGQQQRLCIAR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 147 AVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKEtnITVFLITHDLHIVSQYSD 202
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
46-196 |
2.12e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.69 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 46 RGTTLAIVGPNGAGKTTLFRVLLGLvphtgtvewsgsvrIGYVPQNFVVTDVPITVRDFLGFKSGAGFEESLAAvglgsa 125
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE--------------LGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKAS------ 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1670356525 126 vlpkrldvLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDML-----YESLNRLEKETNITVFLITHDLHI 196
Cdd:smart00382 61 --------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLLLLLKSEKNLTVILTTNDEKD 128
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
37-212 |
2.37e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.04 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSVRIGYVPQNFVVTDVPI-----------TVRDF 104
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATsGRIVFDGKDITDWQTAKIMREAVAIvpegrrvfsrmTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 105 LG----FKSGAGFEESLAAV-GLGSAVLPKRLD---VLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESL 176
Cdd:PRK11614 101 LAmggfFAERDQFQERIKWVyELFPRLHERRIQragTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1670356525 177 NRLeKETNITVFLITHDL----------------HIVSQYSDAVLALNRTVR 212
Cdd:PRK11614 181 EQL-REQGMTIFLVEQNAnqalkladrgyvlengHVVLEDTGDALLANEAVR 231
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
35-207 |
2.85e-09 |
|
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: 55.41 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGSVR---------------IGYVPQNFVVTDVp 98
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNKNEsepsfeatrsrnrysVAYAAQKPWLLNA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 iTVRDFLGFksGAGFEESLAAVGLGSAVLPKRLDVL---------------SGGEMQRVLIAWAVLDRPNVLLFDEPTAT 163
Cdd:cd03290 94 -TVEENITF--GSPFNKQRYKAVTDACSLQPDIDLLpfgdqteigerginlSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1670356525 164 VDIG-SEDMLYESLNRLEKETNITVFLITHDLHIVSqYSDAVLAL 207
Cdd:cd03290 171 LDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLP-HADWIIAM 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
36-199 |
3.65e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.66 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGsvrigyvpQNFVVTD---VPITVRDFLGF---- 107
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLdKPTSGTYRVAG--------QDVATLDadaLAQLRREHFGFifqr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 108 ------------------KSGAGFEES-------LAAVGLGSAVlPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTA 162
Cdd:PRK10535 95 yhllshltaaqnvevpavYAGLERKQRllraqelLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1670356525 163 TVDIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQ 199
Cdd:PRK10535 174 ALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ 209
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
37-204 |
3.83e-09 |
|
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: 56.37 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPH---TGTVEWSGS------VR------IGYVPQNF-VVTDVPIT 100
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtwDGEIYWSGSplkasnIRdteragIVIIHQELtLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 101 VRDFLGFK-SGAGFEESLAAVGLGSAVLPKRLDV-----------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGS 168
Cdd:TIGR02633 97 ENIFLGNEiTLPGGRMAYNAMYLRAKNLLRELQLdadnvtrpvgdYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKE 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1670356525 169 EDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAV 204
Cdd:TIGR02633 177 TEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTI 211
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
36-194 |
4.91e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 55.25 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGTVEWSG----SVRI-------GYVPQNFVVTDVPITVR-D 103
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGvswnSVPLqkwrkafGVIPQKVFIFSGTFRKNlD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 104 FLGFKSGAGFEESLAAVGLGSAV--LPKRLD--------VLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDigseDMLY 173
Cdd:cd03289 99 PYGKWSDEEIWKVAEEVGLKSVIeqFPGQLDfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD----PITY 174
|
170 180
....*....|....*....|...
gi 1670356525 174 ESLNRLEKE--TNITVFLITHDL 194
Cdd:cd03289 175 QVIRKTLKQafADCTVILSEHRI 197
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-194 |
5.77e-09 |
|
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: 56.18 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 15 AGAAADVLRVAHLGVRLD--HAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSGSV-------- 83
Cdd:TIGR01257 1931 GGNKTDILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTsGDATVAGKSiltnisdv 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 --RIGYVPQnFVVTDVPITVRDFLGFKS---GAGFEE-----SLAAVGLGSAVLPKRL-DVLSGGEMQRVLIAWAVLDRP 152
Cdd:TIGR01257 2011 hqNMGYCPQ-FDAIDDLLTGREHLYLYArlrGVPAEEiekvaNWSIQSLGLSLYADRLaGTYSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1670356525 153 NVLLFDEPTATVDIGSEDMLYESLNRLEKETNiTVFLITHDL 194
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSM 2130
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-209 |
1.08e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 1.08e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1670356525 134 LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVsQYSDAVLAL-NR 209
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLsNR 655
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
36-208 |
1.19e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.89 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVP---HTGTVEWSGSV-------RIGYVPQNFVVTDvPITVRDFL 105
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnnFTGTILANNRKptkqilkRTGFVTQDDILYP-HLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 106 GF-------KSGAGFEESLAA------VGL----GSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGS 168
Cdd:PLN03211 162 VFcsllrlpKSLTKQEKILVAesviseLGLtkceNTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1670356525 169 EDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALN 208
Cdd:PLN03211 242 AYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLS 281
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-207 |
1.35e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTV------------EWSGSVRIGYV 88
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIhEPTKGTItinninynkldhKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 89 PQNFVVTD------------------VPITVRDFLGFKSGAgfEESLAAVGLgSAVLPKRLDVLSGGEMQRVLIAWAVLD 150
Cdd:PRK09700 86 YQELSVIDeltvlenlyigrhltkkvCGVNIIDWREMRVRA--AMMLLRVGL-KVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1670356525 151 RPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFlITHDLHIVSQYSDAVLAL 207
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVY-ISHKLAEIRRICDRYTVM 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
127-222 |
1.68e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 127 LPKRLDV--------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNITVFLITHDLHIVS 198
Cdd:PTZ00265 1344 LPNKYDTnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
90 100
....*....|....*....|....*..
gi 1670356525 199 QySDAVLALN---RTVRFFGASSRFSE 222
Cdd:PTZ00265 1424 R-SDKIVVFNnpdRTGSFVQAHGTHEE 1449
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
37-229 |
2.63e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.47 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVphtgtVEWSGSVRIG--YVPQNFV----VTDVPITVRDFLGFKSG 110
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-----ISETGQTIVGdyAIPANLKkikeVKRLRKEIGLVFQFPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 111 AGFEESL------AAVGLGS------AVLPKRLDV--------------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATV 164
Cdd:PRK13645 102 QLFQETIekdiafGPVNLGEnkqeayKKVPELLKLvqlpedyvkrspfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1670356525 165 DIGSEDMLYESLNRLEKETNITVFLITHDLHIVSQYSDAVLALN--RTVRFFGASSRFSEPELLMEI 229
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHegKVISIGSPFEIFSNQELLTKI 248
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-205 |
2.69e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 13 REAGAAAdvLRVAHL---GVRldhapilEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG-SVRI-- 85
Cdd:PRK11288 251 RPLGEVR--LRLDGLkgpGLR-------EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATrRTAGQVYLDGkPIDIrs 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 86 -------------------GYVPQNFVVTDVPITVR---DFLGFKSGAGFEESLAAVGLgsavlpKRLDV---------- 133
Cdd:PRK11288 322 prdairagimlcpedrkaeGIIPVHSVADNINISARrhhLRAGCLINNRWEAENADRFI------RSLNIktpsreqlim 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1670356525 134 -LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVL 205
Cdd:PRK11288 396 nLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIV 467
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-193 |
2.75e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 34 APILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVP-HTGTVEWSGSVRIGYVPQNfVVTDVPITVRDFL--GFKSG 110
Cdd:PRK11147 16 APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLlDDGRIIYEQDLIVARLQQD-PPRNVEGTVYDFVaeGIEEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 111 AG--------------------------------------FE----ESLAAVGLGSAvlpKRLDVLSGGEMQRVLIAWAV 148
Cdd:PRK11147 95 AEylkryhdishlvetdpseknlnelaklqeqldhhnlwqLEnrinEVLAQLGLDPD---AALSSLSGGWLRKAALGRAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1670356525 149 LDRPNVLLFDEPTATVDIGSEDMLYESLnrleKETNITVFLITHD 193
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIETIEWLEGFL----KTFQGSIIFISHD 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
35-209 |
4.87e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.18 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSG---------SVR--IGYVPQNFVVTD----VP 98
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTeGEIRLDGrplsslshsVLRqgVAMVQQDPVVLAdtflAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 ITV-RDFlgfkSGAGFEESLAAVGLGSAV--LPKRL--------DVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIG 167
Cdd:PRK10790 435 VTLgRDI----SEEQVWQALETVQLAELArsLPDGLytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG 510
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1670356525 168 SEDMLYESLNRLEKETniTVFLITHDLHIVSQySDAVLALNR 209
Cdd:PRK10790 511 TEQAIQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHR 549
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
51-233 |
4.98e-08 |
|
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: 53.48 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 51 AIVGPNGAGKTTLFRVLLGLVPHT-GTVEWSG--------SVR--IGYVPQNFVVTDvPITVRDFLGFKS---GAGFEES 116
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTsGTVLVGGkdietnldAVRqsLGMCPQHNILFH-HLTVAEHILFYAqlkGRSWEEA 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 117 -------LAAVGLGSAVLPKRLDvLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLnrLEKETNITVFL 189
Cdd:TIGR01257 1039 qlemeamLEDTGLHHKRNEEAQD-LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIM 1115
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1670356525 190 ITHDLHIVSQYSDAVLALNRTvRFFGASSrfsePELLMEIFGSG 233
Cdd:TIGR01257 1116 STHHMDEADLLGDRIAIISQG-RLYCSGT----PLFLKNCFGTG 1154
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-208 |
5.25e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 30 RLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG-----------SVRIGYVPQNFVVtdV 97
Cdd:PLN03130 1248 RPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVeLERGRILIDGcdiskfglmdlRKVLGIIPQAPVL--F 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 PITVR---DFLGFKSGAGFEESLAAVGLGSAVL--PKRLD--VLSGGEM----QRVL--IAWAVLDRPNVLLFDEPTATV 164
Cdd:PLN03130 1326 SGTVRfnlDPFNEHNDADLWESLERAHLKDVIRrnSLGLDaeVSEAGENfsvgQRQLlsLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1670356525 165 DIGSeDMLYESLNRlEKETNITVFLITHDLHIVSQySDAVLALN 208
Cdd:PLN03130 1406 DVRT-DALIQKTIR-EEFKSCTMLIIAHRLNTIID-CDRILVLD 1446
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-194 |
1.25e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 50.74 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHAPILEDvsFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGSVRIGYVPQNFVVTDV--- 97
Cdd:PRK10771 2 LKLTDITWLYHHLPMRFD--LTVERGERVAILGPSGAGKSTLLNLIAGfLTPASGSLTLNGQDHTTTPPSRRPVSMLfqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 -----PITVRDFL------GFKSGAGFEESLAA----VGLgSAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTA 162
Cdd:PRK10771 80 nnlfsHLTVAQNIglglnpGLKLNAAQREKLHAiarqMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190
....*....|....*....|....*....|...
gi 1670356525 163 TVDIG-SEDMLyESLNRLEKETNITVFLITHDL 194
Cdd:PRK10771 159 ALDPAlRQEML-TLVSQVCQERQLTLLMVSHSL 190
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-165 |
1.31e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSV----RIGYVPQNFVV- 94
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnPEKGEILFERQSikkdLCTYQKQLCFVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 95 ----TDVPITVRDF----LGFKSGA-GFEESLAAVGLGSaVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVD 165
Cdd:PRK13540 81 hrsgINPYLTLRENclydIHFSPGAvGITELCRLFSLEH-LIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
33-213 |
1.45e-07 |
|
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: 49.67 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 33 HAPILEDVSFHvrRGTTLAIVGPNGAGKTTLFRvllglvphtgtvewsgsvRIGYVpqnfvvtdvpitvrdfLGFKSGAG 112
Cdd:cd03227 9 SYFVPNDVTFG--EGSLTIITGPNGSGKSTILD------------------AIGLA----------------LGGAQSAT 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 113 FEESLAAVGLGSA----VLPKRLDVLSGGEMQRVLIA-----WAVLDRPnVLLFDEPTATVDIGSEDMLYESLNRLEKET 183
Cdd:cd03227 53 RRRSGVKAGCIVAavsaELIFTRLQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKG 131
|
170 180 190
....*....|....*....|....*....|
gi 1670356525 184 NiTVFLITHDlHIVSQYSDAVLALNRTVRF 213
Cdd:cd03227 132 A-QVIVITHL-PELAELADKLIHIKKVITG 159
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
37-217 |
1.46e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPH-TGTVEWSGSVR------------IGYVPQNF-VVTDVPITVR 102
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRdAGSILYLGKEVtfngpkssqeagIGIIHQELnLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 103 DFLG--FKSGAG-------FEESLAavglgsavLPKRLDV----------LSGGEMQRVLIAWAVLDRPNVLLFDEPT-A 162
Cdd:PRK10762 100 IFLGreFVNRFGridwkkmYAEADK--------LLARLNLrfssdklvgeLSIGEQQMVEIAKVLSFESKVIIMDEPTdA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 163 TVDIGSEDmLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLALnRTVRFFGAS 217
Cdd:PRK10762 172 LTDTETES-LFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVF-RDGQFIAER 223
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
41-193 |
2.01e-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: 49.91 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 41 SFHV------RRGTTLaIVGPNGAGKTTLFRVLL----GLVP-------HTGTVEWSGSVRiGYVPQNF-VVTDVPITV- 101
Cdd:cd03240 11 SFHErseiefFSPLTL-IVGQNGAGKTTIIEALKyaltGELPpnskggaHDPKLIREGEVR-AQVKLAFeNANGKKYTIt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 102 RDFLGFKSgAGF---EESLaavglgsAVLPKRLDVLSGGemQRVL--------IAWAVLDRPNVLLFDEPTATVDigsED 170
Cdd:cd03240 89 RSLAILEN-VIFchqGESN-------WPLLDMRGRCSGG--EKVLasliirlaLAETFGSNCGILALDEPTTNLD---EE 155
|
170 180
....*....|....*....|....*..
gi 1670356525 171 MLYESLNRL----EKETNITVFLITHD 193
Cdd:cd03240 156 NIEESLAEIieerKSQKNFQLIVITHD 182
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
6-81 |
4.89e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.08 E-value: 4.89e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1670356525 6 PPSRSPTreagaaadvLRVAH-LGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG 81
Cdd:PRK13543 4 PLHTAPP---------LLAAHaLAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLhVESGQIQIDG 72
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
37-194 |
6.23e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 49.65 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSG---------------SVRIGYVPQNFVVTDvPIT 100
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIePTRGQVLIDGvdiakisdaelrevrRKKIAMVFQSFALMP-HMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 101 VRDFLGFK---SGAGFEE-------SLAAVGLGSAV--LPkrlDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGS 168
Cdd:PRK10070 123 VLDNTAFGmelAGINAEErrekaldALRQVGLENYAhsYP---DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180
....*....|....*....|....*.
gi 1670356525 169 EDMLYESLNRLEKETNITVFLITHDL 194
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDL 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-182 |
1.36e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 1 MVAAPPPSRSPTREAGAAADVLRVAHLGVRldHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT-GTVEW 79
Cdd:PRK10982 230 MVGRSLTQRFPDKENKPGEVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSaGTITL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 80 SG----------SVRIGYVpqnfVVTD----VPITVRDFLGFKSG-AGFEESLAAVGLGSAVLPKR-------------- 130
Cdd:PRK10982 308 HGkkinnhnaneAINHGFA----LVTEerrsTGIYAYLDIGFNSLiSNIRNYKNKVGLLDNSRMKSdtqwvidsmrvktp 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1670356525 131 -----LDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKE 182
Cdd:PRK10982 384 ghrtqIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK 440
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
37-195 |
1.81e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFH--------------VRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGSVRIGYVPQNF------VVT 95
Cdd:PRK10522 325 LRNVTFAyqdngfsvgpinltIKRGELLFLIGGNGSGKSTLAMLLTGLYqPQSGEILLDGKPVTAEQPEDYrklfsaVFT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 96 DVPITVRdFLGfksGAGFEESLAAVG--LGSAVLPKRLDV---------LSGGEMQRVLIAWAVLDRPNVLLFDEPTATV 164
Cdd:PRK10522 405 DFHLFDQ-LLG---PEGKPANPALVEkwLERLKMAHKLELedgrisnlkLSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
170 180 190
....*....|....*....|....*....|.
gi 1670356525 165 DIGSEDMLYESLNRLEKETNITVFLITHDLH 195
Cdd:PRK10522 481 DPHFRREFYQVLLPLLQEMGKTIFAISHDDH 511
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
35-193 |
2.19e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.92 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 35 PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTgtvewSGSVRIGyvpqNFVVTDV-P--------------- 98
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERIT-----SGEIWIG----GRVVNELePadrdiamvfqnyaly 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 --ITVRDFL--GFKSgAGF---------EESLAAVGLGsAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVD 165
Cdd:PRK11650 89 phMSVRENMayGLKI-RGMpkaeieervAEAARILELE-PLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
170 180
....*....|....*....|....*....
gi 1670356525 166 IGSE-DMLYEsLNRLEKETNITVFLITHD 193
Cdd:PRK11650 167 AKLRvQMRLE-IQRLHRRLKTTSLYVTHD 194
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
115-207 |
4.15e-06 |
|
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: 47.32 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 115 ESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDR---PNVLLFDEPTATVDIGSEDMLYESLNRLEKETNiTVFLIT 191
Cdd:TIGR00630 811 QTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIE 889
|
90
....*....|....*.
gi 1670356525 192 HDLHIVSQySDAVLAL 207
Cdd:TIGR00630 890 HNLDVIKT-ADYIIDL 904
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-165 |
4.15e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 28 GVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVpHTGTVEW------------SGSVRIGYVPQNfvvt 95
Cdd:TIGR00956 770 KIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV-TTGVITGgdrlvngrpldsSFQRSIGYVQQQ---- 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 96 DVPI---TVRDFLGF-------KSGAGFE--------------ESL--AAVGL-GSAvlpkrldvLSGGEMQRVLIAWAV 148
Cdd:TIGR00956 845 DLHLptsTVRESLRFsaylrqpKSVSKSEkmeyveevikllemESYadAVVGVpGEG--------LNVEQRKRLTIGVEL 916
|
170
....*....|....*...
gi 1670356525 149 LDRPNVLLF-DEPTATVD 165
Cdd:TIGR00956 917 VAKPKLLLFlDEPTSGLD 934
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
3-193 |
4.81e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.10 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 3 AAPPPSRSPTREAGAAADVLRVAHLGVRLDHAPILEDVSFHV-------RRGTTLAIVGPNGAGKTTLFRVLLGL-VPHT 74
Cdd:COG4615 307 AAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDEGFTLgpidltiRRGELVFIVGGNGSGKSTLAKLLTGLyRPES 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 75 GTVEWSGSV-----RIGYvPQNF--VVTDVpitvrdFLgfksgagFEESLaavGLGSAVLPKRLDV-------------- 133
Cdd:COG4615 387 GEILLDGQPvtadnREAY-RQLFsaVFSDF------HL-------FDRLL---GLDGEADPARAREllerleldhkvsve 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1670356525 134 --------LSGGEMQRV-LIAwAVL-DRPnVLLFDEPTATVDIGSEDMLY-ESLNRLeKETNITVFLITHD 193
Cdd:COG4615 450 dgrfsttdLSQGQRKRLaLLV-ALLeDRP-ILVFDEWAADQDPEFRRVFYtELLPEL-KARGKTVIAISHD 517
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
33-194 |
8.51e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 46.24 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 33 HAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL--------------VPHTGTVEWSGsvRIGYVPQN-FVVTDv 97
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHfdvsegdirfhdipLTKLQLDSWRS--RLAVVSQTpFLFSD- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 98 piTVRD--FLGfKSGAGFEESLAAVGLGSA-----VLPKRLD--------VLSGGEMQRVLIAWAVLDRPNVLLFDEPTA 162
Cdd:PRK10789 404 --TVANniALG-RPDATQQEIEHVARLASVhddilRLPQGYDtevgergvMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190
....*....|....*....|....*....|..
gi 1670356525 163 TVDIGSEDMLYESLNRLEKETniTVFLITHDL 194
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGR--TVIISAHRL 510
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
115-207 |
8.63e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 115 ESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVL---DRPNVLLFDEPTATVDIGSEDMLYESLNRLEKETNiTVFLIT 191
Cdd:PRK00635 791 HALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH-TVVIIE 869
|
90
....*....|....*.
gi 1670356525 192 HDLHIVsQYSDAVLAL 207
Cdd:PRK00635 870 HNMHVV-KVADYVLEL 884
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
22-209 |
1.12e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 45.28 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 22 LRVAHLGVRLDHA--PILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVP-HTGTVEWSGsVRIGYVPQNFVVTDVP 98
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIVIDG-IDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 99 ITVRDFLGFKSGAGFE-------------ESLAAVGLGSAV--LPKRLD--VLSGGEM----QRVL--IAWAVLDRPNVL 155
Cdd:cd03288 99 IILQDPILFSGSIRFNldpeckctddrlwEALEIAQLKNMVksLPGGLDavVTEGGENfsvgQRQLfcLARAFVRKSSIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1670356525 156 LFDEPTATVDIGSEDMLYESLnrLEKETNITVFLITHDLHIVSQySDAVLALNR 209
Cdd:cd03288 179 IMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTILD-ADLVLVLSR 229
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
115-197 |
1.14e-05 |
|
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: 45.30 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 115 ESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAVLDR---PNVLLFDEPTATVDIGSEDMLYESLNRLEKETNiTVFLIT 191
Cdd:cd03271 151 QTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIE 229
|
....*.
gi 1670356525 192 HDLHIV 197
Cdd:cd03271 230 HNLDVI 235
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
37-207 |
1.15e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL-VPHTGTVEWSGSVRIGYVPQNFVVTDVPITVRDFLGFKSGAGFEE 115
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPNKGTVDIKGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 116 ---------SLAAVGlgsAVLPKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLeKETNIT 186
Cdd:PRK13545 120 ikeiipeiiEFADIG---KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKT 195
|
170 180
....*....|....*....|.
gi 1670356525 187 VFLITHDLHIVSQYSDAVLAL 207
Cdd:PRK13545 196 IFFISHSLSQVKSFCTKALWL 216
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-192 |
1.62e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.78 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT---GTVEWSGS--------------- 82
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtgGTVEFKGKdllelspedragegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 83 -------VRIGYVPQNFVVTDVPITVRDFLG------FKSGAGFEESLAAVGLGSAVLPKRLDV-LSGGEMQRVLIAWAV 148
Cdd:PRK09580 81 fmafqypVEIPGVSNQFFLQTALNAVRSYRGqepldrFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1670356525 149 LDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKEtNITVFLITH 192
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTH 203
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
28-165 |
2.18e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 28 GVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLvPHTGTVEwsGSVRI--------------GYVPQNFV 93
Cdd:PLN03140 887 GVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR-KTGGYIE--GDIRIsgfpkkqetfarisGYCEQNDI 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 94 VTDvPITVRD------FLGFKSGAGFEESLAAV----------GLGSAV--LPKrLDVLSGGEMQRVLIAWAVLDRPNVL 155
Cdd:PLN03140 964 HSP-QVTVREsliysaFLRLPKEVSKEEKMMFVdevmelveldNLKDAIvgLPG-VTGLSTEQRKRLTIAVELVANPSII 1041
|
170
....*....|
gi 1670356525 156 LFDEPTATVD 165
Cdd:PLN03140 1042 FMDEPTSGLD 1051
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-182 |
7.23e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 8 SRSPTREAGAAADVLRVAHLGVrldHAP------ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGL---VPHTGTVE 78
Cdd:NF040905 244 DRYPERTPKIGEVVFEVKNWTV---YHPlhperkVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygRNISGTVF 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 79 WSG------SVR------IGYV----PQNFVVTDVPI---TVRDFLGFKSGAGF----EESLAAVGLGSAVLPKRLDV-- 133
Cdd:NF040905 321 KDGkevdvsTVSdaidagLAYVtedrKGYGLNLIDDIkrnITLANLGKVSRRGVidenEEIKVAEEYRKKMNIKTPSVfq 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1670356525 134 ----LSGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKE 182
Cdd:NF040905 401 kvgnLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE 453
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
36-200 |
1.51e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 36 ILEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLVPHTGtvewsGSVR-----IG------------YVPQNFVVTD-- 96
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCG-----GEIRvngreIGayglrelrrqfsMIPQDPVLFDgt 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 97 VPITVRDFLGFKSG--------AGFEESLAAV--GLGSAVLPKRLDvLSGGEMQRVLIAWAVLDR-PNVLLFDEPTATVD 165
Cdd:PTZ00243 1400 VRQNVDPFLEASSAevwaalelVGLRERVASEseGIDSRVLEGGSN-YSVGQRQLMCMARALLKKgSGFILMDEATANID 1478
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1670356525 166 igsedmlyESLNRLEKET------NITVFLITHDLHIVSQY 200
Cdd:PTZ00243 1479 --------PALDRQIQATvmsafsAYTVITIAHRLHTVAQY 1511
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
37-207 |
1.55e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLGLV-PHTGTVEWSGS------------------------VR------- 84
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYqKDSGSILFQGKeidfksskealengismvhqelnlVLqrsvmdn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 85 --IGYVPQNFVVTDVPITVRDflgfkSGAGFEEslaavgLGSAVLPK-RLDVLSGGEMQRVLIAWAVLDRPNVLLFDEPT 161
Cdd:PRK10982 94 mwLGRYPTKGMFVDQDKMYRD-----TKAIFDE------LDIDIDPRaKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1670356525 162 ATVDIGSEDMLYESLNRLeKETNITVFLITHDLHIVSQYSDAVLAL 207
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-165 |
2.29e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 21 VLRVAHLGVRLDHAPILEDVSFHVRRGTTLAIVGPNGAGKTTlfrvLLGLV-----PHTGTVEWSG----------SV-- 83
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIagarkIQQGRVEVLGgdmadarhrrAVcp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 84 RIGYVPQ----NFVVTdvpITVR---DFLG--FKSGAG-----FEESLAAVGLgsAVLPKRL-DVLSGGEMQRVLIAWAV 148
Cdd:NF033858 77 RIAYMPQglgkNLYPT---LSVFenlDFFGrlFGQDAAerrrrIDELLRATGL--APFADRPaGKLSGGMKQKLGLCCAL 151
|
170
....*....|....*..
gi 1670356525 149 LDRPNVLLFDEPTATVD 165
Cdd:NF033858 152 IHDPDLLILDEPTTGVD 168
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
37-200 |
4.76e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.57 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 37 LEDVSFHVRRGTTLAIVGPNGAGKTTLFRVLLG-LVPHTGTVEWSGSVRIGYVPQNFVVTDVPITVRDF----LGFKS-- 109
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGsLSPTVGKVDRNGEVSVIAISAGLSGQLTGIENIEFkmlcMGFKRke 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 110 -GAGFEESLAAVGLGSAVLpKRLDVLSGGEMQRVLIAWAVLDRPNVLLFDEptaTVDIGSEDMLYESLNRLE--KETNIT 186
Cdd:PRK13546 120 iKAMTPKIIEFSELGEFIY-QPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTFAQKCLDKIYefKEQNKT 195
|
170
....*....|....
gi 1670356525 187 VFLITHDLHIVSQY 200
Cdd:PRK13546 196 IFFVSHNLGQVRQF 209
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
37-64 |
5.16e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.79 E-value: 5.16e-04
10 20
....*....|....*....|....*...
gi 1670356525 37 LEDVSFHVRRGTTLaIVGPNGAGKTTLF 64
Cdd:pfam13476 9 FRDQTIDFSKGLTL-ITGPNGSGKTTIL 35
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
51-230 |
5.50e-04 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 39.36 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 51 AIVGPNGAGKTTLFRVLLGL-------VPHTGTVEWSGSVRIGYVPQNFVVTDVPitvrdflgfksgaGFEEslaavglg 123
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGevgevsdVPGTTRDPDVYVKELDKGKVKLVLVDTP-------------GLDE-------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 124 savlpkrldvlsGGEMQRVLIAWAVLDRPN--VLLFDeptATVDIGSEDMLYESLNRLEKETNITVFLITH-DL----HI 196
Cdd:cd00882 60 ------------FGGLGREELARLLLRGADliLLVVD---STDRESEEDAKLLILRRLRKEGIPIILVGNKiDLleerEV 124
|
170 180 190
....*....|....*....|....*....|....
gi 1670356525 197 VSQYSDAVLALNRTVRFFGASSRfsEPELLMEIF 230
Cdd:cd00882 125 EELLRLEELAKILGVPVFEVSAK--TGEGVDELF 156
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
30-70 |
8.63e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.63e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1670356525 30 RLDHAPILEDVSFHVRRGTTLaIVGPNGAGKTTLFRVLLGL 70
Cdd:COG4717 7 EIYGFGKFRDRTIEFSPGLNV-IYGPNEAGKSTLLAFIRAM 46
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
123-198 |
1.18e-03 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 39.49 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 123 GSAVLPKrLDVLSGGEMQRVLIAWAVL----DRPNVLLFDEptatVDIG----SEDMLYESLNRLEKETNitVFLITHDL 194
Cdd:cd03241 161 GEPLKPL-AKIASGGELSRLMLALKAIlarkDAVPTLIFDE----IDTGisgeVAQAVGKKLKELSRSHQ--VLCITHLP 233
|
....
gi 1670356525 195 HIVS 198
Cdd:cd03241 234 QVAA 237
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
39-67 |
1.93e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.83 E-value: 1.93e-03
10 20
....*....|....*....|....*....
gi 1670356525 39 DVSFHVRRGTTLaIVGPNGAGKTTLFRVL 67
Cdd:COG3950 18 EIDFDNPPRLTV-LVGENGSGKTTLLEAI 45
|
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
44-78 |
3.37e-03 |
|
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443988 [Multi-domain] Cd Length: 386 Bit Score: 38.22 E-value: 3.37e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1670356525 44 VRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT---GTVE 78
Cdd:COG4962 179 VRARLNILVSGGTGSGKTTLLNALSGFIPPDeriVTIE 216
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
49-90 |
3.58e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 37.96 E-value: 3.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1670356525 49 TLAIVGPNGAGKTTLFRVLL---GLVPHTGTVEwSGSVRIGYVPQ 90
Cdd:cd04170 1 NIALVGHSGSGKTTLAEALLyatGAIDRLGRVE-DGNTVSDYDPE 44
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
50-81 |
3.59e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 36.70 E-value: 3.59e-03
10 20 30
....*....|....*....|....*....|....*
gi 1670356525 50 LAIVGPNGAGKTTLFRVLLGLVPH---TGTVEWSG 81
Cdd:COG4917 4 IMLIGRSGAGKTTLTQALNGEELEyrkTQAVEYYD 38
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
115-197 |
3.87e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 115 ESLAAVGLG------SAVlpkrldVLSGGEMQRVLIAwAVLDRPN----VLLFDEPTA---TVDIgseDMLYESLNRLEK 181
Cdd:COG0178 808 QTLQDVGLGyiklgqPAT------TLSGGEAQRVKLA-SELSKRStgktLYILDEPTTglhFHDI---RKLLEVLHRLVD 877
|
90
....*....|....*.
gi 1670356525 182 ETNiTVFLITHDLHIV 197
Cdd:COG0178 878 KGN-TVVVIEHNLDVI 892
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
115-193 |
4.07e-03 |
|
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: 37.62 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1670356525 115 ESLAAVGLGSAVLPKRLDVLSGGEMQRVLIAWAV---LDrpNVL-LFDEPTATVDIGSEDMLYESLNRLEKETNiTVFLI 190
Cdd:cd03270 119 GFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgsgLT--GVLyVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVV 195
|
...
gi 1670356525 191 THD 193
Cdd:cd03270 196 EHD 198
|
|
| FeoB_N |
pfam02421 |
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ... |
49-105 |
4.74e-03 |
|
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.
Pssm-ID: 460552 [Multi-domain] Cd Length: 156 Bit Score: 36.66 E-value: 4.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 49 TLAIVG-PNgAGKTTLFRVLLGLVPHTG-----TVEWSgSVRIGYVPQNFVVTDVP------------ITVRDFL 105
Cdd:pfam02421 2 TIALVGnPN-VGKTTLFNALTGANQHVGnwpgvTVEKK-EGKFKYKGYEIEIVDLPgiyslspyseeeRVARDYL 74
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
135-209 |
5.41e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 37.41 E-value: 5.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1670356525 135 SGGEMQRVLIAWAVLDRPNVLLFDEPTATVDIGSEDMLYESLNRLEKEtNITVFLITHDLHIVSQYSDAVLALNR 209
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDR 219
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
51-117 |
5.84e-03 |
|
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: 37.37 E-value: 5.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1670356525 51 AIVGPNGAGKTTLFRVLLGLvphtgTVEWSGSVRIGYVPQNFVVTDVPITVRDFLGFKSGAGFEESL 117
Cdd:pfam13304 3 VLIGPNGSGKSNLLEALRFL-----ADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISE 64
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
37-67 |
6.19e-03 |
|
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: 37.29 E-value: 6.19e-03
10 20 30
....*....|....*....|....*....|.
gi 1670356525 37 LEDVSFHVRRGTTlAIVGPNGAGKTTLFRVL 67
Cdd:COG3593 14 IKDLSIELSDDLT-VLVGENNSGKSSILEAL 43
|
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
44-78 |
6.99e-03 |
|
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.
Pssm-ID: 410874 [Multi-domain] Cd Length: 177 Bit Score: 36.36 E-value: 6.99e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1670356525 44 VRRGTTLAIVGPNGAGKTTLFRVLLGLVPHT---GTVE 78
Cdd:cd01130 9 VRARKNILISGGTGSGKTTLLNALLSFIPPDeriVTIE 46
|
|
| |
