|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-243 |
9.49e-127 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 359.02 E-value: 9.49e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIAYVPQ 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RNDLDWTFPIHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFC 160
Cdd:COG1121 83 RAEVDWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 161 LDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPVHDILRPEVMLQAYETQLPFL 240
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSRAYGGPVALL 242
|
...
gi 518573420 241 KSA 243
Cdd:COG1121 243 AHG 245
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-218 |
3.58e-105 |
|
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: 302.92 E-value: 3.58e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 7 IDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIAYVPQRNDLDW 86
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 87 TFPIHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFV 166
Cdd:cd03235 82 DFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518573420 167 GIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAG 218
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-235 |
1.17e-78 |
|
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: 237.25 E-value: 1.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP-----FKQVRKQIAYV 78
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslsRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRNDLDwtFPIHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQL 158
Cdd:COG1120 81 PQEPPAP--FGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518573420 159 FCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQAYET 235
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDgRIVAQGPPEEVLTPELLEEVYGV 237
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-247 |
1.05e-71 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 220.52 E-value: 1.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSY-HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQ--IAY 77
Cdd:PRK15056 3 QQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKnlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRNDLDWTFPIHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQ 157
Cdd:PRK15056 83 VPQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 158 LFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPVHDILRPEVMLQAYETQL 237
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELAFSGVL 242
|
250
....*....|
gi 518573420 238 PFLKSAGGDA 247
Cdd:PRK15056 243 RHVALNGSEE 252
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-210 |
5.41e-68 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 207.86 E-value: 5.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRffeqpfKQVRKQIAYVPQRNDLDWTFPIHV 92
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------RAGGARVAYVPQRSEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 93 LDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMAS 172
Cdd:NF040873 75 RDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 518573420 173 EETMIRILKELRDEGKTILVVHHDLSKADDYFsHLVLL 210
Cdd:NF040873 155 RERIIALLAEEHARGATVVVVTHDLELVRRAD-PCVLL 191
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-244 |
3.51e-64 |
|
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: 199.31 E-value: 3.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 25 LSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIAYVPQRNDLDWTFPIHVLDTVLLGTYPKL 104
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 105 GLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELR 184
Cdd:TIGR03771 81 GWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518573420 185 DEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPVHDILRPEVMLQAY--ETQLPFLKSAG 244
Cdd:TIGR03771 161 GAGTAILMTTHDLAQAMATCDRVVLLNGRVIADGTPQQLQDPAPWMTTFgvSDSSPLLRIVG 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-225 |
6.81e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 194.13 E-value: 6.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF----KQVRKQIAYVPQ 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVardpAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RNDLDWTFPihVLDTV-LLGtypklGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLF 159
Cdd:COG1131 81 EPALYPDLT--VRENLrFFA-----RLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILR 225
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKgRIVADGTPDELKA 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-218 |
4.88e-55 |
|
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: 174.55 E-value: 4.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 6 TIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP-----FKQVRKQIAYVPQ 80
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslsPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 rndldwtfpihvldtvllgtypklglikrpkkedrayayhCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFC 160
Cdd:cd03214 81 ----------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 161 LDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLL-NKKLVKAG 218
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLkDGRIVAQG 180
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-237 |
5.23e-55 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 177.23 E-value: 5.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVR-----KQIAYVP 79
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSpwelaRRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 80 QRNDLdwTFPIHVLDTVLLGTYPKLglikRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQ-- 157
Cdd:COG4559 82 QHSSL--AFPFTVEEVVALGRAPHG----SSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEpv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 158 ------LFcLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVML 230
Cdd:COG4559 156 dggprwLF-LDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQgRLVAQGTPEEVLTDELLE 234
|
....*..
gi 518573420 231 QAYETQL 237
Cdd:COG4559 235 RVYGADL 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-223 |
7.12e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 176.40 E-value: 7.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQD-ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF--------KQVRKQ 74
Cdd:COG3638 2 MLELRNLSKRYPGGTpALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalrgralRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 75 IAYVPQRNDLdwtfpIH---VLDTVLLGTYPKLG----LIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVF 147
Cdd:COG3638 82 IGMIFQQFNL-----VPrlsVLTNVLAGRLGRTStwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518573420 148 LARALAQNAQLFCLDEPFVGID-MASEETMiRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDI 223
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDpKTARQVM-DLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDgRVVFDGPPAEL 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-232 |
1.73e-54 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 174.83 E-value: 1.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQ-DALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP-----FKQVRKQIAYV 78
Cdd:COG1122 1 IELENLSFSYPGGtPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitkknLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQrndldwtFPIH------VLDTVLLGtyPK-LGLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARA 151
Cdd:COG1122 81 FQ-------NPDDqlfaptVEEDVAFG--PEnLGL---PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 152 LAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVML 230
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDgRIVADGTPREVFSDYELL 228
|
..
gi 518573420 231 QA 232
Cdd:COG1122 229 EE 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-236 |
2.35e-52 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 170.19 E-value: 2.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF-----KQVRKQIAYVP 79
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsmlssRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 80 QRNdldwTFP--IHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQ 157
Cdd:PRK11231 83 QHH----LTPegITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 158 LFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQAYETQ 236
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANgHVMAQGTPEEVMTPGLLRTVFDVE 238
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-211 |
6.38e-52 |
|
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: 168.52 E-value: 6.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSY-HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF--------KQVRKQI 75
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgkalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 76 AYVPQrnDLDWTFPIHVLDTVL---LGTYPKL-GLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARA 151
Cdd:cd03256 81 GMIFQ--QFNLIERLSVLENVLsgrLGRRSTWrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 152 LAQNAQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLLN 211
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLK 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-233 |
5.96e-51 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 166.87 E-value: 5.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVR-----KQIAYV 78
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaelaRRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRNDLdwTFPIHVLDTVLLGTYPklglIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQ- 157
Cdd:PRK13548 82 PQHSSL--SFPFTVEEVVAMGRAP----HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 158 ------LFcLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVM 229
Cdd:PRK13548 156 dgpprwLL-LDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQgRLVADGTPAEVLTPETL 234
|
....
gi 518573420 230 LQAY 233
Cdd:PRK13548 235 RRVY 238
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-212 |
1.13e-50 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 164.56 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 7 IDRLYVSYHGQD--ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP-----FKQVRKQIAYVP 79
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklsLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 80 QRNDlDWTFPIHVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLF 159
Cdd:cd03225 82 QNPD-DQFFGPTVEEEVAFG----LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK 212
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-200 |
4.12e-50 |
|
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: 163.41 E-value: 4.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQD----ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIAYVPQ 80
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RNDLdwtFP-IHVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLF 159
Cdd:cd03293 81 QDAL---LPwLTVLDNVALG----LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518573420 160 CLDEPFVGIDMASEETMIR-ILKELRDEGKTILVVHHDLSKA 200
Cdd:cd03293 154 LLDEPFSALDALTREQLQEeLLDIWRETGKTVLLVTHDIDEA 195
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-235 |
1.32e-49 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 162.95 E-value: 1.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 6 TIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRF-----FEQPFKQVRKQIAYVPQ 80
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdgldvATTPSRELAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RNDLdwTFPIHVLDTVLLGTYP--KlGlikRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQL 158
Cdd:COG4604 83 ENHI--NSRLTVRELVAFGRFPysK-G---RLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518573420 159 FCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLL-NKKLVKAGPVHDILRPEVMLQAYET 235
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMkDGRVVAQGTPEEIITPEVLSDIYDT 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-224 |
1.32e-49 |
|
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: 162.72 E-value: 1.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF----KQVRKQIAYVPQ 80
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrkepREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RNDLDWTFpihvldTVL--LGTYPKLGLIKRPKKEDRAYAYhcLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQL 158
Cdd:COG4555 82 ERGLYDRL------TVRenIRYFAELYGLFDEELKKRIEEL--IELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 159 FCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLL-NKKLVKAGPVHDIL 224
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILhKGKVVAQGSLDELR 220
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
5-233 |
4.94e-49 |
|
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: 161.91 E-value: 4.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRK-----QIAYVP 79
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRrararRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 80 QRNDLDwtFPIHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLF 159
Cdd:TIGR03873 82 QDSDTA--VPLTVRDVVALGRIPHRSLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQAY 233
Cdd:TIGR03873 160 LLDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGgRVVAAGPPREVLTPALIRAVY 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-200 |
2.77e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 159.87 E-value: 2.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQD----ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIAYVP 79
Cdd:COG1116 7 ALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 80 QRNDLdwtFP-IHVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQL 158
Cdd:COG1116 87 QEPAL---LPwLTVLDNVALG----LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518573420 159 FCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKA 200
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEA 202
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-201 |
4.33e-48 |
|
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: 158.04 E-value: 4.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQD----ALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCLDLIEK-DQGDIRFFEQPFKQ--------- 70
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRpTSGEVRVDGTDISKlsekelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 71 VRKQIAYVPQRNDL--DWTfpihVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFL 148
Cdd:cd03255 80 RRRHIGFVFQSFNLlpDLT----ALENVELP----LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518573420 149 ARALAQNAQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKAD 201
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAE 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-237 |
6.19e-48 |
|
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: 158.71 E-value: 6.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 12 VSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACL-DLIEKDQGDIRFFEQPFKQV-----RKQIAYVpqRNDLD 85
Cdd:COG1119 11 VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgDLPPTYGNDVRLFGERRGGEdvwelRKRIGLV--SPALQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 86 WTFPIH--VLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDE 163
Cdd:COG1119 89 LRFPRDetVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 164 PFVGIDMASEETMIRILKELRDEGKT--ILVVHHdLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQAYETQL 237
Cdd:COG1119 169 PTAGLDLGARELLLALLDKLAAEGAPtlVLVTHH-VEEIPPGITHVLLLKDgRVVAAGPKEEVLTSENLSEAFGLPV 244
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-228 |
1.41e-46 |
|
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: 154.90 E-value: 1.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQ------PFKQVRKQIAYV 78
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglpPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRNDLdwtFP-IHVLDTVLLGTYPKLGL------IKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARA 151
Cdd:cd03219 81 FQIPRL---FPeLTVLENVMVAAQARTGSglllarARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 152 LAQNAQLFCLDEPFVGidMASEET--MIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLN--KKLVKaGPVHDILR-P 226
Cdd:cd03219 158 LATDPKLLLLDEPAAG--LNPEETeeLAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDqgRVIAE-GTPDEVRNnP 234
|
..
gi 518573420 227 EV 228
Cdd:cd03219 235 RV 236
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-212 |
3.18e-46 |
|
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: 151.78 E-value: 3.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF----KQVRKQIAYVPQ 80
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkkepEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RNDLDWTFpihvldTVllgtypklglikrpkkedrayayhclekvgmqdfakRQIGELSGGQQQRVFLARALAQNAQLFC 160
Cdd:cd03230 81 EPSLYENL------TV------------------------------------RENLKLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518573420 161 LDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK 212
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-225 |
6.43e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 154.88 E-value: 6.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ-VRKQIAYVPQ-R 81
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPeDRRRIGYLPEeR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 ndldwtfpihvldtvllGTYPKL-------------GLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFL 148
Cdd:COG4152 81 -----------------GLYPKMkvgeqlvylarlkGL---SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 149 ARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILR 225
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKgRKVLSGSVDEIRR 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-232 |
1.22e-45 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 156.93 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF-----KQVRKQIAYVP 79
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaRAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 80 QRNDLDWTFpiHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLF 159
Cdd:PRK09536 84 QDTSLSFEF--DVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNKklvkaGPVHDILRPEVMLQA 232
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLAD-----GRVRAAGPPADVLTA 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-218 |
7.78e-45 |
|
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: 149.59 E-value: 7.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV---RKQIAYVPQR 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVppeRRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 NDLdwtFPiH--VLDTVLLGtyPKLGLIKRPKKEDRAYAYhcLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLF 159
Cdd:cd03259 81 YAL---FP-HltVAENIAFG--LKLRGVPKAEIRARVREL--LELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLLNK-KLVKAG 218
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEgRIVQVG 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-211 |
4.30e-44 |
|
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: 148.60 E-value: 4.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQD-ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQ--------PFKQVRKQI 75
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditklrgkKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 76 AYVPQRNDLdwTFPIHVLDTVL---LGTYPKL-GLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARA 151
Cdd:TIGR02315 82 GMIFQHYNL--IERLTVLENVLhgrLGYKPTWrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 152 LAQNAQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLLN 211
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLK 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-225 |
4.02e-43 |
|
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: 152.36 E-value: 4.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSY-----HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP--------FKQV 71
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklsrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 72 RKQIAYVPQrnD----LDwtfPIH-VLDTVllgTYP--KLGLIKRPKKEDRAYAYhcLEKVGMQ-DFAKRQIGELSGGQQ 143
Cdd:COG1123 341 RRRVQMVFQ--DpyssLN---PRMtVGDII---AEPlrLHGLLSRAERRERVAEL--LERVGLPpDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 144 QRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVH 221
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDgRIVEDGPTE 490
|
....
gi 518573420 222 DILR 225
Cdd:COG1123 491 EVFA 494
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-212 |
6.88e-43 |
|
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: 142.77 E-value: 6.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 6 TIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF-----KQVRKQIAYVPQ 80
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaklplEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 rndldwtfpihvldtvllgtypklglikrpkkedrayayhclekvgmqdfakrqigeLSGGQQQRVFLARALAQNAQLFC 160
Cdd:cd00267 81 ---------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518573420 161 LDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK 212
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-198 |
1.37e-42 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 145.18 E-value: 1.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQ------PFKQVRKQ 74
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 75 IAyvpqRndldwTFPI-------HVLDTVLLGTYPKLG-----------LIKRPKKEDRAYAYHCLEKVGMQDFAKRQIG 136
Cdd:COG0411 81 IA----R-----TFQNprlfpelTVLENVLVAAHARLGrgllaallrlpRARREEREARERAEELLERVGLADRADEPAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 137 ELSGGQQQRVFLARALAQNAQLFCLDEPFVGidMASEET--MIRILKELRDE-GKTILVVHHDLS 198
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAG--LNPEETeeLAELIRRLRDErGITILLIEHDMD 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-196 |
1.59e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.42 E-value: 1.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFK-----QVRKQIAYVP 79
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSampppEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 80 QRNDLdwtFPihvlDTVllGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQ-DFAKRQIGELSGGQQQRVFLARALAQNAQL 158
Cdd:COG4619 81 QEPAL---WG----GTV--RDNLPFPFQLRERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 518573420 159 FCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHD 196
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHD 190
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-198 |
2.24e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 143.98 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCLDLIEK-DQGDIRFFEQPF-------KQVRKQIA 76
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLR-CINLLEEpDSGTITVDGEDLtdskkdiNKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 77 YVPQRNDLdwtFPiH--VLDTVLLGtyPKLGLiKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQ 154
Cdd:COG1126 81 MVFQQFNL---FP-HltVLENVTLA--PIKVK-KMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518573420 155 NAQLFCLDEPFVGID--MASE--ETMirilKELRDEGKTILVVHHDLS 198
Cdd:COG1126 154 EPKVMLFDEPTSALDpeLVGEvlDVM----RDLAKEGMTMVVVTHEMG 197
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-226 |
4.42e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 146.40 E-value: 4.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV---RKQIAY 77
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppeKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRNDLdwtFPiH--VLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQN 155
Cdd:COG3842 82 VFQDYAL---FP-HltVAENVAFG----LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 156 AQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHD----LSKADdyfsHLVLLNK-KLVKAGPVHDIL-RP 226
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDqeeaLALAD----RIAVMNDgRIEQVGTPEEIYeRP 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-232 |
5.43e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 149.28 E-value: 5.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQD--ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKD---QGDIRFFEQPFKQVR--- 72
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDvpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSeal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 73 --KQIAYVPQrNDLDWTFPIHVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLAR 150
Cdd:COG1123 81 rgRRIGMVFQ-DPMTQLNPVTVGDQIAEA----LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 151 ALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEV 228
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDgRIVEDGPPEEILAAPQ 235
|
....
gi 518573420 229 MLQA 232
Cdd:COG1123 236 ALAA 239
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-224 |
1.50e-41 |
|
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: 141.42 E-value: 1.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQ------PFKQVRKQIAYV 78
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglpPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRNDLdwtFP-IHVLDTVLLGTYPklgLIKRPKKEDRAYAYHCLEKvgMQDFAKRQIGELSGGQQQRVFLARALAQNAQ 157
Cdd:cd03224 81 PEGRRI---FPeLTVEENLLLGAYA---RRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 158 LFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKA----DDYFshlVLLNKKLVKAGPVHDIL 224
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFAleiaDRAY---VLERGRVVLEGTAAELL 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-225 |
1.56e-41 |
|
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: 148.75 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYH-GQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV-----RKQIAY 77
Cdd:COG4988 336 SIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLdpaswRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRNdldWTFPIHVLDTVLLGtypklglikRPKKEDRAyAYHCLEKVGMQDFAKR-------QIGE----LSGGQQQRV 146
Cdd:COG4988 416 VPQNP---YLFAGTIRENLRLG---------RPDASDEE-LEAALEAAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518573420 147 FLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPVHDILR 225
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-197 |
2.75e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 140.95 E-value: 2.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQD----ALENVSLSIQEGTMTGIIGPNGAGKSTLLK--ACLDLIekDQGDIRFFEQPFKQV--- 71
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNilGGLDRP--TSGEVLIDGQDISSLser 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 72 ------RKQIAYVPQRNDL--DWTfpihVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQ 143
Cdd:COG1136 79 elarlrRRHIGFVFQFFNLlpELT----ALENVALP----LLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 144 QRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDL 197
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDP 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-211 |
4.95e-41 |
|
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: 138.86 E-value: 4.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF-------KQVRKQIAY 77
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdledelPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRNDLdwtFPiH--VLDTVLLGtypklglikrpkkedrayayhclekvgmqdfakrqigeLSGGQQQRVFLARALAQN 155
Cdd:cd03229 81 VFQDFAL---FP-HltVLENIALG--------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 156 AQLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLLN 211
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-223 |
5.60e-41 |
|
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: 140.01 E-value: 5.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKAC---LDLI--EKDQGDIRFFEQPFKQ-------VR 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlNDLIpgAPDEGEVLLDGKDIYDldvdvleLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 73 KQIAYVPQRNDLdwtFPIHVLDTVLLGtyPKLGLIKrPKKEDRAYAYHCLEKVGMQDFAKRQIG--ELSGGQQQRVFLAR 150
Cdd:cd03260 81 RRVGMVFQKPNP---FPGSIYDNVAYG--LRLHGIK-LKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518573420 151 ALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEgKTILVVHHDLSKA---DDYFshLVLLNKKLVKAGPVHDI 223
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAarvADRT--AFLLNGRLVEFGPTEQI 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-196 |
5.74e-41 |
|
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: 139.54 E-value: 5.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ----VRKQIAYVPQ 80
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDaredYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RNDL--DWTfpihVLDtvLLGTYPKLglikRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQL 158
Cdd:COG4133 83 ADGLkpELT----VRE--NLRFWAAL----YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 518573420 159 FCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHD 196
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-225 |
7.73e-41 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 140.13 E-value: 7.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSY-HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRF-----FEQPFKQVRKQIAYV 78
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdgediREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRNDLdwtFPiHVldTVL--LGTYPKLGLIKRPKKEDRAYayHCLEKVGM--QDFAKRQIGELSGGQQQRVFLARALAQ 154
Cdd:cd03295 81 IQQIGL---FP-HM--TVEenIALVPKLLKWPKEKIRERAD--ELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518573420 155 NAQLFCLDEPFVGID----MASEETMIRILKELrdeGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILR 225
Cdd:cd03295 153 DPPLLLMDEPFGALDpitrDQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNgEIVQVGTPDEILR 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-212 |
7.93e-41 |
|
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: 139.20 E-value: 7.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCLDLIEK-DQGDIRFFEQP-------FKQVRKQIA 76
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLR-CINLLEEpDSGTIIIDGLKltddkknINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 77 YVPQRNDLdwtFPiH--VLDTVllgtypKLGLIK---RPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARA 151
Cdd:cd03262 80 MVFQQFNL---FP-HltVLENI------TLAPIKvkgMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518573420 152 LAQNAQLFCLDEPFVGID--MASEetMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK 212
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDpeLVGE--VLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-225 |
1.27e-40 |
|
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: 139.94 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSY----HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF-----KQVRKQ 74
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtrrrrKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 75 IAYVPQ--RNDLDwtfPIHVLDTVLLGTypkLGLIKRPKKEDRAYAYhcLEKVGM-QDFAKRQIGELSGGQQQRVFLARA 151
Cdd:COG1124 81 VQMVFQdpYASLH---PRHTVDRILAEP---LRIHGLPDREERIAEL--LEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 152 LAQNAQLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKAdDYFSH--LVLLNKKLVKAGPVHDILR 225
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVV-AHLCDrvAVMQNGRIVEELTVADLLA 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-218 |
1.35e-40 |
|
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: 138.48 E-value: 1.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGtMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFK----QVRKQIAYVPQ 80
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLkqpqKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RNDLDWTFPIH-VLDTvllgtypkLGLIKR-PKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQL 158
Cdd:cd03264 80 EFGVYPNFTVReFLDY--------IAWLKGiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 159 FCLDEPFVGIDMASEETMIRILKELrDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAG 218
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKgKLVFEG 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-233 |
1.65e-40 |
|
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: 138.96 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQ------PFKQVRKQIAYV 78
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpPHRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRNDLdwtFP-IHVLDTVLLGTYPKLGLIKRPKKEDRAYAYhclekvgmqdF------AKRQIGELSGGQQQRVFLARA 151
Cdd:COG0410 84 PEGRRI---FPsLTVEENLLLGAYARRDRAEVRADLERVYEL----------FprlkerRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 152 LAQNAQLFCLDEPFVGI--DMASEetMIRILKELRDEGKTILVVHHDLSKA---DDYFshLVLLNKKLVKAGPVHDILRP 226
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLapLIVEE--IFEIIRRLNREGVTILLVEQNARFAleiADRA--YVLERGRIVLEGTAAELLAD 226
|
....*..
gi 518573420 227 EVMLQAY 233
Cdd:COG0410 227 PEVREAY 233
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
10-225 |
5.96e-40 |
|
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: 137.63 E-value: 5.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 10 LYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP--------FKQVRKQIAYVPQR 81
Cdd:cd03261 6 LTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglseaeLYRLRRRMGMLFQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 NDL--DWTfpihVLDTVLLGTYPKLGLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLF 159
Cdd:cd03261 86 GALfdSLT----VFENVAFPLREHTRL---SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKAD---DYFshLVLLNKKLVKAGPVHDILR 225
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFaiaDRI--AVLYDGKIVAEGTPEELRA 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-198 |
8.07e-40 |
|
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: 137.25 E-value: 8.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQD----ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP--------FKQVR 72
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 73 KQIAYVPQ--RNDLDWTFPI--HVLDTVLLGTypklglIKRPKKEDRAYAYHCLEKVGM-QDFAKRQIGELSGGQQQRVF 147
Cdd:cd03257 82 KEIQMVFQdpMSSLNPRMTIgeQIAEPLRIHG------KLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518573420 148 LARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLS 198
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLG 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-225 |
1.56e-39 |
|
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: 143.37 E-value: 1.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 2 SYALTIDRLYVSYHGQD--ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ-----VRKQ 74
Cdd:COG4987 331 GPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDldeddLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 75 IAYVPQRNDLdwtFPIHVLDTVLLGtypklglikRPKKEDRAyAYHCLEKVGMQDFAKRQ-------IGE----LSGGQQ 143
Cdd:COG4987 411 IAVVPQRPHL---FDTTLRENLRLA---------RPDATDEE-LWAALERVGLGDWLAALpdgldtwLGEggrrLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 144 QRVFLARALAQNAQLFCLDEPFVGIDMASEEtmiRILKELRD--EGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPVH 221
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQ---ALLADLLEalAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHE 554
|
....
gi 518573420 222 DILR 225
Cdd:COG4987 555 ELLA 558
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-166 |
2.34e-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: 2.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF-----KQVRKQIAYVPQrndLDWTFPIH-VL 93
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderKSLRKEIGYVFQ---DPQLFPRLtVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 94 DTVLLGTYpkLGLIKRPKKEDRAYAYhcLEKVGMQDFAKR----QIGELSGGQQQRVFLARALAQNAQLFCLDEPFV 166
Cdd:pfam00005 78 ENLRLGLL--LKGLSKREKDARAEEA--LEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-200 |
2.74e-39 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 136.92 E-value: 2.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSyALTIDRLYVSYHG----QDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIA 76
Cdd:COG4525 1 MS-MLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 77 YVPQRNDLdwtFP-IHVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQN 155
Cdd:COG4525 80 VVFQKDAL---LPwLNVLDNVAFG----LRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518573420 156 AQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKA 200
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEA 198
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-238 |
5.63e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 136.43 E-value: 5.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 17 QDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQ--------PFKQVRKQIAYVPQrndldwtF 88
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditakkkkKLKDLRKKVGLVFQ-------F 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 89 PIH------VLDTVLLGtyPK-LGLikrPKKEDRAYAYHCLEKVGM-QDFAKRQIGELSGGQQQRVFLARALAQNAQLFC 160
Cdd:TIGR04521 91 PEHqlfeetVYKDIAFG--PKnLGL---SEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 161 LDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQAYETQLP 238
Cdd:TIGR04521 166 LDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKgKIVLDGTPREVFSDVDELEKIGLDVP 245
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
13-201 |
6.54e-39 |
|
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: 134.28 E-value: 6.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKAcLDLIEK-DQGDIRFFEQPFKQVRKQIAYVPQRNDLDWTFPIH 91
Cdd:TIGR03608 7 KFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNI-IGLLEKfDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 92 VL---DTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGI 168
Cdd:TIGR03608 86 ALienETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSL 165
|
170 180 190
....*....|....*....|....*....|...
gi 518573420 169 DMASEETMIRILKELRDEGKTILVVHHDLSKAD 201
Cdd:TIGR03608 166 DPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK 198
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-229 |
9.36e-39 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 137.59 E-value: 9.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSyaLTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCLDLIEK-DQGDIRFFEQPFK---QVRK-QI 75
Cdd:COG1118 1 MS--IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLR-IIAGLETpDSGRIVLNGRDLFtnlPPRErRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 76 AYVPQRNDLdwtFPiH--VLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALA 153
Cdd:COG1118 78 GFVFQHYAL---FP-HmtVAENIAFG----LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 154 QNAQLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILR----PE 227
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQgRIEQVGTPDEVYDrpatPF 229
|
..
gi 518573420 228 VM 229
Cdd:COG1118 230 VA 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-198 |
2.22e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 133.25 E-value: 2.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSY-HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLdLIEK-DQGDIRFFEQ-----PFKQV---RKQ 74
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLY-GEERpTSGQVLVNGQdlsrlKRREIpylRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 75 IAYVPQRNDL--DWTfpihVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARAL 152
Cdd:COG2884 81 IGVVFQDFRLlpDRT----VYENVALP----LRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518573420 153 AQNAQLFCLDEPFVGIDMA-SEETMiRILKELRDEGKTILVVHHDLS 198
Cdd:COG2884 153 VNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIATHDLE 198
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
19-212 |
2.25e-38 |
|
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: 132.79 E-value: 2.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFK-QVRKQIAYVPQRNdldwtfpihvldtvl 97
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiAARNRIGYLPEER--------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 98 lGTYPKLGLIKR----------PKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVG 167
Cdd:cd03269 80 -GLYPKMKVIDQlvylaqlkglKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518573420 168 IDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK 212
Cdd:cd03269 159 LDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNK 203
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-225 |
8.49e-38 |
|
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: 132.41 E-value: 8.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF--------KQVR 72
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsekelYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 73 KQIAYVPQRNDL--DWTfpihVLDTVLLGTYPKLGLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLAR 150
Cdd:COG1127 82 RRIGMLFQGGALfdSLT----VFENVAFPLREHTDL---SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518573420 151 ALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKAD---DYFshLVLLNKKLVKAGPVHDILR 225
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFaiaDRV--AVLADGKIIAEGTPEELLA 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-210 |
2.51e-37 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 131.36 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ-------VRKQIA 76
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGpgaergvVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 77 YVPQRNdldwtfpihVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNA 156
Cdd:PRK11248 81 LLPWRN---------VQDNVAFG----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 157 QLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLL 210
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLL 202
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-224 |
2.99e-37 |
|
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: 138.43 E-value: 2.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQD--ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ-----VRKQIA 76
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQidpasLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 77 YVPQRNDLdwtFPIHVLDTVLLGtYPKLglikrpkkeDRAYAYHCLEKVGMQDFAKR-------QIGE----LSGGQQQR 145
Cdd:COG2274 553 VVLQDVFL---FSGTIRENITLG-DPDA---------TDEEIIEAARLAGLHDFIEAlpmgydtVVGEggsnLSGGQRQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 146 VFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLS---KADdyfSHLVLLNKKLVKAGPvHD 222
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLStirLAD---RIIVLDKGRIVEDGT-HE 694
|
..
gi 518573420 223 IL 224
Cdd:COG2274 695 EL 696
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-224 |
3.38e-37 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 131.08 E-value: 3.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 3 YALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCLDLIEK-DQGDIRFFEQPF------------- 68
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLR-CINLLETpDSGEIRVGGEEIrlkpdrdgelvpa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 69 --KQV---RKQIAYVPQRNDLdWTF----------PIHVLdtvllgtypklgliKRPKKEDRAYAYHCLEKVGMQDFAKR 133
Cdd:COG4598 86 drRQLqriRTRLGMVFQSFNL-WSHmtvlenvieaPVHVL--------------GRPKAEAIERAEALLAKVGLADKRDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 134 QIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGID--MASEetMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLN 211
Cdd:COG4598 151 YPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDpeLVGE--VLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLH 228
|
250
....*....|....
gi 518573420 212 KKLVK-AGPVHDIL 224
Cdd:COG4598 229 QGRIEeQGPPAEVF 242
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-201 |
7.36e-37 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 127.50 E-value: 7.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQD--ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV-----RKQIAY 77
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLdleslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQrndldwtfpihvlDTVLL-GTypklglikrpkkedrayayhclekvgmqdfakrqIGE--LSGGQQQRVFLARALAQ 154
Cdd:cd03228 81 VPQ-------------DPFLFsGT----------------------------------IREniLSGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518573420 155 NAQLFCLDEPFVGIDMASEETMIRILKELRDeGKTILVVHHDLS---KAD 201
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLStirDAD 162
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-233 |
1.48e-36 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 129.72 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 8 DRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDI-----RFFEQPFKQVRKQIAYVPQrn 82
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgeHIQHYASKEVARRIGLLAQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 83 dlDWTFP--IHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFC 160
Cdd:PRK10253 89 --NATTPgdITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 161 LDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQAY 233
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREgKIVAQGAPKEIVTAELIERIY 241
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-211 |
3.76e-36 |
|
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: 126.99 E-value: 3.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 6 TIDRLYVSY-HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF--KQVRKQIAYVPQrn 82
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkaKERRKSIGYVMQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 83 DLDWTFpihVLDTVllgtYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLD 162
Cdd:cd03226 79 DVDYQL---FTDSV----REELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518573420 163 EPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLN 211
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-233 |
7.48e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.79 E-value: 7.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDAleNVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQ------PFKqvRKqIAYV 78
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalpPAE--RP-VSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRNDLdwtFPiH--VLDTVLLGTYPKLglikRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNA 156
Cdd:COG3840 77 FQENNL---FP-HltVAQNIGLGLRPGL----KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 157 QLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEV--MLQA 232
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADgRIAADGPTAALLDGEPppALAA 228
|
.
gi 518573420 233 Y 233
Cdd:COG3840 229 Y 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-198 |
1.12e-35 |
|
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: 132.41 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 2 SYALTIDRLYVSYHGQD-ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF-----KQVRKQI 75
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLadadaDSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 76 AYVPQRndlDWTFPIHVLDTVLLGTypklglikrpKKEDRAYAYHCLEKVGMQDFAK-------RQIGE----LSGGQQQ 144
Cdd:TIGR02857 399 AWVPQH---PFLFAGTIAENIRLAR----------PDASDAEIREALERAGLDEFVAalpqgldTPIGEggagLSGGQAQ 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518573420 145 RVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLS 198
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLA 518
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
19-227 |
3.12e-35 |
|
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: 125.39 E-value: 3.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCLDLIEK-DQGDIRFFEQPFKQV--------RKQIAYVPQRNDLDWTFP 89
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERpTSGSVLVDGTDLTLLsgkelrkaRRRIGMIFQHFNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 90 ihVLDTVllgTYPkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGID 169
Cdd:cd03258 99 --VFENV---ALP-LEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 170 MASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSH-LVLLNKKLVKAGPVHDIL-RPE 227
Cdd:cd03258 173 PETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRvAVMEKGEVVEEGTVEEVFaNPQ 233
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-196 |
7.04e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.50 E-value: 7.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSyALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV---RKQIAY 77
Cdd:COG3839 1 MA-SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLppkDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRNDLdwtFPiH--VLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQN 155
Cdd:COG3839 80 VFQSYAL---YP-HmtVYENIAFP----LKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518573420 156 AQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHD 196
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHD 193
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-247 |
5.03e-34 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 123.36 E-value: 5.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 6 TIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF-----KQVRKQIAYVPQ 80
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswssKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RndLDWTFPIHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFC 160
Cdd:PRK10575 93 Q--LPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 161 LDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQAYETQLP 238
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGgEMIAQGTPAELMRGETLEQIYGIPMG 250
|
....*....
gi 518573420 239 FLKSAGGDA 247
Cdd:PRK10575 251 ILPHPAGAA 259
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-201 |
1.02e-33 |
|
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: 121.07 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDI----RFFEQPFKQVRKQIAYVPQRNDLDWTFPihVLD 94
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingYSIRTDRKAARQSLGYCPQFDALFDELT--VRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 95 TVLLgtypkLGLIK-RPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASE 173
Cdd:cd03263 95 HLRF-----YARLKgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASR 169
|
170 180
....*....|....*....|....*...
gi 518573420 174 ETMIRILKELRdEGKTILVVHHDLSKAD 201
Cdd:cd03263 170 RAIWDLILEVR-KGRSIILTTHSMDEAE 196
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-218 |
6.81e-33 |
|
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: 118.47 E-value: 6.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF---KQVRKQIAyvpqr 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqknIEALRRIG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 ndldwtfpihvldtVLL---GTYPKL-----------GLIKRPKKEDRayayhCLEKVGMQDFAKRQIGELSGGQQQRVF 147
Cdd:cd03268 76 --------------ALIeapGFYPNLtarenlrllarLLGIRKKRIDE-----VLDVVGLKDSAKKKVKGFSLGMKQRLG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518573420 148 LARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAG 218
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKgKLIEEG 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
19-212 |
2.16e-32 |
|
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: 118.21 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV---RKQIAYVPQRNDLdwtFP-IHVLD 94
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVpvqERNVGFVFQHYAL---FRhMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 95 TVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEE 174
Cdd:cd03296 94 NVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 518573420 175 TMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLLNK 212
Cdd:cd03296 174 ELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNK 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-240 |
3.22e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 118.68 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYH-GQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFF-----EQPFKQVRKQ 74
Cdd:PRK13647 1 MDNIIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMgrevnAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 75 IAYVPQRNDlDWTFPIHVLDTVLLGTYpKLGLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQ 154
Cdd:PRK13647 81 VGLVFQDPD-DQVFSSTVWDDVAFGPV-NMGL---DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 155 NAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPVHDILRPEVMLQAYE 234
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAG 235
|
....*.
gi 518573420 235 TQLPFL 240
Cdd:PRK13647 236 LRLPLV 241
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-223 |
4.03e-32 |
|
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: 117.34 E-value: 4.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV---RKQIAYVPQR 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLpphKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 NDLdwtFP-IHVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFC 160
Cdd:cd03300 81 YAL---FPhLTVFENIAFG----LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 161 LDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDI 223
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKgKIQQIGTPEEI 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-228 |
4.66e-32 |
|
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: 117.24 E-value: 4.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQ------PFKQVRKQIAYV 78
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEditklpPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRNDLdwtFP-IHVLDTVLLGtypkLGLIKRPKKE--DRAYAyhcLEKVgMQDFAKRQIGELSGGQQQRVFLARALAQN 155
Cdd:TIGR03410 81 PQGREI---FPrLTVEENLLTG----LAALPRRSRKipDEIYE---LFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 156 AQLFCLDEPFVGIDMASEETMIRILKELRDEGK-TILVVHHDLS----KADDYfshLVLLNKKLVKAGPVHDILRPEV 228
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDfareLADRY---YVMERGRVVASGAGDELDEDKV 224
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
13-224 |
4.49e-31 |
|
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: 120.74 E-value: 4.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQD--ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ-----VRKQIAYVPQRNDLd 85
Cdd:TIGR03375 472 AYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQidpadLRRNIGYVPQDPRL- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 86 wtFPIHVLDTVLLGtypklglikRPKKED----RAyayhcLEKVGMQDFAKR-------QIGE----LSGGQQQRVFLAR 150
Cdd:TIGR03375 551 --FYGTLRDNIALG---------APYADDeeilRA-----AELAGVTEFVRRhpdgldmQIGErgrsLSGGQRQAVALAR 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 151 ALAQNAQLFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLSkADDYFSHLVLLNK-KLVKAGPVHDIL 224
Cdd:TIGR03375 615 ALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTS-LLDLVDRIIVMDNgRIVADGPKDQVL 687
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-236 |
7.75e-31 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 114.17 E-value: 7.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKdQGDIRFFEQPFKQVR-----KQIAYVPQRNDLdwTFPIHVLD 94
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSaaelaRHRAYLSQQQSP--PFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 95 TVLLGTYPKLglikRPKKEDRAYAYHClEKVGMQDFAKRQIGELSGGQQQRVFLARALAQ-------NAQLFCLDEPFVG 167
Cdd:COG4138 89 YLALHQPAGA----SSEAVEQLLAQLA-EALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 168 IDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQAYETQ 236
Cdd:COG4138 164 LDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQgKLVASGETAEVMTPENLSEVFGVK 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-224 |
9.28e-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: 113.97 E-value: 9.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQ---PFKQVRKQIAYVPQRNDLdwtFP-IHVLDT 95
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEKRDISYVPQNYAL---FPhMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 96 VLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEET 175
Cdd:cd03299 92 IAYG----LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518573420 176 MIRILKELRDE-GKTILVVHHDLSKA----DDYfshLVLLNKKLVKAGPVHDIL 224
Cdd:cd03299 168 LREELKKIRKEfGVTVLHVTHDFEEAwalaDKV---AIMLNGKLIQVGKPEEVF 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-201 |
1.80e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 118.34 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHG-QDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV-----RKQIAY 77
Cdd:COG1132 339 EIEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLtleslRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRNDLdwtFPIHVLDTVLLGtypklglikRPkKEDRAYAYHCLEKVGMQDFAKR-------QIGE----LSGGQQQRV 146
Cdd:COG1132 419 VPQDTFL---FSGTIRENIRYG---------RP-DATDEEVEEAAKAAQAHEFIEAlpdgydtVVGErgvnLSGGQRQRI 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 147 FLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLS---KAD 201
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLStirNAD 542
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-200 |
1.99e-30 |
|
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: 113.89 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCLD-LIEKDQGDIRFFEQPFKQV---------RKQIAYV-------PQR 81
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLR-CINrLIEPTSGKVLIDGQDIAAMsrkelrelrRKKISMVfqsfallPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 NdldwtfpihVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCL 161
Cdd:cd03294 118 T---------VLENVAFG----LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518573420 162 DEPFVGIDmaseeTMIRilKELRDE--------GKTILVVHHDLSKA 200
Cdd:cd03294 185 DEAFSALD-----PLIR--REMQDEllrlqaelQKTIVFITHDLDEA 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-243 |
2.33e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.96 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQD--ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFK-----QVRKQIAY 77
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeetvwDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRNDLDW---TfpihVLDTVLLGT----YPKLGLIKRPkkeDRAyayhcLEKVGMQDFAKRQIGELSGGQQQRVFLAR 150
Cdd:PRK13635 86 VFQNPDNQFvgaT----VQDDVAFGLenigVPREEMVERV---DQA-----LRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 151 ALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGK-TILVVHHDL---SKADdyfsHLVLLNK-KLVKAGPVHDILR 225
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLdeaAQAD----RVIVMNKgEILEEGTPEEIFK 229
|
250 260
....*....|....*....|.
gi 518573420 226 PEVMLQAYETQLPF---LKSA 243
Cdd:PRK13635 230 SGHMLQEIGLDVPFsvkLKEL 250
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
2.75e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.21 E-value: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCL----DLIE--KDQGDIRFFEQ-------P 67
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLR-CLnrmnDLIPgaRVEGEILLDGEdiydpdvD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 68 FKQVRKQIAYVPQR-NdldwTFPIHVLDTVLLGtyPKLGLIKRPKKEDRAyAYHCLEKVGM----QDFAKRQIGELSGGQ 142
Cdd:COG1117 87 VVELRRRVGMVFQKpN----PFPKSIYDNVAYG--LRLHGIKSKSELDEI-VEESLRKAALwdevKDRLKKSALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 143 QQRVFLARALAQNAQLFCLDEPFVGIDMAS----EETMirilKELRDEgKTILVVHHDLSKA---DDY--FshlvLLNKK 213
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPIStakiEELI----LELKKD-YTIVIVTHNMQQAarvSDYtaF----FYLGE 230
|
250
....*....|
gi 518573420 214 LVKAGPVHDI 223
Cdd:COG1117 231 LVEFGPTEQI 240
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-227 |
3.34e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 114.79 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQD----ALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCLDLIEK-DQGDIRFFEQPFK--------QV 71
Cdd:COG1135 2 IELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIR-CINLLERpTSGSVLVDGVDLTalserelrAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 72 RKQIAYVPQ-------RNdldwtfpihVLDTVLlgtYPkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQ 144
Cdd:COG1135 81 RRKIGMIFQhfnllssRT---------VAENVA---LP-LEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 145 RVFLARALAQNAQ-LFClDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLS--K--ADDYfshLVLLNKKLVKAG 218
Cdd:COG1135 148 RVGIARALANNPKvLLC-DEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDvvRriCDRV---AVLENGRIVEQG 223
|
250
....*....|
gi 518573420 219 PVHDI-LRPE 227
Cdd:COG1135 224 PVLDVfANPQ 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-238 |
4.52e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.25 E-value: 4.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 10 LYVSY-HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFK-------QVRKQIAYVPQR 81
Cdd:PRK13639 7 LKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkksllEVRKTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 NDlDWTFPIHVLDTVLLGTYpKLGLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCL 161
Cdd:PRK13639 87 PD-DQLFAPTVEEDVAFGPL-NLGL---SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 162 DEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQAYETQLP 238
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDgKIIKEGTPKEVFSDIETIRKANLRLP 239
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-239 |
4.78e-30 |
|
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: 112.91 E-value: 4.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 7 IDRLYVSYHGQD--ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFF------EQPFKQVRKQIAYV 78
Cdd:TIGR04520 3 VENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDgldtldEENLWEIRKKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRNDLDWTFPIhVLDTVLLGtyPK-LGLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQ 157
Cdd:TIGR04520 83 FQNPDNQFVGAT-VEDDVAFG--LEnLGV---PREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 158 LFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLS---KADDyfshLVLLNK-KLVKAGPVHDILRPEVMLQA 232
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEeavLADR----VIVMNKgKIVAEGTPREIFSQVELLKE 232
|
....*..
gi 518573420 233 YETQLPF 239
Cdd:TIGR04520 233 IGLDVPF 239
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-209 |
5.76e-30 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 112.13 E-value: 5.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRffeqpfKQVRKQIAYVPQ 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RNDLDWTFPIHVLDTVLLgtypklglikRP--KKEDRAYAyhcLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQL 158
Cdd:PRK09544 75 KLYLDTTLPLTVNRFLRL----------RPgtKKEDILPA---LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518573420 159 FCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLskaddyfsHLVL 209
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL--------HLVM 185
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-224 |
1.45e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.95 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 12 VSYH-GQ-DALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCLDLIEK-DQGDIRFFEQPFK-------QVRKQIAYVPQR 81
Cdd:PRK09493 7 VSKHfGPtQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLR-CINKLEEiTSGDLIVDGLKVNdpkvderLIRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 NDLdwtFP-IHVLDTVLLGTYPKLGLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFC 160
Cdd:PRK09493 86 FYL---FPhLTALENVMFGPLRVRGA---SKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 161 LDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDIL 224
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKgRIAEDGDPQVLI 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-198 |
4.67e-29 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 108.83 E-value: 4.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQD--ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ-----VRKQIAYVPQRNDLd 85
Cdd:cd03245 11 SYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQldpadLRRNIGYVPQDVTL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 86 wtFPIHVLDTVLLGtypklglikRPKKEDRAyAYHCLEKVGMQDFAKR-------QIGE----LSGGQQQRVFLARALAQ 154
Cdd:cd03245 90 --FYGTLRDNITLG---------APLADDER-ILRAAELAGVTDFVNKhpngldlQIGErgrgLSGGQRQAVALARALLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518573420 155 NAQLFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLS 198
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS 200
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-212 |
4.71e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 110.10 E-value: 4.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQ--------------------GD 60
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellgrtvqregrlaRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 61 IRffeqpfkQVRKQIAYVPQRNDLdwTFPIHVLDTVLLGTYPKLGL----IKRPKKEDRAYAYHCLEKVGMQDFAKRQIG 136
Cdd:PRK09984 81 IR-------KSRANTGYIFQQFNL--VNRLSVLENVLIGALGSTPFwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 137 ELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLLNK 212
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQ 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-228 |
5.14e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.96 E-value: 5.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCLD-LIEKDQGDIRFFEQPF-----KQVRKQ 74
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMK-ILSgVYQPDSGEILLDGEPVrfrspRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 75 -IAYVPQRNDL--DWTfpihVLDTVLLGTYP-KLGLIKRPKKEDRAYAYhcLEKVGMQDFAKRQIGELSGGQQQRVFLAR 150
Cdd:COG1129 80 gIAIIHQELNLvpNLS----VAENIFLGREPrRGGLIDWRAMRRRAREL--LARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 151 ALAQNAQLFCLDEPfvgidMAS----E-ETMIRILKELRDEGKTILVVHHDLSK----ADDYfshLVLLNKKLVKAGPVH 221
Cdd:COG1129 154 ALSRDARVLILDEP-----TASlterEvERLFRIIRRLKAQGVAIIYISHRLDEvfeiADRV---TVLRDGRLVGTGPVA 225
|
....*..
gi 518573420 222 DILRPEV 228
Cdd:COG1129 226 ELTEDEL 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-233 |
5.47e-29 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 110.30 E-value: 5.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACL-DLIEKD-------QGDIRFFEQPFKQVRKQI- 75
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 76 ----AYVPQRNDLdwTFPIHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARA 151
Cdd:PRK13547 82 arlrAVLPQAAQP--AFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 152 LAQ---------NAQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLL-NKKLVKAGPV 220
Cdd:PRK13547 160 LAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLaDGAIVAHGAP 239
|
250
....*....|...
gi 518573420 221 HDILRPEVMLQAY 233
Cdd:PRK13547 240 ADVLTPAHIARCY 252
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-224 |
7.61e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 109.29 E-value: 7.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCLDLIEK------------------DQGDIRFFEQ 66
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLR-CINFLEKpsegsivvngqtinlvrdKDGQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 67 -PFKQVRKQIAYVPQRNDLdWTFpIHVLDTVLLGTYPKLGLIKRPKKEdRAYAYhcLEKVGMQDFAKRQI-GELSGGQQQ 144
Cdd:PRK10619 85 nQLRLLRTRLTMVFQHFNL-WSH-MTVLENVMEAPIQVLGLSKQEARE-RAVKY--LAKVGIDERAQGKYpVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 145 RVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNKKLV-KAGPVHDI 223
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIeEEGAPEQL 239
|
.
gi 518573420 224 L 224
Cdd:PRK10619 240 F 240
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-219 |
5.33e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 107.14 E-value: 5.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSyALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCLDLIEK-DQGDIRFFE------QPF----- 68
Cdd:PRK11264 1 MS-AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLR-CINLLEQpEAGTIRVGDitidtaRSLsqqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 69 --KQVRKQIAYVPQRNDLdwtFPiH--VLDTVLLGtypKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQ 144
Cdd:PRK11264 79 liRQLRQHVGFVFQNFNL---FP-HrtVLENIIEG---PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518573420 145 RVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGP 219
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQgRIVEQGP 227
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-200 |
5.65e-28 |
|
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: 107.00 E-value: 5.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCL----DLIE--KDQGDIRFFEQPF-------KQ 70
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLR-SLnrmnDLVPgvRIEGKVLFDGQDIydkkidvVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 71 VRKQIAYVPQRNDLdwtFPIHVLDTVLLGtyPKLGLIKrPKKEDRAYAYHCLEKVGMQDFAKRQIGE----LSGGQQQRV 146
Cdd:TIGR00972 80 LRRRVGMVFQKPNP---FPMSIYDNIAYG--PRLHGIK-DKKELDEIVEESLKKAALWDEVKDRLHDsalgLSGGQQQRL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518573420 147 FLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEgKTILVVHHDLSKA 200
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQA 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-212 |
6.87e-28 |
|
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: 105.91 E-value: 6.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGD-----IRFFEQPFkQVRKQIAYVPQRNDL-DWTfpihv 92
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatvdgFDVVKEPA-EARRRLGFVSDSTGLyDRL----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 93 ldTVL--LGTYPKLGLIKRPKKEDRayayhcLEKV----GMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFV 166
Cdd:cd03266 94 --TARenLEYFAGLYGLKGDELTAR------LEELadrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518573420 167 GIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK 212
Cdd:cd03266 166 GLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHR 211
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
16-203 |
9.22e-28 |
|
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: 105.41 E-value: 9.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 16 GQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFK--------QVRKQIAYVPQRNDL--D 85
Cdd:TIGR02673 14 GVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNrlrgrqlpLLRRRIGVVFQDFRLlpD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 86 WTfpihVLDTVLLgtypKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPF 165
Cdd:TIGR02673 94 RT----VYENVAL----PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPT 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 518573420 166 VGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDY 203
Cdd:TIGR02673 166 GNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRV 203
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-212 |
1.71e-27 |
|
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: 104.17 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLK--ACLDLIEKDQGDIRFFEQPF--KQVRKQIAYVPQrndldwtfpihvlDT 95
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNalAGRRTGLGVSGEVLINGRPLdkRSFRKIIGYVPQ-------------DD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 96 VLLGTypklgLIKRpkkEDRAYAYHClekvgmqdfakRQIgelSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEET 175
Cdd:cd03213 92 ILHPT-----LTVR---ETLMFAAKL-----------RGL---SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 518573420 176 MIRILKELRDEGKTILVVHHDLSkADDY--FSHLVLLNK 212
Cdd:cd03213 150 VMSLLRRLADTGRTIICSIHQPS-SEIFelFDKLLLLSQ 187
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-240 |
1.93e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.84 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQD--ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFF-----EQPFKQVRKQIA 76
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDgitisKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 77 YVPQRNDLDWtFPIHVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNA 156
Cdd:PRK13632 87 IIFQNPDNQF-IGATVEDDIAFG----LENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 157 QLFCLDEPFVGIDMASEETMIRILKELRDEG-KTILVVHHDLSKA--DDYFshLVLLNKKLVKAGPVHDILRPEVMLQAY 233
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAilADKV--IVFSEGKLIAQGKPKEILNNKEILEKA 239
|
....*..
gi 518573420 234 ETQLPFL 240
Cdd:PRK13632 240 KIDSPFI 246
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-197 |
2.48e-27 |
|
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: 109.37 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHG-QDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQG-----DIRFFEQPFKQVRKQIAYV 78
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGevtldGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRndldwtfpIHVLDTVLLGTYpklgLIKRPKKEDrAYAYHCLEKVGMQDFAKR-------QIGE----LSGGQQQRVF 147
Cdd:TIGR02868 415 AQD--------AHLFDTTVRENL----RLARPDATD-EELWAALERVGLADWLRAlpdgldtVLGEggarLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518573420 148 LARALAQNAQLFCLDEPFVGIDMASEETMIRILKELrDEGKTILVVHHDL 197
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITHHL 530
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-230 |
4.02e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 105.94 E-value: 4.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFF-------EQP----------------------FK 69
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkKKTkekekvleklviqktrfkkikkIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 70 QVRKQIAYVPQRNDLDwTFPIHVLDTVLLGTYpKLGLIKRPKKEdRAYAYhcLEKVGM-QDFAKRQIGELSGGQQQRVFL 148
Cdd:PRK13651 102 EIRRRVGVVFQFAEYQ-LFEQTIEKDIIFGPV-SMGVSKEEAKK-RAAKY--IELVGLdESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 149 ARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSH-LVLLNKKLVKAGPVHDILRPE 227
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRtIFFKDGKIIKDGDTYDILSDN 256
|
...
gi 518573420 228 VML 230
Cdd:PRK13651 257 KFL 259
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-195 |
7.20e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 107.69 E-value: 7.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP--FKQVRKQIA-- 76
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrFASTTAALAag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 77 ---------YVPQrndldwtfpIHVLDTVLLGTYP-KLGLIKRpkKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRV 146
Cdd:PRK11288 81 vaiiyqelhLVPE---------MTVAENLYLGQLPhKGGIVNR--RLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518573420 147 FLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHH 195
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-203 |
9.09e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.96 E-value: 9.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCLDLIEKDQGDIR------FFEQP-------FKQ 70
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRvegrveFFNQNiyerrvnLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 71 VRKQIAYVPQRNDLdwtFPIHVLDTVLLGtypkLGLIK-RPKKEDRAYAYHCLEKVGMQDFAKRQIG----ELSGGQQQR 145
Cdd:PRK14258 86 LRRQVSMVHPKPNL---FPMSVYDNVAYG----VKIVGwRPKLEIDDIVESALKDADLWDEIKHKIHksalDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518573420 146 VFLARALAQNAQLFCLDEPFVGIDMASE---ETMIRILKeLRDEGKTILVVH--HDLSKADDY 203
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLR-LRSELTMVIVSHnlHQVSRLSDF 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-241 |
1.01e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 104.89 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYA-LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF----KQVRKQI 75
Cdd:PRK13537 3 MSVApIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpsraRHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 76 AYVPQRNDLDWTFPIHVlDTVLLGTYpkLGLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQN 155
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRE-NLLVFGRY--FGL---SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 156 AQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHL-VLLNKKLVKAGPVHDILRPEV---MLQ 231
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLcVIEEGRKIAEGAPHALIESEIgcdVIE 236
|
250
....*....|
gi 518573420 232 AYETQLPFLK 241
Cdd:PRK13537 237 IYGPDPVALR 246
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-239 |
1.37e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.68 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP-----FKQVRKQIAYVPQRNDLDWTFPIHVL 93
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnFEKLRKHIGIVFQNPDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 94 DTVLlgtypklGLIKR--PKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMA 171
Cdd:PRK13648 104 DVAF-------GLENHavPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 172 SEETMIRILKELRDEGK-TILVVHHDLSKADDYfSHLVLLNKKLV-KAGPVHDILRPEVMLQAYETQLPF 239
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNiTIISITHDLSEAMEA-DHVIVMNKGTVyKEGTPTEIFDHAEELTRIGLDLPF 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-224 |
2.86e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 102.30 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIE-----KDQGDIRF-----FEQPFKQVRKQ 74
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLdgqdiFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 75 IAYVPQRNDldwtfPI---HVLDTVLLGtyPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQI----GELSGGQQQRVF 147
Cdd:PRK14247 84 VQMVFQIPN-----PIpnlSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapaGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518573420 148 LARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHH--DLSKADDYFShlVLLNKKLVKAGPVHDIL 224
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFpqQAARISDYVA--FLYKGQIVEWGPTREVF 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-218 |
4.51e-26 |
|
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: 101.29 E-value: 4.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 7 IDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFF-----EQPfKQVRKQIAYVPQr 81
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghdvvREP-REVRRRIGIVFQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 nDLdwtfpihVLDTVLLGT---YPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQL 158
Cdd:cd03265 81 -DL-------SVDDELTGWenlYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518573420 159 FCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAG 218
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHgRIIAEG 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-233 |
4.65e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.89 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF------KQVRKQIAYV 78
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplhARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRNDLdwTFPIHVLDTvLLGTYPKLGLIKRPKKEDRAYayHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQL 158
Cdd:PRK10895 84 PQEASI--FRRLSVYDN-LMAVLQIRDDLSAEQREDRAN--ELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518573420 159 FCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQAY 233
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQgHLIAHGTPTEILQDEHVKRVY 234
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-212 |
5.97e-26 |
|
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: 103.58 E-value: 5.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRffeqpfkQVRKQIAYV-P 79
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIY-------QGGRDITRLpP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 80 QRNDLDWTFPIHVL-------DTVLLGTYPKlgliKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARAL 152
Cdd:TIGR03265 74 QKRDYGIVFQSYALfpnltvaDNIAYGLKNR----GMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 153 AQNAQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHD----LSKADdyfsHLVLLNK 212
Cdd:TIGR03265 150 ATSPGLLLLDEPLSALDARVREHLRTEIRQLqRRLGVTTIMVTHDqeeaLSMAD----RIVVMNH 210
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-197 |
6.47e-26 |
|
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: 101.25 E-value: 6.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFF-EQPFKQ---VRKQIAYV-PQRNDLDWTFPihVL 93
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAgLVPWKRrkkFLRRIGVVfGQKTQLWWDLP--VI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 94 DTVLLgtypkLGLIKR-PKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMAS 172
Cdd:cd03267 114 DSFYL-----LAAIYDlPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180
....*....|....*....|....*.
gi 518573420 173 EETMIRILKEL-RDEGKTILVVHHDL 197
Cdd:cd03267 189 QENIRNFLKEYnRERGTTVLLTSHYM 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-223 |
6.75e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.76 E-value: 6.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV---RKQIAYVPQR 81
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVppyQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 NDLdwtFP-IHVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFC 160
Cdd:PRK11607 100 YAL---FPhMTVEQNIAFG----LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 161 LDEPFVGIDMASEETM-IRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDI 223
Cdd:PRK11607 173 LDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRgKFVQIGEPEEI 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-197 |
9.16e-26 |
|
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: 98.65 E-value: 9.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKqvrkqiayvpqrndl 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 85 dwtfpihvldtvllgtypklglIKRPKKEDRAyayhcleKVGMqdfakrqIGELSGGQQQRVFLARALAQNAQLFCLDEP 164
Cdd:cd03216 66 ----------------------FASPRDARRA-------GIAM-------VYQLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190
....*....|....*....|....*....|...
gi 518573420 165 FVGIDMASEETMIRILKELRDEGKTILVVHHDL 197
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRL 142
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-195 |
1.01e-25 |
|
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: 98.83 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDA--LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV-----RKQIAY 77
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdpnelGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRndldwtfpihvlDTVLLGTypklglikrpkkedrayayhclekvgmqdfakrqIGE--LSGGQQQRVFLARALAQN 155
Cdd:cd03246 81 LPQD------------DELFSGS----------------------------------IAEniLSGGQRQRLGLARALYGN 114
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518573420 156 AQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHH 195
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAH 154
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-196 |
1.17e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 100.58 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLlkacLDLI----EKDQGDIRFFEQPFKQV----- 71
Cdd:COG4674 7 HGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTL----MDVItgktRPDSGSVLFGGTDLTGLdehei 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 72 ------RK-QIAYVpqrndldwtFPIH-VLDTVLLGTYPKLG----LIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELS 139
Cdd:COG4674 83 arlgigRKfQKPTV---------FEELtVFENLELALKGDRGvfasLFARLTAEERDRIEEVLETIGLTDKADRLAGLLS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518573420 140 GGQQQRVFLARALAQNAQLFCLDEPFVGidMASEETM--IRILKELRdEGKTILVVHHD 196
Cdd:COG4674 154 HGQKQWLEIGMLLAQDPKLLLLDEPVAG--MTDAETErtAELLKSLA-GKHSVVVVEHD 209
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-224 |
1.21e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 101.04 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 17 QDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV-RKQIAYVpqRNDLDWTF-----PI 90
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdRKQRRAF--RRDVQLVFqdspsAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 91 HVLDTV--LLGTyPKLGLIKRPKKEDRAYAYHCLEKVGMQ-DFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVG 167
Cdd:TIGR02769 102 NPRMTVrqIIGE-PLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518573420 168 IDMASEETMIRILKELRDEGKT-ILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDIL 224
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKgQIVEECDVAQLL 239
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-218 |
1.94e-25 |
|
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: 98.15 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQD--ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF----KQVRKQIAYV 78
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVsdleKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRndldwtfpIHVLDTVLLgtypklglikrpkkedrayayhclEKVGMQdfakrqigeLSGGQQQRVFLARALAQNAQL 158
Cdd:cd03247 81 NQR--------PYLFDTTLR------------------------NNLGRR---------FSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 159 FCLDEPFVGIDMASEETMIR-ILKELRDegKTILVVHHDLSKADDYFSHLVLLNKKLVKAG 218
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSlIFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-224 |
2.11e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.51 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIE------KDQGDIRFFEQPFKQV-----RK 73
Cdd:PRK14246 11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIdaiklRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 74 QIAYVPQRNDldwTFP-IHVLDTVllgTYPKLGLIKRPKKEDRAYAYHCLEKVGM----QDFAKRQIGELSGGQQQRVFL 148
Cdd:PRK14246 91 EVGMVFQQPN---PFPhLSIYDNI---AYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 149 ARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHH--DLSKADDYFShlVLLNKKLVKAGPVHDIL 224
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNpqQVARVADYVA--FLYNGELVEWGSSNEIF 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-218 |
2.40e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 99.70 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKAcLDLIE-KDQGDIRFFEQPF-----------KQVRKQIAYVPQ 80
Cdd:COG4161 11 FYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRV-LNLLEtPDSGQLNIAGHQFdfsqkpsekaiRLLRQKVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RNDLdWtfP-IHVLDTVLLGTYPKLGLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLF 159
Cdd:COG4161 90 QYNL-W--PhLTVMENLIEAPCKVLGL---SKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAG 218
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKgRIIEQG 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-211 |
2.42e-25 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 98.70 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIrffeqpfkQVRKQIAYVPQrndLDWTFPIHVLDTVLL 98
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV--------SVPGSIAYVSQ---EPWIQNGTIRENILF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 99 GtypklglikRPKKEDRayaYH------CLEKvgmqDFA------KRQIGE----LSGGQQQRVFLARALAQNAQLFCLD 162
Cdd:cd03250 89 G---------KPFDEER---YEkvikacALEP----DLEilpdgdLTEIGEkginLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518573420 163 EPFVGIDMASEETMIR--ILKELRDeGKT-ILVVH--HDLSKADdyfsHLVLLN 211
Cdd:cd03250 153 DPLSAVDAHVGRHIFEncILGLLLN-NKTrILVTHqlQLLPHAD----QIVVLD 201
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-224 |
3.53e-25 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 98.84 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SY-HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV-----RKQIAYVPQRndlDW 86
Cdd:cd03254 11 SYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrkslRSMIGVVLQD---TF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 87 TFPIHVLDTVLLGTypklgliKRPKKEDRAYAyhcLEKVGMQDFAKR-------QIGE----LSGGQQQRVFLARALAQN 155
Cdd:cd03254 88 LFSGTIMENIRLGR-------PNATDEEVIEA---AKEAGAHDFIMKlpngydtVLGEnggnLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518573420 156 AQLFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPvHDIL 224
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGT-HDEL 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-234 |
3.61e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.45 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF----KQVRKQIAYVPQRNDLDWTF 88
Cdd:PRK13536 50 SYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVparaRLARARIGVVPQFDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 89 PIHVlDTVLLGTYpkLGLIKRpkkEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGI 168
Cdd:PRK13536 130 TVRE-NLLVFGRY--FGMSTR---EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 169 DMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK--KLVKAGPvHDILRPEVMLQAYE 234
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAgrKIAEGRP-HALIDEHIGCQVIE 270
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-225 |
4.01e-25 |
|
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: 100.90 E-value: 4.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQD----ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEK---DQGDIRFFEQP--------FK 69
Cdd:COG0444 2 LEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDllklsekeLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 70 QVR-KQIAYVPQrnD----LDWTFPI--HVLDTVLLGTypklgliKRPKKEDRAYAYHCLEKVGMQD---FAKRQIGELS 139
Cdd:COG0444 82 KIRgREIQMIFQ--DpmtsLNPVMTVgdQIAEPLRIHG-------GLSKAEARERAIELLERVGLPDperRLDRYPHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 140 GGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKAdDYFSH--LVLLNKKLVK 216
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVV-AEIADrvAVMYAGRIVE 231
|
....*....
gi 518573420 217 AGPVHDILR 225
Cdd:COG0444 232 EGPVEELFE 240
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-238 |
4.33e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.19 E-value: 4.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRF---------FEQPFKQVRKQIAYVPQRNDlDWTFP 89
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstsKQKEIKPVRKKVGVVFQFPE-SQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 90 IHVLDTVLLGTyPKLGLikrPKKEDRAYAYHCLEKVGM-QDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGI 168
Cdd:PRK13643 100 ETVLKDVAFGP-QNFGI---PKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 169 DMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQAYETQLP 238
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKgHIISCGTPSDVFQEVDFLKAHELGVP 246
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-218 |
4.35e-25 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 98.33 E-value: 4.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDAleNVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV---RKQIAYVPQR 81
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppaDRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 NDLdwtFP-IHVLDTVLLGTYPKLGLikrpKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFC 160
Cdd:cd03298 79 NNL---FAhLTVEQNVGLGLSPGLKL----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 161 LDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLL-NKKLVKAG 218
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLdNGRIAAQG 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-218 |
5.33e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.00 E-value: 5.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 12 VSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIeKDQGDIR-----FFEQPFKQVRKQIAYVPQRNDLdw 86
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKingieLRELDPESWRKHLSWVGQNPQL-- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 87 tFPIHVLDTVLLGtypklglikRPKKEDRAyAYHCLEKVGMQDFAKRQ-------IGE----LSGGQQQRVFLARALAQN 155
Cdd:PRK11174 435 -PHGTLRDNVLLG---------NPDASDEQ-LQQALENAWVSEFLPLLpqgldtpIGDqaagLSVGQAQRLALARALLQP 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518573420 156 AQLFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAG 218
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-200 |
7.18e-25 |
|
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: 97.75 E-value: 7.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 22 NVSLSIQEGTmTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQ---------IAYVPQRNDLdwtFPiHv 92
Cdd:cd03297 16 KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlppqqrkIGLVFQQYAL---FP-H- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 93 ldtvlLGTYPKL--GLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDM 170
Cdd:cd03297 90 -----LNVRENLafGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190
....*....|....*....|....*....|.
gi 518573420 171 ASEETMIRILKELRDE-GKTILVVHHDLSKA 200
Cdd:cd03297 165 ALRLQLLPELKQIKKNlNIPVIFVTHDLSEA 195
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-209 |
8.91e-25 |
|
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: 97.48 E-value: 8.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 15 HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVR-KQIAYVPQR-----NDLDWTF 88
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgRAIPYLRRKigvvfQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 89 PIHVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGI 168
Cdd:cd03292 92 DRNVYENVAFA----LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518573420 169 DMASEETMIRILKELRDEGKTILVVHHDLSKADDYfSHLVL 209
Cdd:cd03292 168 DPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTT-RHRVI 207
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-195 |
8.94e-25 |
|
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: 98.00 E-value: 8.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQ------PFKQVRKQIAYV 78
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRNDL--DWTfpihVLDTVLLgtypKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNA 156
Cdd:cd03218 81 PQEASIfrKLT----VEENILA----VLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 518573420 157 QLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHH 195
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-236 |
9.17e-25 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 98.47 E-value: 9.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLkACLDLIEKDQGDIRFFEQPFKQVR-----KQIAYVPQRNDLdwTFPIHVLD 94
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLL-ARMAGLLPGSGSIQFAGQPLEAWSaaelaRHRAYLSQQQTP--PFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 95 TVLLGTYPKlglikRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQ-------NAQLFCLDEPFVG 167
Cdd:PRK03695 89 YLTLHQPDK-----TRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 168 IDMASEETMIRILKELRDEGKTILVVHHDLSKADDYfSHLVLL--NKKLVKAGPVHDILRPEVMLQAYETQ 236
Cdd:PRK03695 164 LDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRH-ADRVWLlkQGKLLASGRRDEVLTPENLAQVFGVN 233
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-227 |
9.27e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.21 E-value: 9.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 2 SYALTIDRLYVSYHGQD--ALENVSLSIQEGTMTGIIGPNGAGKSTLLKacldLI----EKDQGDIRFFEQPFK-----Q 70
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ----LLtrawDPQQGEILLNGQPIAdyseaA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 71 VRKQIAYVPQRndldwtfpIHVLDTVL---LgtypklgLIKRPKKEDRAYAyHCLEKVGMQDFAKRQ------IGE---- 137
Cdd:PRK11160 412 LRQAISVVSQR--------VHLFSATLrdnL-------LLAAPNASDEALI-EVLQQVGLEKLLEDDkglnawLGEggrq 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 138 LSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLsKADDYFSHLVLL-NKKLVK 216
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRL-TGLEQFDRICVMdNGQIIE 553
|
250
....*....|.
gi 518573420 217 AGPVHDILRPE 227
Cdd:PRK11160 554 QGTHQELLAQQ 564
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-212 |
1.09e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.16 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSyaLTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVR---KQIAY 77
Cdd:PRK10851 1 MS--IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHardRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRNDLdwtFP-IHVLDTVLLGtypkLGLIKRPKKEDRAY----AYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARAL 152
Cdd:PRK10851 79 VFQHYAL---FRhMTVFDNIAFG----LTVLPRRERPNAAAikakVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 153 AQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGK-TILVVHHDLSKADDYFSHLVLLNK 212
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQ 212
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
1.19e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 98.38 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIE-----KDQGDIRFFEQPFK------ 69
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYspdvdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 70 -QVRKQIAYVPQRNDldwTFP-IHVLDTVLLGTypKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQI----GELSGGQQ 143
Cdd:PRK14267 81 iEVRREVGMVFQYPN---PFPhLTIYDNVAIGV--KLNGLVKSKKELDERVEWALKKAALWDEVKDRLndypSNLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 144 QRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHH--DLSKADDYFSHLVLlnKKLVKAGPVH 221
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpaQAARVSDYVAFLYL--GKLIEVGPTR 233
|
....*..
gi 518573420 222 DILR-PE 227
Cdd:PRK14267 234 KVFEnPE 240
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-196 |
1.59e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 7 IDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIrffeqpFKQVRKQIAYVPQRNDLDW 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV------SIPKGLRIGYLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 87 TFPihVLDTVLLGTYPKLGLIKR----------PKKEDRAYA--YHCLEKVG-----------------MQDFAKRQIGE 137
Cdd:COG0488 75 DLT--VLDTVLDGDAELRALEAEleeleaklaePDEDLERLAelQEEFEALGgweaearaeeilsglgfPEEDLDRPVSE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 138 LSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASeetmIRILKE-LRDEGKTILVVHHD 196
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEfLKNYPGTVLVVSHD 208
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-238 |
1.63e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.15 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIR---FFEQP------------------FKQVRKQIAY 77
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdIYIGDkknnhelitnpyskkiknFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQrndldwtFPIHVL--DTV----LLGTYPklglIKRPKKEDRAYAYHCLEKVGMQD-FAKRQIGELSGGQQQRVFLAR 150
Cdd:PRK13631 121 VFQ-------FPEYQLfkDTIekdiMFGPVA----LGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 151 ALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVM 229
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKgKILKTGTPYEIFTDQHI 269
|
....*....
gi 518573420 230 LQAYETQLP 238
Cdd:PRK13631 270 INSTSIQVP 278
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-200 |
1.73e-24 |
|
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: 96.94 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVR---KQIAYVPQR 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkdRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 NDLdwtFP-IHVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFC 160
Cdd:cd03301 81 YAL---YPhMTVYDNIAFG----LKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518573420 161 LDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKA 200
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEA 194
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-225 |
2.45e-24 |
|
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: 100.98 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDA--LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQ-----IAY 77
Cdd:COG4618 331 LSVENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREelgrhIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRNDLdwtFPihvldtvllGTypklglIK----RPKKEDRAYAYHCLEKVGMQDFAKR-------QIGE----LSGGQ 142
Cdd:COG4618 411 LPQDVEL---FD---------GT------IAeniaRFGDADPEKVVAAAKLAGVHEMILRlpdgydtRIGEggarLSGGQ 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 143 QQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHD---LSKADDyfsHLVLLNKKLVKAGP 219
Cdd:COG4618 473 RQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRpslLAAVDK---LLVLRDGRVQAFGP 549
|
....*.
gi 518573420 220 VHDILR 225
Cdd:COG4618 550 RDEVLA 555
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-198 |
2.47e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 98.62 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFF-EQPFKQ---VRKQIAYV-PQRNDLDWTFPihVL 93
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgYVPFKRrkeFARRIGVVfGQRSQLWWDLP--AI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 94 DTVLLgtypkLGLIKR-PKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMAS 172
Cdd:COG4586 115 DSFRL-----LKAIYRiPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180
....*....|....*....|....*..
gi 518573420 173 EETMIRILKEL-RDEGKTILVVHHDLS 198
Cdd:COG4586 190 KEAIREFLKEYnRERGTTILLTSHDMD 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-211 |
3.35e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 96.01 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKA---CLDLIEKDQGDIRFFEQPFKQV---RKQIAYV 78
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAiagTLSPAFSASGEVLLNGRRLTALpaeQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQrnDlDWTFPiH--VLDTVLLGTYPKLGlikrpKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNA 156
Cdd:COG4136 82 FQ--D-DLLFP-HlsVGENLAFALPPTIG-----RAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518573420 157 QLFCLDEPFVGIDMASEETMIR-ILKELRDEGKTILVVHHDLSKADDYFSHLVLLN 211
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-201 |
3.44e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.42 E-value: 3.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 18 DALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIAYVPQRNDLDWTFPIHVL--D- 94
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLlpDf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 95 TVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEE 174
Cdd:PRK11629 103 TALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180
....*....|....*....|....*...
gi 518573420 175 TMIRILKEL-RDEGKTILVVHHDLSKAD 201
Cdd:PRK11629 183 SIFQLLGELnRLQGTAFLVVTHDLQLAK 210
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-216 |
3.50e-24 |
|
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: 96.08 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 24 SLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV---RKQIAYVPQRNDLdwtFP-IHVLDTVLLG 99
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLapyQRPVSMLFQENNL---FAhLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 100 TYP--KLGLIKRPKKEDRAyayhclEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMI 177
Cdd:TIGR01277 95 LHPglKLNAEQQEKVVDAA------QQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518573420 178 RILKELRDEGK-TILVVHHDLSKADDYFSHLVLLNKKLVK 216
Cdd:TIGR01277 169 ALVKQLCSERQrTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-225 |
3.82e-24 |
|
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: 98.63 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 22 NVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF----KQV-----RKQIAYVPQRNDLdwtFPiH- 91
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsaRGIflpphRRRIGYVFQEARL---FP-Hl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 92 -VLDTVLLGtypklglIKRPKKEDRAYAY-HCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGID 169
Cdd:COG4148 93 sVRGNLLYG-------RKRAPRAERRISFdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518573420 170 MASEETMIRILKELRDEGKT-ILVVHHDLSK----ADdyfsHLVLLNK-KLVKAGPVHDILR 225
Cdd:COG4148 166 LARKAEILPYLERLRDELDIpILYVSHSLDEvarlAD----HVVLLEQgRVVASGPLAEVLS 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-196 |
7.24e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.80 E-value: 7.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 7 IDRLYVSYHGQ-DALENVSLSIQEGTMTGIIGPNGAGKSTLLK--ACLDliEKDQGDIRFFEQPFKQV---------RKQ 74
Cdd:PRK10535 10 IRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNilGCLD--KPTSGTYRVAGQDVATLdadalaqlrREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 75 IAYVPQRNDL--DWTFPIHV-LDTVLLGTypklglikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARA 151
Cdd:PRK10535 88 FGFIFQRYHLlsHLTAAQNVeVPAVYAGL---------ERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518573420 152 LAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHD 196
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-212 |
9.96e-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: 95.03 E-value: 9.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 18 DALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKD---QGDIRFFEQPFK--QVRKQIAYVPQRNDL-------- 84
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKpdQFQKCVAYVRQDDILlpgltvre 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 85 DWTFPIHvldtvLLGTYPKLGliKRPKKEDrayayhclEKVGMQDFAKRQIGE-----LSGGQQQRVFLARALAQNAQLF 159
Cdd:cd03234 101 TLTYTAI-----LRLPRKSSD--AIRKKRV--------EDVLLRDLALTRIGGnlvkgISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRDEGKTILV-VHHDLSKADDYFSHLVLLNK 212
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSS 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-197 |
1.36e-23 |
|
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: 93.65 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLyvsyHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRF------FEQPFKQVRKQIAY 77
Cdd:cd03215 4 VLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdgkpvtRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPqrndldwtfpihvldtvllgtypklglikrpkkEDRAyayhcleKVGMqdFAKRQIGE-------LSGGQQQRVFLAR 150
Cdd:cd03215 80 VP---------------------------------EDRK-------REGL--VLDLSVAEnialsslLSGGNQQKVVLAR 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518573420 151 ALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDL 197
Cdd:cd03215 118 WLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSEL 164
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-195 |
2.45e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 94.33 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP------FKQVRKQIAYV 78
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlpmHKRARLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQ-----RNdldwtfpIHVLDTVLLgtypKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALA 153
Cdd:COG1137 84 PQeasifRK-------LTVEDNILA----VLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518573420 154 QNAQLFCLDEPFVGID-MASEEtmIR-ILKELRDEGKTILVVHH 195
Cdd:COG1137 153 TNPKFILLDEPFAGVDpIAVAD--IQkIIRHLKERGIGVLITDH 194
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-239 |
2.80e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.25 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGD--------IRFFEQPFKQVRKQIAYVPQRNDLDWtfpi 90
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVWDIREKVGIVFQNPDNQF---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 91 hVLDTVllGTYPKLGLIKR--PKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGI 168
Cdd:PRK13640 98 -VGATV--GDDVAFGLENRavPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518573420 169 DMASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPVHDILRPEVMLQAYETQLPF 239
Cdd:PRK13640 175 DPAGKEQILKLIRKLkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGLDIPF 246
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-216 |
3.48e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.90 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFF---------EQPFKQVRKQIAYVPQ--RNDLdwtF 88
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhitpetgNKNLKKLRKKVSLVFQfpEAQL---F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 89 PIHVLDTVLLGtyPK-LGLikrPKKEDRAYAYHCLEKVGM-QDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFV 166
Cdd:PRK13641 100 ENTVLKDVEFG--PKnFGF---SEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518573420 167 GIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSH-LVLLNKKLVK 216
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDvLVLEHGKLIK 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-196 |
5.55e-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: 5.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFfeqpfkQVRKQIAYVPQRN-- 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL------GETVKIGYFDQHQee 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 83 -DLDWTfpihVLDTVLLGtypklglikRPKKED---RAYayhclekvgMQDF------AKRQIGELSGGQQQRVFLARAL 152
Cdd:COG0488 390 lDPDKT----VLDELRDG---------APGGTEqevRGY---------LGRFlfsgddAFKPVGVLSGGEKARLALAKLL 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518573420 153 AQNAQLFCLDEPFVGIDMASeetmIRILKE-LRD-EGkTILVVHHD 196
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIET----LEALEEaLDDfPG-TVLLVSHD 488
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-225 |
6.20e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.98 E-value: 6.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 17 QDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIAYVPQRnDLDWTF-------- 88
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRR-DIQMVFqdsisavn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 89 PIHVLDTVLlgTYPKLGLIKRPKKEDRAYAYHCLEKVGMQD-FAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVG 167
Cdd:PRK10419 104 PRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 168 IDMASEETMIRILKELRDEGKT-ILVVHHDLSKAdDYFSHLVLL--NKKLVKAGPVHDILR 225
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTaCLFITHDLRLV-ERFCQRVMVmdNGQIVETQPVGDKLT 241
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-224 |
6.66e-23 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 96.71 E-value: 6.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 16 GQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ-----VRKQIAYVPQRNDLdwtFPI 90
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytlasLRRQVALVSQDVVL---FND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 91 HVLDTVLLGtypklglikRPKKEDRAYAYHCLEKVGMQDFAKR-------QIGE----LSGGQQQRVFLARALAQNAQLF 159
Cdd:TIGR02203 421 TIANNIAYG---------RTEQADRAEIERALAAAYAQDFVDKlplgldtPIGEngvlLSGGQRQRLAIARALLKDAPIL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLS---KADDYfshLVLLNKKLVKAGPVHDIL 224
Cdd:TIGR02203 492 ILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLStieKADRI---VVMDDGRIVERGTHNELL 555
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-209 |
8.98e-23 |
|
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: 92.17 E-value: 8.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVR----KQIAYVPQ 80
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdsiaRGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RN----------DLDWTFPIHVLDTVLlgtypklglikrpkkedrayayHCLEKVGMQDFAKRQIGELSGGQQQRVFLAR 150
Cdd:cd03231 81 APgikttlsvleNLRFWHADHSDEQVE----------------------EALARVGLNGFEDRPVAQLSAGQQRRVALAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 151 ALAQNAQLFCLDEPFVGIDMASEET-MIRILKELRDEGKTILVVHHDLSKADDYFSHLVL 209
Cdd:cd03231 139 LLLSGRPLWILDEPTTALDKAGVARfAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-200 |
1.15e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 93.20 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIAYVPQRNDL 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 85 -DWTfpiHVLDTVLLGTypklglikrpKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDE 163
Cdd:PRK11247 93 lPWK---KVIDNVGLGL----------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 518573420 164 PFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKA 200
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEA 197
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-224 |
1.16e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 96.35 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSY-HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV-----RKQIAYV 78
Cdd:TIGR01193 474 IVINDVSYSYgYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIdrhtlRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRndlDWTFPIHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKV--GMQDFAKRQIGELSGGQQQRVFLARALAQNA 156
Cdd:TIGR01193 554 PQE---PYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMplGYQTELSEEGSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 157 QLFCLDEPFVGIDMASEETMIRILKELRDegKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPvHDIL 224
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGS-HDEL 695
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
10-196 |
1.99e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 94.24 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 10 LYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV---RKQIAYVPQRNDLdw 86
Cdd:PRK09452 20 ISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaeNRHVNTVFQSYAL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 87 tFPiH--VLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEP 164
Cdd:PRK09452 98 -FP-HmtVFENVAFG----LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190
....*....|....*....|....*....|...
gi 518573420 165 FVGIDMASEETMIRILKEL-RDEGKTILVVHHD 196
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALqRKLGITFVFVTHD 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-197 |
2.34e-22 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 90.88 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVR----KQIAYVPQ 80
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRdephENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RN----------DLDWTFPIHvldtvllgtypklglikrpKKEDRAyAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLAR 150
Cdd:TIGR01189 81 LPglkpelsaleNLHFWAAIH-------------------GGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALAR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518573420 151 ALAQNAQLFCLDEPFVGIDMASEETMIRILKE-LRDEGKTILVVHHDL 197
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQDL 188
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-219 |
2.84e-22 |
|
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: 91.02 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 7 IDRLYVSY--HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV-----RKQIAYVP 79
Cdd:cd03244 5 FKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIglhdlRSRISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 80 Q---------RNDLDwtfPihvldtvlLGTYpklglikrpkkeDRAYAYHCLEKVGMQDFAKRQIGEL-----------S 139
Cdd:cd03244 85 QdpvlfsgtiRSNLD---P--------FGEY------------SDEELWQALERVGLKEFVESLPGGLdtvveeggenlS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 140 GGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKElRDEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGP 219
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-238 |
3.53e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.22 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 2 SYALTIDRLYVSY-HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFK-------QVRK 73
Cdd:PRK13636 3 DYILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkglmKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 74 QIAYVPQRNDlDWTFPIHVLDTVLLGTYpKLGLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALA 153
Cdd:PRK13636 83 SVGMVFQDPD-NQLFSASVYQDVSFGAV-NLKL---PEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 154 QNAQLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQ 231
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEgRVILQGNPKEVFAEKEMLR 237
|
....*..
gi 518573420 232 AYETQLP 238
Cdd:PRK13636 238 KVNLRLP 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-197 |
4.69e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 91.72 E-value: 4.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQD---ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDI-----RFFEQPFKQVR 72
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 73 KQIAYVPQRNDLDWTFPIhVLDTVLLGTYPKlGLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARAL 152
Cdd:PRK13650 81 HKIGMVFQNPDNQFVGAT-VEDDVAFGLENK-GI---PHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518573420 153 AQNAQLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDL 197
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDL 201
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-200 |
5.28e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.80 E-value: 5.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 24 SLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV---RKQIAYVPQRNDLdwtFP-IHVLDTVLLG 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppsRRPVSMLFQENNL---FShLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 100 TYPKLGLIKRPKKEDRAYAyhclEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRI 179
Cdd:PRK10771 96 LNPGLKLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180
....*....|....*....|..
gi 518573420 180 LKEL-RDEGKTILVVHHDLSKA 200
Cdd:PRK10771 172 VSQVcQERQLTLLMVSHSLEDA 193
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-193 |
6.59e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.93 E-value: 6.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 16 GQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ------VRKQIAYVP---QRNDLdw 86
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprdaIRAGIAYVPedrKGEGL-- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 87 tFPIH-VLDTVLLGTYPKL---GLIKRPKKEDRAYAYhclekvgMQDF------AKRQIGELSGGQQQRVFLARALAQNA 156
Cdd:COG1129 342 -VLDLsIRENITLASLDRLsrgGLLDRRRERALAEEY-------IKRLriktpsPEQPVGNLSGGNQQKVVLAKWLATDP 413
|
170 180 190
....*....|....*....|....*....|....*..
gi 518573420 157 QLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVV 193
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI 450
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-226 |
6.88e-22 |
|
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: 90.37 E-value: 6.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 8 DRLYVSYH-GQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV-----RKQIAYVPQr 81
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtldslRRAIGVVPQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 ndldwtfpihvlDTVLLGT-------YPKLGLIKRpKKEDRAYAYHCLEKV-GMQDFAKRQIGE----LSGGQQQRVFLA 149
Cdd:cd03253 83 ------------DTVLFNDtigynirYGRPDATDE-EVIEAAKAAQIHDKImRFPDGYDTIVGErglkLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 150 RALAQNAQLFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPVHDILRP 226
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-198 |
7.03e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.82 E-value: 7.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFK-QVRKQIAyvpqRND 83
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEgLPGHQIA----RMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 84 LDWTF-------PIHVLDTVLLGTYPKL------GLIKRP---KKEDRA--YAYHCLEKVGMQDFAKRQIGELSGGQQQR 145
Cdd:PRK11300 82 VVRTFqhvrlfrEMTVIENLLVAQHQQLktglfsGLLKTPafrRAESEAldRAATWLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518573420 146 VFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLS 198
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMK 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-224 |
7.26e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.31 E-value: 7.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEK-----DQGDIR------FFEQPFKQVR 72
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLlggrsiFNYRDVLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 73 KQIAYVPQRNDldwTFPIHVLDTVLLGTYPKLGLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGE----LSGGQQQRVFL 148
Cdd:PRK14271 101 RRVGMLFQRPN---PFPMSIMDNVLAGVRAHKLV---PRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 149 ARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEgKTILVVHHDLSKADDYFSHLVL-LNKKLVKAGPVHDIL 224
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALfFDGRLVEEGPTEQLF 250
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-237 |
1.12e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 89.85 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYH--GQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQG-------DIRFFEQPFkqVRKQI 75
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghDLALADPAW--LRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 76 AYVPQRNDLdwtFPIHVLDTVLLG-TYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQ 154
Cdd:cd03252 79 GVVLQENVL---FNRSIRDNIALAdPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 155 NAQLFCLDEPFVGIDMASEETMIRILKELRDeGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPvHDILRPEVMLQAYE 234
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGS-HDELLAENGLYAYL 233
|
...
gi 518573420 235 TQL 237
Cdd:cd03252 234 YQL 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-197 |
1.13e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.17 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCL-DLIEKDQGDIRFFEQPFKQ------VRKQIAYVPQrndldwtfpiH 91
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMK-ILyGLYQPDSGEILIDGKPVRIrsprdaIALGIGMVHQ----------H 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 92 --------VLDTVLLGTYPKLGLIKRPKKED---RAYAyhclEKVGMQ-DFAKRqIGELSGGQQQRVFLARALAQNAQLF 159
Cdd:COG3845 89 fmlvpnltVAENIVLGLEPTKGGRLDRKAARariRELS----ERYGLDvDPDAK-VEDLSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518573420 160 CLDEPfvgidmaseeT----------MIRILKELRDEGKTILVVHHDL 197
Cdd:COG3845 164 ILDEP----------TavltpqeadeLFEILRRLAAEGKSIIFITHKL 201
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-215 |
1.44e-21 |
|
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: 89.45 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIAYVPQRNDLdwtFP-IHVLDTVLL 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSL---LPwLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 99 GTypKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGID-MASEETMI 177
Cdd:TIGR01184 78 AV--DRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDaLTRGNLQE 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 518573420 178 RILKELRDEGKTILVVHHDLSKAddyfshlVLLNKKLV 215
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEA-------LLLSDRVV 186
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
18-201 |
1.46e-21 |
|
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: 89.42 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 18 DALENVSLSIQEGTMTGIIGPNGAGKSTLLK--ACLDLIekDQGDIRFFEQPFKQ--------VRKQ-IAYVPQrndldw 86
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGllAGLDRP--TSGTVRLAGQDLFAldedararLRARhVGFVFQ------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 87 TFPI----HVLDTVLLgtyPklgLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLD 162
Cdd:COG4181 98 SFQLlptlTALENVML---P---LELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFAD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518573420 163 EPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKAD 201
Cdd:COG4181 172 EPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAA 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-209 |
1.71e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 88.71 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 21 ENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVR----KQIAYV-----------PQRNdLD 85
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRdeyhQDLLYLghqpgikteltALEN-LR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 86 WTFPIHvldtvllGTYpklglikrpkkeDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPF 165
Cdd:PRK13538 97 FYQRLH-------GPG------------DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518573420 166 VGIDMASEETMIRILKE-LRDEGKTILVVHHDLSKADDYFSHLVL 209
Cdd:PRK13538 158 TAIDKQGVARLEALLAQhAEQGGMVILTTHQDLPVASDKVRKLRL 202
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-197 |
2.43e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.39 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 14 YHGQDAL-ENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP--FKQVRKQIAYVPQRNDLDWTFpi 90
Cdd:PRK13539 11 VRGGRVLfSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDidDPDVAEACHYLGHRNAMKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 91 hvldTV---------LLGTypklglikrpkkeDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCL 161
Cdd:PRK13539 89 ----TVaenlefwaaFLGG-------------EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 518573420 162 DEPFVGIDMASEETMIRILKELRDEGKTILVV-HHDL 197
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAHLAQGGIVIAAtHIPL 188
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-218 |
3.03e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.92 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKAcLDLIE-KDQGDI-----RF-FEQP-----FKQV 71
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRV-LNLLEmPRSGTLniagnHFdFSKTpsdkaIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 72 RKQIAYVPQRNDLdWtfPiHVldTVLLGtypklgLIKRP-------KKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQ 144
Cdd:PRK11124 81 RRNVGMVFQQYNL-W--P-HL--TVQQN------LIEAPcrvlglsKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 145 RVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAG 218
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENgHIVEQG 223
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-218 |
3.07e-21 |
|
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: 90.25 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 35 IIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV---RKQIAYVPQRNDLdwtFP-IHVLDTVLLGtypkLGLIKRP 110
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVpphLRHINMVFQSYAL---FPhMTVEENVAFG----LKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 111 KKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDE-GKT 189
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGIT 153
|
170 180 190
....*....|....*....|....*....|
gi 518573420 190 ILVVHHDLSKADDYFSHLVLLNK-KLVKAG 218
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIMRKgKIAQIG 183
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-200 |
3.22e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.06 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACL---DLIEK--DQGDIRFFEQPFK-------QVR 72
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPEvtITGSIVYNGHNIYsprtdtvDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 73 KQIAYVPQRNDldwTFPIHVLDTVLLGTypKLGLIKRPKKEDRAYAyHCLEKVGMQDFAKRQIGE----LSGGQQQRVFL 148
Cdd:PRK14239 86 KEIGMVFQQPN---PFPMSIYENVVYGL--RLKGIKDKQVLDEAVE-KSLKGASIWDEVKDRLHDsalgLSGGQQQRVCI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518573420 149 ARALAQNAQLFCLDEPFVGIDMAS----EETMIrilkELRDEgKTILVVHHDLSKA 200
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISagkiEETLL----GLKDD-YTMLLVTRSMQQA 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-237 |
3.56e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.42 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQ---------PFKQVRKQIAYV---PQRNDLDW 86
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkDIKQIRKKVGLVfqfPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 87 TfpihVLDTVLLGtyPK-LGLikrPKKEDRAYAYHCLEKVGM-QDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEP 164
Cdd:PRK13649 102 T----VLKDVAFG--PQnFGV---SQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518573420 165 FVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQayETQL 237
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKgKLVLSGKPKDIFQDVDFLE--EKQL 244
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-218 |
5.27e-21 |
|
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: 88.06 E-value: 5.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 15 HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQG-------DIRFFEqpFKQVRKQIAYVPQrndldwt 87
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGrilidghDVRDYT--LASLRRQIGLVSQ------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 88 fpihvlDTVLL-GT------YPKLGlikrpkkEDRAYAYHCLEKVGMQDFAKR-------QIGE----LSGGQQQRVFLA 149
Cdd:cd03251 84 ------DVFLFnDTvaeniaYGRPG-------ATREEVEEAARAANAHEFIMElpegydtVIGErgvkLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518573420 150 RALAQNAQLFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLS---KADDYfshLVLLNKKLVKAG 218
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLStieNADRI---VVLEDGKIVERG 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-201 |
6.41e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.67 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 21 ENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRF--------FEQPFKQVRKQIAYVPQRNDLdWTfPIHV 92
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdgenipamSRSRLYTVRKRMSMLFQSGAL-FT-DMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 93 LDTVllgTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMAS 172
Cdd:PRK11831 102 FDNV---AYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180 190
....*....|....*....|....*....|....
gi 518573420 173 EETMIRILKELRDE-GKTILVVHHD----LSKAD 201
Cdd:PRK11831 179 MGVLVKLISELNSAlGVTCVVVSHDvpevLSIAD 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-238 |
1.11e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 88.15 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 17 QDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQ---------PFKQVRKQIAYVPQrndldwt 87
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitagkknkKLKPLRKKVGIVFQ------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 88 FPIHVL--DTVL----LGtyPK-LGLikrPKKEDRAYAYHCLEKVGM-QDFAKRQIGELSGGQQQRVFLARALAQNAQLF 159
Cdd:PRK13634 93 FPEHQLfeETVEkdicFG--PMnFGV---SEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQAYETQL 237
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKgTVFLQGTPREIFADPDELEAIGLDL 247
|
.
gi 518573420 238 P 238
Cdd:PRK13634 248 P 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-197 |
1.77e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.70 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYV-SYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF-----KQVRKQ-IA 76
Cdd:COG3845 257 VLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglspRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 77 YVPQ-RND----LDWTfpihVLDTVLLGTYPKLGLIKRP---KKEDRAYAyhclEKVgMQDF------AKRQIGELSGGQ 142
Cdd:COG3845 337 YIPEdRLGrglvPDMS----VAENLILGRYRRPPFSRGGfldRKAIRAFA----EEL-IEEFdvrtpgPDTPARSLSGGN 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 143 QQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDL 197
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDL 462
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-218 |
1.90e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.14 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 2 SYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCL----DLIE--KDQGDIRFFEQPFK------ 69
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILR-CFnrlnDLIPgfRVEGKVTFHGKNLYapdvdp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 70 -QVRKQIAYVPQRNDldwTFPIHVLDTVLLGtyPKLGLIKRPKKE--DRAyayhcLEKVGMQDFAK---RQIG-ELSGGQ 142
Cdd:PRK14243 87 vEVRRRIGMVFQKPN---PFPKSIYDNIAYG--ARINGYKGDMDElvERS-----LRQAALWDEVKdklKQSGlSLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518573420 143 QQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAG 218
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSDMTAFFNVELTEGG 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-226 |
2.08e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 88.32 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKaCLDLIEK-DQGDI--------RFFEQPFKQVRKQIAYVPQrndldwtfp 89
Cdd:PRK11153 20 ALNNVSLHIPAGEIFGVIGASGAGKSTLIR-CINLLERpTSGRVlvdgqdltALSEKELRKARRQIGMIFQ--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 90 iH--------VLDTVLLgtyPkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQ-LFC 160
Cdd:PRK11153 90 -HfnllssrtVFDNVAL---P-LELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKvLLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518573420 161 lDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHH--DLSK--ADdyfSHLVLLNKKLVKAGPVHDI-LRP 226
Cdd:PRK11153 165 -DEATSALDPATTRSILELLKDInRELGLTIVLITHemDVVKriCD---RVAVIDAGRLVEQGTVSEVfSHP 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-196 |
2.79e-20 |
|
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: 83.65 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEqpfkqvRKQIAYVPQrndl 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------TVKIGYFEQ---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 85 dwtfpihvldtvllgtypklglikrpkkedrayayhclekvgmqdfakrqigeLSGGQQQRVFLARALAQNAQLFCLDEP 164
Cdd:cd03221 71 -----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|..
gi 518573420 165 FVGIDMASEETMIRILKELRdegKTILVVHHD 196
Cdd:cd03221 98 TNHLDLESIEALEEALKEYP---GTVILVSHD 126
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-198 |
5.16e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 87.09 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF--------KQVRKQIAYVPQrndlDwtfPI 90
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglsgrelRPLRRRMQMVFQ----D---PY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 91 HVLD---TV--LLGTYPKL-GLikRPKKEDRAYAYHCLEKVGM-QDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDE 163
Cdd:COG4608 106 ASLNprmTVgdIIAEPLRIhGL--ASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 518573420 164 PFVGIDMASEETMIRILKELRDE-GKTILVVHHDLS 198
Cdd:COG4608 184 PVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLS 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-213 |
5.40e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.54 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQD--ALENVSLSIQEGTMTGIIGPNGAGKST---LLKACLDL----IEKDQGDIRffEQPFKQVRKQIAYVPQRnd 83
Cdd:PRK11176 350 TYPGKEvpALRNINFKIPAGKTVALVGRSGSGKSTianLLTRFYDIdegeILLDGHDLR--DYTLASLRNQVALVSQN-- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 84 ldwtfpIHVL-DTVLLG-TYPKLGLIKRPKKEDRAYAYHCLEKV-GMQDFAKRQIGE----LSGGQQQRVFLARALAQNA 156
Cdd:PRK11176 426 ------VHLFnDTIANNiAYARTEQYSREQIEEAARMAYAMDFInKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 157 QLFCLDEPFVGIDMASEETMIRILKELRDEgKTILVVHHDLS---KAD-----------DYFSHLVLLNKK 213
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLStieKADeilvvedgeivERGTHAELLAQN 569
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-247 |
6.77e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.08 E-value: 6.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDI---------RFFEQpfkqvrKQIAYVPQRNDLdwtFP- 89
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvthRSIQQ------RDICMVFQSYAL---FPh 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 90 IHVLDTVLLGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGID 169
Cdd:PRK11432 93 MSLGENVGYG----LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 170 MASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDI-LRPEVMlqayetqlpFLKSAGGD 246
Cdd:PRK11432 169 ANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKgKIMQIGSPQELyRQPASR---------FMASFMGD 239
|
.
gi 518573420 247 A 247
Cdd:PRK11432 240 A 240
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-224 |
6.97e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 88.23 E-value: 6.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 15 HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV-----RKQIAYVPQRNDLdwtFP 89
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqldswRSRLAVVSQTPFL---FS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 90 IHVLDTVLLGtypklglikRP--KKEDRAYAyHCLEKV---------GMQDfakrQIGE----LSGGQQQRVFLARALAQ 154
Cdd:PRK10789 403 DTVANNIALG---------RPdaTQQEIEHV-ARLASVhddilrlpqGYDT----EVGErgvmLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518573420 155 NAQLFCLDEPFVGIDMASEEtmiRILKELRD--EGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPvHDIL 224
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEH---QILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGN-HDQL 536
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
16-197 |
1.37e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.16 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 16 GQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRF----------FEQPFkqVRKQIAYVPQRNDL- 84
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsghditrlknREVPF--LRRQIGMIFQDHHLl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 85 -DWTfpihVLDTVLLGTypklgLIKRPKKED-RAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLD 162
Cdd:PRK10908 92 mDRT----VYDNVAIPL-----IIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190
....*....|....*....|....*....|....*
gi 518573420 163 EPFVGIDMASEETMIRILKELRDEGKTILVVHHDL 197
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-240 |
3.04e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.29 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFK-------QVRKQIAY 77
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrgllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQrnDLDWTFPIHVLDTVLLGTYPKLGLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQ 157
Cdd:PRK13638 82 VFQ--DPEQQIFYTDIDSDIAFSLRNLGV---PEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 158 LFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNKK--LVKAGPVHDILRPEVMLQAYET 235
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGqiLTHGAPGEVFACTEAMEQAGLT 236
|
....*
gi 518573420 236 QlPFL 240
Cdd:PRK13638 237 Q-PWL 240
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-224 |
4.98e-19 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 82.97 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTllkaCLDLIEK-----------DQGDIRffEQPFKQVRKQIAYVPQRNDLdwtF 88
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKST----VVSLLERfydptsgeillDGVDIR--DLNLRWLRSQIGLVSQEPVL---F 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 89 PIHVLDTVLLGTYPklglikRPKKEDRAYAyhclEKVGMQDFAKR-------QIGE----LSGGQQQRVFLARALAQNAQ 157
Cdd:cd03249 90 DGTIAENIRYGKPD------ATDEEVEEAA----KKANIHDFIMSlpdgydtLVGErgsqLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 158 LFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLS---KADDYFshlVLLNKKLVKAGPvHDIL 224
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLStirNADLIA---VLQNGQVVEQGT-HDEL 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
13-204 |
5.41e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 85.55 E-value: 5.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP--FKQ-----------VRKQIAYVP 79
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidFKSskealengismVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 80 QRNdldwtfpihVLDTVLLGTYPKLGLIKRPKKEDRAyAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLF 159
Cdd:PRK10982 87 QRS---------VMDNMWLGRYPTKGMFVDQDKMYRD-TKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHdlsKADDYF 204
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISH---KMEEIF 198
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-210 |
1.06e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.47 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYV-SYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFfeqPfkqVRKQIAYVPQRN 82
Cdd:COG4178 362 ALALEDLTLrTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---P---AGARVLFLPQRP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 83 DLdwtfPIHVLDTVLLgtYPKlglikRPKKEDRAYAYHCLEKVGMQDFAKR--------QIgeLSGGQQQRVFLARALAQ 154
Cdd:COG4178 436 YL----PLGTLREALL--YPA-----TAEAFSDAELREALEAVGLGHLAERldeeadwdQV--LSLGEQQRLAFARLLLH 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 155 NAQLFCLDEPFVGIDMASEETMIRILKElRDEGKTILVV-HHdlSKADDYFSHLVLL 210
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVgHR--STLAAFHDRVLEL 556
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-201 |
1.24e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 81.15 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVR----KQIAYVPQ 80
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLctyqKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RNDL--------DWTFPIHVLDTVL----LGTYPKLGlikrpkkedrayayHCLekvgmqDFAkrqIGELSGGQQQRVFL 148
Cdd:PRK13540 82 RSGInpyltlreNCLYDIHFSPGAVgiteLCRLFSLE--------------HLI------DYP---CGLLSSGQKRQVAL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518573420 149 ARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHD---LSKAD 201
Cdd:PRK13540 139 LRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQdlpLNKAD 194
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-224 |
1.30e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.93 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDAlenvSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDI--------RFFEQPFKQVR 72
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDA----SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiaKISDAELREVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 73 -KQIAYVPQrndldwTFPIHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARA 151
Cdd:PRK10070 105 rKKIAMVFQ------SFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 152 LAQNAQLFCLDEPFVGID-MASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLL-NKKLVKAGPVHDIL 224
Cdd:PRK10070 179 LAINPDILLMDEAFSALDpLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMqNGEVVQVGTPDEIL 253
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-229 |
1.34e-18 |
|
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: 83.62 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 23 VSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIAYVPQRNDLDWTFPIHVLdtvllgtYP 102
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARL-------FP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 103 KLGL-------IKRPKKEDRAYAY-HCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEE 174
Cdd:TIGR02142 89 HLSVrgnlrygMKRARPSERRISFeRVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 175 TMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLL-NKKLVKAGPVHDILRPEVM 229
Cdd:TIGR02142 169 EILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLeDGRVAAAGPIAEVWASPDL 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-236 |
1.51e-18 |
|
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: 83.97 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEkDQGDIRFFEQP--------FKQVRKQIAYVPQrnD----LDw 86
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDldglsrraLRPLRRRMQVVFQ--DpfgsLS- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 87 tfPIH-VLDTVLLGtypkLGL--IKRPKKEDRAYAYHCLEKVGMQ-DFAKRQIGELSGGQQQRVFLARALAQNAQLFCLD 162
Cdd:COG4172 377 --PRMtVGQIIAEG----LRVhgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLD 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 163 EPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLS--KAddyFSH--LVLLNKKLVKAGPVHDIL-RPEvmlQAYeTQ 236
Cdd:COG4172 451 EPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAvvRA---LAHrvMVMKDGKVVEQGPTEQVFdAPQ---HPY-TR 523
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-201 |
1.59e-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: 81.69 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 24 SLSIQEGTMT-----GIIGPNGAGKSTLLKACLDLIEKDQGDIRFFeqpfkqvRKQIAYVPQRNDLDwtFPIHVLDTvll 98
Cdd:cd03237 14 TLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-------LDTVSYKPQYIKAD--YEGTVRDL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 99 gtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDmaSEETMI- 177
Cdd:cd03237 82 -----LSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRLMa 154
|
170 180
....*....|....*....|....*.
gi 518573420 178 -RILKELRDEG-KTILVVHHDLSKAD 201
Cdd:cd03237 155 sKVIRRFAENNeKTAFVVEHDIIMID 180
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-238 |
1.74e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.13 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFE---------QPFKQVRKQIAYVPQrndldwtFP 89
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdKYIRPVRKRIGMVFQ-------FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 90 IHVL--DTV----LLGtyPKLglIKRPKKEDRAYAYHCLEKVGM-QDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLD 162
Cdd:PRK13646 95 ESQLfeDTVereiIFG--PKN--FKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 163 EPFVGIDMASEETMIRILKELR-DEGKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQAYETQLP 238
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEgSIVSQTSPKELFKDKKKLADWHIGLP 248
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-226 |
1.80e-18 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 80.53 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSY--HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQ-----PFKQVRKQIAY 77
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQrndldwtfpihvlDTVLLGTYPKLGLIKRPKKEDRayayhclekvgmQDFAKRQIGE----LSGGQQQRVFLARALA 153
Cdd:cd03369 87 IPQ-------------DPTLFSGTIRSNLDPFDEYSDE------------EIYGALRVSEgglnLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518573420 154 QNAQLFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLSKADDYFSHLVLlnkklvKAGPVHDILRP 226
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLRTIIDYDKILVM------DAGEVKEYDHP 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-196 |
1.90e-18 |
|
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: 83.83 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQpfkqvrKQIAYVPQ-RNDLD-----WTFPIHVL 93
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET------VKLAYVDQsRDALDpnktvWEEISGGL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 94 DTVLLGTYpklglikrpKKEDRAYayhclekVGMQDFA----KRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGID 169
Cdd:TIGR03719 412 DIIKLGKR---------EIPSRAY-------VGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
170 180
....*....|....*....|....*...
gi 518573420 170 MaseETMiRILKE-LRDEGKTILVVHHD 196
Cdd:TIGR03719 476 V---ETL-RALEEaLLNFAGCAVVISHD 499
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-201 |
2.36e-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: 81.26 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 28 QEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGD----------IRFF-----EQPFKQVRK---QIAYVPQRNDLdwtFP 89
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeiLDEFrgselQNYFTKLLEgdvKVIVKPQYVDL---IP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 90 IHVLDTVLLgtypklgLIKrpKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGID 169
Cdd:cd03236 101 KAVKGKVGE-------LLK--KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190
....*....|....*....|....*....|..
gi 518573420 170 MASEETMIRILKELRDEGKTILVVHHDLSKAD 201
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYVLVVEHDLAVLD 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-208 |
2.80e-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: 83.30 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 28 QEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGD----------IRFF-----EQPFKQVRKQ---IAYVPQRNDLdwtFP 89
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdevLKRFrgtelQDYFKKLANGeikVAHKPQYVDL---IP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 90 IHVLDTV--LLgtypklglikrpKKED-RAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFV 166
Cdd:COG1245 174 KVFKGTVreLL------------EKVDeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518573420 167 GIDMASEETMIRILKELRDEGKTILVVHHDLSkADDYFSHLV 208
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEEGKYVLVVEHDLA-ILDYLADYV 282
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-206 |
3.30e-18 |
|
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: 80.45 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRF---------FEQPFKQVRKQIAYVPQRndlDWTFPI 90
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnknesepsFEATRSRNRYSVAYAAQK---PWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 91 HVLDTVLLGTypklglikrPKKEDRAYAyhCLEKVGMQ---DFA----KRQIGE----LSGGQQQRVFLARALAQNAQLF 159
Cdd:cd03290 94 TVEENITFGS---------PFNKQRYKA--VTDACSLQpdiDLLpfgdQTEIGErginLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518573420 160 CLDEPFVGIDMASEETMIR--ILKELRDEGKTILVVHHDLSkaddYFSH 206
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ----YLPH 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-225 |
3.30e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 83.23 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ-----VRKQIAYVPQRNDLdwtFPIHVLD 94
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhhyLHRQVALVGQEPVL---FSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 95 TVllgTYpklGLIKRPKKEDRAYAYHCLEKVGMQDFAK---RQIGE----LSGGQQQRVFLARALAQNAQLFCLDEPFVG 167
Cdd:TIGR00958 574 NI---AY---GLTDTPDEEIMAAAKAANAHDFIMEFPNgydTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518573420 168 IDMASEETmiriLKELRD-EGKTILVVHHDLS---KADdyfsHLVLLNKKLVKAGPVHDILR 225
Cdd:TIGR00958 648 LDAECEQL----LQESRSrASRTVLLIAHRLStveRAD----QILVLKKGSVVEMGTHKQLM 701
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-240 |
3.57e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.59 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLI--EKDQGDIRFFEQP--------FKQVRKQIAYVPQrndldwtF 88
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisETGQTIVGDYAIPanlkkikeVKRLRKEIGLVFQ-------F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 89 PIHVLDTVLLGTYPKLGLIKRPKKEDRAYAY--HCLEKVGM-QDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPF 165
Cdd:PRK13645 99 PEYQLFQETIEKDIAFGPVNLGENKQEAYKKvpELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 166 VGIDMASEETMIRILKEL-RDEGKTILVVHHDLSK----ADDYfshLVLLNKKLVKAGPVHDILRPEVMLQAYETQLPFL 240
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQvlriADEV---IVMHEGKVISIGSPFEIFSNQELLTKIEIDPPKL 255
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-220 |
4.87e-18 |
|
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: 79.11 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDL--IEKDQGDIRFFEQ------PFKQVRKQIA 76
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEditdlpPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 77 yvpqrndLDWTFPIHVldtvllgtypklglikrpkkedrayayhclEKVGMQDFAkRQIGE-LSGGQQQRVFLARALAQN 155
Cdd:cd03217 81 -------LAFQYPPEI------------------------------PGVKNADFL-RYVNEgFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 156 AQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHH-----DLSKADdyFSHlVLLNKKLVKAGPV 220
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyqrllDYIKPD--RVH-VLYDGRIVKSGDK 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-195 |
5.18e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.54 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKAC--LDLIEKDQGDI----------RFFEQP----- 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcGYVERPskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 68 -----------------------FKQVRKQIAYVPQRndldwTFPIHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEK 124
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdklRRRIRKRIAIMLQR-----TFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518573420 125 VGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHH 195
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSH 227
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-221 |
7.46e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.40 E-value: 7.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKD---QGDIRFFEQPF--KQVRKQIAYVpQRNDLdwTFP-IHVL 93
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIdaKEMRAISAYV-QQDDL--FIPtLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 94 DTVLLGTYPKLGLiKRPKKEDRAYAYHCLEKVGMQDFAKRQIGE------LSGGQQQRVFLARALAQNAQLFCLDEPFVG 167
Cdd:TIGR00955 118 EHLMFQAHLRMPR-RVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518573420 168 IDMASEETMIRILKELRDEGKT-ILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVH 221
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTiICTIHQPSSELFELFDKIILMAEgRVAYLGSPD 252
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-231 |
7.73e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.52 E-value: 7.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQ---DALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDI-----RFFEQPFKQVR 72
Cdd:PRK13642 1 MNKILEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVkidgeLLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 73 KQIAYVPQRNDLDWTFPIhVLDTVLLGT----YPKLGLIKRPKKedrayayhCLEKVGMQDFAKRQIGELSGGQQQRVFL 148
Cdd:PRK13642 81 RKIGMVFQNPDNQFVGAT-VEDDVAFGMenqgIPREEMIKRVDE--------ALLAVNMLDFKTREPARLSGGQKQRVAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 149 ARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGK-TILVVHHDLSKADDYFSHLVLLNKKLVK-AGPVHDILRP 226
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAGEIIKeAAPSELFATS 231
|
....*
gi 518573420 227 EVMLQ 231
Cdd:PRK13642 232 EDMVE 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-197 |
8.22e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.90 E-value: 8.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKAcLDLIEKD---QGDIRFFEQP--FKQVR--- 72
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKV-LSGVYPHgtyEGEIIFEGEElqASNIRdte 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 73 -KQIAYVPQrnDLDWTFPIHVLDTVLLGTYP-KLGLIKRPKKEDRAYAYhcLEKVGMQDFAKRQIGELSGGQQQRVFLAR 150
Cdd:PRK13549 81 rAGIAIIHQ--ELALVKELSVLENIFLGNEItPGGIMDYDAMYLRAQKL--LAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518573420 151 ALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDL 197
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKL 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-197 |
8.47e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 8.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 22 NVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFF------EQPFKQVRKQIAYVPQRNDLDWTFP------ 89
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNgkdispRSPLDAVKKGMAYITESRRDNGFFPnfsiaq 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 90 -IHVLDTVLLGTYP-KLGLIKrpKKEDRAYAYHCLEKVGMQDFAKRQ-IGELSGGQQQRVFLARALAQNAQLFCLDEPFV 166
Cdd:PRK09700 361 nMAISRSLKDGGYKgAMGLFH--EVDEQRTAENQRELLALKCHSVNQnITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190
....*....|....*....|....*....|.
gi 518573420 167 GIDMASEETMIRILKELRDEGKTILVVHHDL 197
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
5-195 |
9.22e-18 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 82.01 E-value: 9.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHG--QDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVR-----KQIAY 77
Cdd:TIGR01842 317 LSVENVTIVPPGgkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDretfgKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRNDLdwtFPihvldtvllgtypklGLIKR--PKKEDRAYAyhclEKV-------GMQDFAKR-------QIGE---- 137
Cdd:TIGR01842 397 LPQDVEL---FP---------------GTVAEniARFGENADP----EKIieaaklaGVHELILRlpdgydtVIGPggat 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 138 LSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHH 195
Cdd:TIGR01842 455 LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITH 512
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-198 |
9.44e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.68 E-value: 9.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDAL----ENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDL-----IEKDQGDIRFF--------EQP 67
Cdd:PRK15134 6 LAIENLSVAFRQQQTVrtvvNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHgesllhasEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 68 FKQVR-KQIAYVPQRNDLDWTfPIHVLDTVLlgtYPKLGLIKRPKKED-RAYAYHCLEKVGMQDFAKRQIG---ELSGGQ 142
Cdd:PRK15134 86 LRGVRgNKIAMIFQEPMVSLN-PLHTLEKQL---YEVLSLHRGMRREAaRGEILNCLDRVGIRQAAKRLTDyphQLSGGE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 143 QQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLS 198
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLS 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-240 |
2.12e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.08 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 6 TIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF-----KQVRKQIAYVPQ 80
Cdd:PRK13652 6 TRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItkeniREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RNDlDWTFPIHVLDTVLLGTYpKLGLIKRPKKEDRAYAYHCLekvGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFC 160
Cdd:PRK13652 86 NPD-DQIFSPTVEQDIAFGPI-NLGLDEETVAHRVSSALHML---GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 161 LDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILRPEVMLQAYETQLP 238
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKgRIVAYGTVEEIFLQPDLLARVHLDLP 240
|
..
gi 518573420 239 FL 240
Cdd:PRK13652 241 SL 242
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-198 |
3.32e-17 |
|
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: 80.25 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV-----RKQIAYVPQrndldwtfpihvlD 94
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVtqaslRAAIGIVPQ-------------D 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 95 TVLLGT-------YPKLGlIKRPKKEDRAYAYHclekvgMQDFAKR-------QIGE----LSGGQQQRVFLARALAQNA 156
Cdd:COG5265 441 TVLFNDtiayniaYGRPD-ASEEEVEAAARAAQ------IHDFIESlpdgydtRVGErglkLSGGEKQRVAIARTLLKNP 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518573420 157 QLFCLDEPFVGIDMASEEtmiRILKELRD--EGKTILVVHHDLS 198
Cdd:COG5265 514 PILIFDEATSALDSRTER---AIQAALREvaRGRTTLVIAHRLS 554
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
12-240 |
3.37e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.49 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 12 VSYH---GQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQG-------DIRFFEQpFKQVRKQIAYVPQR 81
Cdd:PRK13644 7 VSYSypdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGkvlvsgiDTGDFSK-LQGIRKLVGIVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 NDLDWtfpihVLDTVL--LGTYPK---LGLIKRPKKEDRAyayhcLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNA 156
Cdd:PRK13644 86 PETQF-----VGRTVEedLAFGPEnlcLPPIEIRKRVDRA-----LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 157 QLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPVHDILRpEVMLQAYETQ 236
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS-DVSLQTLGLT 234
|
....
gi 518573420 237 LPFL 240
Cdd:PRK13644 235 PPSL 238
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
18-224 |
3.65e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 78.34 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 18 DALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP-----FKQVRKQIAYVPQ--RNDLDWTFPI 90
Cdd:COG4167 27 EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKleygdYKYRCKHIRMIFQdpNTSLNPRLNI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 91 -HVLDTVL-LGTypKLGLIKRPKKedrayAYHCLEKVGM-QDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVG 167
Cdd:COG4167 107 gQILEEPLrLNT--DLTAEEREER-----IFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518573420 168 IDMASEETMIRILKELRDE-GKTILVVHHDLskadDYFSH-----LVLLNKKLVKAGPVHDIL 224
Cdd:COG4167 180 LDMSVRSQIINLMLELQEKlGISYIYVSQHL----GIVKHisdkvLVMHQGEVVEYGKTAEVF 238
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-200 |
4.17e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 77.61 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ------VRKQ 74
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtakiMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 75 IAYVPQRNDLdwtFP-IHVLDTVLLGTYpklgLIKRPKKEDR-AYAYHCLEKvgMQDFAKRQIGELSGGQQQRVFLARAL 152
Cdd:PRK11614 82 VAIVPEGRRV---FSrMTVEENLAMGGF----FAERDQFQERiKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518573420 153 AQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKA 200
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQA 200
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-196 |
5.30e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 79.67 E-value: 5.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 12 VSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLlkacLDLIEKD--QG---DIRFFEQ------PFKQVRKQIAYVPQ 80
Cdd:PRK10938 268 VSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTL----LSLITGDhpQGysnDLTLFGRrrgsgeTIWDIKKHIGYVSS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 RNDLDWTFPIHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQD-FAKRQIGELSGGQQQRVFLARALAQNAQLF 159
Cdd:PRK10938 344 SLHLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPTLL 423
|
170 180 190
....*....|....*....|....*....|....*....
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRDEGKTIL--VVHHD 196
Cdd:PRK10938 424 ILDEPLQGLDPLNRQLVRRFVDVLISEGETQLlfVSHHA 462
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
19-195 |
6.10e-17 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 76.68 E-value: 6.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKAcLDLIEK-DQGDIRF---------FEQPFKQVRKQIAYVPQRNDLdwtF 88
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNI-IGMFDSlDSGSLTLagkevtnlsYSQKIILRRELIGYIFQSFNL---I 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 89 P-IHVLDTVllgtypKLGLIKR--PKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPF 165
Cdd:NF038007 96 PhLSIFDNV------ALPLKYRgvAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPT 169
|
170 180 190
....*....|....*....|....*....|
gi 518573420 166 VGIDMASEETMIRILKELRDEGKTILVVHH 195
Cdd:NF038007 170 GNLDSKNARAVLQQLKYINQKGTTIIMVTH 199
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
10-198 |
7.91e-17 |
|
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: 75.44 E-value: 7.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 10 LYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLdliekdqgdirffeqpFKQVRKQIAYVPQRNDLDWTFP 89
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----------------YASGKARLISFLPKFSRNKLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 90 IHVLDTVLlgtypKLGLikrpkkedrayAYHCLEkvgmqdfakRQIGELSGGQQQRVFLARALAQNAQ--LFCLDEPFVG 167
Cdd:cd03238 65 IDQLQFLI-----DVGL-----------GYLTLG---------QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190
....*....|....*....|....*....|.
gi 518573420 168 IDMASEETMIRILKELRDEGKTILVVHHDLS 198
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-236 |
1.21e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.05 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLI----------------EKDQGDIR-----FFEQPFKQ-----VR 72
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLipsegkvyvdgldtsdEENLWDIRnkagmVFQNPDNQivatiVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 73 KQIAYVPQrndldwtfpihvldtvllgtypKLGLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARAL 152
Cdd:PRK13633 105 EDVAFGPE----------------------NLGI---PPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 153 AQNAQLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPVHDILR------ 225
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKevemmk 239
|
250
....*....|....*..
gi 518573420 226 ------PEVMLQAYETQ 236
Cdd:PRK13633 240 kigldvPQVTELAYELK 256
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-218 |
1.74e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.87 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKAcldlI------EKDQGDIRFFEQ------PFKQVR 72
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKV----LmghpkyEVTSGSILLDGEdilelsPDERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 73 KQIAYVPQRndldwtfPIHV----LDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGM-QDFAKRQIGE-LSGGQQQRV 146
Cdd:COG0396 77 AGIFLAFQY-------PVEIpgvsVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRN 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 147 FLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHH-----DLSKADdyFSHlVLLNKKLVKAG 218
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqrilDYIKPD--FVH-VLVDGRIVKSG 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-198 |
1.86e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.05 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFF--------EQPFKQVRKQIAYVPQRndldwtfPI 90
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLgkdllgmkDDEWRAVRSDIQMIFQD-------PL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 91 HVLD---TV-------LLGTYPKLgliKRPKKEDRAYAYhcLEKVGM-QDFAKRQIGELSGGQQQRVFLARALAQNAQLF 159
Cdd:PRK15079 109 ASLNprmTIgeiiaepLRTYHPKL---SRQEVKDRVKAM--MLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLS 198
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLA 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-202 |
2.03e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.52 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 16 GQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF-----KQVRKQIAYVPQRNDLdwtFPI 90
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIstlkpEIYRQQVSYCAQTPTL---FGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 91 HVLDTVLlgtYPKlgLIKRPKKEDRAYAYHcLEKVGM-QDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEpfvgID 169
Cdd:PRK10247 96 TVYDNLI---FPW--QIRNQQPDPAIFLDD-LERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE----IT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518573420 170 MASEETMIRILKEL-----RDEGKTILVVHHD---LSKADD 202
Cdd:PRK10247 166 SALDESNKHNVNEIihryvREQNIAVLWVTHDkdeINHADK 206
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-197 |
2.64e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.74 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP--FKQVRKQ----IAYVPQrnDLDW 86
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEvtFNGPKSSqeagIGIIHQ--ELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 87 TFPIHVLDTVLLGTYP--KLGLIKRPKKEDRAYAYhcLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEP 164
Cdd:PRK10762 91 IPQLTIAENIFLGREFvnRFGRIDWKKMYAEADKL--LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190
....*....|....*....|....*....|...
gi 518573420 165 FVGIDMASEETMIRILKELRDEGKTILVVHHDL 197
Cdd:PRK10762 169 TDALTDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-225 |
3.66e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.85 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQG-------DIRFFEQPFKQVRKQIAYVPQrndldwtFPIH 91
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGkiiidgvDITDKKVKLSDIRKKVGLVFQ-------YPEY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 92 VL--DTVL--LGTYPK-LGLikrPKKEDRAYAYHCLEKVGM--QDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEP 164
Cdd:PRK13637 95 QLfeETIEkdIAFGPInLGL---SEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518573420 165 FVGIDMASEETMIRILKELRDEGK-TILVVHHDLSKADDYFSHLVLLNK-KLVKAGPVHDILR 225
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKgKCELQGTPREVFK 234
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-197 |
3.68e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.16 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 27 IQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGD----------IRFF-----EQPFKQVRKQ---IAYVPQRndldwtf 88
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeepswdevLKRFrgtelQNYFKKLYNGeikVVHKPQY------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 89 pIHVLDTVLLGTYPKLgLIK---RPKKEDrayayhCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPF 165
Cdd:PRK13409 169 -VDLIPKVFKGKVREL-LKKvdeRGKLDE------VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190
....*....|....*....|....*....|..
gi 518573420 166 VGIDMASEETMIRILKELRdEGKTILVVHHDL 197
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELA-EGKYVLVVEHDL 271
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-218 |
4.30e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.07 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSY-HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ-----VRKQ 74
Cdd:PRK10790 337 QSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlshsvLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 75 IAYVPQRndldwtfPIHVLDTVLLGTypKLGlikRPKKEDRAYayHCLEKVGMQDFAKR-------QIGE----LSGGQQ 143
Cdd:PRK10790 417 VAMVQQD-------PVVLADTFLANV--TLG---RDISEEQVW--QALETVQLAELARSlpdglytPLGEqgnnLSVGQK 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 144 QRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAG 218
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVR-EHTTLVVIAHRLSTIVEADTILVLHRGQAVEQG 556
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-212 |
5.14e-16 |
|
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: 74.43 E-value: 5.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ-----VRKQIAYVPQRNDLdwtFPIHVLD 94
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkyLHSKVSLVGQEPVL---FARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 95 TVLLG-TYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASE 173
Cdd:cd03248 107 NIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518573420 174 ETMIRILKElRDEGKTILVVHHDLS---KADdyfsHLVLLNK 212
Cdd:cd03248 187 QQVQQALYD-WPERRTVLVIAHRLStveRAD----QILVLDG 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-197 |
5.43e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.94 E-value: 5.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQ---DALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLdliekdqGDIRFFEQPFKQVRKQIAYVPQ 80
Cdd:PLN03232 614 AISIKNGYFSWDSKtskPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML-------GELSHAETSSVVIRGSVAYVPQ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 rndLDWTFPIHVLDTVLLGTypKLGLIKRPKKEDRAYAYHCLEKVGMQDFAkrQIGE----LSGGQQQRVFLARALAQNA 156
Cdd:PLN03232 687 ---VSWIFNATVRENILFGS--DFESERYWRAIDVTALQHDLDLLPGRDLT--EIGErgvnISGGQKQRVSMARAVYSNS 759
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518573420 157 QLFCLDEPFVGIDMASEETMIR--ILKELRdeGKTILVVHHDL 197
Cdd:PLN03232 760 DIYIFDDPLSALDAHVAHQVFDscMKDELK--GKTRVLVTNQL 800
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-197 |
5.55e-16 |
|
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: 74.39 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSY--HGQD-----ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQ------- 66
Cdd:COG4778 1 MTTLLEVENLSKTFtlHLQGgkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 67 ---PFK--QVRKQ-IAYVPQrndldwtFpIHVLDTVllgtyPKLGLIKRPkkedrayayhcLEKVGM-QDFAKRQIGEL- 138
Cdd:COG4778 81 qasPREilALRRRtIGYVSQ-------F-LRVIPRV-----SALDVVAEP-----------LLERGVdREEARARARELl 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518573420 139 -----------------SGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDL 197
Cdd:COG4778 137 arlnlperlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDE 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-197 |
8.44e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.00 E-value: 8.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 27 IQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIrffeqpFKQVRkqIAYVPQ--RNDLDWTfpihvLDTVLLGTYPKL 104
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------DPELK--ISYKPQyiKPDYDGT-----VEDLLRSITDDL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 105 glikrpkkeDRAYAYH-CLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDmaSEETMI--RILK 181
Cdd:PRK13409 429 ---------GSSYYKSeIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLAvaKAIR 497
|
170
....*....|....*..
gi 518573420 182 ELRDE-GKTILVVHHDL 197
Cdd:PRK13409 498 RIAEErEATALVVDHDI 514
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-197 |
8.52e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 75.98 E-value: 8.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 26 SIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIrffeqpFKQVRkqIAYVPQ--RNDLDWTfpihvLDTVLLGTYPK 103
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLK--ISYKPQyiSPDYDGT-----VEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 104 lglikrpkKEDRAYAYH-CLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDmaSEETMI--RIL 180
Cdd:COG1245 429 --------DFGSSYYKTeIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLAvaKAI 498
|
170
....*....|....*...
gi 518573420 181 KEL-RDEGKTILVVHHDL 197
Cdd:COG1245 499 RRFaENRGKTAMVVDHDI 516
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-200 |
9.28e-16 |
|
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: 74.10 E-value: 9.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIAYVPQRNDL 84
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 85 ---DWTF-PIHVLDTVLLGTYPKLGLIKRPKK-------EDRAYAYHCLEKVGM-QDFAKRQIGELSGGQQQRVFLARAL 152
Cdd:TIGR02323 84 mrtEWGFvHQNPRDGLRMRVSAGANIGERLMAigarhygNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518573420 153 AQNAQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKA 200
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLRGLvRDLGLAVIIVTHDLGVA 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-201 |
9.99e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 76.10 E-value: 9.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFfeqpfkqvRKQIAYVPQrndLDWTFPIHV 92
Cdd:TIGR01271 435 SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKH--------SGRISFSPQ---TSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 93 LDTVLLGT----YPKLGLIKRPKKEDRayayhcLEKVGMQDfaKRQIGE----LSGGQQQRVFLARALAQNAQLFCLDEP 164
Cdd:TIGR01271 504 KDNIIFGLsydeYRYTSVIKACQLEED------IALFPEKD--KTVLGEggitLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518573420 165 FVGIDMASE-ETMIRILKELRDEGKTILVVH--HDLSKAD 201
Cdd:TIGR01271 576 FTHLDVVTEkEIFESCLCKLMSNKTRILVTSklEHLKKAD 615
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-199 |
1.13e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.63 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKD--QGDIRFFEQPFKQV------RKQIA 76
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASnirdteRAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 77 YVPQrnDLDWTFPIHVLDTVLLG---TYPKlGLIKRPKKEDRAYAYhcLEKVGMQDF-AKRQIGELSGGQQQRVFLARAL 152
Cdd:TIGR02633 82 IIHQ--ELTLVPELSVAENIFLGneiTLPG-GRMAYNAMYLRAKNL--LRELQLDADnVTRPVGDYGGGQQQLVEIAKAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518573420 153 AQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSK 199
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNE 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-247 |
1.54e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.59 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIrffeqpfkQVRKQIAYVPQRNdldWTFPIHVLDTVLLG 99
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------WAERSIAYVPQQA---WIMNATVRGNILFF 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 100 TypklglikRPKKEDRAYAYHC--LEKvgmqDFA------KRQIGE----LSGGQQQRVFLARALAQNAQLFCLDEPFVG 167
Cdd:PTZ00243 745 D--------EEDAARLADAVRVsqLEA----DLAqlggglETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 168 IDMASEETMIR--ILKELRdeGKT-ILVVH--HDLSKADdyfsHLVLLNKKLVK-AGPVHDILRP--EVMLQAYETQLPF 239
Cdd:PTZ00243 813 LDAHVGERVVEecFLGALA--GKTrVLATHqvHVVPRAD----YVVALGDGRVEfSGSSADFMRTslYATLAAELKENKD 886
|
....*...
gi 518573420 240 LKSAGGDA 247
Cdd:PTZ00243 887 SKEGDADA 894
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-197 |
1.73e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.21 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLK--------ACLDliekdqGDIRFFEQP--FKQVR---------- 72
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKvlsgvyphGSYE------GEILFDGEVcrFKDIRdsealgivii 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 73 -KQIAYVPQrndldwtfpIHVLDTVLLGTYP-KLGLIKRPKKEDRAYAYhcLEKVGMQDFAKRQIGELSGGQQQRVFLAR 150
Cdd:NF040905 84 hQELALIPY---------LSIAENIFLGNERaKRGVIDWNETNRRAREL--LAKVGLDESPDTLVTDIGVGKQQLVEIAK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518573420 151 ALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDL 197
Cdd:NF040905 153 ALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKL 199
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-225 |
2.43e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.81 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 1 MSYALTIDRLYVSYHGQD----------------------ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQ 58
Cdd:COG1134 1 MSSMIEVENVSKSYRLYHepsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 59 GDIRffeqpfkqVRKQIA--------YVPQ----RNdldwtfpihvldTVLLGTYpkLGLikrPKKEDRAYAYHCLEKVG 126
Cdd:COG1134 81 GRVE--------VNGRVSallelgagFHPEltgrEN------------IYLNGRL--LGL---SRKEIDEKFDEIVEFAE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 127 MQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPF-VGiDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFS 205
Cdd:COG1134 136 LGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLaVG-DAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCD 214
|
250 260
....*....|....*....|.
gi 518573420 206 HLVLLNK-KLVKAGPVHDILR 225
Cdd:COG1134 215 RAIWLEKgRLVMDGDPEEVIA 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-232 |
2.64e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.48 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLD----------LIEKDQGDIRffeQPFKQVRKQIAYVPQRNDLDWTFP 89
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaypgkfegnvFINGKPVDIR---NPAQAIRAGIAMVPEDRKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 90 I----HVLDTVLLGTYPKLGLIKRPKKEDrayayhCLEKvGMQDFAKRQ------IGELSGGQQQRVFLARALAQNAQLF 159
Cdd:TIGR02633 353 IlgvgKNITLSVLKSFCFKMRIDAAAELQ------IIGS-AIQRLKVKTaspflpIGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPVHDILRPEVMLQA 232
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVLAA 498
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-219 |
3.23e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.51 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQiAYVPQRNDLDWTF--PIHVLDTV 96
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPG-KLQALRRDIQFIFqdPYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 97 LLGTYPKL------GLIkrPKKEDRAYAYHCLEKVGMQ-DFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGID 169
Cdd:PRK10261 418 QTVGDSIMeplrvhGLL--PGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518573420 170 MASEETMIRILKEL-RDEGKTILVVHHDLSKADDyFSH--LVLLNKKLVKAGP 219
Cdd:PRK10261 496 VSIRGQIINLLLDLqRDFGIAYLFISHDMAVVER-ISHrvAVMYLGQIVEIGP 547
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-224 |
3.97e-15 |
|
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: 74.60 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIrffeqpfkQVRKQIAYVPQRNdldWTFPIHVLDTVLLG 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV--------HMKGSVAYVPQQA---WIQNDSLRENILFG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 100 TYpklglIKRPKKEDRAYAYHCLEKVGMQDFAKR-QIGE----LSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEE 174
Cdd:TIGR00957 723 KA-----LNEKYYQQVLEACALLPDLEILPSGDRtEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518573420 175 TMIR--ILKELRDEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPVHDIL 224
Cdd:TIGR00957 798 HIFEhvIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-169 |
4.42e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.39 E-value: 4.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLL------KA----CLDLIEKDQGDIRFFEQpfkqVRK 73
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKiqqgRVEVLGGDMADARHRRA----VCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 74 QIAYVPQ---RNdLdwtfpihvldtvllgtYPKL-------------GLikrPKKEDRAYAYHCLEKVGMQDFAKRQIGE 137
Cdd:NF033858 77 RIAYMPQglgKN-L----------------YPTLsvfenldffgrlfGQ---DAAERRRRIDELLRATGLAPFADRPAGK 136
|
170 180 190
....*....|....*....|....*....|..
gi 518573420 138 LSGGQQQRVFLARALAQNAQLFCLDEPFVGID 169
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-174 |
5.13e-15 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 72.58 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFfeqpfkqvRKQIAYVPQrndLDWTFPIHV 92
Cdd:cd03291 46 CLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKH--------SGRISFSSQ---FSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 93 LDTVLLGT----YPKLGLIKRPKKEDRayayhcLEKVGMQDfaKRQIGE----LSGGQQQRVFLARALAQNAQLFCLDEP 164
Cdd:cd03291 115 KENIIFGVsydeYRYKSVVKACQLEED------ITKFPEKD--NTVLGEggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170
....*....|
gi 518573420 165 FVGIDMASEE 174
Cdd:cd03291 187 FGYLDVFTEK 196
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-197 |
5.57e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 21 ENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFK------QVRKQIAYVPQRNDLDWTFPIH-VL 93
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdAIRAGIMLCPEDRKAEGIIPVHsVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 94 DTVLLGT---YPKLGLIKRPKKEdRAYAYHCLEKVGMQDFAKRQ-IGELSGGQQQRVFLARALAQNAQLFCLDEPFVGID 169
Cdd:PRK11288 350 DNINISArrhHLRAGCLINNRWE-AENADRFIRSLNIKTPSREQlIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180
....*....|....*....|....*...
gi 518573420 170 MASEETMIRILKELRDEGKTILVVHHDL 197
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQGVAVLFVSSDL 456
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-197 |
6.35e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 6.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 12 VSYHgqDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIeKDQGDIRFFEQPFKQ--------VRKQIAYVPQRND 83
Cdd:PRK15134 296 VDHN--VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNlnrrqllpVRHRIQVVFQDPN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 84 LDWTFPIHVLDTVLLGT---YPKLGLIKRpkkEDRAYAyhCLEKVGMqDFAKRQ--IGELSGGQQQRVFLARALAQNAQL 158
Cdd:PRK15134 373 SSLNPRLNVLQIIEEGLrvhQPTLSAAQR---EQQVIA--VMEEVGL-DPETRHryPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518573420 159 FCLDEPFVGIDMASEETMIRILKELRDEGK-TILVVHHDL 197
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDL 486
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-213 |
6.35e-15 |
|
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: 70.26 E-value: 6.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEqpfkqvRKQIAYVPQRNdldwTFPIHVLDTVLLg 99
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE------GEDLLFLPQRP----YLPLGTLREQLI- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 100 tYPklglikrpkkedrayayhcLEKVgmqdfakrqigeLSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRI 179
Cdd:cd03223 86 -YP-------------------WDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170 180 190
....*....|....*....|....*....|....
gi 518573420 180 LKElrdEGKTILVVHHDlSKADDYFSHLVLLNKK 213
Cdd:cd03223 134 LKE---LGITVISVGHR-PSLWKFHDRVLDLDGE 163
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-196 |
9.14e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 9.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 21 ENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEqpfkQVrkQIAYVPQ-RNDLD-----WtfpiHV-- 92
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE----TV--KLAYVDQsRDALDpnktvW----EEis 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 93 --LDTVLLGtypklglikrpKKE--DRAYayhclekVGMQDFA----KRQIGELSGGQQQRVFLARALAQNAQLFCLDEP 164
Cdd:PRK11819 411 ggLDIIKVG-----------NREipSRAY-------VGRFNFKggdqQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
170 180 190
....*....|....*....|....*....|...
gi 518573420 165 FVGIDMaseETMiRILKE-LRDEGKTILVVHHD 196
Cdd:PRK11819 473 TNDLDV---ETL-RALEEaLLEFPGCAVVISHD 501
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-199 |
1.81e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIAY------VPQrnDLDW 86
Cdd:PRK09700 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAqlgigiIYQ--ELSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 87 TFPIHVLDTVLLGTYPK---LGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDE 163
Cdd:PRK09700 92 IDELTVLENLYIGRHLTkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 518573420 164 PFVGIDMASEETMIRILKELRDEGKTILVVHHDLSK 199
Cdd:PRK09700 172 PTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAE 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-201 |
1.95e-14 |
|
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: 72.35 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 16 GQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDI----RFFEQPFKQVRKQIAYVPQRNDL--DWTFP 89
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggKDIETNLDAVRQSLGMCPQHNILfhHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 90 IHVLdtvllgTYPKLGliKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGID 169
Cdd:TIGR01257 1022 EHIL------FYAQLK--GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190
....*....|....*....|....*....|..
gi 518573420 170 MASEETMIRILKELRdEGKTILVVHHDLSKAD 201
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYR-SGRTIIMSTHHMDEAD 1124
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-212 |
2.27e-14 |
|
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: 69.87 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIrffeqpfkQVRKQIAYVPQRN---DLDWTfpihVLDT 95
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV--------TVRGRVSSLLGLGggfNPELT----GREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 96 VLLgtypkLGLIK-RPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPF-VGiDMASE 173
Cdd:cd03220 105 IYL-----NGRLLgLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLaVG-DAAFQ 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 518573420 174 ETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK 212
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEK 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-214 |
2.91e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.81 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVR---------KQIAYVPQRNDLDWTfpI 90
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearaklraKHVGFVFQSFMLIPT--L 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 91 HVLDTVLLgtyPKLgLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDM 170
Cdd:PRK10584 104 NALENVEL---PAL-LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518573420 171 ASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLLNKKL 214
Cdd:PRK10584 180 QTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-218 |
3.17e-14 |
|
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: 68.81 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLkaclDLI--EKDQ----GDIRFFEQPFKQ-VRKQIAYVPQrndldwtFPIHV 92
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLL----DVLagRKTAgvitGEILINGRPLDKnFQRSTGYVEQ-------QDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 93 ldtvllgtyPKLGLIKrpkkedrAYAYHCLekvgmqdfakrqIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMAS 172
Cdd:cd03232 92 ---------PNLTVRE-------ALRFSAL------------LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518573420 173 EETMIRILKELRDEGKTILVVHHDLSKAD-DYFSHLVLLNK--KLVKAG 218
Cdd:cd03232 144 AYNIVRFLKKLADSGQAILCTIHQPSASIfEKFDRLLLLKRggKTVYFG 192
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-225 |
3.20e-14 |
|
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: 71.37 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 3 YALTIDRLYVSyhgqdALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDI--------------RFFEQpf 68
Cdd:TIGR03269 288 RYISVDRGVVK-----AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpGPDGR-- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 69 KQVRKQIAYVPQRNDLdwtFPiHvlDTVLLGTYPKLGLiKRPKKEDRAYAYHCLEKVGMQDFAKRQI-----GELSGGQQ 143
Cdd:TIGR03269 361 GRAKRYIGILHQEYDL---YP-H--RTVLDNLTEAIGL-ELPDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 144 QRVFLARALAQNAQLFCLDEPFVGIDMASEETMIR-ILKELRDEGKTILVVHHDLSKADDYFSHLVLL-NKKLVKAGPVH 221
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMrDGKIVKIGDPE 513
|
....
gi 518573420 222 DILR 225
Cdd:TIGR03269 514 EIVE 517
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-225 |
7.00e-14 |
|
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: 70.48 E-value: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQD----ALENVSLSIQEGTMTGIIGPNGAGKS-TLLkACLDL----IEKDQGDIRFFEQ-----PFKQ 70
Cdd:COG4172 7 LSVEDLSVAFGQGGgtveAVKGVSFDIAAGETLALVGESGSGKSvTAL-SILRLlpdpAAHPSGSILFDGQdllglSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 71 VRK----QIAYVPQR-----NdldwtfPIH-----VLDTVLLgtypKLGLikrPKKEDRAYAYHCLEKVGMQDfAKRQIG 136
Cdd:COG4172 86 LRRirgnRIAMIFQEpmtslN------PLHtigkqIAEVLRL----HRGL---SGAAARARALELLERVGIPD-PERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 137 ----ELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSHLVLLN 211
Cdd:COG4172 152 ayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMR 231
|
250
....*....|....*
gi 518573420 212 K-KLVKAGPVHDILR 225
Cdd:COG4172 232 QgEIVEQGPTAELFA 246
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-225 |
7.60e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.96 E-value: 7.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 21 ENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDL----IEKDQGDIRFFEQPF--KQVR-KQIAYVPQ--RNDLDwtfPIH 91
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVapCALRgRKIATIMQnpRSAFN---PLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 92 VLDTVLLGTYPKLGlikrpKKEDRAYAYHCLEKVGMQDfAKRQIG----ELSGGQQQRVFLARALAQNAQLFCLDEPFVG 167
Cdd:PRK10418 97 TMHTHARETCLALG-----KPADDATLTAALEAVGLEN-AARVLKlypfEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518573420 168 IDMASEETMIRILKEL-RDEGKTILVVHHDLSK----ADDYfshLVLLNKKLVKAGPVHDILR 225
Cdd:PRK10418 171 LDVVAQARILDLLESIvQKRALGMLLVTHDMGVvarlADDV---AVMSHGRIVEQGDVETLFN 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-218 |
1.40e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.60 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKST---LLKACLD----LIEKDQGDIRffEQPFKQVRKQIAYVPQRNDLdwtFPIH 91
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTlinLLQRVFDpqsgRILIDGTDIR--TVTRASLRRNIAVVFQDAGL---FNRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 92 VLDTVLLGtypklglikRPKKEDrAYAYHCLEKVGMQDFAKRQ-------IGE----LSGGQQQRVFLARALAQNAQLFC 160
Cdd:PRK13657 425 IEDNIRVG---------RPDATD-EEMRAAAERAQAHDFIERKpdgydtvVGErgrqLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 161 LDEPFVGIDMASEETMIRILKELRdEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAG 218
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRNADRILVFDNGRVVESG 551
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-216 |
2.14e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.38 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLdliekdqGDIRFFEQPFKQVRKQIAYVPQrndLDWTFPIHVLDTVLLG 99
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAML-------GELPPRSDASVVIRGTVAYVPQ---VSWIFNATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 100 TypKLGLIKRPKKEDRAYAYHCLEKVGMQDFAkrQIGE----LSGGQQQRVFLARALAQNAQLFCLDEPFVGIDM-ASEE 174
Cdd:PLN03130 703 S--PFDPERYERAIDVTALQHDLDLLPGGDLT--EIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQ 778
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518573420 175 TMIRILK-ELRdeGKT-ILVVH--HDLSKADdyfsHLVLLNKKLVK 216
Cdd:PLN03130 779 VFDKCIKdELR--GKTrVLVTNqlHFLSQVD----RIILVHEGMIK 818
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-196 |
2.26e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 12 VSYH--GQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFfeqpfkQVRKQIAYVPQ-RNDLDwtf 88
Cdd:PRK11147 325 VNYQidGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC------GTKLEVAYFDQhRAELD--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 89 PIH-VLDTVLLGtypklglikrpKKE------DRayayHCLEKvgMQDF------AKRQIGELSGGQQQRVFLARALAQN 155
Cdd:PRK11147 396 PEKtVMDNLAEG-----------KQEvmvngrPR----HVLGY--LQDFlfhpkrAMTPVKALSGGERNRLLLARLFLKP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518573420 156 AQLFCLDEPFVGIDMaseETMiRILKELRDEGK-TILVVHHD 196
Cdd:PRK11147 459 SNLLILDEPTNDLDV---ETL-ELLEELLDSYQgTVLLVSHD 496
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-196 |
2.36e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.52 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 22 NVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQV---RKQIAYVPQRNDLdwtFP-IHVLDTVL 97
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVppaERGVGMVFQSYAL---YPhLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 98 LGtypkLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETM- 176
Cdd:PRK11000 98 FG----LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMr 173
|
170 180
....*....|....*....|
gi 518573420 177 IRILKELRDEGKTILVVHHD 196
Cdd:PRK11000 174 IEISRLHKRLGRTMIYVTHD 193
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-204 |
2.89e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 68.81 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 3 YALTIDRLYVSYHGQDA-LENVSLSIQEGTMTGIIGPNGAGKSTLLK--ACLDlieKD-QGDIRFfeQP-FKqvrkqIAY 77
Cdd:TIGR03719 3 YIYTMNRVSKVVPPKKEiLKDISLSFFPGAKIGVLGLNGAGKSTLLRimAGVD---KDfNGEARP--QPgIK-----VGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRNDLDWTfpIHVLDTVLLGTYPKLGLIKRpkkEDRAYAYHCLEKVGMQDFAKRQ----------------------- 134
Cdd:TIGR03719 73 LPQEPQLDPT--KTVRENVEEGVAEIKDALDR---FNEISAKYAEPDADFDKLAAEQaelqeiidaadawdldsqleiam 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 135 -----------IGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELrdEGKTILVVHhdlskaDDY 203
Cdd:TIGR03719 148 dalrcppwdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVAVTH------DRY 219
|
.
gi 518573420 204 F 204
Cdd:TIGR03719 220 F 220
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-196 |
5.33e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.99 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQpfkqvrKQIAYVPQ--- 80
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN------ANIGYYAQdha 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 ---RNDLD-------WTFPIHvLDTVLLGTYPKLgLIKrpkkedrayayhclekvgmQDFAKRQIGELSGGQQQRVFLAR 150
Cdd:PRK15064 393 ydfENDLTlfdwmsqWRQEGD-DEQAVRGTLGRL-LFS-------------------QDDIKKSVKVLSGGEKGRMLFGK 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518573420 151 ALAQNAQLFCLDEPFVGIDMASEETMIRILKELrdEGkTILVVHHD 196
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMESIESLNMALEKY--EG-TLIFVSHD 494
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
13-232 |
5.45e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIAY------VPQRNDLdw 86
Cdd:PRK15439 20 QYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHqlgiylVPQEPLL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 87 tFP-IHVLDTVLlgtypkLGLIKRPKKEDRAYAYhcLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPF 165
Cdd:PRK15439 98 -FPnLSVKENIL------FGLPKRQASMQKMKQL--LAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 166 VGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHL-VLLNKKLVKAGPVHDiLRPEVMLQA 232
Cdd:PRK15439 169 ASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRIsVMRDGTIALSGKTAD-LSTDDIIQA 235
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-225 |
1.22e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 66.30 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQD----ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLI-----------EKDQGDIRFFEQPFK 69
Cdd:PRK11022 4 LNVDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgrvmaeklEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 70 Q--VRKQIAYVPQRndldwtfPIHVLDTVLLGTYPKLGLIKR----PKKEDRAYAYHCLEKVGMQDFAKR---QIGELSG 140
Cdd:PRK11022 84 RnlVGAEVAMIFQD-------PMTSLNPCYTVGFQIMEAIKVhqggNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 141 GQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKADDYFSH-LVLLNKKLVKAG 218
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKiIVMYAGQVVETG 236
|
....*..
gi 518573420 219 PVHDILR 225
Cdd:PRK11022 237 KAHDIFR 243
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-212 |
2.15e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.72 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRF------FEQPFKqvR-KQIAYVPQrnDldwtfPih 91
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIdgkdvtKLPEYK--RaKYIGRVFQ--D-----P-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 92 vldtvLLGTYP----------------KLGLIKRPKKEDRAYAYHCLEKVGM--QDFAKRQIGELSGGQQQRVFLARALA 153
Cdd:COG1101 90 -----MMGTAPsmtieenlalayrrgkRRGLRRGLTKKRRELFRELLATLGLglENRLDTKVGLLSGGQRQALSLLMATL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 154 QNAQLFCLDEPFVGIDMASEETMIRILKELRDEGK-TILVVHHDLSKADDYFSHLVLLNK 212
Cdd:COG1101 165 TKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHE 224
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-196 |
3.74e-12 |
|
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: 63.82 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLlkaCLDLIEKdQGDIRFFEQPFKQVRKQIAYVPqRNDLDW------------- 86
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL---AFDTIYA-EGQRRYVESLSAYARQFLGQMD-KPDVDSieglspaiaidqk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 87 TFPIHVLDTVllGT-----------YPKLGLIKRPKKedrayayhcLEKVGMQDFA-KRQIGELSGGQQQRVFLARALAQ 154
Cdd:cd03270 86 TTSRNPRSTV--GTvteiydylrllFARVGIRERLGF---------LVDVGLGYLTlSRSAPTLSGGEAQRIRLATQIGS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518573420 155 N--AQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHD 196
Cdd:cd03270 155 GltGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD 198
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-212 |
3.76e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 63.44 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKAC---LDLIEKDQGDIRF----FEQPFKQVRKQIAYVPQRndlDWTFP-IH 91
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYngipYKEFAEKYPGEIIYVSEE---DVHFPtLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 92 VLDTVllgtypklglikrpkkedrayayhclekvgmqDFAKRQIGE-----LSGGQQQRVFLARALAQNAQLFCLDEPFV 166
Cdd:cd03233 100 VRETL--------------------------------DFALRCKGNefvrgISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518573420 167 GIDMASEETMIRILKELRDEGKTILVVhhDLSKADD----YFSHLVLLNK 212
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFV--SLYQASDeiydLFDKVLVLYE 195
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-196 |
4.02e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 17 QDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEK--DQGDIRFFEQPFKQVRKQIAYVPQRNDLDWTfpIHVLD 94
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGtpVAGCVDVPDNQFGREASLIDAIGRKGDFKDA--VELLN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 95 TVLLGTypklglikrpkkedrAYAYhclekvgmqdfaKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGID-MASE 173
Cdd:COG2401 121 AVGLSD---------------AVLW------------LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrQTAK 173
|
170 180
....*....|....*....|....
gi 518573420 174 ETMIRILKELRDEGKTILVV-HHD 196
Cdd:COG2401 174 RVARNLQKLARRAGITLVVAtHHY 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-237 |
4.17e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.04 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 24 SLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRF-FEQP----FKQVRKQIAYVPQRNDLDWTFPIH------V 92
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSqFSHItrlsFEQLQKLVSDEWQRNNTDMLSPGEddtgrtT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 93 LDTVLLGTypklglikrpKKEDRAYAYHclEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMAS 172
Cdd:PRK10938 103 AEIIQDEV----------KDPARCEQLA--QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 173 EETMIRILKELRDEGKTILVVHHDLSKADDYFSHL-VLLNKKLVKAGPVHDILRPEVMLQ-AYETQL 237
Cdd:PRK10938 171 RQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAgVLADCTLAETGEREEILQQALVAQlAHSEQL 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-221 |
5.56e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.22 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKAcLDLIEK-DQGDIRFFEQPF--------KQVRKQIAYVPQrNDLDWTFP 89
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARL-LTMIETpTGGELYYQGQDLlkadpeaqKLLRQKIQIVFQ-NPYGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 90 IHVLDTVLlgTYPKLGLIKRPKKEDRAYAYHCLEKVGMQ-DFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGI 168
Cdd:PRK11308 108 RKKVGQIL--EEPLLINTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518573420 169 DMASEETMIRILKELRDEGKTILV-VHHDLSK----ADD----YFSHLVLL-NKKLVKAGPVH 221
Cdd:PRK11308 186 DVSVQAQVLNLMMDLQQELGLSYVfISHDLSVvehiADEvmvmYLGRCVEKgTKEQIFNNPRH 248
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
37-194 |
6.51e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.94 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 37 GPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQ--IAYVPQ----RNDLDWTFPIHVLDTvLLGTYPKlgliKRP 110
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSrfMAYLGHlpglKADLSTLENLHFLCG-LHGRRAK----QMP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 111 KkedrayayHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILK-ELRDEGKT 189
Cdd:PRK13543 119 G--------SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISaHLRGGGAA 190
|
....*
gi 518573420 190 ILVVH 194
Cdd:PRK13543 191 LVTTH 195
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
5-221 |
9.68e-12 |
|
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: 62.66 E-value: 9.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACL--DLIEKDQGDIRFFEQ------PFKQVRKQIA 76
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQdllelePDERARAGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 77 YVPQrndldwtFPIH---VLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQ------DFAKRQIGE-LSGGQQQRV 146
Cdd:TIGR01978 81 LAFQ-------YPEEipgVSNLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLAlldmdeEFLNRSVNEgFSGGEKKRN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 147 FLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHH-----DLSKADdyFSHlVLLNKKLVKAGPVH 221
Cdd:TIGR01978 154 EILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHyqrllNYIKPD--YVH-VLLDGRIVKSGDVE 230
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-225 |
1.28e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 63.39 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIeKDQGDI---RFF-----------EQPFKQVRKQIAYV---PQR 81
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGIT-KDNWHVtadRFRwngidllklspRERRKIIGREIAMIfqePSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 NdLDWTFPI-HVLDTVLLGTYPKLGLIKRpKKEDRAYAYHCLEKVGMQDFakRQI-----GELSGGQQQRVFLARALAQN 155
Cdd:COG4170 101 C-LDPSAKIgDQLIEAIPSWTFKGKWWQR-FKWRKKRAIELLHRVGIKDH--KDImnsypHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518573420 156 AQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKaddyFSHL-----VLLNKKLVKAGPVHDILR 225
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLES----ISQWadtitVLYCGQTVESGPTEQILK 248
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-212 |
2.50e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.97 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKD--QGDIRFFE-QPFKQVRKQIAYVPQRndlDWTFP-IHVLDT 95
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNrKPTKQILKRTGFVTQD---DILYPhLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 96 VLLgtypkLGLIKRP----KKEDRAYAYHCLEKVGMQDFAKRQIGE-----LSGGQQQRVFLARALAQNAQLFCLDEPFV 166
Cdd:PLN03211 161 LVF-----CSLLRLPksltKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518573420 167 GIDMASEETMIRILKELRDEGKTILV-VHHDLSKADDYFSHLVLLNK 212
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSE 282
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
13-206 |
3.42e-11 |
|
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: 62.51 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 13 SYHGQD-----ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPfkqvrkqiayVPQRNdLDW- 86
Cdd:COG4615 336 RYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP----------VTADN-REAy 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 87 ---------TFpiHVLDTvLLGtypklglIKRPKKEDRAYAYhcLEKVGMQD--------FAKRqigELSGGQQQRVFLA 149
Cdd:COG4615 405 rqlfsavfsDF--HLFDR-LLG-------LDGEADPARAREL--LERLELDHkvsvedgrFSTT---DLSQGQRKRLALL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 150 RALAQNAQLFCLDEpfvgidMAS-----------EEtmirILKELRDEGKTILVVHHDlskaDDYFSH 206
Cdd:COG4615 470 VALLEDRPILVFDE------WAAdqdpefrrvfyTE----LLPELKARGKTVIAISHD----DRYFDL 523
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-186 |
3.89e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.34 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 18 DALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP-------FKQVRKQIAYVPQRNDLDWTFPI 90
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlhfgdysYRSQRIRMIFQDPSTSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 91 -HVLDTVL-LGTYpklglIKRPKKEDRAYAyhCLEKVGM-QDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVG 167
Cdd:PRK15112 107 sQILDFPLrLNTD-----LEPEQREKQIIE--TLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170
....*....|....*....
gi 518573420 168 IDMASEETMIRILKELRDE 186
Cdd:PRK15112 180 LDMSMRSQLINLMLELQEK 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-244 |
5.29e-11 |
|
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: 62.27 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRF-----FEQPFKQVRKQIAYVPQrndldwtfpihvlD 94
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdglniAKIGLHDLRFKITIIPQ-------------D 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 95 TVLLGTYPKLGLIKRPKKEDRAyAYHCLEKVGMQDFAKRQI----------GE-LSGGQQQRVFLARALAQNAQLFCLDE 163
Cdd:TIGR00957 1369 PVLFSGSLRMNLDPFSQYSDEE-VWWALELAHLKTFVSALPdkldhecaegGEnLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 164 PFVGIDMASEEtMIRILKELRDEGKTILVVHHDLSKADDYfSHLVLLNKklvkaGPVHDILRPEVMLQAYETQLPFLKSA 243
Cdd:TIGR00957 1448 ATAAVDLETDN-LIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDK-----GEVAEFGAPSNLLQQRGIFYSMAKDA 1520
|
.
gi 518573420 244 G 244
Cdd:TIGR00957 1521 G 1521
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-197 |
6.01e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 22 NVSLSIQEGTMTGIIGPNGAGKsTLLKACL-----------DLIEKDQGDIRffeQPFKQVRKQIAYVPQRNDLDWTFPI 90
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGR-TELVQCLfgaypgrwegeIFIDGKPVKIR---NPQQAIAQGIAMVPEDRKRDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 91 ----HVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRqIGELSGGQQQRVFLARALAQNAQLFCLDEPFV 166
Cdd:PRK13549 356 mgvgKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELA-IARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190
....*....|....*....|....*....|.
gi 518573420 167 GIDMASEETMIRILKELRDEGKTILVVHHDL 197
Cdd:PRK13549 435 GIDVGAKYEIYKLINQLVQQGVAIIVISSEL 465
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-197 |
7.45e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 9 RLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQ------IAYVPQ-- 80
Cdd:PRK10762 257 RLKVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangIVYISEdr 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 81 -RNDLdwtfpihVLD---------TVLLGTYPKLGLIKrpkkedrayayHCLEKVGMQDFAK----------RQIGELSG 140
Cdd:PRK10762 337 kRDGL-------VLGmsvkenmslTALRYFSRAGGSLK-----------HADEQQAVSDFIRlfniktpsmeQAIGLLSG 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 141 GQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDL 197
Cdd:PRK10762 399 GNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEM 455
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-197 |
7.47e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 22 NVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ------VRKQIAYVP---QRNDLDWTFPIHv 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlstaqrLARGLVYLPedrQSSGLYLDAPLA- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 93 LDTVLLgTYPKLGLIKRPKKEDRAYA-YHCLEKVGMQDfAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMA 171
Cdd:PRK15439 360 WNVCAL-THNRRGFWIKPARENAVLErYRRALNIKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180
....*....|....*....|....*.
gi 518573420 172 SEETMIRILKELRDEGKTILVVHHDL 197
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVLFISSDL 463
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-197 |
7.47e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.89 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQD----ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKD---QGDIRFFEQ-----PFKQVR 72
Cdd:PRK09473 13 LDVKDLRVTFSTPDgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGReilnlPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 73 K----QIAYVPQRndldwtfPIHVLDTvllgtYPKLG-----LIKRPKKEDRAYAYHclEKVGMQDF-----AKRQIG-- 136
Cdd:PRK09473 93 KlraeQISMIFQD-------PMTSLNP-----YMRVGeqlmeVLMLHKGMSKAEAFE--ESVRMLDAvkmpeARKRMKmy 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518573420 137 --ELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKT-ILVVHHDL 197
Cdd:PRK09473 159 phEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDL 222
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-208 |
1.14e-10 |
|
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: 58.74 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 27 IQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIrffEQPfkqvRKQIAYVPQRNDLdwtfpihvldtvllgtypklgl 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND---EWD----GITPVYKPQYIDL---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 107 ikrpkkedrayayhclekvgmqdfakrqigelSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDE 186
Cdd:cd03222 73 --------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|...
gi 518573420 187 G-KTILVVHHDLSKAdDYFSHLV 208
Cdd:cd03222 121 GkKTALVVEHDLAVL-DYLSDRI 142
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-212 |
2.09e-10 |
|
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: 60.41 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQD--ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDI----RFFEQPFKQVRKQIAYV 78
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDAtvagKSILTNISDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRNDLDwtfpihvldtVLLGTYPKLGLIKR----PKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQ 154
Cdd:TIGR01257 2018 PQFDAID----------DLLTGREHLYLYARlrgvPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 155 NAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNK 212
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVK 2145
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-194 |
2.82e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.92 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSY--HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDqGDIR-----FFEQPFKQVRKQIAY 77
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQidgvsWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRndldwTFpihvldtVLLGTYPK-LGLIKRPKKEDrayAYHCLEKVGMQ----------DFAKRQIGE-LSGGQQQR 145
Cdd:TIGR01271 1297 IPQK-----VF-------IFSGTFRKnLDPYEQWSDEE---IWKVAEEVGLKsvieqfpdklDFVLVDGGYvLSNGHKQL 1361
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518573420 146 VFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVH 194
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEH 1410
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-200 |
5.21e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.01 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQIAYVPQRNDL 84
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 85 ---DWTFpIHvldtvllgTYPKLGLikRPK-------------------KEDRAYAYHCLEKVgmqDFAKRQIGEL---- 138
Cdd:PRK11701 87 lrtEWGF-VH--------QHPRDGL--RMQvsaggnigerlmavgarhyGDIRATAGDWLERV---EIDAARIDDLpttf 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518573420 139 SGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDLSKA 200
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVA 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-225 |
5.98e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQ----DALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGD---------------IRFFE 65
Cdd:PRK10261 13 LAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdkmllrrrsrqvIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 66 QPFKQVRK----QIAYVPQR--NDLDWTFPI--HVLDTVLLgtYPKLGlikrpKKEDRAYAYHCLEKVGM---QDFAKRQ 134
Cdd:PRK10261 93 QSAAQMRHvrgaDMAMIFQEpmTSLNPVFTVgeQIAESIRL--HQGAS-----REEAMVEAKRMLDQVRIpeaQTILSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 135 IGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDE-GKTILVVHHDLSKADDYFSH-LVLLNK 212
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRvLVMYQG 245
|
250
....*....|...
gi 518573420 213 KLVKAGPVHDILR 225
Cdd:PRK10261 246 EAVETGSVEQIFH 258
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-194 |
6.15e-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: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSY--HGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDqGDIR-----FFEQPFKQVRKQIAY 77
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQidgvsWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRndldwTFpihvldtVLLGTYPKlGLIKRPKKEDRAYaYHCLEKVGMQDFAKRQIGE-----------LSGGQQQRV 146
Cdd:cd03289 82 IPQK-----VF-------IFSGTFRK-NLDPYGKWSDEEI-WKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLM 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518573420 147 FLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVH 194
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEH 195
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-220 |
6.49e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 6.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKAcldLIEKD-----QGDIRFFEQPFKQ--VRKQIAYVpQRNDldwtfpIH- 91
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNV---LAERVttgviTGGDRLVNGRPLDssFQRSIGYV-QQQD------LHl 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 92 ----VLDTVLLGTY---PKlgliKRPKKEDRAYAYHCLEKVGMQDFAKRQIGE----LSGGQQQRVFLARALAQNAQLFC 160
Cdd:TIGR00956 849 ptstVRESLRFSAYlrqPK----SVSKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLL 924
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 161 -LDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLSkAD--DYFSHLVLLNK--KLVKAGPV 220
Cdd:TIGR00956 925 fLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPS-AIlfEEFDRLLLLQKggQTVYFGDL 988
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-229 |
8.12e-10 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 58.69 E-value: 8.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 133 RQIGELSGGQQQRVFLARALAqnAQLF----CLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDlskaddyfSHLV 208
Cdd:PRK00635 472 RALATLSGGEQERTALAKHLG--AELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD--------EQMI 541
|
90 100
....*....|....*....|.
gi 518573420 209 LLNKKLVKAGPVHDILRPEVM 229
Cdd:PRK00635 542 SLADRIIDIGPGAGIFGGEVL 562
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-218 |
1.52e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.57 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 2 SYALTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKA-----CLDLIEkdqGDIRFFEQ------PFKQ 70
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKViaghpAYKILE---GDILFKGEsildlePEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 71 VRKQIAyvpqrndLDWTFPIHV--------LDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQD-FAKRQIGE-LSG 140
Cdd:CHL00131 82 AHLGIF-------LAFQYPIEIpgvsnadfLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPsFLSRNVNEgFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 141 GQQQR-VFLARALAqNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHH-----DLSKADdyFSHlVLLNKKL 214
Cdd:CHL00131 155 GEKKRnEILQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqrllDYIKPD--YVH-VMQNGKI 230
|
....
gi 518573420 215 VKAG 218
Cdd:CHL00131 231 IKTG 234
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-226 |
1.66e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.19 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 22 NVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQVRKQ---------IAYVPQRNDLdwtFPiH- 91
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclppekrrIGYVFQDARL---FP-Hy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 92 -VLDTVLLGTypklglikrpKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDM 170
Cdd:PRK11144 92 kVRGNLRYGM----------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518573420 171 ASEETMIRILKELRDEGKT-ILVVHHDLSK----ADdyfsHLVLLNKKLVKA-GPV-----HDILRP 226
Cdd:PRK11144 162 PRKRELLPYLERLAREINIpILYVSHSLDEilrlAD----RVVVLEQGKVKAfGPLeevwaSSAMRP 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-196 |
1.95e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLK--ACLDlieKD-QGDIRFfeQP-FKqvrkqIAYVPQRNDLDWTFPihVLDT 95
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRimAGVD---KEfEGEARP--APgIK-----VGYLPQEPQLDPEKT--VREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 96 VLLGTYPKLGLIKRpkkEDRAYAYHCLEKVGMQDFAKRQ----------------------------------IGELSGG 141
Cdd:PRK11819 91 VEEGVAEVKAALDR---FNEIYAAYAEPDADFDALAAEQgelqeiidaadawdldsqleiamdalrcppwdakVTKLSGG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 142 QQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELrdEGkTILVVHHD 196
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY--PG-TVVAVTHD 219
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-197 |
2.19e-09 |
|
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: 54.67 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 29 EGTMTGIIGPNGAGKSTLLKAcldliekdqgdirffeqpfkqvrkqIAYVpqrndldwtfpihvldtvLLGTYPKLglik 108
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDA-------------------------IGLA------------------LGGAQSAT---- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 109 RPKKEDRAYAYHCLEKVGMQDFakrqIGELSGGQQQRVFLARALA----QNAQLFCLDEPFVGIDMASEETMIRILKELR 184
Cdd:cd03227 53 RRRSGVKAGCIVAAVSAELIFT----RLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHL 128
|
170
....*....|...
gi 518573420 185 DEGKTILVVHHDL 197
Cdd:cd03227 129 VKGAQVIVITHLP 141
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-225 |
2.44e-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: 57.33 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 133 RQIGELSGGQQQRVFLARALAQN--AQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHD---LSKADdyfsHL 207
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDedtIRAAD----YV 559
|
90 100
....*....|....*....|....*
gi 518573420 208 VLLNKK-------LVKAGPVHDILR 225
Cdd:TIGR00630 560 IDIGPGagehggeVVASGTPEEILA 584
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
12-206 |
3.03e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 12 VSYHGQD---ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPF-----KQVRKQIAYVpqrnd 83
Cdd:PRK10522 328 VTFAYQDngfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtaeqpEDYRKLFSAV----- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 84 ldwtFPIHVLDTVLLGtypklglikrPKKE--DRAYAYHCLEKVGMQDFAKRQIGE-----LSGGQQQRVFLARALAQNA 156
Cdd:PRK10522 403 ----FTDFHLFDQLLG----------PEGKpaNPALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518573420 157 QLFCLDEPfvgidMASEETMIR------ILKELRDEGKTILVVHHDlskaDDYFSH 206
Cdd:PRK10522 469 DILLLDEW-----AADQDPHFRrefyqvLLPLLQEMGKTIFAISHD----DHYFIH 515
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-230 |
4.19e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQPFKQ-----VRKQIAYVPQRndldwtfPIHVLD 94
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgltdLRRVLSIIPQS-------PVLFSG 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 95 TVLLGTYPKlglikrpKKEDRAYAYHCLEKVGMQDFAKR-------QIGE----LSGGQQQRVFLARALAQNAQLFCLDE 163
Cdd:PLN03232 1325 TVRFNIDPF-------SEHNDADLWEALERAHIKDVIDRnpfgldaEVSEggenFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518573420 164 PFVGIDMASEETmirILKELRDEGK--TILVVHHDLSKADDYFSHLVLlnkklvKAGPVHDILRPEVML 230
Cdd:PLN03232 1398 ATASVDVRTDSL---IQRTIREEFKscTMLVIAHRLNTIIDCDKILVL------SSGQVLEYDSPQELL 1457
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-196 |
6.29e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 55.62 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 4 ALTIDRLYVSYHG-QDALENVSLSIQEGTMTGIIGPNGAGKSTLLK--ACLDLIEKdqGDIRFFEQPFKQVR---KQIAY 77
Cdd:PRK11650 3 GLKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRmvAGLERITS--GEIWIGGRVVNELEpadRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQRNDLdwtfpihvldtvllgtYPKL--------GLIKR--PKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVF 147
Cdd:PRK11650 81 VFQNYAL----------------YPHMsvrenmayGLKIRgmPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518573420 148 LARALAQNAQLFCLDEPFVGIDMASEETMiRI-LKEL-RDEGKTILVVHHD 196
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLDAKLRVQM-RLeIQRLhRRLKTTSLYVTHD 194
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
9-228 |
7.26e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.13 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 9 RLYVSYHGQ-DALENVSLSIQEGTMTGIIGPNGAGKST-LLKACLDLIEKDQGDIRFFE--QPFKQVRKQIA-YVPQRND 83
Cdd:NF000106 17 RGLVKHFGEvKAVDGVDLDVREGTVLGVLGP*GAA**RgALPAHV*GPDAGRRPWRF*TwcANRRALRRTIG*HRPVR*G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 84 LDWTFPIHVlDTVLLGTYPKLGlikrpKKEDRAYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDE 163
Cdd:NF000106 97 RRESFSGRE-NLYMIGR*LDLS-----RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518573420 164 PFVGIDMASEETMIRILKELRDEGKTILVVHHDLSKADDYFSHLVLLNKKLVKAGPVHDILRPEV 228
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKV 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-231 |
1.03e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQG-------DIRFFEqpFKQVRKQIAYVPQRndldwtfPIHV 92
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGrilidgcDISKFG--LMDLRKVLGIIPQA-------PVLF 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 93 LDTVLLGTYPKlglikrpKKEDRAYAYHCLEKVGMQDFAKR----------QIGE-LSGGQQQRVFLARALAQNAQLFCL 161
Cdd:PLN03130 1326 SGTVRFNLDPF-------NEHNDADLWESLERAHLKDVIRRnslgldaevsEAGEnFSVGQRQLLSLARALLRRSKILVL 1398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518573420 162 DEPFVGIDMaseETMIRILKELRDEGK--TILVVHHDLSKADDYFSHLVLlnkklvKAGPVHDILRPEVMLQ 231
Cdd:PLN03130 1399 DEATAAVDV---RTDALIQKTIREEFKscTMLIIAHRLNTIIDCDRILVL------DAGRVVEFDTPENLLS 1461
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
137-203 |
1.11e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.16 E-value: 1.11e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518573420 137 ELSGGQQQRVFLARALAQNAQ---LFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLS--KADDY 203
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDviKCADW 240
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
133-196 |
4.37e-08 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 53.49 E-value: 4.37e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 133 RQIGELSGGQQQRVFLARALAqnAQL----FCLDEPFVGI---DMaseETMIRILKELRDEGKTILVVHHD 196
Cdd:COG0178 481 RSAGTLSGGEAQRIRLATQIG--SGLvgvlYVLDEPSIGLhqrDN---DRLIETLKRLRDLGNTVIVVEHD 546
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-224 |
4.69e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.88 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDlIEKDQ----------GDIRFFEQPFKQVRKQIAY-------VPQr 81
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNwrvtadrmrfDDIDLLRLSPRERRKLVGHnvsmifqEPQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 NDLDwtfPIHVLDTVLLGTYP----------KLGLIKRpkkedraYAYHCLEKVGMQDFaKRQIG----ELSGGQQQRVF 147
Cdd:PRK15093 100 SCLD---PSERVGRQLMQNIPgwtykgrwwqRFGWRKR-------RAIELLHRVGIKDH-KDAMRsfpyELTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 148 LARALAQNAQLFCLDEPFVGIDMASEETMIRILKEL-RDEGKTILVVHHDL---SKADDYFShlVLLNKKLVKAGPVHDI 223
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLqmlSQWADKIN--VLYCGQTVETAPSKEL 246
|
.
gi 518573420 224 L 224
Cdd:PRK15093 247 V 247
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-196 |
5.07e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRF---------------FEQP-----------FKQVRK 73
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgnwqlawvnqetpaLPQPaleyvidgdreYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 74 QIAYVPQRNDLDWTFPIH-VLDTVLLGTYpklglikrpkkedRAYAYHCLEKVGM-QDFAKRQIGELSGGQQQRVFLARA 151
Cdd:PRK10636 97 QLHDANERNDGHAIATIHgKLDAIDAWTI-------------RSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518573420 152 LAQNAQLFCLDEPFVGIDMaseETMIRILKELRDEGKTILVVHHD 196
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDL---DAVIWLEKWLKSYQGTLILISHD 205
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-210 |
8.95e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 18 DALENVSLSIQEGTMTGIIGPNGAGKSTLLKAC---LD--LIEKDqGDIRF----FEQPFKQVRKQIAYVPQrndLDWTF 88
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasnTDgfHIGVE-GVITYdgitPEEIKKHYRGDVVYNAE---TDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 89 PI----HVLDTVLLGTYPKLglikRPKKEDR-AYAYHCLE--------------KVGmQDFakrqIGELSGGQQQRVFLA 149
Cdd:TIGR00956 151 PHltvgETLDFAARCKTPQN----RPDGVSReEYAKHIADvymatyglshtrntKVG-NDF----VRGVSGGERKRVSIA 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518573420 150 RALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGK-TILVVHHDLS-KADDYFSHLVLL 210
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDtTPLVAIYQCSqDAYELFDKVIVL 284
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-203 |
9.46e-08 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 52.34 E-value: 9.46e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 138 LSGGQQQRVFLARALAQNAQ---LFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLS--KADDY 203
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDviKTADW 897
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-198 |
1.06e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKacldLIEKDQG--DIRF-FEQPFKQVRKQIAyvPQR 81
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK----ILNGEVLldDGRIiYEQDLIVARLQQD--PPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 82 NDLDWTFPI----------------HVLDtvLLGTYPKLGLIKRPKK-------------EDRAYayHCLEKVGMQdfAK 132
Cdd:PRK11147 78 NVEGTVYDFvaegieeqaeylkryhDISH--LVETDPSEKNLNELAKlqeqldhhnlwqlENRIN--EVLAQLGLD--PD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518573420 133 RQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDegkTILVVHHDLS 198
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFISHDRS 214
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-203 |
1.49e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.94 E-value: 1.49e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518573420 138 LSGGQQQRVFLARALAQNAQ---LFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLS--KADDY 203
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDviKTADY 900
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-193 |
1.68e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 17 QDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFF------EQPFKQVRKQIAYVPQRN-------D 83
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHgkkinnHNANEAINHGFALVTEERrstgiyaY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 84 LDWTFP--IHVLDTVLlgtyPKLGLIKRPK-KEDRAYAYHCLE-KVGMQdfaKRQIGELSGGQQQRVFLARALAQNAQLF 159
Cdd:PRK10982 341 LDIGFNslISNIRNYK----NKVGLLDNSRmKSDTQWVIDSMRvKTPGH---RTQIGSLSGGNQQKVIIGRWLLTQPEIL 413
|
170 180 190
....*....|....*....|....*....|....
gi 518573420 160 CLDEPFVGIDMASEETMIRILKELRDEGKTILVV 193
Cdd:PRK10982 414 MLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII 447
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
7-204 |
2.11e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.91 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 7 IDRLYV----SYHgqdalENVSLSIQEGtMTGIIGPNGAGKSTLLKACLDLIEKDQgdirffeqpfkqvrkqiayvPQRN 82
Cdd:cd03240 1 IDKLSIrnirSFH-----ERSEIEFFSP-LTLIVGQNGAGKTTIIEALKYALTGEL--------------------PPNS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 83 DLDWTFPiHVLDTVLLGTYPKLGLIKRPKKEDRAY-AYHCLEKV------GMQDFAKRQIGELSGGQQQ------RVFLA 149
Cdd:cd03240 55 KGGAHDP-KLIREGEVRAQVKLAFENANGKKYTITrSLAILENVifchqgESNWPLLDMRGRCSGGEKVlasliiRLALA 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 150 RALAQNAQLFCLDEPFVGIDMAS-EETMIRILKELR-DEGKTILVVHHD---LSKADDYF 204
Cdd:cd03240 134 ETFGSNCGILALDEPTTNLDEENiEESLAEIIEERKsQKNFQLIVITHDeelVDAADHIY 193
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
33-196 |
3.96e-07 |
|
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: 49.19 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 33 TGIIGPNGAGKSTLLKA-CLDLIEKDQGDIRFfeqpfKQVRKQIAYVPQRNDLDWTFPIHvldtvllgtyPKLGLIKRPK 111
Cdd:cd03279 31 FLICGPTGAGKSTILDAiTYALYGKTPRYGRQ-----ENLRSVFAPGEDTAEVSFTFQLG----------GKKYRVERSR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 112 KED----RAYAYhcLEKVGMQDFAKRQIGELSGGQQQRVFLARALA-----QNA-----QLFCLDEPFVGIDMASEETMI 177
Cdd:cd03279 96 GLDydqfTRIVL--LPQGEFDRFLARPVSTLSGGETFLASLSLALAlsevlQNRggarlEALFIDEGFGTLDPEALEAVA 173
|
170
....*....|....*....
gi 518573420 178 RILKELRDEGKTILVVHHD 196
Cdd:cd03279 174 TALELIRTENRMVGVISHV 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-198 |
1.48e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 21 ENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDI------RFFEQPFKQVRKQIAYVPQ---------RNDLD 85
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshNLKDINLKWWRSKIGVVSQdpllfsnsiKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 86 WT-FPIHVLDTV-------------------------------LLGTYPKLGLIKRPKKE---DRAYAYHCLEKVGMQDF 130
Cdd:PTZ00265 482 YSlYSLKDLEALsnyynedgndsqenknkrnscrakcagdlndMSNTTDSNELIEMRKNYqtiKDSEVVDVSKKVLIHDF 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 131 AK-----------RQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELR-DEGKTILVVHHDLS 198
Cdd:PTZ00265 562 VSalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLS 641
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
136-193 |
2.00e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 2.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 518573420 136 GELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVV 193
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI 460
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-218 |
2.01e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLK--ACLDLIEKDQGDIRFfeqpfkQVRKQIAYVPQRN 82
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSAtlAGREDYEVTGGTVEF------KGKDLLELSPEDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 83 D-----LDWTFPIH---VLDTVLLGTypKLGLIKRPKKEDRayayhcLEKVGMQDFAKRQIGEL---------------S 139
Cdd:PRK09580 76 AgegifMAFQYPVEipgVSNQFFLQT--ALNAVRSYRGQEP------LDRFDFQDLMEEKIALLkmpedlltrsvnvgfS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 140 GGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHH-----DLSKADdyFSHlVLLNKKL 214
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHyqrilDYIKPD--YVH-VLYQGRI 224
|
....
gi 518573420 215 VKAG 218
Cdd:PRK09580 225 VKSG 228
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-195 |
2.08e-06 |
|
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: 48.21 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 16 GQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIrffeqpFKQVRKQIAYVPQRndldwtfPIHVL-- 93
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL------TKPAKGKLFYVPQR-------PYMTLgt 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 94 --DTVLlgtYP--KLGLIKRPKKEDRAYAYhcLEKVGMQDFAKRQIG---------ELSGGQQQRVFLARALAQNAQLFC 160
Cdd:TIGR00954 531 lrDQII---YPdsSEDMKRRGLSDKDLEQI--LDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*..
gi 518573420 161 LDE--PFVGIDMasEETMIRILKELrdeGKTILVVHH 195
Cdd:TIGR00954 606 LDEctSAVSVDV--EGYMYRLCREF---GITLFSVSH 637
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-198 |
2.23e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 2.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518573420 138 LSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRILKELRDEG-KTILVVHHDLS 198
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIA 1420
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-196 |
2.52e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 21 ENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIrffeqpFKQVRKQIAYVPQrndldwtfpiHVLDTVLLGT 100
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVRMAVFSQ----------HHVDGLDLSS 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 101 YPKLGLIK----RPKKEDRAYayhcLEKVGMQ-DFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEET 175
Cdd:PLN03073 590 NPLLYMMRcfpgVPEQKLRAH----LGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEA 665
|
170 180
....*....|....*....|.
gi 518573420 176 MIRILKELRDegkTILVVHHD 196
Cdd:PLN03073 666 LIQGLVLFQG---GVLMVSHD 683
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-220 |
3.71e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLL-----KACLDLIEkdqGDIRFFEQPFKQ-VRKQIAYVPQRNDLDwTFPIHVL 93
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMdvlagRKTGGYIE---GDIRISGFPKKQeTFARISGYCEQNDIH-SPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 94 DTVLLGTYpkLGLIKRPKKEDR-AYAYHCLEKVGMQDFAKRQIG-----ELSGGQQQRVFLARALAQNAQLFCLDEPFVG 167
Cdd:PLN03140 972 ESLIYSAF--LRLPKEVSKEEKmMFVDEVMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518573420 168 IDMASEETMIRILKELRDEGKTILVVHH----DLSKAddyFSHLVLLNK--KLVKAGPV 220
Cdd:PLN03140 1050 LDARAAAIVMRTVRNTVDTGRTVVCTIHqpsiDIFEA---FDELLLMKRggQVIYSGPL 1105
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
5-180 |
7.41e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 46.06 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHG--QDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDI-----RFFEQPFKQVRKQIAY 77
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIvidgiDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 78 VPQrndldwtfpihvlDTVLLGTYPKLGLIKRPKKEDRAYaYHCLEKVGMQDFAKRQIGEL-----------SGGQQQRV 146
Cdd:cd03288 100 ILQ-------------DPILFSGSIRFNLDPECKCTDDRL-WEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 165
|
170 180 190
....*....|....*....|....*....|....
gi 518573420 147 FLARALAQNAQLFCLDEPFVGIDMASEETMIRIL 180
Cdd:cd03288 166 CLARAFVRKSSILIMDEATASIDMATENILQKVV 199
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
138-197 |
9.12e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.22 E-value: 9.12e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518573420 138 LSGGQQQRVFLARALAQNAQ---LFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDL 197
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNL 893
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-171 |
9.95e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFEQP-----FKQVRKQIAYVPQRndldwtfPIHVLD 94
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREigaygLRELRRQFSMIPQD-------PVLFDG 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 95 TVLLGTYPKLglikrpkKEDRAYAYHCLEKVGMQDfakRQIGELSG--------------GQQQRVFLARALAQNAQLFC 160
Cdd:PTZ00243 1399 TVRQNVDPFL-------EASSAEVWAALELVGLRE---RVASESEGidsrvleggsnysvGQRQLMCMARALLKKGSGFI 1468
|
170
....*....|..
gi 518573420 161 L-DEPFVGIDMA 171
Cdd:PTZ00243 1469 LmDEATANIDPA 1480
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-202 |
1.10e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.29 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 30 GTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFFeqpfkqvrkqiayvpqrnDLDWTFPIHVLDTVLLGTYPKLglikr 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYI------------------DGEDILEEVLDQLLLIIVGGKK----- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 110 pkkedrayayhclekvgmqdfakrqiGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETMIRI------LKEL 183
Cdd:smart00382 59 --------------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrllLLLK 112
|
170
....*....|....*....
gi 518573420 184 RDEGKTILVVHHDLSKADD 202
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGP 131
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-206 |
1.95e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 5 LTIDRLYVSYHGQDALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDIRFfeqpFKQVRkqIAYVPQrndl 84
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----AKGIK--LGYFAQ---- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 85 dwtfpiHVLDTVLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQ-DFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDE 163
Cdd:PRK10636 383 ------HQLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDE 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518573420 164 PFVGIDMASEETMIRILKELrdEGkTILVVHHD----LSKADD-YFSH 206
Cdd:PRK10636 457 PTNHLDLDMRQALTEALIDF--EG-ALVVVSHDrhllRSTTDDlYLVH 501
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-196 |
2.03e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 21 ENVSLSIQEGTMTGIIGPNGAGKSTLLKA-CLDLiEKDQGDIrfFEQPFKQVRK----QIAYVPQRndldwtfpihVLDT 95
Cdd:PRK15064 18 ENISVKFGGGNRYGLIGANGCGKSTFMKIlGGDL-EPSAGNV--SLDPNERLGKlrqdQFAFEEFT----------VLDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 96 VLLGtYPKLGLIKrpKKEDRAYAY-HCLEKVGMQ------DF-------AKRQIGEL------------------SGGQQ 143
Cdd:PRK15064 85 VIMG-HTELWEVK--QERDRIYALpEMSEEDGMKvadlevKFaemdgytAEARAGELllgvgipeeqhyglmsevAPGWK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518573420 144 QRVFLARALAQNAQLFCLDEPFVGIDMASeetmIRILKE-LRDEGKTILVVHHD 196
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDvLNERNSTMIIISHD 211
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-219 |
2.30e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 133 RQIGELSGGQQQRVFLARAL---AQNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHDLskaddyfsHLVL 209
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM--------HVVK 876
|
90
....*....|
gi 518573420 210 LNKKLVKAGP 219
Cdd:PRK00635 877 VADYVLELGP 886
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
20-213 |
3.43e-05 |
|
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: 44.22 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 20 LENVSLSIQEGTMTgIIGPNGAGKSTLLKAcLDLIEKDQGDIRF---------------------FEQPFKQVRKQIAYV 78
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEA-LRLLLGPSSSRKFdeedfylgddpdlpeieieltFGSLLSRLLRLLLKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 79 PQRNDLDWTF------------PI-----HVLDTVLLGTYPKLGLIKRPKKEDRAYAyhcleKVGMQDFAKRQIGELSGG 141
Cdd:COG3593 92 EDKEELEEALeelneelkealkALnellsEYLKELLDGLDLELELSLDELEDLLKSL-----SLRIEDGKELPLDRLGSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 142 QQQRVFLA--RALAQNAQ-----LFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHD---LSKADdyFSHLVLLN 211
Cdd:COG3593 167 FQRLILLAllSALAELKRapanpILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSphlLSEVP--LENIRRLR 244
|
..
gi 518573420 212 KK 213
Cdd:COG3593 245 RD 246
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
133-196 |
6.39e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.91 E-value: 6.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518573420 133 RQIGELSGGQQQRVFLAralaqnAQ--------LFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHHD 196
Cdd:PRK00349 485 RSAGTLSGGEAQRIRLA------TQigsgltgvLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHD 550
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-203 |
1.00e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTL--LKACLDLIEKDQGDIrffeqpfKQVRKQIAYVPQRNDldwtfPIHVLDTV 96
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLsnLIAGVTMPNKGTVDI-------KGSAALIAISSGLNG-----QLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 97 LLGTYpKLGLIKRPKKEdraYAYHCLEKVGMQDFAKRQIGELSGGQQQRVFLARALAQNAQLFCLDEPFVGIDMASEETM 176
Cdd:PRK13545 107 ELKGL-MMGLTKEKIKE---IIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180
....*....|....*....|....*..
gi 518573420 177 IRILKELRDEGKTILVVHHDLSKADDY 203
Cdd:PRK13545 183 LDKMNEFKEQGKTIFFISHSLSQVKSF 209
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
132-182 |
1.98e-04 |
|
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: 39.14 E-value: 1.98e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518573420 132 KRQIGELSGGQQQRVF---LARALAQNAQLFC----------LDEPFVGIDMASEETMIRILKE 182
Cdd:pfam13558 27 YRRSGGLSGGEKQLLAylpLAAALAAQYGSAEgrppaprlvfLDEAFAKLDEENIRTALELLRA 90
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
33-197 |
2.28e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 33 TGIIGPNGAGKSTLLKAC-----------------------------LDL--------IEKDQGDIRFFEQPFKQVRKQI 75
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIryalygkarsrsklrsdlinvgseeasveLEFehggkryrIERRQGEFAEFLEAKPSERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 76 ayvpqrndldwtfpihvLDTvLLGTYPKLGLIKRPKKEDRAYAYHCLEKVGMQDFAKRQ---------IGELSGGQQqrv 146
Cdd:COG0419 106 -----------------LKR-LLGLEIYEELKERLKELEEALESALEELAELQKLKQEIlaqlsgldpIETLSGGER--- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518573420 147 fLARALAQNAQLFcLDepFVGIDMASEETMIRILKELRdegktilVVHHDL 197
Cdd:COG0419 165 -LRLALADLLSLI-LD--FGSLDEERLERLLDALEELA-------IITHVI 204
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
32-63 |
4.36e-04 |
|
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: 40.84 E-value: 4.36e-04
10 20 30
....*....|....*....|....*....|..
gi 518573420 32 MTGIIGPNGAGKSTLLKAcLDLIEKDQGDIRF 63
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEA-LRFLADFDALVIG 31
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
128-213 |
6.02e-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: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 128 QDFAKRQIGELSGGQQQRVFLARALA----------QNAQLFCLDEPFVGIDMASEETMIRILKELRDEGKTILVVHH-- 195
Cdd:TIGR00618 941 YTGSVRPSATLSGGETFLASLSLALAladllstsggTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHvp 1020
|
90
....*....|....*...
gi 518573420 196 DLSKAddyFSHLVLLNKK 213
Cdd:TIGR00618 1021 EFRER---IPHRILVKKT 1035
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
13-49 |
6.13e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.19 E-value: 6.13e-04
10 20 30
....*....|....*....|....*....|....*..
gi 518573420 13 SYHGQDalenvsLSIQEGTMTGIIGPNGAGKSTLLKA 49
Cdd:pfam13555 11 TFDGHT------IPIDPRGNTLLTGPSGSGKSTLLDA 41
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
21-72 |
2.30e-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: 37.83 E-value: 2.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 518573420 21 ENVSLSIQEGtMTGIIGPNGAGKSTLLKAcldliekdqgdIRFF--EQPFKQVR 72
Cdd:cd03278 14 DKTTIPFPPG-LTAIVGPNGSGKSNIIDA-----------IRWVlgEQSAKSLR 55
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
19-49 |
2.32e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.76 E-value: 2.32e-03
10 20 30
....*....|....*....|....*....|.
gi 518573420 19 ALENVSLSIqeGTMTGIIGPNGAGKSTLLKA 49
Cdd:COG4637 12 SLRDLELPL--GPLTVLIGANGSGKSNLLDA 40
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
7-65 |
2.50e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.44 E-value: 2.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518573420 7 IDRLYVS-YHGQDALEnVSLSIQEGtMTGIIGPNGAGKSTLLKA---CLDLIEKDQGDIRFFE 65
Cdd:COG3950 3 IKSLTIEnFRGFEDLE-IDFDNPPR-LTVLVGENGSGKTTLLEAialALSGLLSRLDDVKFRK 63
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
19-68 |
5.32e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 37.58 E-value: 5.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 518573420 19 ALENVSLSIQEGTMTgIIGPNGAGKSTLLKAcLDLIEKDqgDIRFFEQPF 68
Cdd:pfam13175 13 CLKDTEIDLDEDLTV-LIGKNNSGKSSILEA-LDIFLNN--KEKFFEDDF 58
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-61 |
5.98e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 37.10 E-value: 5.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 518573420 19 ALENVSLSIQEGTMTGIIGPNGAGKSTLLKACLDLIEKDQGDI 61
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
32-49 |
6.40e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 36.71 E-value: 6.40e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
122-207 |
8.60e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.12 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518573420 122 LEKVGM-QDFAKRQIGELSGGQQQRVFLARALAQNAQ--LFCLDEPFVGIDMASEETMIRILKELRDEGKTILVV--HHD 196
Cdd:PRK00635 1371 IDKVGLsYITLGQEQDTLSDGEHYRLHLAKKISSNLTdiIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATdrSGS 1450
|
90
....*....|.
gi 518573420 197 LSKADDYFSHL 207
Cdd:PRK00635 1451 LAEHADHLIHL 1461
|
|
| |
