|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-257 |
1.79e-142 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 399.08 E-value: 1.79e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 15 ASSPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKRIGYVPQ 94
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 RGSVDWDFPTSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYF 174
Cdd:COG1121 83 RAEVDWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 175 MDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNVQVIASGPMEEVFTPENLKRTYGERMRWG 254
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSRAYGGPVALL 242
|
...
gi 917519534 255 ERH 257
Cdd:COG1121 243 AHG 245
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-232 |
1.79e-116 |
|
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: 332.19 E-value: 1.79e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 20 RVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKRIGYVPQRGSVD 99
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 100 WDFPTSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPF 179
Cdd:cd03235 81 RDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917519534 180 AGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNVQVIASG 232
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
19-252 |
7.04e-86 |
|
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: 256.12 E-value: 7.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA-----QARKRIGYVP 93
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAslsrrELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 94 QRGSVDWDFptSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLY 173
Cdd:COG1120 82 QEPPAPFGL--TVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 174 FMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTPENLKRTYGERM 251
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLkDGRIVAQGPPEEVLTPELLEEVYGVEA 239
|
.
gi 917519534 252 R 252
Cdd:COG1120 240 R 240
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-252 |
4.89e-76 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 231.70 E-value: 4.89e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 15 ASSPLRVRDLTVVYRE-KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKR--IGY 91
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKnlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVDWDFPTSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDAD 171
Cdd:PRK15056 83 VPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 172 LYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNVQVIASGPMEEVFTPENLKRTYGERM 251
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELAFSGVL 242
|
.
gi 917519534 252 R 252
Cdd:PRK15056 243 R 243
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
19-237 |
5.33e-68 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 209.92 E-value: 5.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA----QARKRIGYVPQ 94
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVArdpaEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 RGSVDWDFptSVLDVVMM--GLYGqlgwfkRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADL 172
Cdd:COG1131 81 EPALYPDL--TVRENLRFfaRLYG------LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEV 237
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKgRIVADGTPDEL 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-223 |
2.07e-64 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 199.38 E-value: 2.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 28 YREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRffgqslAQARKRIGYVPQRGSVDWDFPTSVL 107
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------RAGGARVAYVPQRSEVPDSLPLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 108 DVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTE 187
Cdd:NF040873 76 DLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 917519534 188 EAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTL 223
Cdd:NF040873 156 ERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
19-249 |
7.37e-64 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 199.90 E-value: 7.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR-EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQS--------LAQARKRI 89
Cdd:COG3638 3 LELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtalrgraLRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 90 GYVPQrgsvdwDFP----TSVLDVVMMGLYGQLG----WFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVF 161
Cdd:COG3638 83 GMIFQ------QFNlvprLSVLTNVLAGRLGRTStwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 162 LARALAQDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVfT 239
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDgRVVFDGPPAEL-T 235
|
250
....*....|
gi 917519534 240 PENLKRTYGE 249
Cdd:COG3638 236 DAVLREIYGG 245
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-252 |
1.86e-62 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 196.49 E-value: 1.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ------ARKRiGYV 92
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspwelARRR-AVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVdwDFPTSVLDVVMMGLYGQLgwfkRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQ---- 168
Cdd:COG4559 81 PQHSSL--AFPFTVEEVVALGRAPHG----SSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwep 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 169 ---DADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTPENLK 244
Cdd:COG4559 155 vdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLhQGRLVAQGTPEEVLTDELLE 234
|
....*...
gi 917519534 245 RTYGERMR 252
Cdd:COG4559 235 RVYGADLR 242
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-248 |
1.87e-61 |
|
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: 193.76 E-value: 1.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQ-VRFFGQ-----SLAQARKRIGYV 92
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGErrggeDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQrgSVDWDFP--TSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDA 170
Cdd:COG1119 84 SP--ALQLRFPrdETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 171 DLYFMDEPFAGVDAVTEEAILRVLHELKKQG-KTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTPENLKRTYG 248
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLkDGRVVAAGPKEEVLTSENLSEAFG 241
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
39-248 |
6.74e-60 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 188.91 E-value: 6.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 39 LEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKRIGYVPQRGSVDWDFPTSVLDVVMMGLYGQL 118
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 119 GWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELK 198
Cdd:TIGR03771 81 GWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 917519534 199 KQGKTVVVVHHDLETVRDYFDHLTLLNVQVIASGPMEEVFTPENLKRTYG 248
Cdd:TIGR03771 161 GAGTAILMTTHDLAQAMATCDRVVLLNGRVIADGTPQQLQDPAPWMTTFG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-245 |
3.86e-59 |
|
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: 187.15 E-value: 3.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR-EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ-----SLAQARKRIGYV 92
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditkkNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQrgsvdwdFP------TSVLDVVMMGLYgQLGWfkrpgPRE--REAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLAR 164
Cdd:COG1122 81 FQ-------NPddqlfaPTVEEDVAFGPE-NLGL-----PREeiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 165 ALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFT-PEN 242
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDgRIVADGTPREVFSdYEL 227
|
...
gi 917519534 243 LKR 245
Cdd:COG1122 228 LEE 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-232 |
6.15e-58 |
|
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: 182.25 E-value: 6.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 20 RVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA-----QARKRIGYVPQ 94
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAslspkELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 rgsvdwdfptsvldvvmmglygqlgwfkrpgprereaalrCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYF 174
Cdd:cd03214 81 ----------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 175 MDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLL-NVQVIASG 232
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLkDGRIVAQG 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
19-247 |
1.38e-56 |
|
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: 181.23 E-value: 1.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYRE-KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA--------QARKRI 89
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgkalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 90 GYVPQrgsvdwDFP----TSVLDVVMMGLYGQL----GWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVF 161
Cdd:cd03256 81 GMIFQ------QFNlierLSVLENVLSGRLGRRstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 162 LARALAQDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEvFT 239
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDgRIVFDGPPAE-LT 233
|
....*...
gi 917519534 240 PENLKRTY 247
Cdd:cd03256 234 DEVLDEIY 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
19-212 |
2.47e-56 |
|
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: 179.59 E-value: 2.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR----EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKRIGYVPQ 94
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 RGSVdwdFP-TSVLDVVMMGLYGQlgwfKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLY 173
Cdd:cd03293 81 QDAL---LPwLTVLDNVALGLELQ----GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 917519534 174 FMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLE 212
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDID 193
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-225 |
2.85e-56 |
|
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: 179.20 E-value: 2.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 20 RVRDLTVVY--REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ-----SLAQARKRIGYV 92
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQrgsvdwdFP------TSVLDVVMMGLyGQLGWfkrPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARAL 166
Cdd:cd03225 81 FQ-------NPddqffgPTVEEEVAFGL-ENLGL---PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 167 AQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLN 225
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-237 |
1.02e-55 |
|
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: 178.78 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ------ARKRIGYV 92
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlppheiARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVdwdFPT-SVLDVVMMGLYGQLG---WFKRPGPREREA---ALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARA 165
Cdd:cd03219 81 FQIPRL---FPElTVLENVMVAAQARTGsglLLARARREEREArerAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917519534 166 LAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEV 237
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQgRVIAEGTPDEV 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-248 |
7.09e-54 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 174.57 E-value: 7.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ------ARKRiGYV 92
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaelARRR-AVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVdwDFPTSVLDVVMMGLYGqlgwFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDAD- 171
Cdd:PRK13548 82 PQHSSL--SFPFTVEEVVAMGRAP----HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 172 -----LYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTPENLK 244
Cdd:PRK13548 156 dgpprWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLhQGRLVADGTPAEVLTPETLR 235
|
....
gi 917519534 245 RTYG 248
Cdd:PRK13548 236 RVYG 239
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
19-225 |
7.10e-54 |
|
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: 171.81 E-value: 7.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL----AQARKRIGYVPQ 94
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkkepEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 RgsvdwdfptsvldvvmMGLYGQLgwfkrpgprereaalrcleqvsmqafTTRQISQLSGGQQQRVFLARALAQDADLYF 174
Cdd:cd03230 81 E----------------PSLYENL--------------------------TVRENLKLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 917519534 175 MDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLN 225
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILN 169
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-242 |
8.30e-53 |
|
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: 171.32 E-value: 8.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA--------RKRIG 90
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLsekelyelRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQRG----SVdwdfptSVLDVVMMGL--YGQLgwfkrpgPRE--REAALRCLEQVSMQAFTTRQISQLSGGQQQRVFL 162
Cdd:COG1127 86 MLFQGGalfdSL------TVFENVAFPLreHTDL-------SEAeiRELVLEKLELVGLPGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 163 ARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTP 240
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLaDGKIIAEGTPEELLAS 232
|
..
gi 917519534 241 EN 242
Cdd:COG1127 233 DD 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
19-247 |
1.26e-52 |
|
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: 170.81 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA----QARKRIGYVPQ 94
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkeprEARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 -RGSVDWdfpTSVLDVVMMglygqLGWFKRPGPREREAAL-RCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADL 172
Cdd:COG4555 82 eRGLYDR---LTVRENIRY-----FAELYGLFDEELKKRIeELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEV---FTPENLKRTY 247
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILhKGKVVAQGSLDELreeIGEENLEDAF 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
13-212 |
4.18e-52 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 170.27 E-value: 4.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 13 SGASSPLRVRDLTVVYR----EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKR 88
Cdd:COG1116 2 SAAAPALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 89 IGYVPQRGSVdwdFP-TSVLDVVMMGLYGQlgwfKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALA 167
Cdd:COG1116 82 RGVVFQEPAL---LPwLTVLDNVALGLELR----GVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 917519534 168 QDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLE 212
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVD 200
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-236 |
7.15e-51 |
|
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: 174.56 E-value: 7.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 3 TQPKTVQHPESGASSpLRVRDLTVVY-REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQS 81
Cdd:COG4988 322 APAGTAPLPAAGPPS-IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 82 LAQA-----RKRIGYVPQRGSVdwdFPTSVLDVVMMGlygqlgwfkRPGPRErEAALRCLEQVSMQAFTTR-------QI 149
Cdd:COG4988 401 LSDLdpaswRRQIAWVPQNPYL---FAGTIRENLRLG---------RPDASD-EELEAALEAAGLDEFVAAlpdgldtPL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 150 ----SQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKqGKTVVVVHHDLETVRDYFDHLTLLN 225
Cdd:COG4988 468 geggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQADRILVLDD 546
|
250
....*....|.
gi 917519534 226 VQVIASGPMEE 236
Cdd:COG4988 547 GRIVEQGTHEE 557
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-242 |
1.71e-50 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 165.37 E-value: 1.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQS--------LAQARKRIG 90
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglseaeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQRGSVdwdFPT-SVLDVVMMGLYGQlgwFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQD 169
Cdd:cd03261 81 MLFQSGAL---FDSlTVFENVAFPLREH---TRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917519534 170 ADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTPEN 242
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLyDGKIVAEGTPEELRASDD 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-237 |
2.42e-50 |
|
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: 165.60 E-value: 2.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ------ARKRIGYV 92
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpphriARLGIART 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVdwdFPT-SVLDVVMMGLYGQLG------WFKRPGPREREAALR-----CLEQVSMQAFTTRQISQLSGGQQQRV 160
Cdd:COG0411 85 FQNPRL---FPElTVLENVLVAAHARLGrgllaaLLRLPRARREEREAReraeeLLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 161 FLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKK-QGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEV 237
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFgRVIAEGTPAEV 240
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
20-225 |
3.45e-50 |
|
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: 162.03 E-value: 3.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 20 RVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ-----ARKRIGYVPQ 94
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlpleeLRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 rgsvdwdfptsvldvvmmglygqlgwfkrpgprereaalrcleqvsmqafttrqisqLSGGQQQRVFLARALAQDADLYF 174
Cdd:cd00267 81 ---------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 917519534 175 MDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLN 225
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLK 154
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
17-248 |
5.66e-50 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 164.42 E-value: 5.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 17 SPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ--AR---KRIGY 91
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlsSRqlaRRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVDWDFptSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDAD 171
Cdd:PRK11231 81 LPQHHLTPEGI--TVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 172 LYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTPENLKRTYG 248
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLaNGHVMAQGTPEEVMTPGLLRTVFD 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
18-250 |
1.08e-49 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 168.10 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 18 PLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ-----SLAQARKRIGYV 92
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVDWDFptSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADL 172
Cdd:PRK09536 83 PQDTSLSFEF--DVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTPENLKRTYGER 250
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLaDGRVRAAGPPADVLTADTLRAAFDAR 239
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
19-219 |
1.76e-49 |
|
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: 161.89 E-value: 1.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR----EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA--------- 85
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 86 RKRIGYVPQrgsvdwDF---PT-SVLDVVMMGLYGQlgwfKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVF 161
Cdd:cd03255 81 RRHIGFVFQ------SFnllPDlTALENVELPLLLA----GVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 162 LARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRdYFD 219
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAE-YAD 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-239 |
4.80e-49 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 168.93 E-value: 4.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 2 ITQPKTVQHPESGASSP-LRVRDLTVVY-----REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQV 75
Cdd:COG1123 243 LGAARGRAAPAAAAAEPlLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 76 RFFGQ--------SLAQARKRIGYVPQ--RGSVDwdfPT-SVLDVVMMGL--YGQLgwfkrPGPREREAALRCLEQVSMQ 142
Cdd:COG1123 323 LFDGKdltklsrrSLRELRRRVQMVFQdpYSSLN---PRmTVGDIIAEPLrlHGLL-----SRAERRERVAELLERVGLP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 143 A-FTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDH 220
Cdd:COG1123 395 PdLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADR 474
|
250 260
....*....|....*....|
gi 917519534 221 LTLLNV-QVIASGPMEEVFT 239
Cdd:COG1123 475 VAVMYDgRIVEDGPTEEVFA 494
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
19-248 |
5.16e-49 |
|
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: 161.70 E-value: 5.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY-REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA--------RKRI 89
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgkklrklRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 90 GYVPQrgsvdwDF----PTSVLDVVMMGLYGQ-------LGWFKRpgpREREAALRCLEQVSMQAFTTRQISQLSGGQQQ 158
Cdd:TIGR02315 82 GMIFQ------HYnlieRLTVLENVLHGRLGYkptwrslLGRFSE---EDKERALSALERVGLADKAYQRADQLSGGQQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 159 RVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEE 236
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAgEIVFDGAPSE 232
|
250
....*....|..
gi 917519534 237 VfTPENLKRTYG 248
Cdd:TIGR02315 233 L-DDEVLRHIYG 243
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-220 |
1.28e-48 |
|
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: 158.32 E-value: 1.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY--REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-----RKRIGY 91
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLdleslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVdwdFPTSVLDVVmmglygqlgwfkrpgprereaalrcleqvsmqafttrqisqLSGGQQQRVFLARALAQDAD 171
Cdd:cd03228 81 VPQDPFL---FSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 917519534 172 LYFMDEPFAGVDAVTEEAILRVLHELKKqGKTVVVVHHDLETVRDyFDH 220
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADR 163
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-247 |
2.18e-48 |
|
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: 159.76 E-value: 2.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ------ARKRIGYV 92
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpphriARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVdwdFPT-SVLDVVMMGLYGqlgwfkRPGPREREAAlrcLEQVsMQAF------TTRQISQLSGGQQQRVFLARA 165
Cdd:COG0410 84 PEGRRI---FPSlTVEENLLLGAYA------RRDRAEVRAD---LERV-YELFprlkerRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 166 LAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFTPENLK 244
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERgRIVLEGTAAELLADPEVR 230
|
...
gi 917519534 245 RTY 247
Cdd:COG0410 231 EAY 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-237 |
2.77e-48 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 159.14 E-value: 2.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA------QARKRIGYV 92
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglppheRARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVdwdFPT-SVLDVVMMGLYGQlgwFKRPGPREREAAL----RCLEQVSMQAfttrqiSQLSGGQQQRVFLARALA 167
Cdd:cd03224 81 PEGRRI---FPElTVEENLLLGAYAR---RRAKRKARLERVYelfpRLKERRKQLA------GTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917519534 168 QDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEV 237
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLeRGRVVLEGTAAEL 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
19-212 |
8.00e-48 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 157.68 E-value: 8.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ---ARKRIGYVPQR 95
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvppERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 96 GSVdwdFPT-SVLDVVMMGLYGQlgwfKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYF 174
Cdd:cd03259 81 YAL---FPHlTVAENIAFGLKLR----GVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 917519534 175 MDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLE 212
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELqRELGITTIYVTHDQE 192
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
19-221 |
1.11e-47 |
|
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: 157.67 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREK----PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA--------R 86
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrlrkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 87 KRIGYVPQ--RGSVDwdfPT-SVLDVVMMGLYGQLGwfKRPGPREREAALRCLEQVSM-QAFTTRQISQLSGGQQQRVFL 162
Cdd:cd03257 82 KEIQMVFQdpMSSLN---PRmTIGEQIAEPLRIHGK--LSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 163 ARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHL 221
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRV 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-212 |
1.29e-47 |
|
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: 156.87 E-value: 1.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA----RKRIGYVPQ 94
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAredyRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 RGSVDWDFptSVLDvvmmglygQLGWFKR--PGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADL 172
Cdd:COG4133 83 ADGLKPEL--TVRE--------NLRFWAAlyGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVV-HHDLE 212
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLE 193
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1-236 |
1.69e-47 |
|
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: 165.71 E-value: 1.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 1 MITQPKTVQHPESGASSP----LRVRDLTVVY--REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQ 74
Cdd:COG4987 312 LLDAPPAVTEPAEPAPAPggpsLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 75 VRFFGQSL-----AQARKRIGYVPQRGSVdwdFPTSVLDVVMMGlygqlgwfkRPGPRErEAALRCLEQVSMQAFTTRQI 149
Cdd:COG4987 392 ITLGGVDLrdldeDDLRRRIAVVPQRPHL---FDTTLRENLRLA---------RPDATD-EELWAALERVGLGDWLAALP 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 150 -----------SQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELkKQGKTVVVVHHDLETVrDYF 218
Cdd:COG4987 459 dgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGL-ERM 536
|
250
....*....|....*....
gi 917519534 219 DH-LTLLNVQVIASGPMEE 236
Cdd:COG4987 537 DRiLVLEDGRIVEQGTHEE 555
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
19-220 |
1.85e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.13 E-value: 1.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR----EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA--------- 85
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLserelarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 86 RKRIGYVPQrgsvdwDF---PT-SVLDVVMMGLYgqlgwFKRPGPREREA-ALRCLEQVSMQAFTTRQISQLSGGQQQRV 160
Cdd:COG1136 85 RRHIGFVFQ------FFnllPElTALENVALPLL-----LAGVSRKERRErARELLERVGLGDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917519534 161 FLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLEtVRDYFDH 220
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPE-LAARADR 213
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
19-250 |
3.21e-47 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 157.67 E-value: 3.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL----AQAR-KRIGYVP 93
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLhglsRRARaRRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 94 QrgSVDWDFPTSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLY 173
Cdd:TIGR03873 82 Q--DSDTAVPLTVRDVVALGRIPHRSLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 174 FMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFTPENLKRTYGER 250
Cdd:TIGR03873 160 LLDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGgRVVAAGPPREVLTPALIRAVYGVD 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-239 |
5.63e-47 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 163.15 E-value: 5.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR--EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVP---VASGQVRFFGQSLAQAR-----KR 88
Cdd:COG1123 5 LEVRDLSVRYPggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSealrgRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 89 IGYVPQRGSVDWDfPTSVLDVVMMGLYGQlgwfKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQ 168
Cdd:COG1123 85 IGMVFQDPMTQLN-PVTVGDQIAEALENL----GLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917519534 169 DADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFT 239
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDgRIVEDGPPEEILA 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-251 |
7.18e-47 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 157.96 E-value: 7.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-RKRIGYVPQ-Rg 96
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEdRRRIGYLPEeR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 97 svdwdfptsvldvvmmGLYG------QLGWFKR----PGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARAL 166
Cdd:COG4152 81 ----------------GLYPkmkvgeQLVYLARlkglSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 167 AQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVftpenlKR 245
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKgRKVLSGSVDEI------RR 218
|
....*.
gi 917519534 246 TYGERM 251
Cdd:COG4152 219 QFGRNT 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
20-248 |
6.05e-46 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 154.09 E-value: 6.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 20 RVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQAR-----KRIGYVPQ 94
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPsrelaKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 rgsvDWDFPT--SVLDVVMMGLY----GqlgwfkRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQ 168
Cdd:COG4604 83 ----ENHINSrlTVRELVAFGRFpyskG------RLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 169 DADLYFMDEPFAGVD---AVteeAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTPENL 243
Cdd:COG4604 153 DTDYVLLDEPLNNLDmkhSV---QMMKLLRRLaDELGKTVVIVLHDINFASCYADHIVAMkDGRVVAQGTPEEIITPEVL 229
|
....*
gi 917519534 244 KRTYG 248
Cdd:COG4604 230 SDIYD 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
19-223 |
7.69e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 152.28 E-value: 7.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-----RKRIGYVP 93
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMpppewRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 94 QRgsVDWdFPTSVLDVVmmglygQLGWFKRPGPREREAALRCLEQVSMQA-FTTRQISQLSGGQQQRVFLARALAQDADL 172
Cdd:COG4619 81 QE--PAL-WGGTVRDNL------PFPFQLRERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFD-HLTL 223
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADrVLTL 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
19-237 |
2.17e-44 |
|
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: 158.84 E-value: 2.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY--REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-----RKRIGY 91
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIdpaslRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVdwdFPTSVLDVVMMGlygqlgwfkRPGPRErEAALRCLEQVSMQAFTTR-------QI----SQLSGGQQQRV 160
Cdd:COG2274 554 VLQDVFL---FSGTIRENITLG---------DPDATD-EEIIEAARLAGLHDFIEAlpmgydtVVgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 161 FLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELkKQGKTVVVVHHDLETVRDyFD-HLTLLNVQVIASGPMEEV 237
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRL-ADrIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
19-225 |
8.07e-44 |
|
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: 147.43 E-value: 8.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL-AQARKRIGYVPQ-RG 96
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLdIAARNRIGYLPEeRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 97 SvdwdFP-TSVLDVVMMglYGQLgwfKRPGPRE-REAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYF 174
Cdd:cd03269 81 L----YPkMKVIDQLVY--LAQL---KGLKKEEaRRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 917519534 175 MDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLN 225
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLN 202
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
15-212 |
1.67e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 150.63 E-value: 1.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 15 ASSPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ--ARKR-IGY 91
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlpPEKRnVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVdwdFP-TSVLDVVMMGLYgqlgwFKRPGPREREA-ALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQD 169
Cdd:COG3842 82 VFQDYAL---FPhLTVAENVAFGLR-----MRGVPKAEIRArVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 917519534 170 ADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLE 212
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQE 197
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
19-225 |
2.00e-43 |
|
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: 145.41 E-value: 2.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA-------QARKRIGY 91
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledelpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVdwdFPT-SVLDVVMMGlygqlgwfkrpgprereaalrcleqvsmqafttrqisqLSGGQQQRVFLARALAQDA 170
Cdd:cd03229 81 VFQDFAL---FPHlTVLENIALG--------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 171 DLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLN 225
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-246 |
2.09e-43 |
|
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: 147.26 E-value: 2.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY----REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-----RKRI 89
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRrrkafRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 90 GYVPQ--RGSVDwdfPT-SVLDVVMMGLYGQlgwfKRPGPREREAALrcLEQVSM-QAFTTRQISQLSGGQQQRVFLARA 165
Cdd:COG1124 82 QMVFQdpYASLH---PRhTVDRILAEPLRIH----GLPDREERIAEL--LEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 166 LAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHltllnVQVIASGPMEEVFTPENLK 244
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDR-----VAVMQNGRIVEELTVADLL 227
|
..
gi 917519534 245 RT 246
Cdd:COG1124 228 AG 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
19-238 |
1.11e-40 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 140.02 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY----REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ--------SLAQAR 86
Cdd:cd03258 2 IELKNVSKVFgdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 87 KRIGYVPQRGSVDWDfpTSVLDVVMMGLygQLGwfKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARAL 166
Cdd:cd03258 82 RRIGMIFQHFNLLSS--RTVFENVALPL--EIA--GVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917519534 167 AQDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVF 238
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMeKGEVVEEGTVEEVF 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
19-246 |
2.70e-40 |
|
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: 139.36 E-value: 2.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYRE-KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-----RKRIGYV 92
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdpvelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVdwdFP-TSVLDVVmmGLYGQL-GWfkrPGPREREAALRCLEQVSM--QAFTTRQISQLSGGQQQRVFLARALAQ 168
Cdd:cd03295 81 IQQIGL---FPhMTVEENI--ALVPKLlKW---PKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 169 DADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLNvqviaSGPMEEVFTPENLKRT 246
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMK-----NGEIVQVGTPDEILRS 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-225 |
6.10e-40 |
|
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: 137.22 E-value: 6.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY-----REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGqslaqarkRIGYVP 93
Cdd:cd03250 1 ISVEDASFTWdsgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------SIAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 94 QrgsVDWDFPTSVLDVVMMGlygqlgwfkRPGPRER-EAALR--CLEQvSMQAFT----T----RQISqLSGGQQQRVFL 162
Cdd:cd03250 73 Q---EPWIQNGTIRENILFG---------KPFDEERyEKVIKacALEP-DLEILPdgdlTeigeKGIN-LSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917519534 163 ARALAQDADLYFMDEPFAGVDAVTEEAILR--VLHELKKqGKTVVVVHHDLETVRdYFDHLTLLN 225
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN-NKTRILVTHQLQLLP-HADQIVVLD 201
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
19-217 |
1.00e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 137.11 E-value: 1.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYRE-KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA--------RKRI 89
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrreipylRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 90 GYVPQrgsvdwDFP----TSVLDVVMMGLYGQlgwfKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARA 165
Cdd:COG2884 82 GVVFQ------DFRllpdRTVYENVALPLRVT----GKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 917519534 166 LAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDY 217
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRM 203
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-212 |
1.98e-39 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 138.69 E-value: 1.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 20 RVRDLTVVYRE-KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-----RKRIGYVP 93
Cdd:COG1125 3 EFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLdpvelRRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 94 QRGSVdwdFPT-SVLDVVMM--GLygqLGWFKRpgpREREAALRCLEQVSMQA--FTTRQISQLSGGQQQRVFLARALAQ 168
Cdd:COG1125 83 QQIGL---FPHmTVAENIATvpRL---LGWDKE---RIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 917519534 169 DADLYFMDEPFAGVDAVTEEA----ILRVLHELkkqGKTVVVVHHDLE 212
Cdd:COG1125 154 DPPILLMDEPFGALDPITREQlqdeLLRLQREL---GKTIVFVTHDID 198
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-224 |
2.06e-39 |
|
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: 143.20 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 3 TQPKTVQHP-ESGASSPLRVRDLTVVYR-EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ 80
Cdd:TIGR02857 305 PRPLAGKAPvTAAPASSLEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 81 SLAQA-----RKRIGYVPQRgsvDWDFPTSVLDVVMMGlygqlgwfkRPGPRE---REAALRC----LEQVSMQAFTTR- 147
Cdd:TIGR02857 385 PLADAdadswRDQIAWVPQH---PFLFAGTIAENIRLA---------RPDASDaeiREALERAgldeFVAALPQGLDTPi 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 148 --QISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELkKQGKTVVVVHHDLETVRDYfDHLTLL 224
Cdd:TIGR02857 453 geGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
36-180 |
2.86e-39 |
|
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: 133.54 E-value: 2.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 36 DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL-----AQARKRIGYVPQrgsVDWDFP-TSVLDV 109
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderKSLRKEIGYVFQ---DPQLFPrLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917519534 110 VMMGLYGQlGWFKRPGPREREAAlrcLEQVSMQAFTTR----QISQLSGGQQQRVFLARALAQDADLYFMDEPFA 180
Cdd:pfam00005 80 LRLGLLLK-GLSKREKDARAEEA---LEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-216 |
6.76e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 142.23 E-value: 6.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 1 MITQPKTVQHPESGASSP-----LRVRDLTVVYR-EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQ 74
Cdd:COG1132 317 LLDEPPEIPDPPGAVPLPpvrgeIEFENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 75 VRFFGQ-----SLAQARKRIGYVPQRGSVdwdFPTSVLDVVMMGlygqlgwfkRPGpREREAALRCLEQVSMQAFTTR-- 147
Cdd:COG1132 397 ILIDGVdirdlTLESLRRQIGVVPQDTFL---FSGTIRENIRYG---------RPD-ATDEEVEEAAKAAQAHEFIEAlp 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 148 -----QISQ----LSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKqGKTVVVVHHDLETVRD 216
Cdd:COG1132 464 dgydtVVGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN 540
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-212 |
8.46e-39 |
|
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: 134.55 E-value: 8.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY--REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA----QARKRIGYV 92
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtdrkAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVDWDFptSVLDVVMmgLYGQL-GWFKRPGPREREAALRCLEqvsMQAFTTRQISQLSGGQQQRVFLARALAQDAD 171
Cdd:cd03263 81 PQFDALFDEL--TVREHLR--FYARLkGLPKSEIKEEVELLLRVLG---LTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 917519534 172 LYFMDEPFAGVDAVTEEAILRVLHELKKqGKTVVVVHHDLE 212
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMD 193
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-246 |
1.09e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 134.74 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL-------AQARKRIGY 91
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskkdiNKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVdwdFP-TSVLDVVMMGLYGQLGWfkrpgPRE--REAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQ 168
Cdd:COG1126 82 VFQQFNL---FPhLTVLENVTLAPIKVKKM-----SKAeaEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 169 DADLYFMDEPFAGVD--AVTEeaILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFT-PENlK 244
Cdd:COG1126 154 EPKVMLFDEPTSALDpeLVGE--VLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMdGGRIVEEGPPEEFFEnPQH-E 230
|
..
gi 917519534 245 RT 246
Cdd:COG1126 231 RT 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-212 |
2.22e-38 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 134.60 E-value: 2.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY----REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAqarkriGYVPQ 94
Cdd:COG4525 4 LTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT------GPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 RGSV---DWDFP-TSVLDVVMMGLYgqlgwFKRPGPREREA-ALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQD 169
Cdd:COG4525 78 RGVVfqkDALLPwLNVLDNVAFGLR-----LRGVPKAERRArAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 917519534 170 ADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLE 212
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVE 196
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
21-212 |
5.18e-38 |
|
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: 132.35 E-value: 5.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 21 VRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA---------RKRIGY 91
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLnskkaskfrREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQR-GSVDWDfptSVLDVVMMGLYGQlgwfKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDA 170
Cdd:TIGR03608 81 LFQNfALIENE---TVEENLDLGLKYK----KLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 917519534 171 DLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLE 212
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPE 195
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-248 |
8.37e-38 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 133.04 E-value: 8.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYRekpaLWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPvASGQVRFFGQSLAQ------ARKRiGYV 92
Cdd:COG4138 1 LQLNDVAVAGR----LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDwsaaelARHR-AYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSvdwdfPTSVLDVvmmGLYGQLGWFKRPGPREREAALRCL-EQVSMQAFTTRQISQLSGGQQQRVFLARALAQ--- 168
Cdd:COG4138 75 SQQQS-----PPFAMPV---FQYLALHQPAGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 169 ----DADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLE-TVRdYFDHLTLL-NVQVIASGPMEEVFTPEN 242
Cdd:COG4138 147 tinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNhTLR-HADRVWLLkQGKLVASGETAEVMTPEN 225
|
....*.
gi 917519534 243 LKRTYG 248
Cdd:COG4138 226 LSEVFG 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
19-243 |
1.12e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 135.27 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL-----AQARkRIGYVP 93
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftnlpPRER-RVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 94 QrgsvDWD-FP-TSVLDVVMMGLYGqlgwfKRPGPREREA-ALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDA 170
Cdd:COG1118 82 Q----HYAlFPhMTVAENIAFGLRV-----RPPSKAEIRArVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 171 DLYFMDEPFAGVDA-VTEE--AILRVLHElkKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFT-PENL 243
Cdd:COG1118 153 EVLLLDEPFGALDAkVRKElrRWLRRLHD--ELGGTTVFVTHDQEEALELADRVVVMNQgRIEQVGTPDEVYDrPATP 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
19-237 |
1.35e-37 |
|
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: 131.92 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAV---LGLVPVA--SGQVRFFGQ-------SLAQAR 86
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlNDLIPGApdEGEVLLDGKdiydldvDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 87 KRIGYVPQRGSVdwdFPTSVLDVVMMGLYGQLgwfKRPGPREREAALRCLEQVSMQAFTTRQIS--QLSGGQQQRVFLAR 164
Cdd:cd03260 81 RRVGMVFQKPNP---FPGSIYDNVAYGLRLHG---IKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 165 ALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQgKTVVVVHHDLETVR---DY--FdhltLLNVQVIASGPMEEV 237
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAArvaDRtaF----LLNGRLVEFGPTEQI 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-215 |
1.71e-37 |
|
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: 129.64 E-value: 1.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY--REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-----RKRIGY 91
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdpnelGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRgsvDWDFPTSVLDVVmmglygqlgwfkrpgprereaalrcleqvsmqafttrqisqLSGGQQQRVFLARALAQDAD 171
Cdd:cd03246 81 LPQD---DELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 917519534 172 LYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVR 215
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLA 160
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
19-225 |
2.48e-37 |
|
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: 130.39 E-value: 2.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGqLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL----AQARKRIGYVPQ 94
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlkqpQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 RGSVDWDFPTS-VLDvvmmglYgqLGWFKR-PGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADL 172
Cdd:cd03264 80 EFGVYPNFTVReFLD------Y--IAWLKGiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHELKKqGKTVVVVHHDLETVRDYFDHLTLLN 225
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLN 203
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
19-220 |
4.79e-37 |
|
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: 129.96 E-value: 4.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL-------AQARKRIGY 91
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkkniNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVdwdFP-TSVLDVVMMGLYGQLGWFKRpgpREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDA 170
Cdd:cd03262 81 VFQQFNL---FPhLTVLENITLAPIKVKGMSKA---EAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 917519534 171 DLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDH 220
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADR 204
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-225 |
7.54e-37 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 129.30 E-value: 7.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 20 RVRDLTVVYREKP-ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA--RKRIGYVPQrg 96
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKerRKSIGYVMQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 97 SVDWDFPT-SVLDVVMMGLygqlgwfkRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFM 175
Cdd:cd03226 79 DVDYQLFTdSVREELLLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 917519534 176 DEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLN 225
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-237 |
9.86e-37 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 129.57 E-value: 9.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL------AQARKRIGYV 92
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklpphERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQ-RGSvdwdFPT-SVLDVVMMGLYGqLGWFKRPGPREREAALRCLEQvsmqaFTTRQISQLSGGQQQRVFLARALAQDA 170
Cdd:TIGR03410 81 PQgREI----FPRlTVEENLLTGLAA-LPRRSRKIPDEIYELFPVLKE-----MLGRRGGDLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 171 DLYFMDEPFAGVDAVTEEAILRVLHELKKQGK-TVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEV 237
Cdd:TIGR03410 151 KLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMeRGRVVASGAGDEL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
21-244 |
2.09e-36 |
|
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: 128.64 E-value: 2.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 21 VRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL----AQARKRIGYVPQRG 96
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrepREVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 97 SVDwDFPTSVLDVVMMG-LYGQlgwfkrPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFM 175
Cdd:cd03265 83 SVD-DELTGWENLYIHArLYGV------PGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917519534 176 DEPFAGVDAVTEEAILRVLHELKK-QGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGpmeevfTPENLK 244
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHgRIIAEG------TPEELK 220
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-248 |
2.31e-36 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 129.88 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR-----EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ--------SLAQA 85
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditakkkkKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 86 RKRIGYVPQrgsvdwdFP------TSVLDVVMMGLygqlgwfKRPGPREREA---ALRCLEQVSM-QAFTTRQISQLSGG 155
Cdd:TIGR04521 81 RKKVGLVFQ-------FPehqlfeETVYKDIAFGP-------KNLGLSEEEAeerVKEALELVGLdEEYLERSPFELSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 156 QQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGP 233
Cdd:TIGR04521 147 QMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKgKIVLDGT 226
|
250
....*....|....*
gi 917519534 234 MEEVFTPENLKRTYG 248
Cdd:TIGR04521 227 PREVFSDVDELEKIG 241
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
19-225 |
5.08e-36 |
|
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: 126.95 E-value: 5.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQS---LAQARKRIGyvpqr 95
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSyqkNIEALRRIG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 96 gsvdwdfptSVLDVvmMGLYG------QLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQD 169
Cdd:cd03268 76 ---------ALIEA--PGFYPnltareNLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 170 ADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLN 225
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIIN 200
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-239 |
1.41e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 129.43 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREK----PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA--------QAR 86
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalserelrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 87 KRIGYVPQ-------RgsvdwdfptSVLDVVMMGLYgQLGWFKRpgprEREA-ALRCLEQVSMQAFTTRQISQLSGGQQQ 158
Cdd:COG1135 82 RKIGMIFQhfnllssR---------TVAENVALPLE-IAGVPKA----EIRKrVAELLELVGLSDKADAYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 159 RVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEE 236
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHEMDVVRRICDRVAVLeNGRIVEQGPVLD 227
|
...
gi 917519534 237 VFT 239
Cdd:COG1135 228 VFA 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-247 |
2.55e-35 |
|
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: 126.12 E-value: 2.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ------ARKRIGYV 92
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmhkrARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVDWDFptSVLDvvmmGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADL 172
Cdd:cd03218 81 PQEASIFRKL--TVEE----NILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDletVRDYF---DHLTLLNV-QVIASGPMEEVFTPENLKRTY 247
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN---VRETLsitDRAYIIYEgKVLAEGTPEEIAANELVRKVY 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
19-242 |
8.71e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 124.48 E-value: 8.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDvdLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQAR--KRigyvP--- 93
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFD--LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpaER----Pvsm 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 94 --QRGSVdwdFP-TSVLDVVMMGLYGQLgwfkRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDA 170
Cdd:COG3840 76 lfQENNL---FPhLTVAQNIGLGLRPGL----KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917519534 171 DLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTPEN 242
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVaDGRIAADGPTAALLDGEP 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-238 |
9.10e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.90 E-value: 9.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYRE--KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-----RKRIGY 91
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtvwdvRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQrgSVDWDF-PTSVLDVVMMGLYGQlgwfkrpG-PRE------REAalrcLEQVSMQAFTTRQISQLSGGQQQRVFLA 163
Cdd:PRK13635 86 VFQ--NPDNQFvGATVQDDVAFGLENI-------GvPREemvervDQA----LRQVGMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 164 RALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGK-TVVVVHHDLETVRDYfDHLTLLNV-QVIASGPMEEVF 238
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQA-DRVIVMNKgEILEEGTPEEIF 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-237 |
1.29e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 129.75 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ-----SLAQARKR-IGYV 92
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrSPRDAQAAgIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVdwdFPT-SVLDVVMMG-LYGQLGWFKRpgPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDA 170
Cdd:COG1129 85 HQELNL---VPNlSVAENIFLGrEPRRGGLIDW--RAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917519534 171 DLYFMDEPFAgvdAVTE---EAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEV 237
Cdd:COG1129 160 RVLILDEPTA---SLTErevERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLrDGRLVGTGPVAEL 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-246 |
2.72e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.99 E-value: 2.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAV---LGLVPVA--SGQVRFFGQ-------SLAQAR 86
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPGArvEGEILLDGEdiydpdvDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 87 KRIGYVPQRGSVdwdFPTSVLDVVMMGLygqlgwfKRPGPRER----EAALRCLEQV----------SMQAFTtrqisqL 152
Cdd:COG1117 92 RRVGMVFQKPNP---FPKSIYDNVAYGL-------RLHGIKSKseldEIVEESLRKAalwdevkdrlKKSALG------L 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 153 SGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQgKTVVVVHHDLET---VRDY--FdhltLLNVQ 227
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQaarVSDYtaF----FYLGE 230
|
250 260
....*....|....*....|
gi 917519534 228 VIASGPMEEVFT-PENlKRT 246
Cdd:COG1117 231 LVEFGPTEQIFTnPKD-KRT 249
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-250 |
4.56e-34 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 123.56 E-value: 4.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ-----ARKRIGYVP 93
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaskeVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 94 QRGSVDWDFptSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLY 173
Cdd:PRK10253 88 QNATTPGDI--TVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 174 FMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHL-TLLNVQVIASGPMEEVFTPENLKRTYGER 250
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLiALREGKIVAQGAPKEIVTAELIERIYGLR 244
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-238 |
5.40e-34 |
|
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: 122.33 E-value: 5.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 20 RVRDLTVVYREK-PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ-----SLAQARKRIGYVP 93
Cdd:cd03254 4 EFENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdiSRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 94 QRgsvDWDFPTSVLDVVMMGlygqlgwfkRPGPRErEAALRCLEQVSMQAFTTR-------QISQ----LSGGQQQRVFL 162
Cdd:cd03254 84 QD---TFLFSGTIMENIRLG---------RPNATD-EEVIEAAKEAGAHDFIMKlpngydtVLGEnggnLSQGERQLLAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 163 ARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKqGKTVVVVHHDLETVRDYFDHLTLLNVQVIASGPMEEVF 238
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-244 |
6.27e-34 |
|
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: 123.31 E-value: 6.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR--EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA------QARKRIG 90
Cdd:TIGR04520 1 IEVENVSFSYPesEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdeenlwEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQRgsvdwdfP------TSVLDVVMMGLYGQlgwfkrpG-PRE--REAALRCLEQVSMQAFTTRQISQLSGGQQQRVF 161
Cdd:TIGR04520 81 MVFQN-------PdnqfvgATVEDDVAFGLENL-------GvPREemRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 162 LARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKK-QGKTVVVVHHDLETVRDYfDHLTLLNV-QVIASGPMEEVFT 239
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDMEEAVLA-DRVIVMNKgKIVAEGTPREIFS 225
|
....*.
gi 917519534 240 -PENLK 244
Cdd:TIGR04520 226 qVELLK 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-224 |
6.62e-34 |
|
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: 120.23 E-value: 6.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQArkrigyvpqrgsv 98
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 99 dwdfptsvldvvmmglygqlgwfkrpGPREREAALrcleqVSMqafttrqISQLSGGQQQRVFLARALAQDADLYFMDEP 178
Cdd:cd03216 68 --------------------------SPRDARRAG-----IAM-------VYQLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 917519534 179 FAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL 224
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVL 155
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
19-253 |
6.95e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 122.45 E-value: 6.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ------ARKRIGYV 92
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmhkrARLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVDWDFptSVLDVVMMGLygQLGWFKRPGPREREAALrcLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADL 172
Cdd:COG1137 84 PQEASIFRKL--TVEDNILAVL--ELRKLSKKEREERLEEL--LEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 173 YFMDEPFAGVD--AVTEeaILRVLHELKKQGKTVVVVHHDletVRDYF---DHLTLLNV-QVIASGPMEEVFTPENLKRT 246
Cdd:COG1137 158 ILLDEPFAGVDpiAVAD--IQKIIRHLKERGIGVLITDHN---VRETLgicDRAYIISEgKVLAEGTPEEILNNPLVRKV 232
|
....*...
gi 917519534 247 Y-GERMRW 253
Cdd:COG1137 233 YlGEDFRL 240
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
19-255 |
7.53e-34 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 122.89 E-value: 7.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKRIGYVPQR-GS 97
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNeGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 98 VDWdfpTSVLDVVMMGLygQLGWFKRPgpREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDE 177
Cdd:PRK11248 82 LPW---RNVQDNVAFGL--QLAGVEKM--QRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 178 PFAGVDAVTEEA----ILRVLHElkkQGKTVVVVHHDLETVRDYFDHLTLLnvqviASGPMEEVftpENLKRTYGERMRW 253
Cdd:PRK11248 155 PFGALDAFTREQmqtlLLKLWQE---TGKQVLLITHDIEEAVFMATELVLL-----SPGPGRVV---ERLPLNFARRFVA 223
|
..
gi 917519534 254 GE 255
Cdd:PRK11248 224 GE 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
19-246 |
1.29e-33 |
|
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: 121.68 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ--ARKR-IGYVPQR 95
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDvpVQERnVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 96 GSVdwdFP-TSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYF 174
Cdd:cd03296 83 YAL---FRhMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917519534 175 MDEPFAGVDA-VTEE--AILRVLHElkKQGKTVVVVHHDLETVRDYFDHLTLLNvqviaSGPMEEVFTPENLKRT 246
Cdd:cd03296 160 LDEPFGALDAkVRKElrRWLRRLHD--ELHVTTVFVTHDQEEALEVADRVVVMN-----KGRIEQVGTPDEVYDH 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
32-215 |
3.04e-33 |
|
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: 121.60 E-value: 3.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 32 PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA---------RKRIGYV-------PQR 95
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkelrelrRKKISMVfqsfallPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 96 gsvdwdfptSVLDVVMMGLYGQlgwfKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFM 175
Cdd:cd03294 118 ---------TVLENVAFGLEVQ----GVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 917519534 176 DEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDL-ETVR 215
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLdEALR 226
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
19-246 |
4.21e-33 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 120.48 E-value: 4.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAV---LGLVPVA--SGQVRFFGQS-------LAQAR 86
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmNDLVPGVriEGKVLFDGQDiydkkidVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 87 KRIGYVPQRGSvdwDFPTSVLDVVMMGLygqlgwfKRPGPRER----EAALRCLEQVSMQAFTTRQISQ----LSGGQQQ 158
Cdd:TIGR00972 82 RRVGMVFQKPN---PFPMSIYDNIAYGP-------RLHGIKDKkeldEIVEESLKKAALWDEVKDRLHDsalgLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 159 RVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQgKTVVVVHHDLETVRDYFDHLTL-LNVQVIASGPMEEV 237
Cdd:TIGR00972 152 RLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFfYDGELVEYGPTEQI 230
|
....*....
gi 917519534 238 FTPENLKRT 246
Cdd:TIGR00972 231 FTNPKEKRT 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
19-210 |
5.20e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 122.87 E-value: 5.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ--ARKR-IGYVPQr 95
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDlpPKDRnIAMVFQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 96 gsvDWD-FPT-SVLDVVMMGLygqlgWFKRPGPREREAALR-CLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADL 172
Cdd:COG3839 83 ---SYAlYPHmTVYENIAFPL-----KLRKVPKAEIDRRVReAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 917519534 173 YFMDEPFAGVDAVteeaiLRV--------LHelKKQGKTVVVVHHD 210
Cdd:COG3839 155 FLLDEPLSNLDAK-----LRVemraeikrLH--RRLGTTTIYVTHD 193
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
36-239 |
8.09e-33 |
|
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: 122.52 E-value: 8.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 36 DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARK---------RIGYVPQRGSVdwdFPT-S 105
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARgiflpphrrRIGYVFQEARL---FPHlS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 106 VLDVVmmgLYGQlgwfKRPGPREREAAL-RCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDA 184
Cdd:COG4148 94 VRGNL---LYGR----KRAPRAERRISFdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 185 VTEEAILRVLHELKKQGKT-VVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFT 239
Cdd:COG4148 167 ARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLeQGRVVASGPLAEVLS 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-248 |
1.32e-32 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 119.27 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPalwdVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPvASGQVRFFGQSLAQ------ARKRiGYV 92
Cdd:PRK03695 1 MQLNDVAVSTRLGP----LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAwsaaelARHR-AYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSvdwdfPTSVLDVV-MMGLYGQLGwfkrPGPREREAALRCL-EQVSMQAFTTRQISQLSGGQQQRVFLARALAQ-- 168
Cdd:PRK03695 75 SQQQT-----PPFAMPVFqYLTLHQPDK----TRTEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvw 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 169 -----DADLYFMDEPFAGVDaVTEEAIL-RVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFTPE 241
Cdd:PRK03695 146 pdinpAGQLLLLDEPMNSLD-VAQQAALdRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQgKLLASGRRDEVLTPE 224
|
....*..
gi 917519534 242 NLKRTYG 248
Cdd:PRK03695 225 NLAQVFG 231
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
32-217 |
1.32e-32 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 118.50 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 32 PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ--------SLAQARKRIGYVPQrgsvdwDF- 102
Cdd:TIGR02673 16 AALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEdvnrlrgrQLPLLRRRIGVVFQ------DFr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 103 --PT-SVLDVVMMGLYGQlGWFKRPGPREREAALRcleQVSM--QAFTTRQisQLSGGQQQRVFLARALAQDADLYFMDE 177
Cdd:TIGR02673 90 llPDrTVYENVALPLEVR-GKKEREIQRRVGAALR---QVGLehKADAFPE--QLSGGEQQRVAIARAIVNSPPLLLADE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 917519534 178 PFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDY 217
Cdd:TIGR02673 164 PTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRV 203
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-239 |
2.38e-32 |
|
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: 120.54 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREK----PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVP---VASGQVRFFGQSLAQAR----- 86
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSekelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 87 ----KRIGYVPQrgsvdwDfPTSVLDVVMMgLYGQLG---WFKRPGPRE--REAALRCLEQVSMQAfTTRQIS----QLS 153
Cdd:COG0444 82 kirgREIQMIFQ------D-PMTSLNPVMT-VGDQIAeplRIHGGLSKAeaRERAIELLERVGLPD-PERRLDryphELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 154 GGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHltlLNV----QV 228
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADR---VAVmyagRI 229
|
250
....*....|.
gi 917519534 229 IASGPMEEVFT 239
Cdd:COG0444 230 VEEGPVEELFE 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
19-212 |
8.49e-32 |
|
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: 116.76 E-value: 8.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDL--TVVYREKP--ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ------AR-- 86
Cdd:COG4181 9 IELRGLtkTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedarARlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 87 -KRIGYVPQrgsvdwDF---PT-SVLDVVMMGLygQLgwfkRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVF 161
Cdd:COG4181 89 aRHVGFVFQ------SFqllPTlTALENVMLPL--EL----AGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 917519534 162 LARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKK-QGKTVVVVHHDLE 212
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPA 208
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-243 |
1.06e-31 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 116.56 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR-EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ-----SLAQARKRIGYV 92
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQrgsvdwdfpTSVL--DVVMMGL-YGqlgwfkRPGPRE---REAALR-CLEQVSM---QAFTT----RQIsQLSGGQQQ 158
Cdd:cd03253 81 PQ---------DTVLfnDTIGYNIrYG------RPDATDeevIEAAKAaQIHDKIMrfpDGYDTivgeRGL-KLSGGEKQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 159 RVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKqGKTVVVVHHDLETVRDYFDHLTLLNVQVIASGPMEEVF 238
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL 223
|
....*
gi 917519534 239 TPENL 243
Cdd:cd03253 224 AKGGL 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-227 |
2.21e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 115.27 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLG-LVPV--ASGQVRFFGQSLAQ---ARKRIGYV 92
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTAlpaEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRgsvDWDFP-TSVLDVVMMGLYGQLGwfkrpGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDAD 171
Cdd:COG4136 82 FQD---DLLFPhLSVGENLAFALPPTIG-----RAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 172 LYFMDEPFAGVDAVTEEAILR-VLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNVQ 227
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGNWQ 210
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
19-252 |
2.25e-31 |
|
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: 115.83 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA------QARKRIGYV 92
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIThlpmheRARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVdwdF-PTSVLDVVMMGLYGQlgwfKRPGPREREAALRCL-EQVSMQAFTTRQISQLSGGQQQRVFLARALAQDA 170
Cdd:TIGR04406 82 PQEASI---FrKLTVEENIMAVLEIR----KDLDRAEREERLEALlEEFQISHLRDNKAMSLSGGERRRVEIARALATNP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 171 DLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFTPENLKRTY-G 248
Cdd:TIGR04406 155 KFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDgKVLAEGTPAEIVANEKVRRVYlG 234
|
....
gi 917519534 249 ERMR 252
Cdd:TIGR04406 235 EQFR 238
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-238 |
2.40e-31 |
|
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: 121.39 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY--REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKR-----IGY 91
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREelgrhIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQrgsvdwD---FPTSVLDVVMMglygqlgwFKRPGPREREAALR---CLEqvsM-----QAFTTRqI----SQLSGGQ 156
Cdd:COG4618 411 LPQ------DvelFDGTIAENIAR--------FGDADPEKVVAAAKlagVHE---MilrlpDGYDTR-IgeggARLSGGQ 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 157 QQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHD---LETVrdyfDHLTLL-NVQVIASG 232
Cdd:COG4618 473 RQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRpslLAAV----DKLLVLrDGRVQAFG 548
|
....*.
gi 917519534 233 PMEEVF 238
Cdd:COG4618 549 PRDEVL 554
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-212 |
2.45e-31 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 119.05 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKP------------------------ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQ 74
Cdd:COG4175 4 IEVRNLYKIFGKRPeralklldqgkskdeilektgqtvGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 75 VRFFGQSLAQA---------RKRIGYV-------PQRgsvdwdfptSVLDVVMMGL--YGQlgwfkrpGPREREA-ALRC 135
Cdd:COG4175 84 VLIDGEDITKLskkelrelrRKKMSMVfqhfallPHR---------TVLENVAFGLeiQGV-------PKAERRErAREA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 136 LEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVteeaILRVLH-EL----KKQGKTVVVVHHD 210
Cdd:COG4175 148 LELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPL----IRREMQdELlelqAKLKKTIVFITHD 223
|
..
gi 917519534 211 LE 212
Cdd:COG4175 224 LD 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-245 |
4.13e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 116.33 E-value: 4.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYRE-KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ-------SLAQARKRIG 90
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkkSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQRGSvDWDFPTSVLDVVMMGLYgQLGWFKRP-GPREREAalrcLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQD 169
Cdd:PRK13639 82 IVFQNPD-DQLFAPTVEEDVAFGPL-NLGLSKEEvEKRVKEA----LKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 170 ADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTPENLKR 245
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMsDGKIIKEGTPKEVFSDIETIR 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-242 |
5.48e-31 |
|
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: 114.74 E-value: 5.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKpALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ---SLAQARKRIGYVPQR 95
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 96 GSVdwdFP-TSVLDVVMMGLYGQlgwfKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYF 174
Cdd:cd03299 80 YAL---FPhMTVYKNIAYGLKKR----KVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917519534 175 MDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHL-TLLNVQVIASGPMEEVF-TPEN 242
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVaIMLNGKLIQVGKPEEVFkKPKN 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-211 |
7.45e-31 |
|
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: 119.77 E-value: 7.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 6 KTVQHPESGASSP----LRVRDLTVVY-REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ 80
Cdd:TIGR02868 318 AEGSAPAAGAVGLgkptLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 81 SLAQA-----RKRIGYVPQRGSVdwdFPTSVLDVVMMGlygqlgwfkRPGPRErEAALRCLEQV-----------SMQAF 144
Cdd:TIGR02868 398 PVSSLdqdevRRRVSVCAQDAHL---FDTTVRENLRLA---------RPDATD-EELWAALERVgladwlralpdGLDTV 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 145 TTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHElKKQGKTVVVVHHDL 211
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
34-250 |
7.74e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 117.11 E-value: 7.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 34 LWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ--ARKR-IGYVPQRGSVdwdFP-TSVLDV 109
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlhARDRkVGFVFQHYAL---FRhMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 110 VMMGLyGQLGWFKRPGPRE-REAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEE 188
Cdd:PRK10851 95 IAFGL-TVLPRRERPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917519534 189 AILRVLHELKKQGK-TVVVVHHDLETVRDYFDHltllnVQVIASGPMEEVFTPENLKRTYGER 250
Cdd:PRK10851 174 ELRRWLRQLHEELKfTSVFVTHDQEEAMEVADR-----VVVMSQGNIEQAGTPDQVWREPATR 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
19-243 |
1.43e-30 |
|
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: 113.49 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ---ARKRIGYVPQR 95
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 96 GSVdwdFP-TSVLDVVMMGLYGQlgwfKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYF 174
Cdd:cd03300 81 YAL---FPhLTVFENIAFGLRLK----KLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917519534 175 MDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLE---TVRDYfdhltllnVQVIASGPMEEVFTPENL 243
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEealTMSDR--------IAVMNKGKIQQIGTPEEI 218
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
31-245 |
1.62e-30 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 116.49 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 31 KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ---------ARKRIGYVPQRGSVdwd 101
Cdd:TIGR01186 6 KKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKqspvelrevRRKKIGMVFQQFAL--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 102 FP-TSVLDVVMMGLyGQLGWfkrPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFA 180
Cdd:TIGR01186 83 FPhMTILQNTSLGP-ELLGW---PEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 181 GVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLLNvqviaSGPMEEVFTPENLKR 245
Cdd:TIGR01186 159 ALDPLIRDSMQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMK-----AGEIVQVGTPDEILR 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
9-251 |
1.88e-30 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 114.11 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 9 QHPESGASspLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ---- 84
Cdd:PRK10575 4 YTNHSDTT--FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwssk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 85 --ARKrIGYVPQRgsvdwdFPT----SVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQ 158
Cdd:PRK10575 82 afARK-VAYLPQQ------LPAaegmTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 159 RVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEE 236
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGgEMIAQGTPAE 234
|
250
....*....|....*
gi 917519534 237 VFTPENLKRTYGERM 251
Cdd:PRK10575 235 LMRGETLEQIYGIPM 249
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-224 |
2.47e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 113.95 E-value: 2.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLV---PVASGQVRFFGQSLAQA---------- 85
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREgrlardirks 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 86 RKRIGYVPQRGSVDWDFptSVLDVVMMGLYGQ-------LGWFKrpgPREREAALRCLEQVSMQAFTTRQISQLSGGQQQ 158
Cdd:PRK09984 85 RANTGYIFQQFNLVNRL--SVLENVLIGALGStpfwrtcFSWFT---REQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 159 RVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLL 224
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVAL 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-216 |
5.48e-30 |
|
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: 112.32 E-value: 5.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR--EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ-----SLAQARKRIGY 91
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQrgsvdwD---FPTSVLDVVMMGlygqlgwfkRPGPrEREAALRCLEQVSMQAFTTR-------QI----SQLSGGQQ 157
Cdd:cd03251 81 VSQ------DvflFNDTVAENIAYG---------RPGA-TREEVEEAARAANAHEFIMElpegydtVIgergVKLSGGQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 158 QRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKqGKTVVVVHHDLETVRD 216
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIEN 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-212 |
9.20e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.27 E-value: 9.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVvyreKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ-----SLAQA-RKRIGYV 92
Cdd:COG1129 257 LEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirSPRDAiRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQrgsvdwD------FPT-SVLDVVMMGLYGQLGWFKR-PGPREREAALRCLEQVSMQAFTTRQ-ISQLSGGQQQRVFLA 163
Cdd:COG1129 333 PE------DrkgeglVLDlSIRENITLASLDRLSRGGLlDRRRERALAEEYIKRLRIKTPSPEQpVGNLSGGNQQKVVLA 406
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 917519534 164 RALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLE 212
Cdd:COG1129 407 KWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELP 455
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
16-237 |
1.20e-29 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 111.74 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 16 SSPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRffgqslAQARKRIGYVPQR 95
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLRIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 96 GSVDWDFPTSVLDVVMMglygqlgwfkRPGPReREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFM 175
Cdd:PRK09544 76 LYLDTTLPLTVNRFLRL----------RPGTK-KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917519534 176 DEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLNVQVIASGPMEEV 237
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPEVV 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-252 |
2.82e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 110.37 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL------AQARKRIGYV 92
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplhARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVDWDFptSVLDVVMMGLYGQLGWFKRpgpREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADL 172
Cdd:PRK10895 84 PQEASIFRRL--SVYDNLMAVLQIRDDLSAE---QREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFTPENLKRTY-GER 250
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQgHLIAHGTPTEILQDEHVKRVYlGED 238
|
..
gi 917519534 251 MR 252
Cdd:PRK10895 239 FR 240
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
28-214 |
4.02e-29 |
|
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: 110.11 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 28 YREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFG----QSLAQARKRIGYV-PQRGSVDWDF 102
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwKRRKKFLRRIGVVfGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 103 PtsvldvVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGV 182
Cdd:cd03267 111 P------VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190
....*....|....*....|....*....|...
gi 917519534 183 DAVTEEAILRVLHEL-KKQGKTVVVVHHDLETV 214
Cdd:cd03267 185 DVVAQENIRNFLKEYnRERGTTVLLTSHYMKDI 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-241 |
5.34e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 111.44 E-value: 5.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 14 GASSPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA----QARKRI 89
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPsrarHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 90 GYVPQRGSVDWDFpTSVLDVVMMGLYgqlgwFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQD 169
Cdd:PRK13537 83 GVVPQFDNLDPDF-TVRENLLVFGRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917519534 170 ADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTPE 241
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIeEGRKIAEGAPHALIESE 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
18-210 |
5.72e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 110.15 E-value: 5.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 18 PLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKRIGYVPQRGS 97
Cdd:PRK11247 12 PLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 98 -VDWdfpTSVLDVVMMGLYGQlgWfkrpgpreREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMD 176
Cdd:PRK11247 92 lLPW---KKVIDNVGLGLKGQ--W--------RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190
....*....|....*....|....*....|....*
gi 917519534 177 EPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHD 210
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHD 193
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-232 |
7.09e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 109.87 E-value: 7.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 10 HPESGASSPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKA---VLGLVPV--ASGQVRFFGQSL-- 82
Cdd:PRK14243 2 STLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLya 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 83 -----AQARKRIGYVPQRGSvdwDFPTSVLDVV-----MMGLYGQLGwfkrpgprerEAALRCLEQVSMQAFTTRQISQ- 151
Cdd:PRK14243 82 pdvdpVEVRRRIGMVFQKPN---PFPKSIYDNIaygarINGYKGDMD----------ELVERSLRQAALWDEVKDKLKQs 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 152 ---LSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQgKTVVVVHHDLETVRDYFDHLTLLNVQV 228
Cdd:PRK14243 149 glsLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNVEL 227
|
....
gi 917519534 229 IASG 232
Cdd:PRK14243 228 TEGG 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
32-217 |
9.42e-29 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 108.26 E-value: 9.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 32 PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKR-IGYVPQR-GSVDWDF---PT-S 105
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaIPYLRRKiGVVFQDFrllPDrN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 106 VLDVVMMGLygQLGWFKRPGPREREAALrcLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAV 185
Cdd:cd03292 95 VYENVAFAL--EVTGVPPREIRKRVPAA--LELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190
....*....|....*....|....*....|..
gi 917519534 186 TEEAILRVLHELKKQGKTVVVVHHDLETVRDY 217
Cdd:cd03292 171 TTWEIMNLLKKINKAGTTVVVATHAKELVDTT 202
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-252 |
1.24e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 109.47 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 21 VRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQS--------LAQARKRIGYV 92
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipamsrsrLYTVRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVDWDFptSVLDVVMMGL--YGQLgwfkrPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDA 170
Cdd:PRK11831 90 FQSGALFTDM--NVFDNVAYPLreHTQL-----PAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 171 DLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLNVQ-VIASGpmeevfTPENLKRTYG 248
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKkIVAHG------SAQALQANPD 236
|
....
gi 917519534 249 ERMR 252
Cdd:PRK11831 237 PRVR 240
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
36-212 |
1.49e-28 |
|
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: 107.77 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 36 DVDLEVPaGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARK---------RIGYVPQRGSVdwdFPTsv 106
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKkinlppqqrKIGLVFQQYAL---FPH-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 107 LDVVMMGLYGQLgwFKRPGP-REREAALrcLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAV 185
Cdd:cd03297 90 LNVRENLAFGLK--RKRNREdRISVDEL--LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180
....*....|....*....|....*...
gi 917519534 186 TEEAILRVLHELKKQ-GKTVVVVHHDLE 212
Cdd:cd03297 166 LRLQLLPELKQIKKNlNIPVIFVTHDLS 193
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-239 |
1.59e-28 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 113.81 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY--REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ-----ARKRIGY 91
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQidpadLRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVdwdFPTSVLDVVMMGlygqlgwfkRPGPRErEAALRCLEQVSMQAFTTR-------QISQ----LSGGQQQRV 160
Cdd:TIGR03375 544 VPQDPRL---FYGTLRDNIALG---------APYADD-EEILRAAELAGVTEFVRRhpdgldmQIGErgrsLSGGQRQAV 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 161 FLARALAQDADLYFMDEPFAGVDAVTEEailRVLHELKK--QGKTVVVVHHDLeTVRDYFDHLTLL-NVQVIASGPMEEV 237
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMDNRSEE---RFKDRLKRwlAGKTLVLVTHRT-SLLDLVDRIIVMdNGRIVADGPKDQV 686
|
..
gi 917519534 238 FT 239
Cdd:TIGR03375 687 LE 688
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-232 |
2.71e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.67 E-value: 2.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 21 VRDLTVVYRE-KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-----RKRIGYVPQ 94
Cdd:PRK13647 7 VEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEnekwvRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 RGSvDWDFPTSVLDVVMMGLYgQLGWFKRPGPREREAALRCleqVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYF 174
Cdd:PRK13647 87 DPD-DQVFSSTVWDDVAFGPV-NMGLDKDEVERRVEEALKA---VRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 175 MDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASG 232
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEgRVLAEG 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-232 |
4.59e-28 |
|
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: 105.47 E-value: 4.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY--REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA----RKRIGYV 92
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLekalSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVdwdFPTSvldvvmmgLYGQLGwfkrpgprereaalrcleqvsmqafttrqiSQLSGGQQQRVFLARALAQDADL 172
Cdd:cd03247 81 NQRPYL---FDTT--------LRNNLG------------------------------RRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHELKKqGKTVVVVHHDLETVrDYFDHLTLL-NVQVIASG 232
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTGI-EHMDKILFLeNGKIIMQG 178
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-214 |
5.56e-28 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 105.21 E-value: 5.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVvyreKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ-----SLAQARKR-IGYV 92
Cdd:cd03215 5 LEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrSPRDAIRAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQrgsvdwdfptsvlDVVMMGLYGQLgwfkrpgPREREAALRCLeqvsmqafttrqisqLSGGQQQRVFLARALAQDADL 172
Cdd:cd03215 81 PE-------------DRKREGLVLDL-------SVAENIALSSL---------------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETV 214
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDEL 167
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-242 |
1.08e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.07 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 2 ITQPKTVQHPESGASSP----LRVRDLTVVY--REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLikavLGLVP----VA 71
Cdd:PRK11160 318 TEQKPEVTFPTTSTAAAdqvsLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTL----LQLLTrawdPQ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 72 SGQVRFFGQSL-----AQARKRIGYVPQRGSVdwdFPTSVLDVVMMGLygqlgwfkrpgPREREAALR-CLEQVSMQAFT 145
Cdd:PRK11160 394 QGEILLNGQPIadyseAALRQAISVVSQRVHL---FSATLRDNLLLAA-----------PNASDEALIeVLQQVGLEKLL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 146 T-------------RQisqLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELkKQGKTVVVVHHDLe 212
Cdd:PRK11160 460 EddkglnawlgeggRQ---LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRL- 534
|
250 260 270
....*....|....*....|....*....|.
gi 917519534 213 TVRDYFDHLTLL-NVQVIASGPMEEVFTPEN 242
Cdd:PRK11160 535 TGLEQFDRICVMdNGQIIEQGTHQELLAQQG 565
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-232 |
2.00e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.99 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 11 PESGASSPLRVrDLTVV---YREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ--- 84
Cdd:PRK13536 32 SIPGSMSTVAI-DLAGVsksYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPArar 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 85 -ARKRIGYVPQRGSVDWDFpTSVLDVVMMGLYGQLGwfkrpgPREREAAL-RCLEQVSMQAFTTRQISQLSGGQQQRVFL 162
Cdd:PRK13536 111 lARARIGVVPQFDNLDLEF-TVRENLLVFGRYFGMS------TREIEAVIpSLLEFARLESKADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917519534 163 ARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNVQV-IASG 232
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRkIAEG 254
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-224 |
2.16e-27 |
|
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: 104.76 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKP----ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFG----QSLAQARKRIG 90
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVP-QRGSVDWdfpTSVLDvvMMGLYGQLGWFKRpgpREREAALRCL-EQVSMQAFTTRQISQLSGGQQQRVFLARALAQ 168
Cdd:cd03266 82 FVSdSTGLYDR---LTARE--NLEYFAGLYGLKG---DELTARLEELaDRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 169 DADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL 224
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
15-238 |
2.36e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 105.82 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 15 ASSPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAV-----------------LGLVPVASGQVRF 77
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsegsivvngqtINLVRDKDGQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 78 FGQS-LAQARKRIGYVPQRGSVdWDFPTsVLDVVMMGLYGQLGWFKRPGpreREAALRCLEQVSM-QAFTTRQISQLSGG 155
Cdd:PRK10619 82 ADKNqLRLLRTRLTMVFQHFNL-WSHMT-VLENVMEAPIQVLGLSKQEA---RERAVKYLAKVGIdERAQGKYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 156 QQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNVQVI-ASGPM 234
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIeEEGAP 236
|
....
gi 917519534 235 EEVF 238
Cdd:PRK10619 237 EQLF 240
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
32-216 |
2.49e-27 |
|
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: 104.82 E-value: 2.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 32 PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRF---FGQ-SLAQA---------RKRIGYVPQrgsv 98
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWvDLAQAspreilalrRRTIGYVSQ---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 99 dwdF----P-TSVLDVVMMGLYgQLGWfKRPGPRER-EAALRCLE------QVSMQAFttrqisqlSGGQQQRVFLARAL 166
Cdd:COG4778 101 ---FlrviPrVSALDVVAEPLL-ERGV-DREEARARaRELLARLNlperlwDLPPATF--------SGGEQQRVNIARGF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 917519534 167 AQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLEtVRD 216
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEE-VRE 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
21-242 |
4.32e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.46 E-value: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 21 VRDLTVVYR--EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFG-----QSLAQARKRIGYVP 93
Cdd:PRK13632 10 VENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 94 QrgSVDWDF-PTSVLDVVMMGLYGqlgwfKRPGPREREAALRCL-EQVSMQAFTTRQISQLSGGQQQRVFLARALAQDAD 171
Cdd:PRK13632 90 Q--NPDNQFiGATVEDDIAFGLEN-----KKVPPKKMKDIIDDLaKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917519534 172 LYFMDEPFAGVDAVTEEAILRVLHELKKQG-KTVVVVHHDLETV--RDYFdhLTLLNVQVIASGPMEEVFTPEN 242
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAilADKV--IVFSEGKLIAQGKPKEILNNKE 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-210 |
8.01e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.23 E-value: 8.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 21 VRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFfgqslaQARKRIGYVPQrgSVDW 100
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI------PKGLRIGYLPQ--EPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 101 DFPTSVLDVVMMGLygqlgwfkrpgpREREAALRCLEQVSMQAFTT---------------------------------- 146
Cdd:COG0488 73 DDDLTVLDTVLDGD------------AELRALEAELEELEAKLAEPdedlerlaelqeefealggweaearaeeilsglg 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917519534 147 -------RQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAvteEAILRVLHELKKQGKTVVVVHHD 210
Cdd:COG0488 141 fpeedldRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL---ESIEWLEEFLKNYPGTVLVVSHD 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-242 |
1.36e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 103.77 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKA---VLGLVPVA--SGQVRFFGQSL-------AQAR 86
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIyspdvdpIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 87 KRIGYVPQRGSvdwDFP-TSVLDVVMMGL-YGQLGWFKRPGPREREAALR---CLEQVSMQafTTRQISQLSGGQQQRVF 161
Cdd:PRK14267 85 REVGMVFQYPN---PFPhLTIYDNVAIGVkLNGLVKSKKELDERVEWALKkaaLWDEVKDR--LNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 162 LARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVR--DYFDHLTLlnVQVIASGPMEEVF- 238
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvsDYVAFLYL--GKLIEVGPTRKVFe 237
|
....
gi 917519534 239 TPEN 242
Cdd:PRK14267 238 NPEH 241
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-243 |
2.11e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.03 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL-----AQARKR-IGYV 92
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirspRDAIALgIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVdwdFPT-SVLDVVMMGLYGQLGWFKRPGpREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDAD 171
Cdd:COG3845 86 HQHFML---VPNlTVAENIVLGLEPTKGGRLDRK-AARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 172 LYFMDEPfagvDAV-----TEEaILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVfTPENL 243
Cdd:COG3845 162 ILILDEP----TAVltpqeADE-LFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLrRGKVVGTVDTAET-SEEEL 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-232 |
3.57e-26 |
|
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: 101.42 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPalWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ---ARKRIGYVPQR 95
Cdd:cd03298 1 VRLDKIRFSYGEQP--MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAappADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 96 GSVdwdFP-TSVLDVVMMGLYGQLgwfkRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYF 174
Cdd:cd03298 79 NNL---FAhLTVEQNVGLGLSPGL----KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 175 MDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLL-NVQVIASG 232
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLdNGRIAAQG 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
36-237 |
4.56e-26 |
|
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: 104.42 E-value: 4.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 36 DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARK---------RIGYVPQRGSVdwdFPTsv 106
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKgiflppekrRIGYVFQEARL---FPH-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 107 LDVVMMGLYGQlgWFKRPGPREREAAlRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVT 186
Cdd:TIGR02142 90 LSVRGNLRYGM--KRARPSERRISFE-RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917519534 187 EEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEV 237
Cdd:TIGR02142 167 KYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLeDGRVAAAGPIAEV 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
19-210 |
7.63e-26 |
|
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: 100.79 E-value: 7.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA--QARKR-IGYVPQR 95
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTdlPPKDRdIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 96 GSVdwdFP-TSVLDVVMMGLygQLGWFKRPGPRER--EAAlrclEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADL 172
Cdd:cd03301 81 YAL---YPhMTVYDNIAFGL--KLRKVPKDEIDERvrEVA----ELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 917519534 173 YFMDEPFAGVDA---VTEEAILRVLHelKKQGKTVVVVHHD 210
Cdd:cd03301 152 FLMDEPLSNLDAklrVQMRAELKRLQ--QRLGTTTIYVTHD 190
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-212 |
1.18e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.72 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVV-YREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL-----AQARKR-IGY 91
Cdd:COG3845 258 LEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglspRERRRLgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQ----RGSVDwDFptSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQvsMQAFTTR------QISQLSGGQQQRVF 161
Cdd:COG3845 338 IPEdrlgRGLVP-DM--SVAENLILGRYRRPPFSRGGFLDRKAIRAFAEEL--IEEFDVRtpgpdtPARSLSGGNQQKVI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 917519534 162 LARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLE 212
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLD 463
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
30-209 |
1.33e-25 |
|
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: 100.36 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 30 EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ-----ARKRIGYVPQRGSVdwdFPT 104
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQldpadLRRNIGYVPQDVTL---FYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 105 SVLDVVMMGLygqlgwfkrpGPREREAALRCLEQVSMQAFTTR-------QIS----QLSGGQQQRVFLARALAQDADLY 173
Cdd:cd03245 93 TLRDNITLGA----------PLADDERILRAAELAGVTDFVNKhpngldlQIGergrGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 917519534 174 FMDEPFAGVDAVTEEailRVLHELKK--QGKTVVVVHH 209
Cdd:cd03245 163 LLDEPTSAMDMNSEE---RLKERLRQllGDKTLIIITH 197
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-242 |
1.76e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.89 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 12 ESGASSP--LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPV------ASGQVRFFGQSLA 83
Cdd:PRK14246 2 EAGKSAEdvFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKDIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 84 QA-----RKRIGYVPQRGSvdwDFPtsvldvvMMGLYGQLGW-FKRPGPREREAALRCLEQVSMQAFTTRQI-------- 149
Cdd:PRK14246 82 QIdaiklRKEVGMVFQQPN---PFP-------HLSIYDNIAYpLKSHGIKEKREIKKIVEECLRKVGLWKEVydrlnspa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 150 SQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQgKTVVVVHHDLETVRDYFDHLTLL-NVQV 228
Cdd:PRK14246 152 SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLyNGEL 230
|
250
....*....|....*
gi 917519534 229 IASGPMEEVFT-PEN 242
Cdd:PRK14246 231 VEWGSSNEIFTsPKN 245
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-224 |
2.05e-25 |
|
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: 99.16 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPA------LWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVA--SGQVRFFGQSLAQA--RKR 88
Cdd:cd03213 4 LSFRNLTVTVKSSPSksgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRsfRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 89 IGYVPQRGSVdwdFPTsvLDVvmmglygqlgwfkrpgpreREAalrcleqVSMQAfttrQISQLSGGQQQRVFLARALAQ 168
Cdd:cd03213 84 IGYVPQDDIL---HPT--LTV-------------------RET-------LMFAA----KLRGLSGGERKRVSIALELVS 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 169 DADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDL-ETVRDYFDHLTLL 224
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLL 185
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
33-245 |
3.00e-25 |
|
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: 102.04 E-value: 3.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 33 ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ---SLAQARKRIGYVPQRGSVdwdFPT-SVLD 108
Cdd:TIGR03265 19 ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRditRLPPQKRDYGIVFQSYAL---FPNlTVAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 109 VVMMGLYGQLGwfKRPGPREREAALrcLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEE 188
Cdd:TIGR03265 96 NIAYGLKNRGM--GRAEVAERVAEL--LDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVRE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 189 AILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLNVQVIasgpmEEVFTPENLKR 245
Cdd:TIGR03265 172 HLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVI-----EQVGTPQEIYR 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-217 |
3.22e-25 |
|
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: 99.11 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYRE--KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ-----ARKRIGY 91
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiglhdLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQ-----RGSVdwdfpTSVLDvvmmglygqlgwfkrpgPRER---EAALRCLEQVSMQAFTTRQI-----------SQL 152
Cdd:cd03244 83 IPQdpvlfSGTI-----RSNLD-----------------PFGEysdEELWQALERVGLKEFVESLPggldtvveeggENL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917519534 153 SGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKqGKTVVVVHHDLETVRDY 217
Cdd:cd03244 141 SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAHRLDTIIDS 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
34-212 |
3.49e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 99.50 E-value: 3.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 34 LWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ----AR-----KRIGYVPQRGSVDWDFpT 104
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaAKaelrnQKLGFIYQFHHLLPDF-T 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 105 SVLDVVMMGLYGQlgwfKRPGpREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDA 184
Cdd:PRK11629 104 ALENVAMPLLIGK----KKPA-EINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180
....*....|....*....|....*....
gi 917519534 185 VTEEAILRVLHEL-KKQGKTVVVVHHDLE 212
Cdd:PRK11629 179 RNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-236 |
3.55e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.77 E-value: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 3 TQPKTVQHPESGASSPLRVRDLTVVYRE-KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVaSGQVRFFGQ- 80
Cdd:PRK11174 334 HPQQGEKELASNDPVTIEAEDLEILSPDgKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIe 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 81 ----SLAQARKRIGYVPQRGSVdwdFPTSVLDVVMMGlygqlgwfkrpGPREREAALR-CLEQVSMQAFTTR-------- 147
Cdd:PRK11174 413 lrelDPESWRKHLSWVGQNPQL---PHGTLRDNVLLG-----------NPDASDEQLQqALENAWVSEFLPLlpqgldtp 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 148 ---QISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELkKQGKTVVVVHHDLETVRDYFDHLTLL 224
Cdd:PRK11174 479 igdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA-SRRQTTLMVTHQLEDLAQWDQIWVMQ 557
|
250
....*....|..
gi 917519534 225 NVQVIASGPMEE 236
Cdd:PRK11174 558 DGQIVQQGDYAE 569
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
36-225 |
1.08e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 98.11 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 36 DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVP---VASGQVRFFGQSL--AQARKRIGYVPQRgsvdwDFPTSVLDV- 109
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRkpDQFQKCVAYVRQD-----DILLPGLTVr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 110 ------VMMglygQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVD 183
Cdd:cd03234 100 etltytAIL----RLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 917519534 184 AVTEEAILRVLHELKKQGKTVVV-VHHDLETVRDYFDHLTLLN 225
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLS 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-252 |
1.09e-24 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 99.13 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVP--------VASGQVRFFGQSLAQ------ 84
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAidaprl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 85 ARKRiGYVPQRGSVdwDFPTSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLAR 164
Cdd:PRK13547 82 ARLR-AVLPQAAQP--AFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 165 ALAQ---------DADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKT-VVVVHHDLETVRDYFDHLTLL-NVQVIASGP 233
Cdd:PRK13547 159 VLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLaDGAIVAHGA 238
|
250
....*....|....*....
gi 917519534 234 MEEVFTPENLKRTYGERMR 252
Cdd:PRK13547 239 PADVLTPAHIARCYGFAVR 257
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
32-216 |
1.31e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.24 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 32 PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA-------QARKRIGYVPQRGSVdwdFP- 103
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkvderLIRQEAGMVFQQFYL---FPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 104 TSVLDVVMMGLYGQLGWFKRPGpreREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVD 183
Cdd:PRK09493 92 LTALENVMFGPLRVRGASKEEA---EKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190
....*....|....*....|....*....|...
gi 917519534 184 AVTEEAILRVLHELKKQGKTVVVVHHDLETVRD 216
Cdd:PRK09493 169 PELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEK 201
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-210 |
1.55e-24 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 101.63 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 18 PLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVP-------VASGQVRFFGQSLAQARKRIG 90
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPqgysndlTLFGRRRGSGETIWDIKKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQRGSVDWDFPTSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTTRQ-ISQLSGGQQQRVFLARALAQD 169
Cdd:PRK10938 340 YVSSSLHLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKRTADApFHSLSWGQQRLALIVRALVKH 419
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 917519534 170 ADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKT--VVVVHHD 210
Cdd:PRK10938 420 PTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqlLFVSHHA 462
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
20-239 |
1.69e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 99.88 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 20 RVRDLTVVY----REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ--------SLAQARK 87
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 88 RIGYVPQ-------RgsvdwdfptSVLDVVMMGLygQLGWFKRPGPREREAALrcLEQVSMQAFTTRQISQLSGGQQQRV 160
Cdd:PRK11153 83 QIGMIFQhfnllssR---------TVFDNVALPL--ELAGTPKAEIKARVTEL--LELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 161 FLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVF 238
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIdAGRLVEQGTVSEVF 229
|
.
gi 917519534 239 T 239
Cdd:PRK11153 230 S 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-217 |
1.71e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 99.39 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREK-----PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFG-------------- 79
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 80 ---------------QSLAQARKRIGYVPQRGSVDWdFPTSVLDVVMMGlygqlgwfkrP---GPREREAALRCLEQVSM 141
Cdd:PRK13651 83 vleklviqktrfkkiKKIKEIRRRVGVVFQFAEYQL-FEQTIEKDIIFG----------PvsmGVSKEEAKKRAAKYIEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 142 ----QAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDY 217
Cdd:PRK13651 152 vgldESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEW 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-223 |
2.08e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.42 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 3 TQPKTVQHPESGASSPLRVRDLTVV-YREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFfgqs 81
Cdd:COG4178 347 ALPEAASRIETSEDGALALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 82 laQARKRIGYVPQR-----GSVDwdfptSVLdvvmmgLYgqlgwfkrPGPRER---EAALRCLEQVSMQAFTTR------ 147
Cdd:COG4178 423 --PAGARVLFLPQRpylplGTLR-----EAL------LY--------PATAEAfsdAELREALEAVGLGHLAERldeead 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 148 --QIsqLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHdlETVRDYFDH-LTL 223
Cdd:COG4178 482 wdQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR--STLAAFHDRvLEL 556
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-246 |
2.19e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.19 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVAS-----GQVRFFGQSLAQARKRIGYVP 93
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 94 QRGSVDWD----FPTSVLDVVMMGLyGQLGWfkRPGPREREAALRCLEQVSMQAFTTRQISQ----LSGGQQQRVFLARA 165
Cdd:PRK14258 88 RQVSMVHPkpnlFPMSVYDNVAYGV-KIVGW--RPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 166 LAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGK-TVVVVHHDLETVRDYFDHLTLLN------VQVIASGPMEEVF 238
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKgnenriGQLVEFGLTKKIF 244
|
....*...
gi 917519534 239 TPENLKRT 246
Cdd:PRK14258 245 NSPHDSRT 252
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-238 |
2.77e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.91 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 5 PKTVQHPESGASSPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ 84
Cdd:PRK11607 6 PRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 85 A---RKRIGYVPQRGSVdwdFP-TSVLDVVMMGLygqlgwfKRPGPREREAALRC---LEQVSMQAFTTRQISQLSGGQQ 157
Cdd:PRK11607 86 VppyQRPINMMFQSYAL---FPhMTVEQNIAFGL-------KQDKLPKAEIASRVnemLGLVHMQEFAKRKPHQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 158 QRVFLARALAQDADLYFMDEPFAGVDAVTEEAI-LRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLN----VQViasG 232
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNrgkfVQI---G 232
|
....*.
gi 917519534 233 PMEEVF 238
Cdd:PRK11607 233 EPEEIY 238
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-239 |
2.92e-24 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 101.27 E-value: 2.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY--REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQAR-----KRIGY 91
Cdd:TIGR01842 317 LSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDretfgKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVdwdFPTSVL-DVVMMGlygqlgwfKRPGPREREAALRcLEQVSM------QAFTTrQI----SQLSGGQQQRV 160
Cdd:TIGR01842 397 LPQDVEL---FPGTVAeNIARFG--------ENADPEKIIEAAK-LAGVHElilrlpDGYDT-VIgpggATLSGGQRQRI 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 161 FLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHH--DLETVRDYFdhLTLLNVQVIASGPMEEVF 238
Cdd:TIGR01842 464 ALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHrpSLLGCVDKI--LVLQDGRIARFGERDEVL 541
|
.
gi 917519534 239 T 239
Cdd:TIGR01842 542 A 542
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
30-244 |
4.94e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 97.78 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 30 EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRfFGQSLAQA----------RKRIGYVPQrgsvd 99
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGERVITAgkknkklkplRKKVGIVFQ----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 100 wdFPTSVL-------DVVmmglYGQLGWfkrpGPREREAALRCLEQVSM----QAFTTRQISQLSGGQQQRVFLARALAQ 168
Cdd:PRK13634 93 --FPEHQLfeetvekDIC----FGPMNF----GVSEEDAKQKAREMIELvglpEELLARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 169 DADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFT-PENLK 244
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMhKGTVFLQGTPREIFAdPDELE 241
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-216 |
7.49e-24 |
|
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: 99.89 E-value: 7.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 18 PLRVRDLTVVYR--------EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ---SLAQA- 85
Cdd:COG5265 350 PLVVGGGEVRFEnvsfgydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdirDVTQAs 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 86 -RKRIGYVPQrgsvdwdfptsvlDVVMMG-------LYGqlgwfkRPG--PREREAALRcLEQVSmqAFttrqISQ---- 151
Cdd:COG5265 430 lRAAIGIVPQ-------------DTVLFNdtiayniAYG------RPDasEEEVEAAAR-AAQIH--DF----IESlpdg 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 152 -----------LSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELkKQGKTVVVVHHDLETVRD 216
Cdd:COG5265 484 ydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLVIAHRLSTIVD 558
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
33-238 |
7.77e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.11 E-value: 7.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 33 ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRF--FGQSLAQARKRIGYVPQRGSVDWDFPTSVL--D 108
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdIVVSSTSKQKEIKPVRKKVGVVFQFPESQLfeE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 109 VVMMGL-YGQLGWFKRPGPREREAALRcLEQVSM-QAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVT 186
Cdd:PRK13643 101 TVLKDVaFGPQNFGIPKEKAEKIAAEK-LEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917519534 187 EEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVF 238
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKgHIISCGTPSDVF 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
19-215 |
7.95e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 7.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKaVLGLVPVA-SGQVRFFGQSL-----------AQAR 86
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLETPdSGQLNIAGHQFdfsqkpsekaiRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 87 KRIGYVPQRGSVdWDFPTsVLDVVMMGLYGQLGWFKRpgpREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARAL 166
Cdd:COG4161 82 QKVGMVFQQYNL-WPHLT-VMENLIEAPCKVLGLSKE---QAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 917519534 167 AQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVR 215
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFAR 205
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-214 |
8.00e-24 |
|
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: 95.12 E-value: 8.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQAR----KRIGYVPQ 94
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRdephENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 RGSVDWDFptSVLDvvmmglygQLGWFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYF 174
Cdd:TIGR01189 81 LPGLKPEL--SALE--------NLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 917519534 175 MDEPFAGVDAVTEEAILRVLHE-LKKQGKTVVVVHHDLETV 214
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQDLGLV 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-239 |
8.78e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 99.76 E-value: 8.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR----EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVP----VASGQVRFFGQSLAQA----- 85
Cdd:COG4172 7 LSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLserel 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 86 RK----RIGYVPQRgsvdwdfPTSVLDVVM---------MGLYGQLGwfkrpGPREREAALRCLEQVSMQAFTTRQIS-- 150
Cdd:COG4172 87 RRirgnRIAMIFQE-------PMTSLNPLHtigkqiaevLRLHRGLS-----GAAARARALELLERVGIPDPERRLDAyp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 151 -QLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLL-NVQ 227
Cdd:COG4172 155 hQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMrQGE 234
|
250
....*....|..
gi 917519534 228 VIASGPMEEVFT 239
Cdd:COG4172 235 IVEQGPTAELFA 246
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-251 |
8.97e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.84 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYRE-KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ-------SLAQARKRIG 90
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQrgsvDWD---FPTSVLDVVMMGLYGqlgwFKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALA 167
Cdd:PRK13636 86 MVFQ----DPDnqlFSASVYQDVSFGAVN----LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 168 QDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFTPENLKR 245
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEgRVILQGNPKEVFAEKEMLR 237
|
....*.
gi 917519534 246 TYGERM 251
Cdd:PRK13636 238 KVNLRL 243
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-212 |
1.02e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.00 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAV--LG-LVP--VASGQVRFFGQSL-------AQAR 86
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNdLNPevTITGSIVYNGHNIysprtdtVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 87 KRIGYVPQRGSvdwDFPTSVLDVVMMGLygqlgwfKRPGPREREAALRCLEQVSMQAFTTRQISQ--------LSGGQQQ 158
Cdd:PRK14239 86 KEIGMVFQQPN---PFPMSIYENVVYGL-------RLKGIKDKQVLDEAVEKSLKGASIWDEVKDrlhdsalgLSGGQQQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 917519534 159 RVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQgKTVVVVHHDLE 212
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQ 208
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-243 |
1.67e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.95 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 21 VRDLTVVY---REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-----RKRIGYV 92
Cdd:PRK13650 7 VKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnvwdiRHKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQrgSVDWDF-PTSVLDVVMMGLYGQLGWFKRPGPREREAalrcLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDAD 171
Cdd:PRK13650 87 FQ--NPDNQFvGATVEDDVAFGLENKGIPHEEMKERVNEA----LELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917519534 172 LYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLetvrdyfDHLTLLN-VQVIASGPMEEVFTPENL 243
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDL-------DEVALSDrVLVMKNGQVESTSTPREL 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
28-232 |
1.80e-23 |
|
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: 94.52 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 28 YREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRffgqslaqarkrigyvpQRGSVDWDF----- 102
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-----------------VRGRVSSLLglggg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 103 --PT-SVLD-VVMMG-LYGqlgwFKRPGPREREAalRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDE 177
Cdd:cd03220 95 fnPElTGREnIYLNGrLLG----LSRKEIDEKID--EIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 178 PFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDH-LTLLNVQVIASG 232
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRaLVLEKGKIRFDG 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-239 |
1.81e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 95.36 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 17 SPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLV-----PVASGQVRFFGQS-----LAQAR 86
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDifkmdVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 87 KRIGYVPQrgsVDWDFPT-SVLDVVMMGLYgqlgwFKRPGPREREaalrcLEQVSMQAFTTRQI------------SQLS 153
Cdd:PRK14247 82 RRVQMVFQ---IPNPIPNlSIFENVALGLK-----LNRLVKSKKE-----LQERVRWALEKAQLwdevkdrldapaGKLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 154 GGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVR--DYFDHltLLNVQVIAS 231
Cdd:PRK14247 149 GGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARisDYVAF--LYKGQIVEW 226
|
....*...
gi 917519534 232 GPMEEVFT 239
Cdd:PRK14247 227 GPTREVFT 234
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-237 |
2.07e-23 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 93.75 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGL--VPVASGQVRFFGQSLAQArkrigyvpqrg 96
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDL----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 97 svdwdfptSVLDVVMMGLYgqLGwFKRPgPRereaalrcLEQVSMQAFtTRQISQ-LSGGQQQRVFLARALAQDADLYFM 175
Cdd:cd03217 70 --------PPEERARLGIF--LA-FQYP-PE--------IPGVKNADF-LRYVNEgFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917519534 176 DEPFAGVDAVTEEAILRVLHELKKQGKTVVVV-HHD--LETVRDYFDHLtLLNVQVIASGPMEEV 237
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEGKSVLIItHYQrlLDYIKPDRVHV-LYDGRIVKSGDKELA 192
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-243 |
3.20e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 95.62 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR-----EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFG---------QSLAQ 84
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 85 ARKRIGYVPQrgsvdwdFPTSVL---DVVMMGLYGQLGwFKRPGPREREAALRCLeqvsMQAFTTRQIS-----QLSGGQ 156
Cdd:PRK13646 83 VRKRIGMVFQ-------FPESQLfedTVEREIIFGPKN-FKMNLDEVKNYAHRLL----MDLGFSRDVMsqspfQMSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 157 QQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELK-KQGKTVVVVHHDLETVRDYFDhltllNVQVIASGPME 235
Cdd:PRK13646 151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYAD-----EVIVMKEGSIV 225
|
....*...
gi 917519534 236 EVFTPENL 243
Cdd:PRK13646 226 SQTSPKEL 233
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-215 |
3.55e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 94.31 E-value: 3.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKaVLGLVPVA-SGQVRFFGQ-----------SLAQAR 86
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEMPrSGTLNIAGNhfdfsktpsdkAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 87 KRIGYVPQRGSVdWDFPTsvldvVMMGLYGQ----LGWFKrpgPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFL 162
Cdd:PRK11124 82 RNVGMVFQQYNL-WPHLT-----VQQNLIEApcrvLGLSK---DQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917519534 163 ARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVR 215
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVAR 205
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
28-237 |
4.94e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.99 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 28 YREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRffgqslaqarkrigyvpQRGSVdwdfpTSVL 107
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE-----------------VNGRV-----SALL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 108 DvVMMGLYGQL-GwfkrpgpreRE-AALRCLeqvsMQAFTTRQISQL---------------------SGGQQQRVFLAR 164
Cdd:COG1134 94 E-LGAGFHPELtG---------REnIYLNGR----LLGLSRKEIDEKfdeivefaelgdfidqpvktySSGMRARLAFAV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917519534 165 ALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEV 237
Cdd:COG1134 160 ATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLeKGRLVMDGDPEEV 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
30-247 |
5.04e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.90 E-value: 5.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 30 EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFG---------QSLAQARKRIGYVPQRGSVDW 100
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnKNLKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 101 dFPTSVLDVVMmglYGQLGwFKRPGPREREAALRCLEQVSM-QAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPF 179
Cdd:PRK13641 99 -FENTVLKDVE---FGPKN-FGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 180 AGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDH-LTLLNVQVIASGPMEEVFT-PENLKRTY 247
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDvLVLEHGKLIKHASPKEIFSdKEWLKKHY 243
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-216 |
5.95e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 5.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 18 PLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRfFGQSLaqarkRIGYVPQ-RG 96
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETV-----KIGYFDQhQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 97 SVDWDfpTSVLDvvmmglygqlgWFKRPGPREREAALR-CLEqvSM-----QAFTtrQISQLSGGQQQRVFLARALAQDA 170
Cdd:COG0488 389 ELDPD--KTVLD-----------ELRDGAPGGTEQEVRgYLG--RFlfsgdDAFK--PVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 917519534 171 DLYFMDEPFAGVDAVTEEAILRVLHELKkqGkTVVVVHHD---LETVRD 216
Cdd:COG0488 452 NVLLLDEPTNHLDIETLEALEEALDDFP--G-TVLLVSHDryfLDRVAT 497
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
26-243 |
8.34e-23 |
|
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: 93.32 E-value: 8.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 26 VVYREKP----ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-----RKRIGYVPQRG 96
Cdd:cd03252 6 VRFRYKPdgpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdpawlRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 97 SVdwdFPTSVLDVVMMGlygqlgwfkRPG-PRER-EAALR--------CLEQVSMQAFTTRQISQLSGGQQQRVFLARAL 166
Cdd:cd03252 86 VL---FNRSIRDNIALA---------DPGmSMERvIEAAKlagahdfiSELPEGYDTIVGEQGAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 167 AQDADLYFMDEPFAGVDAVTEEAILRVLHELKKqGKTVVVVHHDLETVRDYFDHLTLLNVQVIASGPMEEVFTPENL 243
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGL 229
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-212 |
9.25e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.77 E-value: 9.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 28 YREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLG-LVPvASGQVRFFGQSLAQAR----KRIGYV-PQRGSVDWD 101
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEVRVLGYVPFKRRkefaRRIGVVfGQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 102 FPtsVLDvvmmglygQLGWFKR----PGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDE 177
Cdd:COG4586 111 LP--AID--------SFRLLKAiyriPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 917519534 178 PFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLE 212
Cdd:COG4586 181 PTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMD 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
11-240 |
9.26e-23 |
|
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: 92.48 E-value: 9.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 11 PESGAsspLRVRDLTVVYREK--PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQS-----LA 83
Cdd:cd03369 2 PEHGE---IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistipLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 84 QARKRIGYVPQRgsvdwdfPTsvldvVMMG-LYGQLGWFKRPGPREREAALRCLEQVsmqafttrqiSQLSGGQQQRVFL 162
Cdd:cd03369 79 DLRSSLTIIPQD-------PT-----LFSGtIRSNLDPFDEYSDEEIYGALRVSEGG----------LNLSQGQRQLLCL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 163 ARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELkKQGKTVVVVHHDLETVRDYfDhltllNVQVIASGPMEEVFTP 240
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYATDALIQKTIREE-FTNSTILTIAHRLRTIIDY-D-----KILVMDAGEVKEYDHP 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-213 |
1.26e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.86 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFG--QSLAQARKRIGYVPQRg 96
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdIDDPDVAEACHYLGHR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 97 svdwDFPTSVLDVV-----MMGLYGQlgwfkrpgprEREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDAD 171
Cdd:PRK13539 82 ----NAMKPALTVAenlefWAAFLGG----------EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 917519534 172 LYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVV-HHDLET 213
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAAtHIPLGL 190
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
19-236 |
1.72e-22 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 96.17 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR--EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKRI-----GY 91
Cdd:TIGR03796 478 VELRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVlansvAM 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQ-----RGSVD-----WDfPT-------------SVLDVVMmglygqlgwfKRPGPREREaalrcLEQVSMQafttrq 148
Cdd:TIGR03796 558 VDQdiflfEGTVRdnltlWD-PTipdadlvrackdaAIHDVIT----------SRPGGYDAE-----LAEGGAN------ 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 149 isqLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEeaiLRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNVQV 228
Cdd:TIGR03796 616 ---LSGGQRQRLEIARALVRNPSILILDEATSALDPETE---KIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKV 689
|
....*...
gi 917519534 229 IASGPMEE 236
Cdd:TIGR03796 690 VQRGTHEE 697
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-216 |
1.92e-22 |
|
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: 92.22 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 20 RVRDLTVVYREKP---ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ-----SLAQARKRIGY 91
Cdd:cd03249 2 EFKNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVdwdFPTSVLDVVmmgLYGqlgwfkRPGPREREAalrclEQVSMQAFTTRQI---------------SQLSGGQ 156
Cdd:cd03249 82 VSQEPVL---FDGTIAENI---RYG------KPDATDEEV-----EEAAKKANIHDFImslpdgydtlvgergSQLSGGQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 157 QQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKqGKTVVVVHHDLETVRD 216
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK-GRTTIVIAHRLSTIRN 203
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-249 |
2.28e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.36 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA----QARKRIGYVPQ 94
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpgHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 RGSVDWDFPTSVLDVVMMGLYGQL------GWFKRPGPR--EREA---ALRCLEQVSMQAFTTRQISQLSGGQQQRVFLA 163
Cdd:PRK11300 86 FQHVRLFREMTVIENLLVAQHQQLktglfsGLLKTPAFRraESEAldrAATWLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 164 RALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFTPE 241
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQgTPLANGTPEEIRNNP 245
|
....*....
gi 917519534 242 NLKRTY-GE 249
Cdd:PRK11300 246 DVIKAYlGE 254
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-243 |
2.67e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.94 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR-EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-----RKRIGYV 92
Cdd:PRK13652 4 IETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnirevRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQrGSVDWDFPTSVLDVVMMGLYgQLGWFKRPGPREREAALRCLeqvSMQAFTTRQISQLSGGQQQRVFLARALAQDADL 172
Cdd:PRK13652 84 FQ-NPDDQIFSPTVEQDIAFGPI-NLGLDEETVAHRVSSALHML---GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFTPENL 243
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKgRIVAYGTVEEIFLQPDL 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
21-245 |
3.03e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.56 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 21 VRDLTVVYR--EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLG-LVP--VASGQVRFFGQSLAQ-----ARKRIG 90
Cdd:PRK13640 8 FKHVSFTYPdsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPddNPNSKITVDGITLTAktvwdIREKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQrgSVDWDF-PTSVLDVVMMGLYgqlgwfKRPGPREREAAL--RCLEQVSMQAFTTRQISQLSGGQQQRVFLARALA 167
Cdd:PRK13640 88 IVFQ--NPDNQFvGATVGDDVAFGLE------NRAVPRPEMIKIvrDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 168 QDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLNVQVIASGPMEEVFT-PENLKR 245
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSkVEMLKE 239
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
30-238 |
3.35e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.50 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 30 EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA---------QARKRIGYVPQrgsvdw 100
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkdikQIRKKVGLVFQ------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 101 dFPTS------VLDVVMMGlygqlgwfkrP---GPREREAALRCLEQVSM----QAFTTRQISQLSGGQQQRVFLARALA 167
Cdd:PRK13649 93 -FPESqlfeetVLKDVAFG----------PqnfGVSQEEAEALAREKLALvgisESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917519534 168 QDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVF 238
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKgKLVLSGKPKDIF 233
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
34-210 |
3.89e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.18 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 34 LWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ--------SLAQARKR-IGYVPQRGSVdWDFPT 104
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvatldadALAQLRREhFGFIFQRYHL-LSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 105 SVLDVVMMGLYGQLGWFKRpgpREREAALrcLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDA 184
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQR---LLRAQEL--LQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180
....*....|....*....|....*.
gi 917519534 185 VTEEAILRVLHELKKQGKTVVVVHHD 210
Cdd:PRK10535 178 HSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-252 |
4.03e-22 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 94.89 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVAS--GQVRFFGQSLAQA------RKRIG 90
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASnirdteRAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQRGSVDWDFptSVLDVVMMGlygqlGWFKRPGPREREAA--LRC---LEQVSMQAF-TTRQISQLSGGQQQRVFLAR 164
Cdd:TIGR02633 82 IIHQELTLVPEL--SVAENIFLG-----NEITLPGGRMAYNAmyLRAknlLRELQLDADnVTRPVGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 165 ALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTPENL 243
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIrDGQHVATKDMSTMSEDDII 234
|
....*....
gi 917519534 244 KRTYGERMR 252
Cdd:TIGR02633 235 TMMVGREIT 243
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-238 |
4.54e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 95.43 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 30 EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASgqvrffgQSLAQARKRIGYVPQrgsVDWDFPTSVLDV 109
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-------TSSVVIRGSVAYVPQ---VSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 110 VMMGlygqlgwfkrpGPREREAALRCLEQVSMQ----AFTTRQISQ-------LSGGQQQRVFLARALAQDADLYFMDEP 178
Cdd:PLN03232 699 ILFG-----------SDFESERYWRAIDVTALQhdldLLPGRDLTEigergvnISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917519534 179 FAGVDAVTEEAILR--VLHELkkQGKTVVVVHHDLETVrDYFDHLTLLNVQVIA-SGPMEEVF 238
Cdd:PLN03232 768 LSALDAHVAHQVFDscMKDEL--KGKTRVLVTNQLHFL-PLMDRIILVSEGMIKeEGTFAELS 827
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-223 |
4.86e-22 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 90.24 E-value: 4.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKR-------IGY 91
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiargllyLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVdwdfpTSVLDvvmmglygQLGWFKRPGprEREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDAD 171
Cdd:cd03231 81 APGIKTT-----LSVLE--------NLRFWHADH--SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRP 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 917519534 172 LYFMDEPFAGVDAVTEEAIL-RVLHELKKQGKTVVVVHHDLETVRDYFDHLTL 223
Cdd:cd03231 146 LWILDEPTTALDKAGVARFAeAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-246 |
5.12e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 91.35 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 17 SPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRF----------FGQS---LA 83
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarsLSQQkglIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 84 QARKRIGYVPQRGSVdwdFP-TSVLDVVMMGLYgqlgwFKRPGPREREAAL--RCLEQVSMQAFTTRQISQLSGGQQQRV 160
Cdd:PRK11264 82 QLRQHVGFVFQNFNL---FPhRTVLENIIEGPV-----IVKGEPKEEATARarELLAKVGLAGKETSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 161 FLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNVQVIA-SGPMEEVFT 239
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVeQGPAKALFA 233
|
....*..
gi 917519534 240 PENLKRT 246
Cdd:PRK11264 234 DPQQPRT 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-239 |
5.73e-22 |
|
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: 94.37 E-value: 5.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 4 QPKTVQHPESGASSP-LRVRDLTVVYREKPALW-----------DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPvA 71
Cdd:COG4172 260 EPRGDPRPVPPDAPPlLEARDLKVWFPIKRGLFrrtvghvkavdGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-S 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 72 SGQVRFFGQSLAQA--------RKRIGYVPQR--GSVDwdfP-TSVLDVVMMGLYGQlgwFKRPGPREREA-ALRCLEQV 139
Cdd:COG4172 339 EGEIRFDGQDLDGLsrralrplRRRMQVVFQDpfGSLS---PrMTVGQIIAEGLRVH---GPGLSAAERRArVAEALEEV 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 140 SMQ-AFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDY 217
Cdd:COG4172 413 GLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRAL 492
|
250 260
....*....|....*....|...
gi 917519534 218 FDHLTLL-NVQVIASGPMEEVFT 239
Cdd:COG4172 493 AHRVMVMkDGKVVEQGPTEQVFD 515
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
49-243 |
6.52e-22 |
|
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: 92.56 E-value: 6.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 49 IVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA---RKRIGYVPQRGSVdwdFP-TSVLDVVMMGLYGQLGWFKRP 124
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVpphLRHINMVFQSYAL---FPhMTVEENVAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 125 GPREREAalrcLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEailRVLHELK----KQ 200
Cdd:TIGR01187 78 KPRVLEA----LRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRD---QMQLELKtiqeQL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 917519534 201 GKTVVVVHHDLETVRDYFDHLTLLNvqviaSGPMEEVFTPENL 243
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSDRIAIMR-----KGKIAQIGTPEEI 188
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
19-243 |
8.28e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 93.09 E-value: 8.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ--ARKR-IGYVPQR 95
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpAENRhVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 96 GSVdwdFP-TSVLDVVMMGLYGQlgwfKRPG----PREREAalrcLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDA 170
Cdd:PRK09452 95 YAL---FPhMTVFENVAFGLRMQ----KTPAaeitPRVMEA----LRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 171 DLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLNVQVIAS-GPMEEVF-TPENL 243
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQdGTPREIYeEPKNL 239
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-238 |
1.27e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.26 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 18 PLRVRDLTVVYR-----EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFG-------QSLAQA 85
Cdd:PRK13637 2 SIKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 86 RKRIGYVPQrgsvdwdFPTSVL-------DVVmmglYGQlgwfKRPGPREREAALRCLEQVSM-----QAFTTRQISQLS 153
Cdd:PRK13637 82 RKKVGLVFQ-------YPEYQLfeetiekDIA----FGP----INLGLSEEEIENRVKRAMNIvgldyEDYKDKSPFELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 154 GGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGK-TVVVVHHDLETVRDYFDHLTLLNV-QVIAS 231
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKgKCELQ 226
|
....*..
gi 917519534 232 GPMEEVF 238
Cdd:PRK13637 227 GTPREVF 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-211 |
1.72e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 93.65 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 30 EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLG-LVPVASGQVRFfgqslaqaRKRIGYVPQrgsVDWDFPTSVLD 108
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVI--------RGTVAYVPQ---VSWIFNATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 109 VVMMGLygqlgwfkrpgPREREAALRCLEQVSMQafttRQISQL---------------SGGQQQRVFLARALAQDADLY 173
Cdd:PLN03130 698 NILFGS-----------PFDPERYERAIDVTALQ----HDLDLLpggdlteigergvniSGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 917519534 174 FMDEPFAGVDA-----VTEEAILRVLhelkkQGKTVVVVHHDL 211
Cdd:PLN03130 763 IFDDPLSALDAhvgrqVFDKCIKDEL-----RGKTRVLVTNQL 800
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
31-236 |
2.51e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 92.72 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 31 KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIkAVLGLV--PvASGQVRFFGQ-----SLAQARKRIGYVPQRGSVdwdFP 103
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVfdP-QSGRILIDGTdirtvTRASLRRNIAVVFQDAGL---FN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 104 TSVLDVVMMGlygqlgwfkRPGPREREAaLRCLEQVSMQAFTTRQI-----------SQLSGGQQQRVFLARALAQDADL 172
Cdd:PRK13657 423 RSIEDNIRVG---------RPDATDEEM-RAAAERAQAHDFIERKPdgydtvvgergRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHELKKqGKTVVVVHHDLETVRDYFDHLTLLNVQVIASGPMEE 236
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDE 555
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
33-238 |
2.93e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.81 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 33 ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRF-----FGQSLAQARKRIGYVPQR------GS-VDW 100
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYnnqaiTDDNFEKLRKHIGIVFQNpdnqfvGSiVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 101 DfptsvldvVMMGLYGQLgwfkRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFA 180
Cdd:PRK13648 104 D--------VAFGLENHA----VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917519534 181 GVDAVTEEAILRVLHELKKQGK-TVVVVHHDL-ETVRDyfDHLTLLNV-QVIASGPMEEVF 238
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNiTIISITHDLsEAMEA--DHVIVMNKgTVYKEGTPTEIF 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-243 |
3.53e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 90.68 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKP-----ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVR----FFGQSLAQARKRI 89
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 90 GYVPQ----------RGSVDWDFP------TSVLDVVMMGLYGqlgwFKRPGPREREAALRCLEQVSMQ-AFTTRQISQL 152
Cdd:PRK13631 102 NPYSKkiknfkelrrRVSMVFQFPeyqlfkDTIEKDIMFGPVA----LGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 153 SGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIAS 231
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKgKILKT 257
|
250
....*....|..
gi 917519534 232 GPMEEVFTPENL 243
Cdd:PRK13631 258 GTPYEIFTDQHI 269
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
19-210 |
4.15e-21 |
|
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: 86.35 E-value: 4.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFfgqslaQARKRIGYVPqrgsv 98
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW------GSTVKIGYFE----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 99 dwdfptsvldvvmmglygqlgwfkrpgprereaalrcleqvsmqafttrqisQLSGGQQQRVFLARALAQDADLYFMDEP 178
Cdd:cd03221 70 ----------------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|..
gi 917519534 179 FAGVDAVTEEAILRVLHELKkqgKTVVVVHHD 210
Cdd:cd03221 98 TNHLDLESIEALEEALKEYP---GTVILVSHD 126
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-183 |
8.86e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 91.34 E-value: 8.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 20 RVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLikavLGLVPVA----SGQVRFFGQSLAQAR------KRI 89
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSL----LSLIAGArkiqQGRVEVLGGDMADARhrravcPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 90 GYVPQrG---------SV--DWDFptsvldvvmMG-LYGQlgwfkrpGPREREAAL-RCLEQVSMQAFTTRQISQLSGGQ 156
Cdd:NF033858 79 AYMPQ-GlgknlyptlSVfeNLDF---------FGrLFGQ-------DAAERRRRIdELLRATGLAPFADRPAGKLSGGM 141
|
170 180
....*....|....*....|....*..
gi 917519534 157 QQRVFLARALAQDADLYFMDEPFAGVD 183
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
32-212 |
1.86e-20 |
|
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: 86.62 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 32 PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRF---------FGQSLAQARKRIGYVPQRgsvDWDF 102
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnknesepsFEATRSRNRYSVAYAAQK---PWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 103 PTSVLDVVMmglygqlgwFKRPGPREREAALrcLEQVSMQA------------FTTRQISqLSGGQQQRVFLARALAQDA 170
Cdd:cd03290 92 NATVEENIT---------FGSPFNKQRYKAV--TDACSLQPdidllpfgdqteIGERGIN-LSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 917519534 171 DLYFMDEPFAGVDA-----VTEEAILRVLHELKkqgKTVVVVHHDLE 212
Cdd:cd03290 160 NIVFLDDPFSALDIhlsdhLMQEGILKFLQDDK---RTLVLVTHKLQ 203
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
13-239 |
2.42e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 87.16 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 13 SGASSPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKRIGyv 92
Cdd:COG4598 3 DTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 pQRGSVD--------------------WDFPTsVLDVVMMGLYGQLGwfkRPGPREREAALRCLEQVSMQAFTTRQISQL 152
Cdd:COG4598 81 -ELVPADrrqlqrirtrlgmvfqsfnlWSHMT-VLENVIEAPVHVLG---RPKAEAIERAEALLAKVGLADKRDAYPAHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 153 SGGQQQRVFLARALAQDADLYFMDEPFAGVDA--VTEeaILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNVQVI- 229
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDPelVGE--VLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIe 233
|
250
....*....|
gi 917519534 230 ASGPMEEVFT 239
Cdd:COG4598 234 EQGPPAEVFG 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
9-236 |
2.96e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.34 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 9 QHPESGASSPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL-----A 83
Cdd:PRK15439 2 QTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltpA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 84 QARKR-IGYVPQRGSVdwdFPT-SVLDVVMMGLYgqlgwfKRPGPREREAALrcLEQVSMQAFTTRQISQLSGGQQQRVF 161
Cdd:PRK15439 82 KAHQLgIYLVPQEPLL---FPNlSVKENILFGLP------KRQASMQKMKQL--LAALGCQLDLDSSAGSLEVADRQIVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 162 LARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNVQVIA-SGPMEE 236
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIAlSGKTAD 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
32-215 |
3.37e-20 |
|
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: 89.58 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 32 PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGqslaqarkRIGYVPQrgsVDWDFPTSVLDVVM 111
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--------RISFSPQ---TSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 112 MGL-YGQLgwfkrpgpREREAALRCLEQVSMQAFTTRQIS-------QLSGGQQQRVFLARALAQDADLYFMDEPFAGVD 183
Cdd:TIGR01271 509 FGLsYDEY--------RYTSVIKACQLEEDIALFPEKDKTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190
....*....|....*....|....*....|...
gi 917519534 184 AVTEEAIL-RVLHELKKQgKTVVVVHHDLETVR 215
Cdd:TIGR01271 581 VVTEKEIFeSCLCKLMSN-KTRILVTSKLEHLK 612
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
19-212 |
4.33e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.79 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDvdLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ---SLAQARKRIGYVPQR 95
Cdd:PRK10771 2 LKLTDITWLYHHLPMRFD--LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtTTPPSRRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 96 GSVdwdFP-TSVLDVVMMGLYgqlgwfkrPGPR----EREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDA 170
Cdd:PRK10771 80 NNL---FShLTVAQNIGLGLN--------PGLKlnaaQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 917519534 171 DLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLE 212
Cdd:PRK10771 149 PILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLE 191
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
32-190 |
4.50e-20 |
|
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: 86.83 E-value: 4.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 32 PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGqslaqarkRIGYVPQrgsVDWDFPTSVLDVVM 111
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--------RISFSSQ---FSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 112 MGL-YGQLgwfkrpgpREREAALRCLEQVSMQAFTTRQIS-------QLSGGQQQRVFLARALAQDADLYFMDEPFAGVD 183
Cdd:cd03291 120 FGVsYDEY--------RYKSVVKACQLEEDITKFPEKDNTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
....*..
gi 917519534 184 AVTEEAI 190
Cdd:cd03291 192 VFTEKEI 198
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-223 |
5.96e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.86 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKR-------IGY 91
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhqdllyLGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPqrgsvdwdfptsvldvvmmGLYGQLG------WFKR-PGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLAR 164
Cdd:PRK13538 82 QP-------------------GIKTELTalenlrFYQRlHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917519534 165 ALAQDADLYFMDEPF-----AGVDAVTEeailRVLHELKKQGKTVVVVHHDLETVRDYFDHLTL 223
Cdd:PRK13538 143 LWLTRAPLWILDEPFtaidkQGVARLEA----LLAQHAEQGGMVILTTHQDLPVASDKVRKLRL 202
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
36-210 |
6.44e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.47 E-value: 6.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 36 DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA----QARKrIGYVPQRGSVdwdFP-TSVLDVV 110
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrsiQQRD-ICMVFQSYAL---FPhMSLGENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 111 MMGLYGQlgwfKRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAI 190
Cdd:PRK11432 100 GYGLKML----GVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180
....*....|....*....|.
gi 917519534 191 LRVLHELKKQ-GKTVVVVHHD 210
Cdd:PRK11432 176 REKIRELQQQfNITSLYVTHD 196
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-253 |
7.43e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.21 E-value: 7.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKriGYVPQRGSV 98
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKR--GLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 99 DWDFPTSVLDVVMMGLYGQLGW-FKRPGPREREAALR---CLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYF 174
Cdd:PRK13638 80 ATVFQDPEQQIFYTDIDSDIAFsLRNLGVPEAEITRRvdeALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 175 MDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTPENLKRTYGERMRW 253
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLrQGQILTHGAPGEVFACTEAMEQAGLTQPW 239
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
19-215 |
7.58e-20 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 84.91 E-value: 7.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPalWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQS---LAQARKRIGYVPQR 95
Cdd:TIGR01277 1 LALDKVRYEYEHLP--MEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQShtgLAPYQRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 96 GSVdwdFP-TSVLDVVMMGLYGQLgwfkRPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYF 174
Cdd:TIGR01277 79 NNL---FAhLTVRQNIGLGLHPGL----KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 917519534 175 MDEPFAGVDAVTEEAILRVLHELKKQGK-TVVVVHHDLETVR 215
Cdd:TIGR01277 152 LDEPFSALDPLLREEMLALVKQLCSERQrTLLMVTHHLSDAR 193
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
33-241 |
8.21e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.06 E-value: 8.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 33 ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVAS--GQVRFFGQSLaQAR-----KRIG---------YVPQrg 96
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEEL-QASnirdtERAGiaiihqelaLVKE-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 97 svdwdfpTSVLDVVMMG----LYGQLGWfkrpgpreREAALRC---LEQVSMQAFTTRQISQLSGGQQQRVFLARALAQD 169
Cdd:PRK13549 97 -------LSVLENIFLGneitPGGIMDY--------DAMYLRAqklLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917519534 170 ADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVFTPE 241
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIrDGRHIGTRPAAGMTEDD 234
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
19-237 |
8.60e-20 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 85.65 E-value: 8.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQS--------LAQARKRig 90
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelyqLSEAERR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 yvpQRGSVDWDFPT-SVLDVVMMGLYGQLGWFKRP---GPRE----REAALRCLEQVSM-QAFTTRQISQLSGGQQQRVF 161
Cdd:TIGR02323 82 ---RLMRTEWGFVHqNPRDGLRMRVSAGANIGERLmaiGARHygniRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 162 LARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEV 237
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQgRVVESGLTDQV 236
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-217 |
1.15e-19 |
|
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: 87.92 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 39 LEVP-AGQLCAIVGPNGAGKSTLIKAVLG-LVP--------VASGQV--RFFG-------QSLAQARKRIGYVPQRgsVD 99
Cdd:COG1245 93 LPVPkKGKVTGILGPNGIGKSTALKILSGeLKPnlgdydeePSWDEVlkRFRGtelqdyfKKLANGEIKVAHKPQY--VD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 100 wdfptsVLDVVMMGLYGQLgwFKRPGprEREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPF 179
Cdd:COG1245 171 ------LIPKVFKGTVREL--LEKVD--ERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|....*....
gi 917519534 180 AGVDaVTEE-AILRVLHELKKQGKTVVVVHHDLeTVRDY 217
Cdd:COG1245 241 SYLD-IYQRlNVARLIRELAEEGKYVLVVEHDL-AILDY 277
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
37-212 |
1.78e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.06 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 37 VDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL--------AQAR-KRIGYVPQRGSVdwdFPT-SV 106
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdeearAKLRaKHVGFVFQSFML---IPTlNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 107 LDVVmmglygQLGWFKRpGPREREA---ALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVD 183
Cdd:PRK10584 106 LENV------ELPALLR-GESSRQSrngAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190
....*....|....*....|....*....|
gi 917519534 184 AVTEEAILRVLHEL-KKQGKTVVVVHHDLE 212
Cdd:PRK10584 179 RQTGDKIADLLFSLnREHGTTLILVTHDLQ 208
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
15-216 |
1.88e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 87.08 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 15 ASSPLRVRDLTVVYRE-KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ-----ARKR 88
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlshsvLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 89 IGYVPQRGSVDWDfptSVLDVVMMGlygqlgwfkrpgpRE--REAALRCLEQVSMQAFT--------TR---QISQLSGG 155
Cdd:PRK10790 417 VAMVQQDPVVLAD---TFLANVTLG-------------RDisEEQVWQALETVQLAELArslpdglyTPlgeQGNNLSVG 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917519534 156 QQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQgKTVVVVHHDLETVRD 216
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVE 540
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
34-215 |
2.16e-19 |
|
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: 83.85 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 34 LWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLglvpVASGQVRFFgQSL-AQARKRIGYVPqRGSVDW------------ 100
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTI----YAEGQRRYV-ESLsAYARQFLGQMD-KPDVDSieglspaiaidq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 101 ----DFPTSVLDVVMmGLYGQLG-WFKRPGPREReaaLRCLEQVSMQAFT-TRQISQLSGGQQQRVFLARALAQDAD--L 172
Cdd:cd03270 85 kttsRNPRSTVGTVT-EIYDYLRlLFARVGIRER---LGFLVDVGLGYLTlSRSAPTLSGGEAQRIRLATQIGSGLTgvL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVR 215
Cdd:cd03270 161 YVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIR 203
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
19-215 |
2.51e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.21 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQS--------LAQARKRI- 89
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyaLSEAERRRl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 90 -----GYVPQ------RGSVdwdfpTSVLDVV--MMGL----YGQLgwfkrpgpreREAALRCLEQVSMQAftTR---QI 149
Cdd:PRK11701 87 lrtewGFVHQhprdglRMQV-----SAGGNIGerLMAVgarhYGDI----------RATAGDWLERVEIDA--ARiddLP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 150 SQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVR 215
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVAR 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-237 |
5.88e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.54 E-value: 5.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 36 DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARK---------RIGYVPQRGSVdwdFP-TS 105
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiclppekrRIGYVFQDARL---FPhYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 106 VldvvmMG--LYGQlgwfkrpGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVD 183
Cdd:PRK11144 93 V-----RGnlRYGM-------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 184 AVTEEAILRVLHELKKQGKT-VVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEV 237
Cdd:PRK11144 161 LPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLeQGKVKAFGPLEEV 216
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
19-239 |
7.28e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 83.35 E-value: 7.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALW---------DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLaqarkri 89
Cdd:COG4167 5 LEVRNLSKTFKYRTGLFrrqqfeavkPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 90 gyvpQRGsvdwDFPTSVLDVVMMglygqlgwFKRPG----PRER-----EAALRCLEQVSMQA-----FTT-RQ------ 148
Cdd:COG4167 78 ----EYG----DYKYRCKHIRMI--------FQDPNtslnPRLNigqilEEPLRLNTDLTAEEreeriFATlRLvgllpe 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 149 -----ISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLT 222
Cdd:COG4167 142 hanfyPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELqEKLGISYIYVSQHLGIVKHISDKVL 221
|
250
....*....|....*...
gi 917519534 223 LL-NVQVIASGPMEEVFT 239
Cdd:COG4167 222 VMhQGEVVEYGKTAEVFA 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-215 |
1.15e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.63 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALW-----------DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-- 85
Cdd:COG4608 8 LEVRDLKKHFPVRGGLFgrtvgvvkavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 86 ------RKRIGYVPQ--RGSVDwdfP-TSVLDVVMMGL--YGQLGwfkRPGPREREAALrcLEQVSMQA-FTTRQISQLS 153
Cdd:COG4608 88 relrplRRRMQMVFQdpYASLN---PrMTVGDIIAEPLriHGLAS---KAERRERVAEL--LELVGLRPeHADRYPHEFS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917519534 154 GGQQQRVFLARALAQDADLYFMDEPFAGVDaVTEEA-ILRVLHELKKQ-GKTVVVVHHDLETVR 215
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALD-VSIQAqVLNLLEDLQDElGLTYLFISHDLSVVR 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-239 |
1.21e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.84 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 14 GASSPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASG-----QVRFFGQSL------ 82
Cdd:PRK14271 17 AAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyrdv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 83 AQARKRIGYVPQRGSvdwDFPTSVLDVVMMGLYGQlgwfkRPGPRE--REAALRCLEQVSMQAFTTRQIS----QLSGGQ 156
Cdd:PRK14271 97 LEFRRRVGMLFQRPN---PFPMSIMDNVLAGVRAH-----KLVPRKefRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 157 QQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQgKTVVVVHHDLETVRDYFDHLTL-LNVQVIASGPME 235
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALfFDGRLVEEGPTE 247
|
....
gi 917519534 236 EVFT 239
Cdd:PRK14271 248 QLFS 251
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-224 |
1.43e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.58 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKR---------- 88
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaalaagvaii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 89 ---IGYVPQrgsvdwdfpTSVLDVVMMG-LYGQLGWFKRPGPREReaALRCLEQVSMQAFTTRQISQLSGGQQQRVFLAR 164
Cdd:PRK11288 85 yqeLHLVPE---------MTVAENLYLGqLPHKGGIVNRRLLNYE--AREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 165 ALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL 224
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVF 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
36-242 |
1.68e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.93 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 36 DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA---------RKRIGYVPQRGSVdwdFP-TS 105
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelrevrRKKIAMVFQSFAL---MPhMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 106 VLDVVMMGLygQLGWFkrPGPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAV 185
Cdd:PRK10070 123 VLDNTAFGM--ELAGI--NAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 186 TEEAILRVLHELK-KQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVF-TPEN 242
Cdd:PRK10070 199 IRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVGTPDEILnNPAN 258
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-217 |
1.72e-18 |
|
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: 82.03 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 39 LEVPA-GQLCAIVGPNGAGKSTLIKAVLGLV----------PVASGQVRFFgqslaqarkrigyvpqRGSVDWDFPTSVL 107
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAGKLkpnlgkfddpPDWDEILDEF----------------RGSELQNYFTKLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 108 DvvmmglyGQLGWFKRPG-----PR--------------EREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQ 168
Cdd:cd03236 84 E-------GDVKVIVKPQyvdliPKavkgkvgellkkkdERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALAR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 917519534 169 DADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLeTVRDY 217
Cdd:cd03236 157 DADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL-AVLDY 204
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
33-212 |
2.51e-18 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 80.92 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 33 ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKaVLGLV-PVASGQVRFFG---------QSLAQARKRIGYVPQrgSVDWDF 102
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLN-IIGMFdSLDSGSLTLAGkevtnlsysQKIILRRELIGYIFQ--SFNLIP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 103 PTSVLDVVMMGLygqlgwfKRPGPREREAALRCLEQVSMQAFTTR---QISQLSGGQQQRVFLARALAQDADLYFMDEPF 179
Cdd:NF038007 97 HLSIFDNVALPL-------KYRGVAKKERIERVNQVLNLFGIDNRrnhKPMQLSGGQQQRVAIARAMVSNPALLLADEPT 169
|
170 180 190
....*....|....*....|....*....|...
gi 917519534 180 AGVDAVTEEAILRVLHELKKQGKTVVVVHHDLE 212
Cdd:NF038007 170 GNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE 202
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-214 |
3.27e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 84.06 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 11 PESGASSPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVrffgqslaQARKRIG 90
Cdd:PTZ00243 653 SERSAKTPKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------WAERSIA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQRGsvdWDFPTSVLDVVMmglygqlgWFKrpgpREREAALRCLEQVSMQAFTTRQIS------------QLSGGQQQ 158
Cdd:PTZ00243 725 YVPQQA---WIMNATVRGNIL--------FFD----EEDAARLADAVRVSQLEADLAQLGggleteigekgvNLSGGQKA 789
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917519534 159 RVFLARALAQDADLYFMDEPFAGVDA-----VTEEAILRVLHelkkqGKTVVVVHHDLETV 214
Cdd:PTZ00243 790 RVSLARAVYANRDVYLLDDPLSALDAhvgerVVEECFLGALA-----GKTRVLATHQVHVV 845
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-238 |
3.31e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 81.28 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVvYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVP----VASGQVRFFGQSLAQARKR---IGY 91
Cdd:PRK10418 5 IELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVAPCALRgrkIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRgsvdwdfPTSVLD-VVMMGLYGQLGWFKRPGPREREAALRCLEQV---------SMQAFttrqisQLSGGQQQRVF 161
Cdd:PRK10418 84 IMQN-------PRSAFNpLHTMHTHARETCLALGKPADDATLTAALEAVglenaarvlKLYPF------EMSGGMLQRMM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 162 LARALAQDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEVF 238
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMsHGRIVEQGDVETLF 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-214 |
3.54e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.42 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 37 VDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA----------------RKRIGYVPQRgsvdw 100
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRsprdairagimlcpedRKAEGIIPVH----- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 101 dfptSV---LDVVMMGLYGQLGWFKRPGpREREAALRCLEQVSMQAFTTRQ-ISQLSGGQQQRVFLARALAQDADLYFMD 176
Cdd:PRK11288 347 ----SVadnINISARRHHLRAGCLINNR-WEAENADRFIRSLNIKTPSREQlIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190
....*....|....*....|....*....|....*...
gi 917519534 177 EPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETV 214
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEV 459
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-211 |
3.54e-18 |
|
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: 83.84 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 4 QPKTVQHP--ESGASSPLRVRDLTVVYR--EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFG 79
Cdd:TIGR00957 620 EPDSIERRtiKPGEGNSITVHNATFTWArdLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 80 QslaqarkrIGYVPQRGsvdWDFPTSVLDVVMMGLYGQLGWFKRPgpREREAALRCLEQVSMQAFTtrQISQ----LSGG 155
Cdd:TIGR00957 700 S--------VAYVPQQA---WIQNDSLRENILFGKALNEKYYQQV--LEACALLPDLEILPSGDRT--EIGEkgvnLSGG 764
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 156 QQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILR--VLHELKKQGKTVVVVHHDL 211
Cdd:TIGR00957 765 QKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKNKTRILVTHGI 822
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-237 |
3.93e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 83.31 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGL--VPVASGQV----------------RFFGQ 80
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 81 SL----------------------AQARKRIGYVPQRGSVDWDFPTsVLDVVMMGLYgQLGWfkrPGPREREAALRCLEQ 138
Cdd:TIGR03269 81 PCpvcggtlepeevdfwnlsdklrRRIRKRIAIMLQRTFALYGDDT-VLDNVLEALE-EIGY---EGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 139 VSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDY 217
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|.
gi 917519534 218 FDHLTLL-NVQVIASGPMEEV 237
Cdd:TIGR03269 236 SDKAIWLeNGEIKEEGTPDEV 256
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-234 |
4.59e-18 |
|
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: 80.53 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 39 LEVPAG-----QLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSlaqarkrIGYVPQRgsVDWDFPTSVLDVVM-- 111
Cdd:cd03237 15 LEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-------VSYKPQY--IKADYEGTVRDLLSsi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 112 -MGLYGQLGWfkrpgprEREAAlrclEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAI 190
Cdd:cd03237 86 tKDFYTHPYF-------KTEIA----KPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 917519534 191 LRVL-HELKKQGKTVVVVHHDLeTVRDYF-DHLTLLN----VQVIASGPM 234
Cdd:cd03237 155 SKVIrRFAENNEKTAFVVEHDI-IMIDYLaDRLIVFEgepsVNGVANPPQ 203
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-244 |
5.04e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.19 E-value: 5.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYRE-KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFG------QSLAQARKRIGY 91
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVDWDFPTSVLDVVMmglygqlgwfkrpGPRE--------REAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLA 163
Cdd:PRK13644 82 VFQNPETQFVGRTVEEDLAF-------------GPENlclppieiRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 164 RALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNVQVIASGPMEEVFTPENL 243
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
.
gi 917519534 244 K 244
Cdd:PRK13644 229 Q 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
34-224 |
5.76e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.89 E-value: 5.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 34 LWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKR----------------IGYVPQRGS 97
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkafrrdiqmvfqdsISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 98 VDWdfptsVLDVVMMGLYGQlgwfkrpGPREREA-ALRCLEQVSMQA-FTTRQISQLSGGQQQRVFLARALAQDADLYFM 175
Cdd:PRK10419 108 VRE-----IIREPLRHLLSL-------DKAERLArASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 917519534 176 DEPFAGVDAVTEEAILRVLHELKKQGKTV-VVVHHDLETVRdYFDHLTLL 224
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVE-RFCQRVMV 224
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
37-239 |
6.06e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 81.49 E-value: 6.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 37 VDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVP----VASGQVRFFGQSL----AQARKRIgyVPQRGSVDWDFPTSVLD 108
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLlklsPRERRKI--IGREIAMIFQEPSSCLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 109 VvMMGLYGQL-----------GWFKRPGPReREAALRCLEQVS-------MQAFTtrqiSQLSGGQQQRVFLARALAQDA 170
Cdd:COG4170 104 P-SAKIGDQLieaipswtfkgKWWQRFKWR-KKRAIELLHRVGikdhkdiMNSYP----HELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917519534 171 DLYFMDEPFAGVDAVTEEAILRVLHELKK-QGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFT 239
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCgQTVESGPTEQILK 248
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
34-212 |
6.08e-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: 80.20 E-value: 6.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 34 LWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKRIGYVPQRGSVdwdFP-TSVLDVVMM 112
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSL---LPwLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 113 GLYGQLGWFKRPgprEREAALR-CLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAIL 191
Cdd:TIGR01184 78 AVDRVLPDLSKS---ERRAIVEeHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180
....*....|....*....|..
gi 917519534 192 RVLHEL-KKQGKTVVVVHHDLE 212
Cdd:TIGR01184 155 EELMQIwEEHRVTVLMVTHDVD 176
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-243 |
6.21e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.91 E-value: 6.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKP---ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA-----QARKRIG 90
Cdd:PRK13642 5 LEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaenvwNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQrgSVDWDF-PTSVLDVVMMGLYGQlgwfkrPGPRER--EAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALA 167
Cdd:PRK13642 85 MVFQ--NPDNQFvGATVEDDVAFGMENQ------GIPREEmiKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 168 QDADLYFMDEPFAGVDAVTEEAILRVLHELK-KQGKTVVVVHHDLETVRDYFDHLTLLNVQVIASGPMEEVF-TPENL 243
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFaTSEDM 234
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-221 |
6.30e-18 |
|
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: 78.35 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYRE-KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFfgqslaQARKRIGYVPQRGS 97
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM------PEGEDLLFLPQRPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 98 vdwdFPTSVLdvvmmglygqlgwfkrpgpreREAALRCLEQVsmqafttrqisqLSGGQQQRVFLARALAQDADLYFMDE 177
Cdd:cd03223 75 ----LPLGTL---------------------REQLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 917519534 178 PFAGVDAVTEEAILRVLHELkkqGKTVVVVHHDlETVRDYFDHL 221
Cdd:cd03223 118 ATSALDEESEDRLYQLLKEL---GITVISVGHR-PSLWKFHDRV 157
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
44-217 |
6.79e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.55 E-value: 6.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 44 GQLCAIVGPNGAGKSTLIKAVLG-LVP--------VASGQV--RFFG-------QSLAQARKRIGYVPQRgsVDwdfpts 105
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGeLIPnlgdyeeePSWDEVlkRFRGtelqnyfKKLYNGEIKVVHKPQY--VD------ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 106 VLDVVMMGLYGQLgwFKRPGprEREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAV 185
Cdd:PRK13409 171 LIPKVFKGKVREL--LKKVD--ERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180 190
....*....|....*....|....*....|..
gi 917519534 186 TEEAILRVLHELKKqGKTVVVVHHDLeTVRDY 217
Cdd:PRK13409 247 QRLNVARLIRELAE-GKYVLVVEHDL-AVLDY 276
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-211 |
8.28e-18 |
|
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: 82.52 E-value: 8.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 39 LEVPAGQL-----CAIVGPNGAGKSTLIKAVLGLVPVASGQVrffgqslaQARKRIGYVPQRGSVDwdFPTSVLDVVMMG 113
Cdd:COG1245 356 LEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLKISYKPQYISPD--YDGTVEEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 114 LYGQLG--WFK----RPgprereaaLRcLEQVsMQafttRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAvtE 187
Cdd:COG1245 426 NTDDFGssYYKteiiKP--------LG-LEKL-LD----KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--E 489
|
170 180 190
....*....|....*....|....*....|
gi 917519534 188 E------AILRVlheLKKQGKTVVVVHHDL 211
Cdd:COG1245 490 QrlavakAIRRF---AENRGKTAMVVDHDI 516
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
30-216 |
9.78e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.23 E-value: 9.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 30 EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVP--VASGQVRFFGQSLAQARKRIGYVPQRGsvdwDFPTSVL 107
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREASLIDAIGRKG----DFKDAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 108 DVVMMGLYGQLGWFKRPgprereaalrcleqvsmqafttrqiSQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTE 187
Cdd:COG2401 118 LLNAVGLSDAVLWLRRF-------------------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190
....*....|....*....|....*....|
gi 917519534 188 EAILRVLHEL-KKQGKTVVVVHHDLETVRD 216
Cdd:COG2401 173 KRVARNLQKLaRRAGITLVVATHHYDVIDD 202
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-211 |
9.81e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.16 E-value: 9.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 39 LEVPAGQL-----CAIVGPNGAGKSTLIKAVLGLVPVASGQVrffgqslaQARKRIGYVPQRgsVDWDFPTSVlDVVMMG 113
Cdd:PRK13409 355 LEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELKISYKPQY--IKPDYDGTV-EDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 114 LYGQLG--WFK----RPgprereaaLRcLEQVsMQafttRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVD---- 183
Cdd:PRK13409 424 ITDDLGssYYKseiiKP--------LQ-LERL-LD----KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqr 489
|
170 180
....*....|....*....|....*....
gi 917519534 184 -AVTeEAILRVLHElkkQGKTVVVVHHDL 211
Cdd:PRK13409 490 lAVA-KAIRRIAEE---REATALVVDHDI 514
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-210 |
1.53e-17 |
|
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: 81.52 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRfFGQSLaqarkRIGYVPQ-RGS 97
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IGETV-----KLAYVDQsRDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 98 VD-----WDFPTSVLDVVMMGLY-----GQLGWFKRPGPREReaalrcleqvsmqafttRQISQLSGGQQQRVFLARALA 167
Cdd:TIGR03719 397 LDpnktvWEEISGGLDIIKLGKReipsrAYVGRFNFKGSDQQ-----------------KKVGQLSGGERNRVHLAKTLK 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 917519534 168 QDADLYFMDEPFAGVDAVTeeaiLRVLHE-LKKQGKTVVVVHHD 210
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVET----LRALEEaLLNFAGCAVVISHD 499
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-214 |
1.58e-17 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 78.67 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPA---LWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ-----ARKRIG 90
Cdd:cd03248 12 VKFQNVTFAYPTRPDtlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkyLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQRGSVdwdFPTSVLDVVMMGLYGqlgwfkRPGPREREAALRCLEQVSMQAF-------TTRQISQLSGGQQQRVFLA 163
Cdd:cd03248 92 LVGQEPVL---FARSLQDNIAYGLQS------CSFECVKEAAQKAHAHSFISELasgydteVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 917519534 164 RALAQDADLYFMDEPFAGVDAVTEEAILRVLHElKKQGKTVVVVHHDLETV 214
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTV 212
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
33-224 |
1.93e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.99 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 33 ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVAS--------GQVRFFG--------------QSLA------- 83
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyegeilfdGEVCRFKdirdsealgiviihQELAlipylsi 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 84 ---------QARkrigyvpqRGSVDWDfptsvldvvmmglygqlgwfkrpgpREREAALRCLEQVSMQAFTTRQISQLSG 154
Cdd:NF040905 96 aeniflgneRAK--------RGVIDWN-------------------------ETNRRARELLAKVGLDESPDTLVTDIGV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 155 GQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL 224
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVL 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-232 |
1.99e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 15 ASSPL-RVRDLTVVYR----EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVA-----SGQVRFFGQSLAQ 84
Cdd:PRK15134 1 MTQPLlAIENLSVAFRqqqtVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 85 ARK---------RIGYVPQRGSVDWDfPtsvLDVVMMGLYGQLGWFKrpGPReREAA----LRCLEQVSMQAFTTRQIS- 150
Cdd:PRK15134 81 ASEqtlrgvrgnKIAMIFQEPMVSLN-P---LHTLEKQLYEVLSLHR--GMR-REAArgeiLNCLDRVGIRQAAKRLTDy 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 151 --QLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDhltllNVQ 227
Cdd:PRK15134 154 phQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLAD-----RVA 228
|
....*
gi 917519534 228 VIASG 232
Cdd:PRK15134 229 VMQNG 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
31-217 |
2.16e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.38 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 31 KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA--------RKRIGYVPQRGSVDWDf 102
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevpflRRQIGMIFQDHHLLMD- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 103 pTSVLDVVMMGLYgqLGWFKRPGPREREAAlrCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGV 182
Cdd:PRK10908 94 -RTVYDNVAIPLI--IAGASGDDIRRRVSA--ALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 917519534 183 DAVTEEAILRVLHELKKQGKTVVVVHHDLETV--RDY 217
Cdd:PRK10908 169 DDALSEGILRLFEEFNRVGVTVLMATHDIGLIsrRSY 205
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
38-237 |
2.21e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 80.83 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 38 DLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQV-----RFFGQSLAQARKRIGYVPQRGSVDW------DFPTSV 106
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqfsHITRLSFEQLQKLVSDEWQRNNTDMlspgedDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 107 LDVVMMGLygqlgwfkrpgprerEAALRCLE---QVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVD 183
Cdd:PRK10938 103 AEIIQDEV---------------KDPARCEQlaqQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 917519534 184 AVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEV 237
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLaDCTLAETGEREEI 222
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-217 |
2.98e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 77.68 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQS----LAQARKRIGYVPQ 94
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikkdLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 RGSVDwdfPTSVL-DVVMMGLYGQLGwfkrpgprereaALRCLEQV---SMQAFTTRQISQLSGGQQQRVFLARALAQDA 170
Cdd:PRK13540 82 RSGIN---PYLTLrENCLYDIHFSPG------------AVGITELCrlfSLEHLIDYPCGLLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 917519534 171 DLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVV-HHDLETVR-DY 217
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTsHQDLPLNKaDY 195
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
30-236 |
3.67e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 80.53 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 30 EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-----RKRIGYVPQrgsVDWDFPT 104
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqldswRSRLAVVSQ---TPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 105 SVLDVVMMGlygqlgwfkRPGPR----EREAALRCLEQVSM---QAFTTrQISQ----LSGGQQQRVFLARALAQDADLY 173
Cdd:PRK10789 404 TVANNIALG---------RPDATqqeiEHVARLASVHDDILrlpQGYDT-EVGErgvmLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917519534 174 FMDEPFAGVDAVTEEAILRVLHELkKQGKTVVVVHHDLETVRDYFDHLTLLNVQVIASGPMEE 236
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQ 535
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-235 |
4.83e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.80 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGL--VPVASGQVRFFGQSLAQ------ARKRIG 90
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILElspderARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQRgsvdwdfPTSVLDVVMMGL----YGQLGWFKRPGPREREAALRCLEQVSM-QAFTTRQISQ-LSGGQQQRVFLAR 164
Cdd:COG0396 81 LAFQY-------PVEIPGVSVSNFlrtaLNARRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 165 ALAQDADLYFMDEPFAG--VDAVteEAILRVLHELKKQGKTVVVV-HHD--LETVRDYFDHLtLLNVQVIASGPME 235
Cdd:COG0396 154 MLLLEPKLAILDETDSGldIDAL--RIVAEGVNKLRSPDRGILIItHYQriLDYIKPDFVHV-LVDGRIVKSGGKE 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-214 |
5.40e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.06 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY--REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ-----SLAQARKRIGY 91
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdyTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVdwdFPTSVLDVVMmglYGQLGWFKRpgpREREAALRcleqvsmQAFTTRQISQ---------------LSGGQ 156
Cdd:PRK11176 422 VSQNVHL---FNDTIANNIA---YARTEQYSR---EQIEEAAR-------MAYAMDFINKmdngldtvigengvlLSGGQ 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 157 QQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQgKTVVVVHHDLETV 214
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTI 542
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
33-236 |
9.76e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.28 E-value: 9.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 33 ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKR------IGYVPQRGSVdwdFPT-S 105
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssqeagIGIIHQELNL---IPQlT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 106 VLDVVMMG-----LYGQLGWfkrpgPREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPfa 180
Cdd:PRK10762 96 IAENIFLGrefvnRFGRIDW-----KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP-- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 181 gVDAVTE---EAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEE 236
Cdd:PRK10762 169 -TDALTDtetESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFrDGQFIAEREVAD 227
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
11-208 |
1.90e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.66 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 11 PESGASSPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-RKR- 88
Cdd:PRK13543 4 PLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdRSRf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 89 IGYVPQRGSVDWDFPTSVLDVVMMGLYGQlgwfkrpgpREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQ 168
Cdd:PRK13543 84 MAYLGHLPGLKADLSTLENLHFLCGLHGR---------RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 917519534 169 DADLYFMDEPFAGVDAvteEAILRVLH----ELKKQGKTVVVVH 208
Cdd:PRK13543 155 PAPLWLLDEPYANLDL---EGITLVNRmisaHLRGGGAALVTTH 195
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
31-224 |
2.48e-16 |
|
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: 74.97 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 31 KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKaVL------GLVpvaSGQVRFFGQSLAQA-RKRIGYVPQrgsVDWDFP 103
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLD-VLagrktaGVI---TGEILINGRPLDKNfQRSTGYVEQ---QDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 104 TSVLDVVMmglygqlgwfkrpgprEREAALRcleqvsmqafttrqisQLSGGQQQRVFLARALAQDADLYFMDEPFAGVD 183
Cdd:cd03232 93 NLTVREAL----------------RFSALLR----------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 917519534 184 AVTEEAILRVLHELKKQGKTVVV-VHHDLETVRDYFDHLTLL 224
Cdd:cd03232 141 SQAAYNIVRFLKKLADSGQAILCtIHQPSASIFEKFDRLLLL 182
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
36-210 |
4.16e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.61 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 36 DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ---SLAQARKRIGYVPQRGSVdwdFP-TSVLDVVM 111
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAERGVGMVFQSYAL---YPhLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 112 MGLygqlgwfKRPGPREREAALRcLEQVS----MQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVte 187
Cdd:PRK11000 98 FGL-------KLAGAKKEEINQR-VNQVAevlqLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA-- 167
|
170 180 190
....*....|....*....|....*....|.
gi 917519534 188 eaiLRV--------LHelKKQGKTVVVVHHD 210
Cdd:PRK11000 168 ---LRVqmrieisrLH--KRLGRTMIYVTHD 193
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
30-238 |
4.48e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.89 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 30 EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFG------QSLAQARKRIGYVPQRgsvdwdfP 103
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLWDIRNKAGMVFQN-------P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 104 ------TSVLDVVMMGLYgQLGwfkrPGPRE-REAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMD 176
Cdd:PRK13633 95 dnqivaTIVEEDVAFGPE-NLG----IPPEEiRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917519534 177 EPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLLNVQVIASGPMEEVF 238
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIF 232
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
37-220 |
4.75e-16 |
|
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: 77.15 E-value: 4.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 37 VDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARkRIGYvPQRGSV---D-WDFPTsvldvvmm 112
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN-REAY-RQLFSAvfsDfHLFDR-------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 113 gLYGqlgwfkRPGPREREAALRCLEQVSMQ--------AFTTRQISQlsgGQQQRVFLARALAQDADLYFMDEPFAGVDA 184
Cdd:COG4615 421 -LLG------LDGEADPARARELLERLELDhkvsvedgRFSTTDLSQ---GQRKRLALLVALLEDRPILVFDEWAADQDP 490
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 917519534 185 V------TEeailrVLHELKKQGKTVVVVHHDletvrD-YFDH 220
Cdd:COG4615 491 EfrrvfyTE-----LLPELKARGKTVIAISHD-----DrYFDL 523
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
9-243 |
6.38e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.07 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 9 QHPESGASSPLRV------RDLTVVY---REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFG 79
Cdd:TIGR00958 463 NIPLTGTLAPLNLegliefQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 80 QSLAQ-----ARKRIGYVPQRGSVdwdFPTSVLDVVMMGLYgqlgwfKRPGPREREAALRCLEQVSMQAFTT-------R 147
Cdd:TIGR00958 543 VPLVQydhhyLHRQVALVGQEPVL---FSGSVRENIAYGLT------DTPDEEIMAAAKAANAHDFIMEFPNgydtevgE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 148 QISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAilrvLHELKK-QGKTVVVVHHDLETVRDyfdhltLLNV 226
Cdd:TIGR00958 614 KGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL----LQESRSrASRTVLLIAHRLSTVER------ADQI 683
|
250
....*....|....*..
gi 917519534 227 QVIASGPMEEVFTPENL 243
Cdd:TIGR00958 684 LVLKKGSVVEMGTHKQL 700
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
37-237 |
6.81e-16 |
|
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: 76.76 E-value: 6.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 37 VDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQV--------------RFFGQslAQARKRIGYVPQRGSVdwdF 102
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpGPDGR--GRAKRYIGILHQEYDL---Y 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 103 P-TSVLDVVMMGLYGQLgwfkrPGPREREAALRCLEQVSMQAFTTRQI-----SQLSGGQQQRVFLARALAQDADLYFMD 176
Cdd:TIGR03269 378 PhRTVLDNLTEAIGLEL-----PDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917519534 177 EPFAGVDAVTEEAILR-VLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEEV 237
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMrDGKIVKIGDPEEI 515
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-215 |
7.76e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 7.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTvvyreKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA----QARKRIG--YV 92
Cdd:PRK15439 269 LTVEDLT-----GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINalstAQRLARGlvYL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 P---QRGSVDWDFPTSvLDVVMMgLYGQLGWFKRPGpREREAALRCLEQVSMQAFTTRQ-ISQLSGGQQQRVFLARALAQ 168
Cdd:PRK15439 344 PedrQSSGLYLDAPLA-WNVCAL-THNRRGFWIKPA-RENAVLERYRRALNIKFNHAEQaARTLSGGNQQKVLIAKCLEA 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 917519534 169 DADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVR 215
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIE 467
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-212 |
8.29e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.74 E-value: 8.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY-----REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ--ARKRIGY 91
Cdd:COG1101 2 LELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlpEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 V------PQRGSvdwdFPT-SVLDVVMMGLY-GQLGWFKRPGPREREAALRclEQVS---------MQAfttrQISQLSG 154
Cdd:COG1101 82 IgrvfqdPMMGT----APSmTIEENLALAYRrGKRRGLRRGLTKKRRELFR--ELLAtlglglenrLDT----KVGLLSG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 155 GQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLE 212
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNME 210
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
19-235 |
8.66e-16 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 74.22 E-value: 8.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLG--LVPVASGQVRFFGQSLAQ------ARKRIG 90
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLElepderARAGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQR-----GSVDWDFPTSVLDVVMMglYGQLGWFKRPGPRER-EAALRCLEQVsmQAFTTRQISQ-LSGGQQQRVFLA 163
Cdd:TIGR01978 81 LAFQYpeeipGVSNLEFLRSALNARRS--ARGEEPLDLLDFEKLlKEKLALLDMD--EEFLNRSVNEgFSGGEKKRNEIL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 164 RALAQDADLYFMDEPFAG--VDAVteEAILRVLHELKKQGKTVVVVHHD---LETVRDYFDHLtLLNVQVIASGPME 235
Cdd:TIGR01978 157 QMALLEPKLAILDEIDSGldIDAL--KIVAEGINRLREPDRSFLIITHYqrlLNYIKPDYVHV-LLDGRIVKSGDVE 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
30-243 |
1.36e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.66 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 30 EKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVrFFG-----------QSLAQARKRIGYVPQrgsv 98
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGdyaipanlkkiKEVKRLRKEIGLVFQ---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 99 dwdFPTSVL-------DV----VMMGLYGQLGWFKRPgprereaalRCLEQVSM-QAFTTRQISQLSGGQQQRVFLARAL 166
Cdd:PRK13645 98 ---FPEYQLfqetiekDIafgpVNLGENKQEAYKKVP---------ELLKLVQLpEDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 167 AQDADLYFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFTPENL 243
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEgKVISIGSPFEIFSNQEL 244
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-248 |
1.95e-15 |
|
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: 75.82 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 21 VRDLTVVYRE--KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ----SLAQARKRIGYVPQ 94
Cdd:TIGR01257 931 VKNLVKIFEPsgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 RGSVDWDFptSVLDVVMmgLYGQLgwfkrPGPREREAALRC---LEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDAD 171
Cdd:TIGR01257 1011 HNILFHHL--TVAEHIL--FYAQL-----KGRSWEEAQLEMeamLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 172 LYFMDEPFAGVDAVTEEAILRVLheLK-KQGKTVVVVHHdletvrdYFDHLTLLN--VQVIASGPMEEVFTPENLKRTYG 248
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLL--LKyRSGRTIIMSTH-------HMDEADLLGdrIAIISQGRLYCSGTPLFLKNCFG 1152
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
33-224 |
2.25e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 33 ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ------ARKRIGYVPQRGSVDWDFptSV 106
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKldhklaAQLGIGIIYQELSVIDEL--TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 107 LDVVMMG------LYGQ--LGWFKRpgpREREAALrcLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEP 178
Cdd:PRK09700 98 LENLYIGrhltkkVCGVniIDWREM---RVRAAMM--LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 917519534 179 FAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL 224
Cdd:PRK09700 173 TSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVM 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-211 |
2.79e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.82 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 21 VRDLTvvYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA------QARKRIGYVPQ 94
Cdd:PRK09700 268 VRNVT--SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldAVKKGMAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 95 RGSVDWDFPT-------SVLDVVMMGLY-GQLGWFKRPgpREREAALRCLEQVSMQAFTTRQ-ISQLSGGQQQRVFLARA 165
Cdd:PRK09700 346 SRRDNGFFPNfsiaqnmAISRSLKDGGYkGAMGLFHEV--DEQRTAENQRELLALKCHSVNQnITELSGGNQQKVLISKW 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 917519534 166 LAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDL 211
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-221 |
5.38e-15 |
|
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: 70.47 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 29 REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLglvpvasgqvrfFGQSLAQARKRIGYVPQRGSVdwdfptsvld 108
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG------------LALGGAQSATRRRSGVKAGCI---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 109 vvmmglygqlgwfkrpgprerEAAlrcleqVSMQAFTTRqiSQLSGGQQQRVFLARALA----QDADLYFMDEPFAGVDA 184
Cdd:cd03227 64 ---------------------VAA------VSAELIFTR--LQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDP 114
|
170 180 190
....*....|....*....|....*....|....*..
gi 917519534 185 VTEEAILRVLHELKKQGKTVVVVHHDLETVRDYfDHL 221
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVITHLPELAELA-DKL 150
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-210 |
7.76e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.95 E-value: 7.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREK-PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQARKRigyvpQRgs 97
Cdd:PRK11650 4 LKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-----DR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 98 vdwdfptsvlDVVM----------MGLYGQLGW------FKRPGPRER-EAALRCLEqvsMQAFTTRQISQLSGGQQQRV 160
Cdd:PRK11650 77 ----------DIAMvfqnyalyphMSVRENMAYglkirgMPKAEIEERvAEAARILE---LEPLLDRKPRELSGGQRQRV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 161 FLARALAQDADLYFMDEPFAGVDAVteeaiLRV-----LHELKKQ-GKTVVVVHHD 210
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLDAK-----LRVqmrleIQRLHRRlKTTSLYVTHD 194
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-239 |
1.01e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 12 ESGASSPLRVRDLTVVY-----------REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPvASGQVRFFGQ 80
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 81 SLAQ-ARKRIGYVPQRGSVDWDFPTS-------VLDVVMMGL---YGQLGwfkrpgPREREAA-LRCLEQVSMQAFTT-R 147
Cdd:PRK15134 348 PLHNlNRRQLLPVRHRIQVVFQDPNSslnprlnVLQIIEEGLrvhQPTLS------AAQREQQvIAVMEEVGLDPETRhR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 148 QISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGK-TVVVVHHDLETVRDYFDHLTLLNV 226
Cdd:PRK15134 422 YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQ 501
|
250
....*....|....
gi 917519534 227 -QVIASGPMEEVFT 239
Cdd:PRK15134 502 gEVVEQGDCERVFA 515
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
33-236 |
1.16e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.84 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 33 ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQS-------------LAQARKRIGYVPQRgsvd 99
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfksskealengISMVHQELNLVLQR---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 100 wdfptSVLDVVMMGLYGQLGWFKRPGPREREAAlRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPF 179
Cdd:PRK10982 89 -----SVMDNMWLGRYPTKGMFVDQDKMYRDTK-AIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 180 AGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLL-NVQVIASGPMEE 236
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILrDGQWIATQPLAG 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
26-210 |
2.57e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.89 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 26 VVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLvpvasgQVRFFGQSLAQARKRIGYVPQRGSVDwdfPT- 104
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKDFNGEARPQPGIKVGYLPQEPQLD---PTk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 105 SVLDVVMMGLygqlgwfkrpgpREREAALRCLEQVSMQ---------AFTTRQ--------------------------- 148
Cdd:TIGR03719 84 TVRENVEEGV------------AEIKDALDRFNEISAKyaepdadfdKLAAEQaelqeiidaadawdldsqleiamdalr 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 149 -------ISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKkqgKTVVVVHHD 210
Cdd:TIGR03719 152 cppwdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP---GTVVAVTHD 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-214 |
1.05e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLT---VVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVAS-GQVRFFGQSL-----AQA---- 85
Cdd:PRK13549 260 LEVRNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVkirnpQQAiaqg 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 86 -------RKRIGYVPQRGsVDWDFPTSVLDVvmmglygqlgwFKRPGPREREAALRCLEQvSMQAFTTR------QISQL 152
Cdd:PRK13549 340 iamvpedRKRDGIVPVMG-VGKNITLAALDR-----------FTGGSRIDDAAELKTILE-SIQRLKVKtaspelAIARL 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917519534 153 SGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETV 214
Cdd:PRK13549 407 SGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEV 468
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-215 |
1.20e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.35 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR---------EKP----ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA-- 83
Cdd:PRK15079 9 LEVADLKVHFDikdgkqwfwQPPktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgm 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 84 ------QARKRIGYVPQRGSVDWDFPTSVLDVVMMGL---YGQLgwfKRPGPREREAALrcLEQVSM-QAFTTRQISQLS 153
Cdd:PRK15079 89 kddewrAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLrtyHPKL---SRQEVKDRVKAM--MLKVGLlPNLINRYPHEFS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917519534 154 GGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVR 215
Cdd:PRK15079 164 GGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVK 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-249 |
1.42e-13 |
|
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: 70.43 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVY--REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL----AQARKRIGYV 92
Cdd:TIGR01257 1938 LRLNELTKVYsgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltniSDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVDwDFPTSVLDVVmmgLYGQLgwfkRPGPRER--EAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDA 170
Cdd:TIGR01257 2018 PQFDAID-DLLTGREHLY---LYARL----RGVPAEEieKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 171 DLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTllnvqVIASGPMEEVFTPENLKRTYGE 249
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLA-----IMVKGAFQCLGTIQHLKSKFGD 2163
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
19-214 |
1.44e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.92 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSlaqarkRIGYVPQRGSV 98
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA------NIGYYAQDHAY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 99 DWDFPTSVLDvvMMGLYGQlgwfkrpgPREREAALRcleqvSMQA---FTTRQISQ----LSGGQQQRVFLARALAQDAD 171
Cdd:PRK15064 394 DFENDLTLFD--WMSQWRQ--------EGDDEQAVR-----GTLGrllFSQDDIKKsvkvLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 917519534 172 LYFMDEPFAGVDAvteEAILRVLHELKKQGKTVVVVHHDLETV 214
Cdd:PRK15064 459 VLVMDEPTNHMDM---ESIESLNMALEKYEGTLIFVSHDREFV 498
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-243 |
1.64e-13 |
|
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: 69.47 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLT---VVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVA-SGQVRFFGQSL-----AQA---- 85
Cdd:TIGR02633 258 LEARNLTcwdVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVdirnpAQAirag 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 86 -------RKRIGYVPQRGsVDWDFPTSVLDVvmmglYGQLGwfKRPGPREREAALRCLEQVSMQAFTTR-QISQLSGGQQ 157
Cdd:TIGR02633 338 iamvpedRKRHGIVPILG-VGKNITLSVLKS-----FCFKM--RIDAAAELQIIGSAIQRLKVKTASPFlPIGRLSGGNQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 158 QRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHltllnVQVIASGPMEEV 237
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDR-----VLVIGEGKLKGD 484
|
....*.
gi 917519534 238 FTPENL 243
Cdd:TIGR02633 485 FVNHAL 490
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-251 |
3.64e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 18 PLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ--------SLAQARKRI 89
Cdd:PRK10261 324 PLRSGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlspgKLQALRRDI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 90 GYVPQRGSVDWDFPTSVLDVVMMGLYGQlGWFKRPGPREREAALrcLEQVSMQA-FTTRQISQLSGGQQQRVFLARALAQ 168
Cdd:PRK10261 404 QFIFQDPYASLDPRQTVGDSIMEPLRVH-GLLPGKAAAARVAWL--LERVGLLPeHAWRYPHEFSGGQRQRICIARALAL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 169 DADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFtpENLKRT 246
Cdd:PRK10261 481 NPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLgQIVEIGPRRAVF--ENPQHP 558
|
....*
gi 917519534 247 YGERM 251
Cdd:PRK10261 559 YTRKL 563
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-210 |
4.99e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 4.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ------ARKRIGYV 92
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtakiMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQrGSVDWDFPTSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQVSMQAFTtrqisqLSGGQQQRVFLARALAQDADL 172
Cdd:PRK11614 86 PE-GRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGT------MSGGEQQMLAIGRALMSQPRL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHD 210
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQN 196
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
33-215 |
8.10e-13 |
|
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: 64.65 E-value: 8.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 33 ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGlvpvasgqvrffgqslAQARKRIGYVPQRGSvdwDFPTSVLD---- 108
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----------------ASGKARLISFLPKFS---RNKLIFIDqlqf 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 109 VVMMGL-YGQLGwfkrpgprereaalrcleqvsmqafttRQISQLSGGQQQRVFLARALAQDAD--LYFMDEPFAGVDAV 185
Cdd:cd03238 71 LIDVGLgYLTLG---------------------------QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190
....*....|....*....|....*....|
gi 917519534 186 TEEAILRVLHELKKQGKTVVVVHHDLETVR 215
Cdd:cd03238 124 DINQLLEVIKGLIDLGNTVILIEHNLDVLS 153
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
36-210 |
8.18e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 36 DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRfFGQSLaqarkRIGYVPQ-RGSVD-----WDFPTSVLDV 109
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IGETV-----KLAYVDQsRDALDpnktvWEEISGGLDI 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 110 VMMGLY-----GQLGWFKRPGPrereaalrclEQvsmQafttRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDA 184
Cdd:PRK11819 416 IKVGNReipsrAYVGRFNFKGG----------DQ---Q----KKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
170 180
....*....|....*....|....*..
gi 917519534 185 VTeeaiLRVLHE-LKKQGKTVVVVHHD 210
Cdd:PRK11819 479 ET----LRALEEaLLEFPGCAVVISHD 501
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
11-224 |
8.67e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.76 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 11 PESGASSPLRVRDLTVVYREKPA---LWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVP---VASGQVRFFGQSL-- 82
Cdd:TIGR00955 15 AQDGSWKQLVSRLRGCFCRERPRkhlLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIda 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 83 AQARKRIGYVPQrgsVDWDFPT-SVLDVVMMGLYGQLGwfKRPGPREREAALR-CLEQVSMQ-AFTTR-----QISQLSG 154
Cdd:TIGR00955 95 KEMRAISAYVQQ---DDLFIPTlTVREHLMFQAHLRMP--RRVTKKEKRERVDeVLQALGLRkCANTRigvpgRVKGLSG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917519534 155 GQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVV-VHHDLETVRDYFDHLTLL 224
Cdd:TIGR00955 170 GERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILM 240
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-210 |
1.04e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.51 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA-----QARKRIGYVP 93
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlkpeIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 94 QRGSVdwdFPTSVLDVVMmglygqLGWFKRPGPREREAALRCLEQVSM-QAFTTRQISQLSGGQQQRVFLARALAQDADL 172
Cdd:PRK10247 88 QTPTL---FGDTVYDNLI------FPWQIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 917519534 173 YFMDEPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHHD 210
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHD 197
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
40-238 |
1.28e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 66.30 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 40 EVPAGQLCAIVGPNGAGKSTLIKAVLGLVP----VASGQVRFFGQSLAQ--ARKRIGYVPQRGSVDWDFPTSVLD----- 108
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRisEKERRNLVGAEVAMIFQDPMTSLNpcytv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 109 --VVMMGLYGQLGWFKRpgpREREAALRCLEQVSMQAFTTR---QISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVD 183
Cdd:PRK11022 109 gfQIMEAIKVHQGGNKK---TRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 184 AVTEEAILRVLHEL-KKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVF 238
Cdd:PRK11022 186 VTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAgQVVETGKAHDIF 242
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-225 |
1.34e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.21 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 18 PLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASgqvrFFGQSLAQARK-------RIG 90
Cdd:PLN03211 68 KPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKptkqilkRTG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQRgsvDWDFPTsvLDVVMMGLYGQLgwFKRPGPREREAALRCLEQVSMQAFTTRQ---------ISQLSGGQQQRVF 161
Cdd:PLN03211 144 FVTQD---DILYPH--LTVRETLVFCSL--LRLPKSLTKQEKILVAESVISELGLTKCentiignsfIRGISGGERKRVS 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917519534 162 LARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVV-VHHDLETVRDYFDHLTLLN 225
Cdd:PLN03211 217 IAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLS 281
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
34-217 |
2.45e-12 |
|
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: 64.94 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 34 LWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLglVPVASgQVRFFGQSLAQARKRI---GYVPQRGSVDWDFP------- 103
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTL--YPALA-RRLHLKKEQPGNHDRIeglEHIDKVIVIDQSPIgrtprsn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 104 -----------------------------------TSVLDVVMMGLYGQLGWFKRPgPREREAaLRCLEQVSMQAFTTRQ 148
Cdd:cd03271 88 patytgvfdeirelfcevckgkrynretlevrykgKSIADVLDMTVEEALEFFENI-PKIARK-LQTLCDVGLGYIKLGQ 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917519534 149 IS-QLSGGQQQRVFLARALAQDAD---LYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVR--DY 217
Cdd:cd03271 166 PAtTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKcaDW 240
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-239 |
6.02e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.44 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYR--EKP--ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVP----VASGQVRFFGQSLAQ--ARKR 88
Cdd:PRK15093 4 LDIRNLTIEFKtsDGWvkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRlsPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 89 IGYVPQRGSVDWDFPTSVLD-------VVMMGLYG---QLGWFKRPGPREREAaLRCLEQVSMQAFTTRQIS---QLSGG 155
Cdd:PRK15093 84 RKLVGHNVSMIFQEPQSCLDpservgrQLMQNIPGwtyKGRWWQRFGWRKRRA-IELLHRVGIKDHKDAMRSfpyELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 156 QQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGP 233
Cdd:PRK15093 163 ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHDLQMLSQWADKINVLYCgQTVETAP 242
|
....*.
gi 917519534 234 MEEVFT 239
Cdd:PRK15093 243 SKELVT 248
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
40-217 |
6.37e-12 |
|
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: 62.59 E-value: 6.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 40 EVPAGQLCAIVGPNGAGKSTLIKAVLGLVpvasgqvrffgqslaqarkrigyVPQRGSVDWDFPTSVLdvvmmglygqlg 119
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQL-----------------------IPNGDNDEWDGITPVY------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 120 wfkRPgprereaalrcleqvsmqafttrQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKK 199
Cdd:cd03222 66 ---KP-----------------------QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170
....*....|....*....
gi 917519534 200 QG-KTVVVVHHDLeTVRDY 217
Cdd:cd03222 120 EGkKTALVVEHDL-AVLDY 137
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
19-212 |
6.47e-12 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 63.06 E-value: 6.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREkpalWDVDLE-VPAGQLCAIVGPNGAGKSTLIKAVlglvpvasgQVRFFGQSLAQARKR-----IGYV 92
Cdd:cd03279 6 LELKNFGPFREE----QVIDFTgLDNNGLFLICGPTGAGKSTILDAI---------TYALYGKTPRYGRQEnlrsvFAPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 93 PQRGSVDWDFptsvldvvmmglygQLGW-----FKRPGPRERE---AALrcLEQVSMQAFTTRQISQLSGGQQQRVFLAR 164
Cdd:cd03279 73 EDTAEVSFTF--------------QLGGkkyrvERSRGLDYDQftrIVL--LPQGEFDRFLARPVSTLSGGETFLASLSL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 917519534 165 ALA-----QDA-----DLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLE 212
Cdd:cd03279 137 ALAlsevlQNRggarlEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEE 194
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-215 |
8.21e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.22 E-value: 8.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREK----------PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA--- 85
Cdd:PRK11308 6 LQAIDLKKHYPVKrglfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 86 -----RKRIGYVPQRgsvdwdfPtsvldvvmmglYGQLGWFKRPG---------------PREREAALRCLEQVSMQA-F 144
Cdd:PRK11308 86 aqkllRQKIQIVFQN-------P-----------YGSLNPRKKVGqileepllintslsaAERREKALAMMAKVGLRPeH 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917519534 145 TTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVR 215
Cdd:PRK11308 148 YDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVE 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-248 |
8.89e-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: 64.97 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 11 PESGAsspLRVRDLTVVYRE--KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA--- 85
Cdd:TIGR00957 1280 PPRGR---VEFRNYCLRYREdlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIglh 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 86 --RKRIGYVPQrgsvdwdfptsvlDVVMMGlyGQLGWFKRP-GPREREAALRCLEQVSMQAFTTRQISQL---------- 152
Cdd:TIGR00957 1357 dlRFKITIIPQ-------------DPVLFS--GSLRMNLDPfSQYSDEEVWWALELAHLKTFVSALPDKLdhecaeggen 1421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 153 -SGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHElKKQGKTVVVVHHDLETVRDYfdhltlLNVQVIAS 231
Cdd:TIGR00957 1422 lSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDY------TRVIVLDK 1494
|
250
....*....|....*..
gi 917519534 232 GPMEEVFTPENLKRTYG 248
Cdd:TIGR00957 1495 GEVAEFGAPSNLLQQRG 1511
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
49-222 |
2.03e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 49 IVGPNGAGKSTLIKAVLGLVPVASGQVRffgqslAQARKRIGYVPQRGSVDwdfPT-SVLDVVMMGLygqlgwfkrpgpR 127
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEAR------PAPGIKVGYLPQEPQLD---PEkTVRENVEEGV------------A 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 128 EREAALRCLEQVS---------MQAFTTRQ----------------------------------ISQLSGGQQQRVFLAR 164
Cdd:PRK11819 97 EVKAALDRFNEIYaayaepdadFDALAAEQgelqeiidaadawdldsqleiamdalrcppwdakVTKLSGGERRRVALCR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 917519534 165 ALAQDADLYFMDEPFAGVDAvteEAILRVLHELKKQGKTVVVVHHDletvRdYF-DHLT 222
Cdd:PRK11819 177 LLLEKPDMLLLDEPTNHLDA---ESVAWLEQFLHDYPGTVVAVTHD----R-YFlDNVA 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
13-238 |
3.23e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.43 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 13 SGASSPLRVRDLTVVYREK----PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVP---VASGQVRFFGQSLAQA 85
Cdd:PRK09473 7 QQADALLDVKDLRVTFSTPdgdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 86 RKR---------IGYVPQrgsvdwDFPTSV----------LDVVMMglygqlgwFKRPGPRER-EAALRCLEQVSMQAFT 145
Cdd:PRK09473 87 PEKelnklraeqISMIFQ------DPMTSLnpymrvgeqlMEVLML--------HKGMSKAEAfEESVRMLDAVKMPEAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 146 TRQI---SQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKT-VVVVHHDLETVRDYFDH- 220
Cdd:PRK09473 153 KRMKmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKv 232
|
250
....*....|....*...
gi 917519534 221 LTLLNVQVIASGPMEEVF 238
Cdd:PRK09473 233 LVMYAGRTMEYGNARDVF 250
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-212 |
4.03e-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: 63.01 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 21 VRDLTVVYRE--KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPvASGQVRFFGQS-----LAQARKRIGYVP 93
Cdd:TIGR01271 1220 VQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSwnsvtLQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 94 QRgsvdwdfptsvldvvmmgLYGQLGWFKRP-GPRER---EAALRCLEQVSMQAFttrqISQ---------------LSG 154
Cdd:TIGR01271 1299 QK------------------VFIFSGTFRKNlDPYEQwsdEEIWKVAEEVGLKSV----IEQfpdkldfvlvdggyvLSN 1356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917519534 155 GQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLhelkKQG---KTVVVVHHDLE 212
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTL----KQSfsnCTVILSEHRVE 1413
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
19-220 |
5.54e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.30 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKP-ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAqARKRIGYVPQRGS 97
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT-AEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 98 VDWDFPtsvLDVVMMGLYGQlgwfkrpgPREREAALRCLEQVSMQ---AFTTRQIS--QLSGGQQQRVFLARALAQDADL 172
Cdd:PRK10522 402 VFTDFH---LFDQLLGPEGK--------PANPALVEKWLERLKMAhklELEDGRISnlKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 917519534 173 YFMDEPFAGVDAVTEEAILRV-LHELKKQGKTVVVVHHDletvrD-YFDH 220
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVlLPLLQEMGKTIFAISHD-----DhYFIH 515
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-238 |
6.15e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.18 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 12 ESGASSPLRVRDLTVVYREK----PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVR----------- 76
Cdd:PRK10261 6 ELDARDVLAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 77 ----FFGQSLAQARKRIG------YVPQRGSVDWDFPTSVLDVVMMGLYGQLGwfkrpgpRERE--AALRCLEQVSM--- 141
Cdd:PRK10261 86 qvieLSEQSAAQMRHVRGadmamiFQEPMTSLNPVFTVGEQIAESIRLHQGAS-------REEAmvEAKRMLDQVRIpea 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 142 QAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQ-GKTVVVVHHDLETVRDYFDH 220
Cdd:PRK10261 159 QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADR 238
|
250
....*....|....*....
gi 917519534 221 -LTLLNVQVIASGPMEEVF 238
Cdd:PRK10261 239 vLVMYQGEAVETGSVEQIF 257
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
29-225 |
7.45e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.97 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 29 REKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVA---SGQVRFFGQSLAQARKR----IGYVPQRgsvDWD 101
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKypgeIIYVSEE---DVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 102 FPTsvLDVvmmglygqlgwfkrpgpRER-EAALRCLeqvsmqafTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFA 180
Cdd:cd03233 95 FPT--LTV-----------------RETlDFALRCK--------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 917519534 181 GVDAVTEEAILRVLHELKKQGKTVVVV--HHDLETVRDYFDHLTLLN 225
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFVslYQASDEIYDLFDKVLVLY 194
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
13-239 |
8.54e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 61.29 E-value: 8.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 13 SGASSPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAG--KSTLIKAVLGlvPVASGQVRFFGQSLAQAR---K 87
Cdd:NF000106 8 NGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G--PDAGRRPWRF*TWCANRRalrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 88 RIG-YVPQRGSVDWDFpTSVLDVVMMGLYGQLgwfKRPGPREREAALrcLEQVSMQAFTTRQISQLSGGQQQRVFLARAL 166
Cdd:NF000106 86 TIG*HRPVR*GRRESF-SGRENLYMIGR*LDL---SRKDARARADEL--LERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917519534 167 AQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYFDHLTLLNV-QVIASGPMEEVFT 239
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRgRVIADGKVDELKT 233
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-214 |
2.13e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTvvyreKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSL---------------- 82
Cdd:PRK10762 258 LKVDNLS-----GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrspqdglangivyi 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 83 AQARKRIGYVpqrgsvdwdFPTSVLDvvMMGLYGqLGWFKRPGPREREAAlrclEQVSMQAFTT----------RQISQL 152
Cdd:PRK10762 333 SEDRKRDGLV---------LGMSVKE--NMSLTA-LRYFSRAGGSLKHAD----EQQAVSDFIRlfniktpsmeQAIGLL 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917519534 153 SGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETV 214
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEV 458
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-243 |
2.63e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.52 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 11 PESGAsspLRVRDLTVVYREK--PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQ-------VRFFGqs 81
Cdd:PLN03130 1233 PSSGS---IKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRilidgcdISKFG-- 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 82 LAQARKRIGYVPQrgsvdwdfpTSVLdvvmmgLYGQLGWFKRPGPREREAAL-RCLEQVSMQAFTTR-------QISQ-- 151
Cdd:PLN03130 1308 LMDLRKVLGIIPQ---------APVL------FSGTVRFNLDPFNEHNDADLwESLERAHLKDVIRRnslgldaEVSEag 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 152 --LSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGkTVVVVHHDLETVRDYfDHLTLLNvqvi 229
Cdd:PLN03130 1373 enFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSC-TMLIIAHRLNTIIDC-DRILVLD---- 1446
|
250
....*....|....
gi 917519534 230 aSGPMEEVFTPENL 243
Cdd:PLN03130 1447 -AGRVVEFDTPENL 1459
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
44-216 |
2.88e-10 |
|
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: 57.38 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 44 GQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGqslaqarkrigyvpqrgsvdwdfptsvldvvmmglygqlgwfkr 123
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 124 pGPREREAALRCLEQVsmqaFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLH------EL 197
Cdd:smart00382 38 -GEDILEEVLDQLLLI----IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllLK 112
|
170
....*....|....*....
gi 917519534 198 KKQGKTVVVVHHDLETVRD 216
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGP 131
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
19-216 |
7.58e-10 |
|
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: 57.94 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYRE--KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVaSGQVRFFGQS-----LAQARKRIGY 91
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSwnsvpLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVDWDFPTSVLDVvmmglYGQlgWfkrpgprEREAALRCLEQVSMQAFTTRQISQ-----------LSGGQQQRV 160
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDP-----YGK--W-------SDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLM 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 161 FLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHElKKQGKTVVVVHHDLETVRD 216
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE 202
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-243 |
1.09e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 11 PESG--ASSPLRVRDLTVVYREK--PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRF-------FG 79
Cdd:PLN03232 1225 PVSGwpSRGSIKFEDVHLRYRPGlpPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIddcdvakFG 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 80 qsLAQARKRIGYVPQrgsvdwdfpTSVLdvvmmgLYGQLGWFKRPGPREREAAL-RCLEQVSMQAFTTR-------QISQ 151
Cdd:PLN03232 1305 --LTDLRRVLSIIPQ---------SPVL------FSGTVRFNIDPFSEHNDADLwEALERAHIKDVIDRnpfgldaEVSE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 152 ----LSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGkTVVVVHHDLETVRDyfdhltLLNVQ 227
Cdd:PLN03232 1368 ggenFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSC-TMLVIAHRLNTIID------CDKIL 1440
|
250
....*....|....*.
gi 917519534 228 VIASGPMEEVFTPENL 243
Cdd:PLN03232 1441 VLSSGQVLEYDSPQEL 1456
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
36-209 |
1.22e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 36 DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLA----QARKRIGYVPQRGSvdwdfptsvldvvm 111
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDagdiATRRRVGYMSQAFS-------------- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 112 mgLYGQLG----------WFKRP----GPREREAALRC-LEQVsMQAFTtrqiSQLSGGQQQRVFLARALAQDADLYFMD 176
Cdd:NF033858 350 --LYGELTvrqnlelharLFHLPaaeiAARVAEMLERFdLADV-ADALP----DSLPLGIRQRLSLAVAVIHKPELLILD 422
|
170 180 190
....*....|....*....|....*....|....
gi 917519534 177 EPFAGVDAVTEEAILRVLHEL-KKQGKTVVVVHH 209
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELsREDGVTIFISTH 456
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-237 |
1.66e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALW---------DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQArkRI 89
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWFrrqtveavkPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG--DY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 90 GYVPQRGSVDWDFPTSVLDvvmmglygqlgwfkrpgPRER-----EAALRCLEQVSMQA------FTTRQIS-------- 150
Cdd:PRK15112 83 SYRSQRIRMIFQDPSTSLN-----------------PRQRisqilDFPLRLNTDLEPEQrekqiiETLRQVGllpdhasy 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 151 ---QLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELK-KQGKTVVVVHHDLETVRDYFDH-LTLLN 225
Cdd:PRK15112 146 yphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQvLVMHQ 225
|
250
....*....|..
gi 917519534 226 VQVIASGPMEEV 237
Cdd:PRK15112 226 GEVVERGSTADV 237
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
48-220 |
1.84e-09 |
|
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: 56.08 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 48 AIVGPNGAGKSTLIKAVLglvpVA-SGQVRFFGQSLAQARKRIGYVPQRGSVDWDFPT------------SVLDVVMMGL 114
Cdd:cd03240 26 LIVGQNGAGKTTIIEALK----YAlTGELPPNSKGGAHDPKLIREGEVRAQVKLAFENangkkytitrslAILENVIFCH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 115 YGQLGWfkrPGPREREaalrcleqvsmqafttrqisQLSGGQQQ------RVFLARALAQDADLYFMDEPFAGVDAVT-E 187
Cdd:cd03240 102 QGESNW---PLLDMRG--------------------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiE 158
|
170 180 190
....*....|....*....|....*....|....
gi 917519534 188 EAILRVLHELKKQG-KTVVVVHHDlETVRDYFDH 220
Cdd:cd03240 159 ESLAEIIEERKSQKnFQLIVITHD-EELVDAADH 191
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
152-237 |
2.22e-09 |
|
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: 57.72 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 152 LSGGQQQRVFLARALAQDAD---LYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYfDHLTLLNV-- 226
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTA-DYIIDLGPeg 908
|
90
....*....|....*.
gi 917519534 227 -----QVIASGPMEEV 237
Cdd:TIGR00630 909 gdgggTVVASGTPEEV 924
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-209 |
2.70e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.19 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLG--LVPVASGQVRFFGQSL----AQARKRIG-- 90
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESIldlePEERAHLGif 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 ----Y---VPqrGSVDWDF------------------PTSVLDVVMmglygqlgwfkrpgprEReaalrcLEQVSMQA-F 144
Cdd:CHL00131 88 lafqYpieIP--GVSNADFlrlaynskrkfqglpeldPLEFLEIIN----------------EK------LKLVGMDPsF 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 145 TTRQISQ-LSGGQQQR-VFLARALAqDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHH 209
Cdd:CHL00131 144 LSRNVNEgFSGGEKKRnEILQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
142-237 |
4.29e-09 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 56.57 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 142 QAFTTrqisqLSGGQQQRVFLARALAQDAD---LYFMDEP-----FAGVDAVteeaiLRVLHELKKQGKTVVVVHHDLET 213
Cdd:COG0178 822 QPATT-----LSGGEAQRVKLASELSKRSTgktLYILDEPttglhFHDIRKL-----LEVLHRLVDKGNTVVVIEHNLDV 891
|
90 100 110
....*....|....*....|....*....|....*...
gi 917519534 214 VR--DYfdhltllnV------------QVIASGPMEEV 237
Cdd:COG0178 892 IKtaDW--------IidlgpeggdgggEIVAEGTPEEV 921
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-178 |
5.22e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 32 PALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFfGQSLAQARkrIGYVPQRgsvdwDFPTSVLDVVM 111
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDLIVAR--LQQDPPR-----NVEGTVYDFVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 112 MGLYGQLGWFKR-------PGPREREAALRCLEQVSMQ-------AFTTR--------------QISQLSGGQQQRVFLA 163
Cdd:PRK11147 89 EGIEEQAEYLKRyhdishlVETDPSEKNLNELAKLQEQldhhnlwQLENRinevlaqlgldpdaALSSLSGGWLRKAALG 168
|
170
....*....|....*
gi 917519534 164 RALAQDADLYFMDEP 178
Cdd:PRK11147 169 RALVSNPDVLLLDEP 183
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
147-237 |
6.81e-09 |
|
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: 56.17 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 147 RQISQLSGGQQQRVFLARALAQD--ADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDYfDHLT-- 222
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAA-DYVIdi 562
|
90 100
....*....|....*....|
gi 917519534 223 -----LLNVQVIASGPMEEV 237
Cdd:TIGR00630 563 gpgagEHGGEVVASGTPEEI 582
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
14-243 |
7.64e-09 |
|
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: 54.91 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 14 GASSPLRVRDLTVVYRE--KPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQA-----R 86
Cdd:cd03288 15 GLGGEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplhtlR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 87 KRIGYVPQ-----RGSVDWDFP---TSVLDVVMMGL-YGQLGWFKRPGPRereaalrcleqvSMQAFTTRQISQLSGGQQ 157
Cdd:cd03288 95 SRLSIILQdpilfSGSIRFNLDpecKCTDDRLWEALeIAQLKNMVKSLPG------------GLDAVVTEGGENFSVGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 158 QRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQgKTVVVVHHDLETVrdyfdhLTLLNVQVIASGPMEEV 237
Cdd:cd03288 163 QLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVSTI------LDADLVLVLSRGILVEC 235
|
....*.
gi 917519534 238 FTPENL 243
Cdd:cd03288 236 DTPENL 241
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-224 |
9.28e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 11 PESGASSPLRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVrffgqSLAQARKrIG 90
Cdd:PRK10636 305 PESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-----GLAKGIK-LG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 91 YVPQRgsvdwdfptsvldvvmmglygQLGWFK----------RPGPREREAALR-CLEQVSMQA-FTTRQISQLSGGQQQ 158
Cdd:PRK10636 379 YFAQH---------------------QLEFLRadesplqhlaRLAPQELEQKLRdYLGGFGFQGdKVTEETRRFSGGEKA 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 159 RVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKkqgKTVVVVHHDLETVRDYFDHLTLL 224
Cdd:PRK10636 438 RLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE---GALVVVSHDRHLLRSTTDDLYLV 500
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
142-237 |
9.48e-09 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 55.46 E-value: 9.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 142 QAFTTrqisqLSGGQQQRVFLARALAQDAD---LYFMDEP-----FAGVDAvteeaILRVLHELKKQGKTVVVVHHDLET 213
Cdd:PRK00349 826 QPATT-----LSGGEAQRVKLAKELSKRSTgktLYILDEPttglhFEDIRK-----LLEVLHRLVDKGNTVVVIEHNLDV 895
|
90 100 110
....*....|....*....|....*....|....*
gi 917519534 214 VR--DYfdhltLLNV---------QVIASGPMEEV 237
Cdd:PRK00349 896 IKtaDW-----IIDLgpeggdgggEIVATGTPEEV 925
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
36-209 |
9.52e-09 |
|
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: 55.53 E-value: 9.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 36 DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVasgqvrfFGQSLAQARK-RIGYVPQR-----GSVDwD---FPTSV 106
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPV-------YGGRLTKPAKgKLFYVPQRpymtlGTLR-DqiiYPDSS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 107 LDvvmmglygqlgwFKRPGPREREaALRCLEQVSMQAFTTRQIS---------QLSGGQQQRVFLARALAQDADLYFMDE 177
Cdd:TIGR00954 542 ED------------MKRRGLSDKD-LEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|..
gi 917519534 178 PFAGVDAVTEEAILRVlheLKKQGKTVVVVHH 209
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRL---CREFGITLFSVSH 637
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
33-217 |
1.58e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 33 ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVpvasgqvrffgqslaqarkrigyVPQRGSVDWDfPTSVLDVVMM 112
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVT-----------------------MPNKGTVDIK-GSAALIAISS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 113 GLYGQL-------------GWFKRpgpREREAALRCLEQVSMQAFTTRQISQLSGGQQQRVFLARALAQDADLYFMDEPF 179
Cdd:PRK13545 95 GLNGQLtgienielkglmmGLTKE---KIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAL 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 917519534 180 AGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDY 217
Cdd:PRK13545 172 SVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSF 209
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
19-82 |
4.14e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.49 E-value: 4.14e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 19 LRVRDLTVVYREKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGL--VPVASGQVRFFGQSL 82
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDL 67
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
147-217 |
6.34e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.29 E-value: 6.34e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 147 RQISQLSGGQQQRVFLARAL---AQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVR--DY 217
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKvaDY 880
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
34-253 |
6.52e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 34 LWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLG-----LVPVaSGQVRFFGQSLAQARKRI-GYVPQRGSVDWDFPtsVL 107
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgfHIGV-EGVITYDGITPEEIKKHYrGDVVYNAETDVHFP--HL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 108 DVvmmglyGQLGWF----KRPGPR----EREAALRCLEQVSMQAF---TTRQ-------ISQLSGGQQQRVFLARALAQD 169
Cdd:TIGR00956 154 TV------GETLDFaarcKTPQNRpdgvSREEYAKHIADVYMATYglsHTRNtkvgndfVRGVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 170 ADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVV--HHDLETVRDYFDHLTLLNV-QVIASGPMEEVftpenlkRT 246
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVaiYQCSQDAYELFDKVIVLYEgYQIYFGPADKA-------KQ 300
|
....*..
gi 917519534 247 YGERMRW 253
Cdd:TIGR00956 301 YFEKMGF 307
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
48-210 |
9.98e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 48 AIVGPNGAGKSTLIKAVLGLVPVASGQVRfFGQSLaqarkRIGYVPQ-RGSVDWDfpTSVLDVVMMGlygqlgwfKRP-- 124
Cdd:PRK11147 349 ALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKL-----EVAYFDQhRAELDPE--KTVMDNLAEG--------KQEvm 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 125 -GPREREaALRCLEQV---SMQAFTTrqISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTeeaiLRVLHEL--K 198
Cdd:PRK11147 413 vNGRPRH-VLGYLQDFlfhPKRAMTP--VKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET----LELLEELldS 485
|
170
....*....|..
gi 917519534 199 KQGkTVVVVHHD 210
Cdd:PRK11147 486 YQG-TVLLVSHD 496
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
147-243 |
2.33e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 147 RQISQLSGGQQQRVFLARALAqdADL----YFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDletvrdyfDHLT 222
Cdd:PRK00635 472 RALATLSGGEQERTALAKHLG--AELigitYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD--------EQMI 541
|
90 100
....*....|....*....|.
gi 917519534 223 LLNVQVIASGPMEEVFTPENL 243
Cdd:PRK00635 542 SLADRIIDIGPGAGIFGGEVL 562
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
147-237 |
2.67e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 51.18 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 147 RQISQLSGGQQQRVFLARAL------AqdadLYFMDEPFAGV---DAvteEAILRVLHELKKQGKTVVVVHHDLETVR-- 215
Cdd:COG0178 481 RSAGTLSGGEAQRIRLATQIgsglvgV----LYVLDEPSIGLhqrDN---DRLIETLKRLRDLGNTVIVVEHDEDTIRaa 553
|
90 100 110
....*....|....*....|....*....|.
gi 917519534 216 DYfdhltLLNV---------QVIASGPMEEV 237
Cdd:COG0178 554 DY-----IIDIgpgagehggEVVAQGTPEEI 579
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
44-234 |
3.65e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 44 GQLCAIVGPNGAGKSTLIKAVLGLVP--VASGQVRFFGQSLAQAR-KRI-GYVPQRgsvdwDFPTSVLDVVMMGLYGqlG 119
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKKQETfARIsGYCEQN-----DIHSPQVTVRESLIYS--A 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 120 WFKRPGPREREAALRCLEQVsMQAFTTRQ----------ISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEA 189
Cdd:PLN03140 979 FLRLPKEVSKEEKMMFVDEV-MELVELDNlkdaivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1057
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 917519534 190 ILRVLHELKKQGKTVV-VVHHDLETVRDYFDHLTLLNV--QVIASGPM 234
Cdd:PLN03140 1058 VMRTVRNTVDTGRTVVcTIHQPSIDIFEAFDELLLMKRggQVIYSGPL 1105
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-236 |
5.78e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 22 RDLTV---VYREKPALWD-VDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVP---VASGQVRFFGQSL-AQARKRIGYVP 93
Cdd:TIGR00956 763 RNLTYevkIKKEKRVILNnVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLdSSFQRSIGYVQ 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 94 QRgsvDWDFPTS-VLDVVMMGLYgqlgwFKRPGPREREAALRCLEQV----SMQAFTTRQI----SQLSGGQQQRVFLAR 164
Cdd:TIGR00956 843 QQ---DLHLPTStVRESLRFSAY-----LRQPKSVSKSEKMEYVEEVikllEMESYADAVVgvpgEGLNVEQRKRLTIGV 914
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 165 AL-AQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVV-VVHHDLETVRDYFDHLTLLN--VQVIASGPMEE 236
Cdd:TIGR00956 915 ELvAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILcTIHQPSAILFEEFDRLLLLQkgGQTVYFGDLGE 990
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-207 |
6.61e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 19 LRVRDLTVVyrEKPALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQSLAQ--ARKRI--GY--- 91
Cdd:PRK10982 251 LEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnANEAInhGFalv 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 92 VPQRGSVDWdfpTSVLDVVMMGLYGQLGWFKRPGPREREAALRCLEQV---SMQAFTTRQ---ISQLSGGQQQRVFLARA 165
Cdd:PRK10982 329 TEERRSTGI---YAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWvidSMRVKTPGHrtqIGSLSGGNQQKVIIGRW 405
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 917519534 166 LAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVV 207
Cdd:PRK10982 406 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII 447
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
150-215 |
8.79e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 8.79e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 150 SQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELK-KQGKTVVVVHHDLETVR 215
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTIR 644
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-215 |
1.09e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 1.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917519534 152 LSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELK-KQGKTVVVVHHDLETVR 215
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASIK 1423
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
33-217 |
1.30e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.27 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 33 ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQslaqarkrigyvpqrgsvdwdfpTSVLdVVMM 112
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------------------VSVI-AISA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 113 GLYGQLgwfkrPGPREREAALRCLeqvsmqAFTTRQISQL---------------------SGGQQQRVFLARALAQDAD 171
Cdd:PRK13546 95 GLSGQL-----TGIENIEFKMLCM------GFKRKEIKAMtpkiiefselgefiyqpvkkySSGMRAKLGFSINITVNPD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 917519534 172 LYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVRDY 217
Cdd:PRK13546 164 ILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQF 209
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
48-221 |
7.56e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 48 AIVGPNGAGKSTLIKAVLGLVPVASGQVrffgqsLAQARKRIGYVPQRGSVDWDFPTSVLdVVMMGLYgqlgwfkrPGPR 127
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVRMAVFSQHHVDGLDLSSNPL-LYMMRCF--------PGVP 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 128 ERE-----AALRCLEQVSMQAFTTrqisqLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLheLKKQGK 202
Cdd:PLN03073 604 EQKlrahlGSFGVTGNLALQPMYT-----LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGG 676
|
170
....*....|....*....
gi 917519534 203 tVVVVHHDLETVRDYFDHL 221
Cdd:PLN03073 677 -VLMVSHDEHLISGSVDEL 694
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-217 |
1.04e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 3 TQPKTVQhpesgASSpLRVRDLTVVYREK-P-ALWDVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ 80
Cdd:PTZ00243 1299 AAPHPVQ-----AGS-LVFEGVQMRYREGlPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGR 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 81 -----SLAQARKRIGYVPQ---------RGSVDWDFPTSVLDVvmmglygqlgW--FKRPGPREREAAlrclEQVSMQAF 144
Cdd:PTZ00243 1373 eigayGLRELRRQFSMIPQdpvlfdgtvRQNVDPFLEASSAEV----------WaaLELVGLRERVAS----ESEGIDSR 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 145 TTRQISQLSGGQQQRVFLARA-LAQDADLYFMDEPFAGVDavteeailrvlHELKKQ----------GKTVVVVHHDLET 213
Cdd:PTZ00243 1439 VLEGGSNYSVGQRQLMCMARAlLKKGSGFILMDEATANID-----------PALDRQiqatvmsafsAYTVITIAHRLHT 1507
|
....
gi 917519534 214 VRDY 217
Cdd:PTZ00243 1508 VAQY 1511
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
152-207 |
1.11e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 1.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 152 LSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVV 207
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI 460
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
28-211 |
1.70e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.62 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 28 YREKpalWDVDLEvpaGQLCAIVGPNGAGKSTLIKAV-LGLvpvasgqvrfFGQSLAQARKRIGYVPqRGSVDwdfpTSV 106
Cdd:COG0419 13 YRDT---ETIDFD---DGLNLIVGPNGAGKSTILEAIrYAL----------YGKARSRSKLRSDLIN-VGSEE----ASV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 107 -LDVVMMG-LY------GQLGWFKRPGPREREAALR---------------------------------CLEQVSMQAFT 145
Cdd:COG0419 72 eLEFEHGGkRYrierrqGEFAEFLEAKPSERKEALKrllgleiyeelkerlkeleealesaleelaelqKLKQEILAQLS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 146 T-RQISQLSGGQQqrvfLARALAQDADLyFMDepFAGVDAVTEEAILRVLHELKkqgktvvVVHHDL 211
Cdd:COG0419 152 GlDPIETLSGGER----LRLALADLLSL-ILD--FGSLDEERLERLLDALEELA-------IITHVI 204
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
38-63 |
2.62e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 44.92 E-value: 2.62e-05
10 20
....*....|....*....|....*.
gi 917519534 38 DLEVPAGQLCAIVGPNGAGKSTLIKA 63
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDA 40
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
44-219 |
5.57e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 44 GQLCAIVGPNGAGKSTLIKAVLGLVPVASGQVRFFGQ-SLAqarkrigYVPQRGSVdwdFPTSVLDVVMMG--------- 113
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLA-------WVNQETPA---LPQPALEYVIDGdreyrqlea 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 114 ----------------LYGQLGWFKRPGPREREAALrcLEQVSM-QAFTTRQISQLSGGQQQRVFLARALAQDADLYFMD 176
Cdd:PRK10636 97 qlhdanerndghaiatIHGKLDAIDAWTIRSRAASL--LHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 917519534 177 EPFAGVDAvteEAILRVLHELKKQGKTVVVVHHDletvRDYFD 219
Cdd:PRK10636 175 EPTNHLDL---DAVIWLEKWLKSYQGTLILISHD----RDFLD 210
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
152-237 |
8.15e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.52 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 152 LSGGQQQRVFLAralAQDAD-----LYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHHDLETVR--DYfdhltLL 224
Cdd:PRK00349 490 LSGGEAQRIRLA---TQIGSgltgvLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRaaDY-----IV 561
|
90 100
....*....|....*....|..
gi 917519534 225 NV---------QVIASGPMEEV 237
Cdd:PRK00349 562 DIgpgagvhggEVVASGTPEEI 583
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
36-77 |
1.22e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.12 E-value: 1.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 917519534 36 DVDLEVPAGQLCAIVGPNGAGKSTLIKAVLGLVpVASGQVRF 77
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL-VPAKRARF 54
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
141-212 |
1.90e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917519534 141 MQaftTRQISQLSGGQQQRVFLARALAQDADLYFMDEPFAGVDAvteEAILRVLHELKKQGKTVVVVHHDLE 212
Cdd:PLN03073 337 MQ---VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVLWLETYLLKWPKTFIVVSHARE 402
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
50-210 |
6.00e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 50 VGPNGAGKSTLIKaVLG--LVPvASGQVrffgqSLaQARKRIGYVPQRGSVDWDFptSVLDVVMMGlYGQLGWFKrpgpR 127
Cdd:PRK15064 33 IGANGCGKSTFMK-ILGgdLEP-SAGNV-----SL-DPNERLGKLRQDQFAFEEF--TVLDTVIMG-HTELWEVK----Q 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 128 EREA-----------ALRC--LEQV--SMQAFT---------------TRQ----ISQLSGGQQQRVFLARALAQDADLY 173
Cdd:PRK15064 98 ERDRiyalpemseedGMKVadLEVKfaEMDGYTaearagelllgvgipEEQhyglMSEVAPGWKLRVLLAQALFSNPDIL 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 917519534 174 FMDEPFAGVDAVTeeaiLRVL-HELKKQGKTVVVVHHD 210
Cdd:PRK15064 178 LLDEPTNNLDINT----IRWLeDVLNERNSTMIIISHD 211
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
139-225 |
8.20e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 139 VSMQAFTTRQISQLSGGQQQRVFLARALA----------QDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVH 208
Cdd:TIGR00618 938 ADAYTGSVRPSATLSGGETFLASLSLALAladllstsggTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIIS 1017
|
90
....*....|....*..
gi 917519534 209 HdLETVRDYFDHLTLLN 225
Cdd:TIGR00618 1018 H-VPEFRERIPHRILVK 1033
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
38-67 |
9.67e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 39.57 E-value: 9.67e-04
10 20 30
....*....|....*....|....*....|
gi 917519534 38 DLEVPAGQLCAIVGPNGAGKSTLIKAVLGL 67
Cdd:COG4938 14 EAELELKPLTLLIGPNGSGKSTLIQALLLL 43
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
37-67 |
1.00e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 38.99 E-value: 1.00e-03
10 20 30
....*....|....*....|....*....|....
gi 917519534 37 VDLEVPAGqLCAIVGPNGAGKSTLIKA---VLGL 67
Cdd:cd03278 16 TTIPFPPG-LTAIVGPNGSGKSNIIDAirwVLGE 48
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
142-209 |
1.13e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.17 E-value: 1.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917519534 142 QAFTTRQISQLSGGQQQRVFLARALA--------QDADLYFMDEPFAGVDAVTEEAILRVLHELKKQGKTVVVVHH 209
Cdd:PRK10246 940 QADAVRDTRTLSGGESFLVSLALALAlsdlvshkTRIDSLFLDEGFGTLDSETLDTALDALDALNASGKTIGVISH 1015
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
145-196 |
1.60e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.83 E-value: 1.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917519534 145 TTRQISQLSGGQQQRVF---LARALAQ---DAD-------LYFMDEPFAGVDAVTEEAILRVLHE 196
Cdd:pfam13558 26 TYRRSGGLSGGEKQLLAylpLAAALAAqygSAEgrppaprLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
36-91 |
1.94e-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: 1.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 917519534 36 DVDLEVPAGqLCAIVGPNGAGKSTLIKA-VLGLVPVASGQVRFFGQSLAQARKRIGY 91
Cdd:COG3950 18 EIDFDNPPR-LTVLVGENGSGKTTLLEAiALALSGLLSRLDDVKFRKLLIRNGEFGD 73
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
141-200 |
2.07e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.40 E-value: 2.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917519534 141 MQAFTTRQISQLSGGQQQRVFLARALA-QDAD---LYFMDEPFAGVDAVTEEAILRVLHELKKQ 200
Cdd:cd03272 148 MKQDEQQEMQQLSGGQKSLVALALIFAiQKCDpapFYLFDEIDAALDAQYRTAVANMIKELSDG 211
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
152-239 |
2.30e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.06 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917519534 152 LSGGQQQRVFLARALAQDADLYFMDEPFAGVDAVTEEAILRVLHElkkqgktvvVVHHDLETVR-----------DYFDH 220
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQ---------IVHLTEATVLmsllqpapetfDLFDD 407
|
90 100
....*....|....*....|
gi 917519534 221 LTLLNV-QVIASGPMEEVFT 239
Cdd:PLN03140 408 IILLSEgQIVYQGPRDHILE 427
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
49-64 |
3.47e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.48 E-value: 3.47e-03
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
43-66 |
3.63e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.76 E-value: 3.63e-03
10 20
....*....|....*....|....
gi 917519534 43 AGQLCAIVGPNGAGKSTLIKAVLG 66
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
48-67 |
4.42e-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: 37.75 E-value: 4.42e-03
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
38-63 |
4.71e-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: 37.67 E-value: 4.71e-03
10 20
....*....|....*....|....*..
gi 917519534 38 DLEVP-AGQLCAIVGPNGAGKSTLIKA 63
Cdd:COG3593 16 DLSIElSDDLTVLVGENNSGKSSILEA 42
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
48-64 |
7.59e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 36.95 E-value: 7.59e-03
|
|