|
Name |
Accession |
Description |
Interval |
E-value |
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-237 |
1.33e-117 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 335.52 E-value: 1.33e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVAYVEQRKD 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 81 LDLNFPINVFDVVLTGTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDE 160
Cdd:COG1121 86 VDWDFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 161 PFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIVDYGPTDQVYNAQNIERAFSADLSAV 237
Cdd:COG1121 166 PFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVLTPENLSRAYGGPVALL 242
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-215 |
6.35e-100 |
|
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: 289.82 E-value: 6.35e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 3 SIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVAYVEQRKDLD 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 83 LNFPINVFDVVLTGTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPF 162
Cdd:cd03235 81 RDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510996587 163 VGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIVDYG 215
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
3.30e-81 |
|
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: 243.80 E-value: 3.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-----RAVQKQVAYV 75
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslsrRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQrkDLDLNFPINVFDVVLTGTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEI 155
Cdd:COG1120 81 PQ--EPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 156 IILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNIERAF 230
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGrIVAQGPPEEVLTPELLEEVY 235
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-243 |
3.05e-63 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 198.57 E-value: 3.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY-DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQ--VAYVEQR 78
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKnlVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 KDLDLNFPINVFDVVLTGTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIIL 158
Cdd:PRK15056 87 EEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 159 DEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIVDYGPTDQVYNAQNIERAFSADLSAVL 238
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELAFSGVLRHVA 246
|
....*
gi 510996587 239 FEKQE 243
Cdd:PRK15056 247 LNGSE 251
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-202 |
1.25e-60 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 189.37 E-value: 1.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 10 AYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLyqgksmRAVQKQVAYVEQRKDLDLNFPINV 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------RAGGARVAYVPQRSEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 90 FDVVLTGTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQS 169
Cdd:NF040873 75 RDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|...
gi 510996587 170 ETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFD 202
Cdd:NF040873 155 RERIIALLAEEHARGATVVVVTHDLELVRRADP 187
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-230 |
5.75e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 183.73 E-value: 5.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR----AVQKQVAYVEQ 77
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVArdpaEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RKDLDLNfpinvfdvvLTGT-----YGklGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQE 152
Cdd:COG1131 81 EPALYPD---------LTVRenlrfFA--RLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 153 AEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYnAQNIERAF 230
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGrIVADGTPDELK-ARLLEDVF 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-215 |
1.09e-57 |
|
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: 181.09 E-value: 1.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 3 SIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK-----SMRAVQKQVAYVEQ 77
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 rkdldlnfpinvfdvvltgtygklglfrdpgkqakaasraALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:cd03214 81 ----------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 158 LDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYG 215
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGrIVAQG 180
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-224 |
2.18e-57 |
|
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: 181.97 E-value: 2.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 25 DAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVAYVEQRKDLDLNFPINVFDVVLTGTYGKLGLF 104
Cdd:TIGR03771 4 DKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRTGHIGWL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 105 RDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAG 184
Cdd:TIGR03771 84 RRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELAGAG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 510996587 185 KTIIVIHHDLNKVSQYFDDLVVMNHGIVDYGPTDQVYNAQ 224
Cdd:TIGR03771 164 TAILMTTHDLAQAMATCDRVVLLNGRVIADGTPQQLQDPA 203
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-235 |
1.11e-56 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 181.47 E-value: 1.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKS-----------MRAVQ 69
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPlaawspwelarRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 70 KQVAyveqrkdlDLNFPINVFDVVLTGTYGklglFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAI 149
Cdd:COG4559 81 PQHS--------SLAFPFTVEEVVALGRAP----HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 150 VQ-------EAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVY 221
Cdd:COG4559 149 AQlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGrLVAQGTPEEVL 228
|
250
....*....|....
gi 510996587 222 NAQNIERAFSADLS 235
Cdd:COG4559 229 TDELLERVYGADLR 242
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-221 |
3.37e-55 |
|
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: 176.75 E-value: 3.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY-DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG-----KSMRAVQKQVAYV 75
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRKDLDLNFPInVFDVVltgTYG--KLGLfrdPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEA 153
Cdd:COG1122 81 FQNPDDQLFAPT-VEEDV---AFGpeNLGL---PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 154 EIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVY 221
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGrIVADGTPREVF 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-234 |
2.36e-51 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 167.64 E-value: 2.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK-----------SMRAVQ 69
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspaelaRRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 70 KQVAyveqrkdlDLNFPINVFDVVLTGTYGklglFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAI 149
Cdd:PRK13548 82 PQHS--------SLSFPFTVEEVVAMGRAP----HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 150 VQEAE------IIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVY 221
Cdd:PRK13548 150 AQLWEpdgpprWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGrLVADGTPAEVL 229
|
250
....*....|...
gi 510996587 222 NAQNIERAFSADL 234
Cdd:PRK13548 230 TPETLRRVYGADV 242
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-210 |
7.83e-51 |
|
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: 164.95 E-value: 7.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 3 SIKNLTVAYDD--TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQ-----KQVAYV 75
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlkelrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRKDLDLnFPINVFDVVLTGtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEI 155
Cdd:cd03225 81 FQNPDDQF-FGPTVEEEVAFG----LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 156 IILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-220 |
1.04e-50 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 165.62 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY-DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG--------KSMRAVQKQ 71
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGqdvtalrgRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 72 VAYVEQrkDLDLNFPINVFDVVLTGTYGKLG----LFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVAR 147
Cdd:COG3638 82 IGMIFQ--QFNLVPRLSVLTNVLAGRLGRTStwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 148 AIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQV 220
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGrVVFDGPPAEL 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-234 |
1.11e-50 |
|
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: 165.42 E-value: 1.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG----KSMRAVQKQVAYVE 76
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 QRKDLDLNfpinvfdvvLTGT-----YGKLglFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQ 151
Cdd:COG4555 81 DERGLYDR---------LTVReniryFAEL--YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 152 EAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNA---QNIE 227
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGkVVAQGSLDELREEigeENLE 229
|
....*..
gi 510996587 228 RAFSADL 234
Cdd:COG4555 230 DAFVALI 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-233 |
1.32e-50 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 165.64 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-----RAVQKQVAYV 75
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVattpsRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQrkDLDLNFPINVFDVVLTGTY----GKLglfrdpGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQ 151
Cdd:COG4604 81 RQ--ENHINSRLTVRELVAFGRFpyskGRL------TAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 152 EAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNIERA 229
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCYADHIVAMKDGrVVAQGTPEEIITPEVLSDI 232
|
....
gi 510996587 230 FSAD 233
Cdd:COG4604 233 YDTD 236
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-193 |
6.65e-50 |
|
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: 162.26 E-value: 6.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR----AVQKQVAYVE 76
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRdareDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 QRKDLDLNfpinvfdvvLTGT-----YGKLglfrDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQ 151
Cdd:COG4133 82 HADGLKPE---------LTVRenlrfWAAL----YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510996587 152 EAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHD 193
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-233 |
9.93e-50 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 163.65 E-value: 9.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK-----SMRAVQKQVAYV 75
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRkdldLNFP--INVFDVVltgTYGK---LGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIV 150
Cdd:PRK11231 82 PQH----HLTPegITVRELV---AYGRspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 151 QEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNIERA 229
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGhVMAQGTPEEVMTPGLLRTV 234
|
....
gi 510996587 230 FSAD 233
Cdd:PRK11231 235 FDVE 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
1.40e-49 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 169.70 E-value: 1.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVH---FD--AGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK--------SMRA 67
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVRAVDdvsLTlrRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklsrrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 68 VQKQVAYVEQRKDLDLNFPINVFDVVLTGtygkLGLFRD-PGKQAKAASRAALEQVALG-DFERRQIGQLSGGQLQRVFV 145
Cdd:COG1123 340 LRRRVQMVFQDPYSSLNPRMTVGDIIAEP----LRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 146 ARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDA-GKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNA 223
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGrIVEDGPTEEVFAN 495
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-223 |
2.66e-47 |
|
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: 156.57 E-value: 2.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY-DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVL--------YQGKSMRAVQKQV 72
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinkLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 73 AYVEQrkDLDLNFPINVFDVVLTGTYGKL----GLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARA 148
Cdd:cd03256 81 GMIFQ--QFNLIERLSVLENVLSGRLGRRstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 149 IVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNA 223
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGrIVFDGPPAELTDE 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-212 |
3.19e-46 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 153.06 E-value: 3.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV---QKQVAYVEQR 78
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVppeRRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 KDLdlnFP-INVFDVVLTGtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:cd03259 81 YAL---FPhLTVAENIAFG----LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 158 LDEPFVGIDLQSETAIMAIMKQ-WRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIV 212
Cdd:cd03259 154 LDEPLSALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
2-237 |
6.66e-46 |
|
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: 153.82 E-value: 6.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK-----SMRAVQKQVAYVE 76
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVdlhglSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 QRKDLDLnfPINVFDVVLTGTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEII 156
Cdd:TIGR03873 82 QDSDTAV--PLTVRDVVALGRIPHRSLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 157 ILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNIERAFSADLS 235
Cdd:TIGR03873 160 LLDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGrVVAAGPPREVLTPALIRAVYGVDAT 239
|
..
gi 510996587 236 AV 237
Cdd:TIGR03873 240 VL 241
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-212 |
3.64e-45 |
|
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: 149.08 E-value: 3.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM----RAVQKQVAYVEQ 77
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkkepEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 rkdlDLNFPINvfdvvLTGtygklglfrdpgkqakaasraaleqvalgdferRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:cd03230 81 ----EPSLYEN-----LTV---------------------------------RENLKLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 158 LDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIV 212
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-232 |
1.49e-44 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 154.23 E-value: 1.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK-----SMRAVQKQVAYV 75
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQrkDLDLNFPINVFDVVLTGTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEI 155
Cdd:PRK09536 83 PQ--DTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510996587 156 IILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVM-NHGIVDYGPTDQVYNAQNIERAFSA 232
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLaDGRVRAAGPPADVLTADTLRAAFDA 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
2.04e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 155.83 E-value: 2.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFD--AGKITGIIGPNGAGKSTLIKAILGLVKAR---QGSVLYQGKSMRAV-----QK 70
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTiaPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELsealrGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 71 QVAYVEQRKDLDLNfPINVFDVVLTGtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIV 150
Cdd:COG1123 84 RIGMVFQDPMTQLN-PVTVGDQIAEA----LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 151 QEAEIIILDEPFVGIDLQSETAIMAIMKQ-WRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNA 223
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIADRVVVMDDGrIVEDGPPEEILAA 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-220 |
2.07e-44 |
|
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: 149.12 E-value: 2.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM------RAVQKQVAYV 75
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglpphEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRKDLdlnFP-INVFDVVLTGTYGKLGL------FRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARA 148
Cdd:cd03219 81 FQIPRL---FPeLTVLENVMVAAQARTGSglllarARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996587 149 IVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG--IVDyGPTDQV 220
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGrvIAE-GTPDEV 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-235 |
8.43e-44 |
|
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: 147.92 E-value: 8.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLV-KARQGSVLYQGK-----SMRAVQKQVAY 74
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGErrggeDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQrkDLDLNFP--INVFDVVLTGTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQE 152
Cdd:COG1119 83 VSP--ALQLRFPrdETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 153 AEIIILDEPFVGIDLQSETAIMAIMKQWRDAG-KTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNIERAF 230
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGrVVAAGPKEEVLTSENLSEAF 240
|
....*
gi 510996587 231 SADLS 235
Cdd:COG1119 241 GLPVE 245
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-220 |
2.82e-43 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 146.49 E-value: 2.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY----DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-----RAVQKQ 71
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtrrrrKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 72 VAYVEQRKDLDLNFPINVFDVVLTGtygkLGLFRDPGKQAKAAsrAALEQVALG-DFERRQIGQLSGGQLQRVFVARAIV 150
Cdd:COG1124 81 VQMVFQDPYASLHPRHTVDRILAEP----LRIHGLPDREERIA--ELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510996587 151 QEAEIIILDEPFVGIDLQSETAIMAIMKQWR-DAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQV 220
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGrIVEELTVADL 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-194 |
7.74e-43 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 144.54 E-value: 7.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDD----TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVAYVEQ 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RkdlDLNFP-INVFDVVLTGtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEII 156
Cdd:cd03293 81 Q---DALLPwLTVLDNVALG----LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 510996587 157 ILDEPFVGIDLQSETAIMA-IMKQWRDAGKTIIVIHHDL 194
Cdd:cd03293 154 LLDEPFSALDALTREQLQEeLLDIWRETGKTVLLVTHDI 192
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-194 |
3.30e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 144.08 E-value: 3.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY----DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVAYVE 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 QRkdlDLNFP-INVFDVVLTGtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEI 155
Cdd:COG1116 87 QE---PALLPwLTVLDNVALG----LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 510996587 156 IILDEPFVGID------LQSEtaimaIMKQWRDAGKTIIVIHHDL 194
Cdd:COG1116 160 LLMDEPFGALDaltrerLQDE-----LLRLWQETGKTVLFVTHDV 199
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-210 |
3.34e-42 |
|
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: 140.84 E-value: 3.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 3 SIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMravqkqvayveqrkdld 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 83 lnfpinvfdvvltgtygklglfrdpgkqAKAASRAALEQVALgdferrqIGQLSGGQLQRVFVARAIVQEAEIIILDEPF 162
Cdd:cd00267 64 ----------------------------AKLPLEELRRRIGY-------VPQLSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510996587 163 VGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-220 |
5.96e-42 |
|
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: 142.19 E-value: 5.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRA------VQKQVAYV 75
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlppherARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRKDLdlnFP-INVFDVVLTGTYGKlglfrdpgkqAKAASRAALEQV-----ALGDFERRQIGQLSGGQLQRVFVARAI 149
Cdd:cd03224 81 PEGRRI---FPeLTVEENLLLGAYAR----------RRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996587 150 VQEAEIIILDEPFVGI--DLQSEtaIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQV 220
Cdd:cd03224 148 MSRPKLLLLDEPSEGLapKIVEE--IFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGrVVLEGTAAEL 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
1.34e-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: 149.14 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDD-TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV-----QKQVAYV 75
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLdpaswRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRKDLdlnFPINVFDVVLTGtygklglfrdpgkqAKAAS----RAALEQVALGDFERR-------QIG----QLSGGQL 140
Cdd:COG4988 417 PQNPYL---FAGTIRENLRLG--------------RPDASdeelEAALEAAGLDEFVAAlpdgldtPLGeggrGLSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 141 QRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRdAGKTIIVIHHDLNKVSQYfDDLVVMNHG-IVDYGPTDQ 219
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQA-DRILVLDDGrIVEQGTHEE 557
|
....*
gi 510996587 220 VYNAQ 224
Cdd:COG4988 558 LLAKN 562
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-215 |
2.68e-41 |
|
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: 140.72 E-value: 2.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDD----TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKS--------MRAV 68
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 69 QKQVAYVEQRKDLDLNFPINVFDVVLTGtygkLGLFRDPGKQAKAASRAALEQVALG---DFERRQIGQLSGGQLQRVFV 145
Cdd:cd03257 81 RKEIQMVFQDPMSSLNPRMTIGEQIAEP----LRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510996587 146 ARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDA-GKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYG 215
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGkIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-225 |
7.80e-40 |
|
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: 137.42 E-value: 7.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKS--------MRAVQKQV 72
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitglsekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 73 AYVEQRKDL--DLnfpiNVFDVVLtgtygkLGL---FRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVAR 147
Cdd:COG1127 85 GMLFQGGALfdSL----TVFENVA------FPLrehTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 148 AIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDA-GKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQN 225
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGkIIAEGTPEELLASDD 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-222 |
1.40e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 139.85 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV---QKQVAYVEQ 77
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppeKRNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 rkDLDLnFP-INVFDVVltgTYGkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEII 156
Cdd:COG3842 85 --DYAL-FPhLTVAENV---AFG-LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 157 ILDEPFVGID------LQSEtaIMAIMKQwrdAGKTIIVIHHDLNK---VSqyfDDLVVMNHG-IVDYGPTDQVYN 222
Cdd:COG3842 158 LLDEPLSALDaklreeMREE--LRRLQRE---LGITFIYVTHDQEEalaLA---DRIAVMNDGrIEQVGTPEEIYE 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-230 |
4.50e-39 |
|
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: 135.49 E-value: 4.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM------RAVQKQVAY 74
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglpphRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRKDLdlnFP-INVFDVVLTGTYgklglfrdpGKQAKAASRAALEQV-----ALGDFERRQIGQLSGGQLQRVFVARA 148
Cdd:COG0410 83 VPEGRRI---FPsLTVEENLLLGAY---------ARRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 149 IVQEAEIIILDEPFVGI--DLQSEtaIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQN 225
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLapLIVEE--IFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGrIVLEGTAAELLADPE 228
|
....*
gi 510996587 226 IERAF 230
Cdd:COG0410 229 VREAY 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-237 |
8.68e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 136.39 E-value: 8.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-RAVQKQVAYV-EQR 78
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLdPEDRRRIGYLpEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 ---KDLdlnfpiNVFDVVLtgtY-GKL-GLfrdPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRV-FVArAIVQE 152
Cdd:COG4152 81 glyPKM------KVGEQLV---YlARLkGL---SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVqLIA-ALLHD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 153 AEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQV---YNAQNIER 228
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGrKVLSGSVDEIrrqFGRNTLRL 227
|
....*....
gi 510996587 229 AFSADLSAV 237
Cdd:COG4152 228 EADGDAGWL 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-210 |
1.17e-38 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 132.12 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDT--PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK-----SMRAVQKQVAY 74
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQrkdldlnfpinvfDVVL-TGTygklglfrdpgkqakaasraaleqvalgdferrqIGQ--LSGGQLQRVFVARAIVQ 151
Cdd:cd03228 81 VPQ-------------DPFLfSGT----------------------------------IREniLSGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 152 EAEIIILDEPFVGIDLQSETAIMAIMKQWRDaGKTIIVIHHDLNKVsQYFDDLVVMNHG 210
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-210 |
1.28e-38 |
|
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: 141.06 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDT--PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR-----AVQKQVAY 74
Cdd:COG4987 334 LELEDVSFRYPGAgrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdldedDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRkdldlnfpINVFDvvltGTYG---KLGlfrDPGkqakaAS----RAALEQVALGDFERRQ-------IG----QLS 136
Cdd:COG4987 414 VPQR--------PHLFD----TTLRenlRLA---RPD-----ATdeelWAALERVGLGDWLAALpdgldtwLGeggrRLS 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996587 137 GGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWrDAGKTIIVIHHDLNKVSQyFDDLVVMNHG 210
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLER-MDRILVLEDG 545
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-210 |
2.91e-37 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 130.01 E-value: 2.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGkITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG----KSMRAVQKQVAYVEQ 77
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RKDLDLNFPinVFDVVltgTYGKLgLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:cd03264 80 EFGVYPNFT--VREFL---DYIAW-LKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510996587 158 LDEPFVGIDLQSETAIMAIMKQwRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSE-LGEDRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-225 |
4.49e-37 |
|
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: 130.31 E-value: 4.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKS--------MRAVQKQVA 73
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglseaeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 74 YVEQRKDL--DLN------FPINVFdvvltgtygklglFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFV 145
Cdd:cd03261 81 MLFQSGALfdSLTvfenvaFPLREH-------------TRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 146 ARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDA-GKTIIVIHHDLN---KVSQYFddLVVMNHGIVDYGPTDQVY 221
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDtafAIADRI--AVLYDGKIVAEGTPEELR 225
|
....
gi 510996587 222 NAQN 225
Cdd:cd03261 226 ASDD 229
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-224 |
7.23e-37 |
|
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: 130.11 E-value: 7.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY-DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLY--------QGKSMRAVQKQ 71
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLegtditklRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 72 VAYVEQrkDLDLNFPINVFDVVLTGTYGKL----GLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVAR 147
Cdd:TIGR02315 81 IGMIFQ--HYNLIERLTVLENVLHGRLGYKptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 148 AIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQ 224
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAGeIVFDGAPSELDDEV 237
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-210 |
7.35e-37 |
|
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: 129.15 E-value: 7.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDD----TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM---------RAV 68
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsekelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 69 QKQVAYVEQRKDLdLNFpINVFDVVLTGtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARA 148
Cdd:cd03255 81 RRHIGFVFQSFNL-LPD-LTALENVELP----LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510996587 149 IVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDlNKVSQYFDDLVVMNHG 210
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDG 216
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-222 |
8.09e-37 |
|
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: 130.65 E-value: 8.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYD-DTP----VFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLY--------QGKSMRAV 68
Cdd:TIGR04521 1 IKLKNVSYIYQpGTPfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIdgrditakKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 69 QKQVAYVEQrkdldlnFP------INVFDVVLtgtYG--KLGLfrdPGKQAKAASRAALEQVALGD-------FErrqig 133
Cdd:TIGR04521 81 RKKVGLVFQ-------FPehqlfeETVYKDIA---FGpkNLGL---SEEEAEERVKEALELVGLDEeylerspFE----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 134 qLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-I 211
Cdd:TIGR04521 143 -LSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGkI 221
|
250
....*....|.
gi 510996587 212 VDYGPTDQVYN 222
Cdd:TIGR04521 222 VLDGTPREVFS 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-232 |
4.13e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.56 E-value: 4.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVhfDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV---QKQVAYVEQ 77
Cdd:COG3840 1 MLRLDDLTYRYGDFPLRFDLTI--AAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppaERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RKDLdlnFP-INVFDVVltgtygklGLFRDPG----KQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQE 152
Cdd:COG3840 79 ENNL---FPhLTVAQNI--------GLGLRPGlkltAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 153 AEIIILDEPFVGID--LQSEtaIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIVDY-GPTDQVYNAQNIEr 228
Cdd:COG3840 148 RPILLLDEPFSALDpaLRQE--MLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAAdGPTAALLDGEPPP- 224
|
....
gi 510996587 229 AFSA 232
Cdd:COG3840 225 ALAA 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-210 |
4.28e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.85 E-value: 4.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQ-----KQVAYVE 76
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppewrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 QRKDL-------DLNFPinvfdvvltgtygkLGLFRDPGKQAKAasRAALEQVALG-DFERRQIGQLSGGQLQRVFVARA 148
Cdd:COG4619 81 QEPALwggtvrdNLPFP--------------FQLRERKFDRERA--LELLERLGLPpDILDKPVERLSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510996587 149 IVQEAEIIILDEPFVGIDLQSETAIMAIMKQWR-DAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREYLaEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
5.24e-36 |
|
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: 134.58 E-value: 5.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY--DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR-----AVQKQVAY 74
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqidpaSLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQrkdldlnfpinvfDVVL-TGT-YGKLGLFRDPGKQAKAasRAALEQVALGDFERR-------QIG----QLSGGQLQ 141
Cdd:COG2274 554 VLQ-------------DVFLfSGTiRENITLGDPDATDEEI--IEAARLAGLHDFIEAlpmgydtVVGeggsNLSGGQRQ 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 142 RVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRdAGKTIIVIHHDLNKVsQYFDDLVVMNHG-IVDYGPTDQV 220
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTI-RLADRIIVLDKGrIVEDGTHEEL 696
|
....
gi 510996587 221 YNAQ 224
Cdd:COG2274 697 LARK 700
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
5.63e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 127.08 E-value: 5.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDD----TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-------RAV- 68
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsereLARl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 69 -QKQVAYVEQRKDLdlnFP-INVFD-VVLTGTYGKLglfrdPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFV 145
Cdd:COG1136 84 rRRHIGFVFQFFNL---LPeLTALEnVALPLLLAGV-----SRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510996587 146 ARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLnKVSQYFDDLVVMNHGIV 212
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-215 |
5.67e-36 |
|
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: 126.63 E-value: 5.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR-AVQKQVAYVEQRKD 80
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 81 LDLNfpINVFDVVLtgtYgkLGLFRD-PGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILD 159
Cdd:cd03269 81 LYPK--MKVIDQLV---Y--LAQLKGlKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 160 EPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYG 215
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGrAVLYG 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-210 |
5.72e-36 |
|
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: 125.76 E-value: 5.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVayVEQRKDL 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL--PPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 82 DLnfpinVFDvvltgtygKLGLFRdpgkqakaaSRAALEQVALGdferrqigqLSGGQLQRVFVARAIVQEAEIIILDEP 161
Cdd:cd03229 79 GM-----VFQ--------DFALFP---------HLTVLENIALG---------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510996587 162 FVGIDLQSETAIMAIMKQWRD-AGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-220 |
8.57e-36 |
|
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: 127.46 E-value: 8.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM------RAVQKQVAY 74
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQR----KDLDlnfpinVFDVVLTGTYGKLG------LFRDPG-----KQAKAASRAALEQVALGDFERRQIGQLSGGQ 139
Cdd:COG0411 84 TFQNprlfPELT------VLENVLVAAHARLGrgllaaLLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 140 LQRVFVARAIVQEAEIIILDEPFVGIDlQSETA-IMAIMKQWRDA-GKTIIVIHHDLNKVSQYFDDLVVMNHG--IVDyG 215
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLN-PEETEeLAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGrvIAE-G 235
|
....*
gi 510996587 216 PTDQV 220
Cdd:COG0411 236 TPAEV 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-200 |
9.08e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 126.32 E-value: 9.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY-DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQ-KQVAYVEQR 78
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 -----------KDLdlnfpiNVFDVV-----LTGTygklglfrdPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQR 142
Cdd:COG2884 81 igvvfqdfrllPDR------TVYENValplrVTGK---------SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 143 VFVARAIVQEAEIIILDEPFVGIDlqSETA--IMAIMKQWRDAGKTIIVIHHDLNKVSQY 200
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLD--PETSweIMELLEEINRRGTTVLIATHDLELVDRM 203
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
1.65e-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: 126.16 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDT----PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG--------KSMRAV 68
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 69 QKQVAYVEQRKDLdLNFPiNVFDVVltgTYgKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARA 148
Cdd:cd03258 81 RRRIGMIFQHFNL-LSSR-TVFENV---AL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 149 IVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNA 223
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGeVVEEGTVEEVFAN 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-210 |
9.29e-35 |
|
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: 123.52 E-value: 9.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 3 SIKNLTVAY-DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK--SMRAVQKQVAYVEQRK 79
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpiKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 DLDLnFPINVFDVVLtgtygkLGLFRDPGKQAKAasRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILD 159
Cdd:cd03226 81 DYQL-FTDSVREELL------LGLKELDAGNEQA--ETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510996587 160 EPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-223 |
2.31e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.03 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK---SMRAVQK-QVAYVEQ 77
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlfTNLPPRErRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RKDLdlnFP-INVFDVVLTGtygkLGLfRDPGKQAKAAsRAA--LEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAE 154
Cdd:COG1118 83 HYAL---FPhMTVAENIAFG----LRV-RPPSKAEIRA-RVEelLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 155 IIILDEPFVGIDLQSETAIMAIMKQ-WRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNA 223
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRlHDELGGTTVFVTHDQEEALELADRVVVMNQGrIEQVGTPDEVYDR 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-163 |
2.68e-34 |
|
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: 120.45 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 17 FTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-----RAVQKQVAYVEQrkDLDLNFPINVFD 91
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderKSLRKEIGYVFQ--DPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 92 VVLTGtyGKLGLFRDPGKQAKAAsrAALEQVALGDFE----RRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFV 163
Cdd:pfam00005 79 NLRLG--LLLKGLSKREKDARAE--EALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-246 |
4.76e-34 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 122.64 E-value: 4.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAyddtPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKArQGSVLYQGKSMRAVQKQV-----AYVE 76
Cdd:COG4138 1 LQLNDVAVA----GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAElarhrAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 QRKdlDLNFPINVFDVvltgtygkLGLFRdPGKQAKAASRAALEQVA----LGDFERRQIGQLSGGQLQRVFVARAIVQ- 151
Cdd:COG4138 76 QQQ--SPPFAMPVFQY--------LALHQ-PAGASSEAVEQLLAQLAealgLEDKLSRPLTQLSGGEWQRVRLAAVLLQv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 152 ------EAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQ 224
Cdd:COG4138 145 wptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGkLVASGETAEVMTPE 224
|
250 260
....*....|....*....|..
gi 510996587 225 NIERAFsadlsAVLFEKQEVDQ 246
Cdd:COG4138 225 NLSEVF-----GVKFRRLEVEG 241
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-222 |
5.53e-34 |
|
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: 121.96 E-value: 5.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV---QKQVAYVEQR 78
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLpphKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 KDLdlnFP-INVFDVVLTGtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:cd03300 81 YAL---FPhLTVFENIAFG----LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 158 LDEPFVGIDLQ-SETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYN 222
Cdd:cd03300 154 LDEPLGALDLKlRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGkIQQIGTPEEIYE 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-229 |
7.80e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 122.02 E-value: 7.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG-------KSMRAVQKQVA 73
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedltdskKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 74 YVEQRKDLdlnFP-INVFDVVltgTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQE 152
Cdd:COG1126 81 MVFQQFNL---FPhLTVLENV---TLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 153 AEIIILDEPFVGID--LQSEtaIMAIMKQWRDAGKTIIVIHHDLN---KVSqyfDDLVVMNHG-IVDYGPTDQVYNAQNI 226
Cdd:COG1126 155 PKVMLFDEPTSALDpeLVGE--VLDVMRDLAKEGMTMVVVTHEMGfarEVA---DRVVFMDGGrIVEEGPPEEFFENPQH 229
|
...
gi 510996587 227 ERA 229
Cdd:COG1126 230 ERT 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-220 |
5.89e-33 |
|
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: 119.21 E-value: 5.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQ-----GSVLYQGKSMRAVQ------- 69
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 70 KQVAYVEQRKDLdlnFPINVFDVVltgTYG-KLGLFRdPGKQAKAASRAALEQVALGD-FERRQIG-QLSGGQLQRVFVA 146
Cdd:cd03260 81 RRVGMVFQKPNP---FPGSIYDNV---AYGlRLHGIK-LKEELDERVEEALRKAALWDeVKDRLHAlGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 147 RAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAgKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQV 220
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGrLVEFGPTEQI 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-223 |
1.63e-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: 118.60 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK---SMRAVQKQVAYVEQRKD 80
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatDVPVQERNVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 81 LdlnFP-INVFDVVLTGTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILD 159
Cdd:cd03296 85 L---FRhMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 160 EPFVGIDLQSETAIMAIMKQWRD-AGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNA 223
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDeLHVTTVFVTHDQEEALEVADRVVVMNKGrIEQVGTPDEVYDH 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-223 |
2.81e-32 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 119.77 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYD-DTPVFT---DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKAR---QGSVLYQG--------KSM 65
Cdd:COG0444 1 LLEVRNLKVYFPtRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGedllklseKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 66 RAV-QKQVAYVEQrkdlDlnfPINVFDVVLT-GTygklgLFRDP--------GKQAKAASRAALEQVALGDFERRqIG-- 133
Cdd:COG0444 81 RKIrGREIQMIFQ----D---PMTSLNPVMTvGD-----QIAEPlrihgglsKAEARERAIELLERVGLPDPERR-LDry 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 134 --QLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMK--QwRDAGKTIIVIHHDLNKVSQYFDDLVVMNH 209
Cdd:COG0444 148 phELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKdlQ-RELGLAILFITHDLGVVAEIADRVAVMYA 226
|
250
....*....|....*
gi 510996587 210 G-IVDYGPTDQVYNA 223
Cdd:COG0444 227 GrIVEEGPVEELFEN 241
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
3.82e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 118.64 E-value: 3.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY-DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVL-------YQGKSMRAVQKQV 72
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLikgepikYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 73 AYVEQRKDLDLNFPINVFDVvltgTYGKLGLfRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQE 152
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEDV----AFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 153 AEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNaqNIERAFS 231
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGkIIKEGTPKEVFS--DIETIRK 233
|
...
gi 510996587 232 ADL 234
Cdd:PRK13639 234 ANL 236
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
5-223 |
6.24e-32 |
|
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: 123.05 E-value: 6.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 5 KNLTVAY--DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR-----AVQKQVAYVEQ 77
Cdd:TIGR03375 467 RNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqidpaDLRRNIGYVPQ 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 rkdldlnfpinvfDVVLTgtYGKLglfRDP---GKQA--KAASRAALEQVALGDFERR-------QIGQ----LSGGQLQ 141
Cdd:TIGR03375 547 -------------DPRLF--YGTL---RDNialGAPYadDEEILRAAELAGVTEFVRRhpdgldmQIGErgrsLSGGQRQ 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 142 RVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRdAGKTIIVIHHdlnKVS--QYFDDLVVMNHG-IVDYGPTD 218
Cdd:TIGR03375 609 AVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTH---RTSllDLVDRIIVMDNGrIVADGPKD 684
|
....*
gi 510996587 219 QVYNA 223
Cdd:TIGR03375 685 QVLEA 689
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-216 |
7.69e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 122.20 E-value: 7.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYD-DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV-----QKQVAYV 75
Cdd:COG1132 340 IEFENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLtleslRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQrkdldlnfpinvfDVVL-TGT------YGKLGlfrdpgkqakaAS----RAALEQVALGDFERR-------QIGQ--- 134
Cdd:COG1132 420 PQ-------------DTFLfSGTirenirYGRPD-----------ATdeevEEAAKAAQAHEFIEAlpdgydtVVGErgv 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 135 -LSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRdAGKTIIVIHHDLNKVsQYFDDLVVMNHG-IV 212
Cdd:COG1132 476 nLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTI-RNADRILVLDDGrIV 553
|
....
gi 510996587 213 DYGP 216
Cdd:COG1132 554 EQGT 557
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-242 |
1.40e-31 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 116.19 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 24 FDAGKITGIIGPNGAGKSTLIKAILGLVKArQGSVLYQGKSMRAVQ-----KQVAYVEQRKDLDLNFPinVFDvvltgtY 98
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSaaelaRHRAYLSQQQTPPFAMP--VFQ------Y 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 99 gkLGLFRdPGKQAKAASRAALEQVA----LGDFERRQIGQLSGGQLQRVFVARAIVQ-------EAEIIILDEPFVGIDL 167
Cdd:PRK03695 90 --LTLHQ-PDKTRTEAVASALNEVAealgLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 168 QSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNIERAFSADLSAVLFEKQ 242
Cdd:PRK03695 167 AQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGkLLASGRRDEVLTPENLAQVFGVNFRRLDVEGH 242
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-229 |
1.46e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 117.03 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR-------AVQKQVA 73
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrgllALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 74 YVEQRKDLDLNFPINVFDVVLTgtygklglFRDPGKQAKAASRAALEQVALGD---FERRQIGQLSGGQLQRVFVARAIV 150
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSDIAFS--------LRNLGVPEAEITRRVDEALTLVDaqhFRHQPIQCLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 151 QEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVY-NAQNIER 228
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGqILTHGAPGEVFaCTEAMEQ 232
|
.
gi 510996587 229 A 229
Cdd:PRK13638 233 A 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-195 |
7.10e-31 |
|
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: 119.31 E-value: 7.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDT-PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV-----QKQVAYV 75
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAdadswRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRKDLdlnFPINVFDVVLtgtygklglFRDPGkQAKAASRAALEQVALGDFER-------RQIGQ----LSGGQLQRVF 144
Cdd:TIGR02857 402 PQHPFL---FAGTIAENIR---------LARPD-ASDAEIREALERAGLDEFVAalpqgldTPIGEggagLSGGQAQRLA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510996587 145 VARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDaGKTIIVIHHDLN 195
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLA 518
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-214 |
8.93e-31 |
|
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: 113.23 E-value: 8.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDtPVFTDVAVH---FDA--GKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG----KSMRAVQKQ 71
Cdd:cd03266 1 MITADALTKRFRD-VKKTVQAVDgvsFTVkpGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 72 VAYVEQRKDLdlnFP-INVFDVVltGTYGKL-GLFRDpgkQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAI 149
Cdd:cd03266 80 LGFVSDSTGL---YDrLTARENL--EYFAGLyGLKGD---ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 150 VQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIVDY 214
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-211 |
1.72e-30 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 113.67 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLyqgksmRAVQKQVAYVEQRKD 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 81 LDLNFPINVfdvvltgtyGKLGLFRdPGKQaKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDE 160
Cdd:PRK09544 78 LDTTLPLTV---------NRFLRLR-PGTK-KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510996587 161 PFVGIDLQSETAIMAIMKQWR-DAGKTIIVIHHDLNKVSQYFDDLVVMNHGI 211
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRrELDCAVLMVSHDLHLVMAKTDEVLCLNHHI 198
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-210 |
3.15e-30 |
|
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: 112.08 E-value: 3.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG----KSMRAVQKQVAYVEQRK 79
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPREVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 DLDlnfpinvfdVVLTGT---YGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEII 156
Cdd:cd03265 83 SVD---------DELTGWenlYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 157 ILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-230 |
3.19e-30 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 113.16 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 5 KNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-RAVQKQVAyveQRKDL-- 81
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVA---RRIGLla 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 82 -DLNFP--INVFDVVLTGTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIIL 158
Cdd:PRK10253 88 qNATTPgdITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996587 159 DEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNIERAF 230
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGkIVAQGAPKEIVTAELIERIY 241
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-210 |
6.98e-30 |
|
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: 110.77 E-value: 6.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMravQKQVAYVEQRKDL 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY---QKNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 82 dLNFPInvFDVVLTGTYGKLGLFRDPGKQAKAASRaALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEP 161
Cdd:cd03268 78 -IEAPG--FYPNLTARENLRLLARLLGIRKKRIDE-VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510996587 162 FVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-212 |
8.77e-30 |
|
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: 110.70 E-value: 8.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKS-------MRAVQKQVAY 74
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltddkknINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRKDLdlnFP-INVFDVVltgTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEA 153
Cdd:cd03262 81 VFQQFNL---FPhLTVLENI---TLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 154 EIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIV 212
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-219 |
9.13e-30 |
|
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: 110.67 E-value: 9.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY--DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKS----MRAVQKQVAYV 75
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSirtdRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRkdldlnfpiNVFDVVLTGT-----YGKL-GLfrdPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAI 149
Cdd:cd03263 81 PQF---------DALFDELTVRehlrfYARLkGL---PKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 150 VQEAEIIILDEPFVGIDLQSETAIMAIMKQWRdAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQ 219
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGkLRCIGSPQE 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-212 |
2.51e-29 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 109.42 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 5 KNLTVAY-DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQ-KQVAYVEQR---- 78
Cdd:cd03292 4 INVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgRAIPYLRRKigvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 -KDLDLNFPINVFDVVLTGtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:cd03292 84 fQDFRLLPDRNVYENVAFA----LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 158 LDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIV 212
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-194 |
3.38e-29 |
|
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: 108.86 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVAYVEQRKDLDL 83
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 84 NFpiNVFDVVLTGTYGK---LGLF--RDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIIL 158
Cdd:TIGR03608 81 LF--QNFALIENETVEEnldLGLKykKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 510996587 159 DEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDL 194
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP 194
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-210 |
6.88e-29 |
|
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: 107.94 E-value: 6.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDD-----TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKsmravqkqVAYVE 76
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 QrkdldlnFP--IN--VFDVVLtgtygkLGLFRDPGKQAKAASRAAL----EQVALGDfeRRQIGQ----LSGGQLQRVF 144
Cdd:cd03250 73 Q-------EPwiQNgtIRENIL------FGKPFDEERYEKVIKACALepdlEILPDGD--LTEIGEkginLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510996587 145 VARAIVQEAEIIILDEPFVGIDLQSETAIM--AIMKQWRDaGKTIIVIHHDLNKVSQyFDDLVVMNHG 210
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFenCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-222 |
7.10e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 109.83 E-value: 7.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDT--PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG------KSMRAVQKQVA 73
Cdd:TIGR04520 1 IEVENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtldeENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 74 YVEQRKDldlnfpiNVF-------DVVltgtYG--KLGLfrdPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVF 144
Cdd:TIGR04520 81 MVFQNPD-------NQFvgatvedDVA----FGleNLGV---PREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 145 VARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYfDDLVVMNHG-IVDYGPTDQVYN 222
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVLA-DRVIVMNKGkIVAEGTPREIFS 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-210 |
7.38e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 109.40 E-value: 7.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVAYVEQRKD 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 81 LdlnFP-INVFDVVLTGtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILD 159
Cdd:PRK11248 81 L---LPwRNVQDNVAFG----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510996587 160 EPFVGID-LQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:PRK11248 154 EPFGALDaFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-222 |
8.22e-29 |
|
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: 108.58 E-value: 8.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTpVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK---SMRAVQKQVAYVEQR 78
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 KDLdlnFP-INVFDVVltgTYGkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:cd03299 80 YAL---FPhMTVYKNI---AYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 158 LDEPFVGIDLQSETAIMAIMKQWRDA-GKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYN 222
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGkLIQVGKPEEVFK 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
1.44e-28 |
|
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: 105.97 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKsmravqkqvayveqrkdl 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 82 dlnfPINvfdvvltgtygklglFRDPgkqaKAASRAALEQVAlgdferrqigQLSGGQLQRVFVARAIVQEAEIIILDEP 161
Cdd:cd03216 63 ----EVS---------------FASP----RDARRAGIAMVY----------QLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510996587 162 FVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-222 |
3.46e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 109.39 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK---SMRAVQKQVAYVEQ 77
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtDLPPKDRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RKDLdlnFP-INVFDVVLTGtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEII 156
Cdd:COG3839 83 SYAL---YPhMTVYENIAFP----LKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 157 ILDEPFVGID----LQSETAIMAIMKQwrdAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYN 222
Cdd:COG3839 156 LLDEPLSNLDaklrVEMRAEIKRLHRR---LGTTTIYVTHDQVEAMTLADRIAVMNDGrIQQVGTPEELYD 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-210 |
1.23e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.84 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY---DDTPV----FTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG---------KSM 65
Cdd:PRK13641 1 MSIKFENVDYiysPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 66 RAVQKQVAYVEQRKDLDLnFPINVFDVVLtgtYGKLGL-FRDpgKQAKAASRAALEQVALG-DFERRQIGQLSGGQLQRV 143
Cdd:PRK13641 81 KKLRKKVSLVFQFPEAQL-FENTVLKDVE---FGPKNFgFSE--DEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 144 FVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-219 |
1.25e-27 |
|
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: 106.43 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 15 PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG--------KSMRAVQKQVAYVEQRKDLDLNfP 86
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrKQRRAFRRDVQLVFQDSPSAVN-P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 87 INVFDVVLTGTYGKLGLFRDPGKQAKAAsrAALEQVAL-GDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGI 165
Cdd:TIGR02769 104 RMTVRQIIGEPLRHLTSLDESEQKARIA--ELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 166 DLQSETAIMAIMKQWRDAGKT-IIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQ 219
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGqIVEECDVAQ 237
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-166 |
1.83e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.49 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKAR---QGSVLYQGKSMRAVQkqvayVEQ 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALP-----AEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RK------DlDLNFP-INVFDVVLtgtygkLGLFRDPGKQA-KAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAI 149
Cdd:COG4136 76 RRigilfqD-DLLFPhLSVGENLA------FALPPTIGRAQrRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRAL 148
|
170
....*....|....*..
gi 510996587 150 VQEAEIIILDEPFVGID 166
Cdd:COG4136 149 LAEPRALLLDEPFSKLD 165
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-199 |
2.41e-27 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 104.12 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV----QKQVAYVE 76
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyHQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 QR---KDL-----DLNFpinvfdvvltgtygklgLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARA 148
Cdd:PRK13538 81 HQpgiKTEltaleNLRF-----------------YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510996587 149 IVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVI-HHDLNKVSQ 199
Cdd:PRK13538 144 WLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTtHQDLPVASD 195
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-212 |
2.60e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.59 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTVAY-DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRA-----VQKQVAYVEQ 77
Cdd:PRK13647 7 VEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAenekwVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RKDlDLNFPINVFDVVltgTYGKLGLFRDPgKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:PRK13647 87 DPD-DQVFSSTVWDDV---AFGPVNMGLDK-DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 158 LDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIV 212
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-221 |
3.13e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.09 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKS---MRAVQKQVAYVEQRKD 80
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDvsrLHARDRKVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 81 LdlnFP-INVFDVVltgTYGKLGLFRDPGKQAKAASRAA---LEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEII 156
Cdd:PRK10851 85 L---FRhMTVFDNI---AFGLTVLPRRERPNAAAIKAKVtqlLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 157 ILDEPFVGIDLQSETAIMAIMKQWRDAGK-TIIVIHHDLNKVSQYFDDLVVMNHGIVD-YGPTDQVY 221
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEqAGTPDQVW 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-221 |
3.19e-27 |
|
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: 104.62 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY--DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQ-----KQVAY 74
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlaslrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRKDLdlnFPINVFDVVltgTYGKLGLFRdpgkqakAASRAALEQVALGDFERR-------QIG----QLSGGQLQRV 143
Cdd:cd03251 81 VSQDVFL---FNDTVAENI---AYGRPGATR-------EEVEEAARAANAHEFIMElpegydtVIGergvKLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 144 FVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRdAGKTIIVIHHDLNKVSQYfDDLVVMNHG-IVDYGPTDQVY 221
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIENA-DRIVVLEDGkIVERGTHEELL 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-212 |
5.66e-27 |
|
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: 102.29 E-value: 5.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDT--PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK-----SMRAVQKQVAY 74
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRkdldlnfpinvfDVVLTGTygklglfrdpgkqakaasraaleqvalgdferrqIGQ--LSGGQLQRVFVARAIVQE 152
Cdd:cd03246 81 LPQD------------DELFSGS----------------------------------IAEniLSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 153 AEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQyFDDLVVMNHGIV 212
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-212 |
6.10e-27 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 103.44 E-value: 6.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 5 KNLTVAYDD--TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRA-----VQKQVAYVEQ 77
Cdd:cd03245 6 RNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQldpadLRRNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 rkdldlnfpinvfDVVLtgTYGKL----GLFRDPGKQA---KAASRAALEQVALGD---FErRQIG----QLSGGQLQRV 143
Cdd:cd03245 86 -------------DVTL--FYGTLrdniTLGAPLADDErilRAAELAGVTDFVNKHpngLD-LQIGergrGLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510996587 144 FVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRdAGKTIIVIHHdlnKVS--QYFDDLVVMNHG-IV 212
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITH---RPSllDLVDRIIVMDSGrIV 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-210 |
6.22e-27 |
|
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: 102.39 E-value: 6.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYD--DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQ----KQVAYV 75
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEkalsSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRkdldlnfpINVFDVVLTGTYGKlglfrdpgkqakaasraaleqvalgdferrqigQLSGGQLQRVFVARAIVQEAEI 155
Cdd:cd03247 81 NQR--------PYLFDTTLRNNLGR---------------------------------RFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 156 IILDEPFVGIDLQSETAIMA-IMKQWRDagKTIIVIHHDLNKVSqYFDDLVVMNHG 210
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSlIFEVLKD--KTLIWITHHLTGIE-HMDKILFLENG 172
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-207 |
1.01e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.79 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYD----DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM------RAVqk 70
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadRGV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 71 qvayVEQRKDLdlnFP-INVFDVVltgtygKLGL-FRDPGKQA-KAASRAALEQVALGDFERRQIGQLSGGQLQRVFVAR 147
Cdd:COG4525 81 ----VFQKDAL---LPwLNVLDNV------AFGLrLRGVPKAErRARAEELLALVGLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 148 AIVQEAEIIILDEPFVGID-LQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVM 207
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDaLTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-220 |
1.14e-26 |
|
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: 102.99 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM------RAVQKQVAYV 75
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklpphERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRKDLdlnFP-INVFDVVLTGTYGklglfrdpgkqAKAASRAALEQV-----ALGDFERRQIGQLSGGQLQRVFVARAI 149
Cdd:TIGR03410 81 PQGREI---FPrLTVEENLLTGLAA-----------LPRRSRKIPDEIyelfpVLKEMLGRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 150 VQEAEIIILDEPFVGID----LQSETAIMAIMKQwrdAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQV 220
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQpsiiKDIGRVIRRLRAE---GGMAILLVEQYLDFARELADRYYVMERGrVVASGAGDEL 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-213 |
1.46e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.09 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG---------KSMRAVQKQVAYVEQRKDLDLnFPINV 89
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdKYIRPVRKRIGMVFQFPESQL-FEDTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 90 FDVVLTGTYGklglFRDPGKQAKAASRAALEQvaLGdFERRQIG----QLSGGQLQRVFVARAIVQEAEIIILDEPFVGI 165
Cdd:PRK13646 104 EREIIFGPKN----FKMNLDEVKNYAHRLLMD--LG-FSRDVMSqspfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510996587 166 DLQSETAIMAIMKQWR-DAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVD 213
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGsIVS 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-214 |
1.66e-26 |
|
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: 102.35 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLV---KARQGSVLYQGKSMRA--VQKQVAYVEQrkdLDLNFPinVFDVV 93
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPdqFQKCVAYVRQ---DDILLP--GLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 94 LTGTYgkLGLFRDPGKQAKAASRAALEQVALGDFERRQIG-----QLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQ 168
Cdd:cd03234 100 ETLTY--TAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510996587 169 SETAIMAIMKQWRDAGKTIIV-IHHDLNKVSQYFDDLVVMNHGIVDY 214
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEIVY 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-195 |
1.67e-26 |
|
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: 101.67 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQ----KQVAYVEQ 77
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRdephENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RKDL--DLNFPINvfdvvltgtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEI 155
Cdd:TIGR01189 81 LPGLkpELSALEN------------LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 510996587 156 IILDEPFVGIDLQSETAIMAIMKQWRDA-GKTIIVIHHDLN 195
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRAHLARgGIVLLTTHQDLG 189
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-194 |
2.19e-26 |
|
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: 106.68 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTP-VFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR-----AVQKQVAYV 75
Cdd:TIGR02868 335 LELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSsldqdEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRKDLdlnFPINVFDVVLTGTygklglfrdpGKQAKAASRAALEQVALGDFERRQIG-----------QLSGGQLQRVF 144
Cdd:TIGR02868 415 AQDAHL---FDTTVRENLRLAR----------PDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510996587 145 VARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQwRDAGKTIIVIHHDL 194
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-222 |
2.43e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 104.40 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYD---DTPVF----------TDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRA 67
Cdd:PRK15079 8 LLEVADLKVHFDikdGKQWFwqppktlkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 68 vQKQVAYVEQRKDL---------DLNFPINVFDVV---LTGTYGKLglfrdPGKQAKAASRAALEQVAL-GDFERRQIGQ 134
Cdd:PRK15079 88 -MKDDEWRAVRSDIqmifqdplaSLNPRMTIGEIIaepLRTYHPKL-----SRQEVKDRVKAMMLKVGLlPNLINRYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 135 LSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IV 212
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGhAV 241
|
250
....*....|
gi 510996587 213 DYGPTDQVYN 222
Cdd:PRK15079 242 ELGTYDEVYH 251
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-230 |
2.45e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.94 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 24 FDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-----RAVQKQVAYVEQRkdLDLNFPINVFDVVLTGTY 98
Cdd:PRK10575 34 FPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswssKAFARKVAYLPQQ--LPAAEGMTVRELVAIGRY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 99 ---GKLGLFrdpGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMA 175
Cdd:PRK10575 112 pwhGALGRF---GAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 176 IMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNIERAF 230
Cdd:PRK10575 189 LVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGeMIAQGTPAELMRGETLEQIY 245
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-220 |
2.54e-26 |
|
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: 102.38 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY-DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV-----QKQVAYV 75
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdpvelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRKDLDLNFPI--NVFDVvltgtygkLGLFRDPGKQAKAASRAALEQVALGD--FERRQIGQLSGGQLQRVFVARAIVQ 151
Cdd:cd03295 81 IQQIGLFPHMTVeeNIALV--------PKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 152 EAEIIILDEPFVGID------LQSEtaiMAIMKQwrDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQV 220
Cdd:cd03295 153 DPPLLLMDEPFGALDpitrdqLQEE---FKRLQQ--ELGKTIVFVTHDIDEAFRLADRIAIMKNGeIVQVGTPDEI 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-220 |
2.65e-26 |
|
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: 106.37 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY--DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQ-----VAY 74
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREelgrhIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRKDLdlnFPINVFDVVltgtygklGLFRDPGKQA--KAASRAALEQVALG-----DFerrQIGQ----LSGGQLQRV 143
Cdd:COG4618 411 LPQDVEL---FDGTIAENI--------ARFGDADPEKvvAAAKLAGVHEMILRlpdgyDT---RIGEggarLSGGQRQRI 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 144 FVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHD---LNKVsqyfDDLVVMNHG-IVDYGPTDQ 219
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRpslLAAV----DKLLVLRDGrVQAFGPRDE 552
|
.
gi 510996587 220 V 220
Cdd:COG4618 553 V 553
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-214 |
3.05e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVlYQGKSMRavqkqVAYVEQ-RK 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETVK-----IGYFDQhQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 DLDLNfpINVFDVVLTGtygklglfRDPGKQAKAASRaaleqvaLGDF----ER--RQIGQLSGGQLQRVFVARAIVQEA 153
Cdd:COG0488 389 ELDPD--KTVLDELRDG--------APGGTEQEVRGY-------LGRFlfsgDDafKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 154 EIIILDEPFVGIDLQSETAIMAIMKQWrdAGkTIIVIHHDlnkvsQYFDD------LVVMNHGIVDY 214
Cdd:COG0488 452 NVLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHD-----RYFLDrvatriLEFEDGGVREY 510
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-220 |
5.80e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.10 E-value: 5.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR------AVQKQVAY 74
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrsprdAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQrkDLDL--NFPI--NVFdvvLTGTYGKLGLFRDpgKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIV 150
Cdd:COG1129 84 IHQ--ELNLvpNLSVaeNIF---LGREPRRGGLIDW--RAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510996587 151 QEAEIIILDEPFVGIDlQSETAIM-AIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQV 220
Cdd:COG1129 157 RDARVLILDEPTASLT-EREVERLfRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGrLVGTGPVAEL 227
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-211 |
7.13e-26 |
|
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: 100.40 E-value: 7.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYD-DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKS-MRAVQKQVAYVEQR 78
Cdd:TIGR02673 1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDvNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 -----KDLDLNFPINVFD-VVLTgtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQE 152
Cdd:TIGR02673 81 igvvfQDFRLLPDRTVYEnVALP-----LEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 153 AEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGI 211
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-197 |
8.22e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.76 E-value: 8.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGksmravQKQVAYVEQRKDLDL 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLRIGYLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 84 NFPinVFDVVLTG-------------TYGKLG-LFRDPGKQAKAASR----------AALEQVALG------DFERRqIG 133
Cdd:COG0488 75 DLT--VLDTVLDGdaelraleaeleeLEAKLAePDEDLERLAELQEEfealggweaeARAEEILSGlgfpeeDLDRP-VS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510996587 134 QLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSetaimaimKQW-----RDAGKTIIVIHHD---LNKV 197
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES--------IEWleeflKNYPGTVLVVSHDryfLDRV 215
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-210 |
1.39e-25 |
|
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: 98.66 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVftDVAVHfdAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR------AVQKQVAY 74
Cdd:cd03215 4 VLEVRGLSVKGAVRDV--SFEVR--AGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrsprdAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 V-EQRKD--LDLNFPInvfdvvltgtygklglfrdpgkqakaasraaLEQVALGDFerrqigqLSGGQLQRVFVARAIVQ 151
Cdd:cd03215 80 VpEDRKRegLVLDLSV-------------------------------AENIALSSL-------LSGGNQQKVVLARWLAR 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 152 EAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-210 |
2.39e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.56 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAyddtPVFTDV--AVHfdAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR------AVQKQV 72
Cdd:COG1129 256 VLEVEGLSVG----GVVRDVsfSVR--AGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdAIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 73 AYV-EQRKD--LDLNFPI--NVFDVVLtGTYGKLGlFRDPGKQAKAASR--AALeQVALGDFERRqIGQLSGGQLQRVFV 145
Cdd:COG1129 330 AYVpEDRKGegLVLDLSIreNITLASL-DRLSRGG-LLDRRRERALAEEyiKRL-RIKTPSPEQP-VGNLSGGNQQKVVL 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 146 ARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREG 470
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-220 |
2.73e-25 |
|
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: 101.72 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIkNLTVAYDDtpvFT-DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGS------VLYQGKSMRAV---QK 70
Cdd:COG4148 2 MLEV-DFRLRRGG---FTlDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRirlggeVLQDSARGIFLpphRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 71 QVAYVEQ----------RKDLDlnfpinvfdvvltgtYGklgLFRDPgkqaKAASRAALEQVA----LGDFERRQIGQLS 136
Cdd:COG4148 78 RIGYVFQearlfphlsvRGNLL---------------YG---RKRAP----RAERRISFDEVVellgIGHLLDRRPATLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 137 GGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKT-IIVIHHDLNKVSQYFDDLVVMNHG-IVDY 214
Cdd:COG4148 136 GGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGrVVAS 215
|
....*.
gi 510996587 215 GPTDQV 220
Cdd:COG4148 216 GPLAEV 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-220 |
2.90e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 101.31 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYD----DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG--------KSMRAV 68
Cdd:COG1135 1 MIELENLSKTFPtkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltalseRELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 69 QKQVAYVEQrkdldlNFPI----NVFDVV-----LTGTygklglfrdPGKQAKAasRAA--LEQVALGDFERRQIGQLSG 137
Cdd:COG1135 81 RRKIGMIFQ------HFNLlssrTVAENValpleIAGV---------PKAEIRK--RVAelLELVGLSDKADAYPSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 138 GQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDA-GKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYG 215
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGrIVEQG 223
|
....*
gi 510996587 216 PTDQV 220
Cdd:COG1135 224 PVLDV 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
11-214 |
3.06e-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: 98.72 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 11 YDDTPVFTDVAvhFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV---QKQVAYVEQRKDLdlnFP- 86
Cdd:cd03298 10 YGEQPMHFDLT--FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppaDRPVSMLFQENNL---FAh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 87 INVFDVVltgtygklGLFRDPG----KQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPF 162
Cdd:cd03298 85 LTVEQNV--------GLGLSPGlkltAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 510996587 163 VGID--LQSETAIMaIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIVDY 214
Cdd:cd03298 157 AALDpaLRAEMLDL-VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-218 |
3.42e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.45 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 6 NLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM----RAVQKQVAYVEQRKDL 81
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVparaRLARARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 82 DLNFPINVfDVVLTGTYgklglFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEP 161
Cdd:PRK13536 126 DLEFTVRE-NLLVFGRY-----FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 162 FVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG--IVDYGPTD 218
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGrkIAEGRPHA 258
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-212 |
3.74e-25 |
|
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: 100.03 E-value: 3.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV---------QKQVAYVEQRKDLdlnFP-IN 88
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkelrelrRKKISMVFQSFAL---LPhRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 89 VFDVVltgTYGkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGID-- 166
Cdd:cd03294 119 VLENV---AFG-LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDpl 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510996587 167 ----LQSEtaimaIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIV 212
Cdd:cd03294 195 irreMQDE-----LLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-221 |
4.83e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 99.70 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDT--PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG-----KSMRAVQKQVAY 74
Cdd:PRK13635 6 IRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRKDldlnfpiNVF-------DVVltgtYG--KLGLFRDpgkQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFV 145
Cdd:PRK13635 86 VFQNPD-------NQFvgatvqdDVA----FGleNIGVPRE---EMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510996587 146 ARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGK-TIIVIHHDLNKVSQYfDDLVVMNHG-IVDYGPTDQVY 221
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQA-DRVIVMNKGeILEEGTPEEIF 228
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-195 |
5.02e-25 |
|
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: 97.95 E-value: 5.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV----QKQVAYVEQ 77
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrdsiARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RkdldlnfpiNVFDVVLTgTYGKLGLFRDPGkqAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:cd03231 81 A---------PGIKTTLS-VLENLRFWHADH--SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 510996587 158 LDEPFVGIDLQSETAIMAIMKQWRDAGKTIIV-IHHDLN 195
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLtTHQDLG 187
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-220 |
5.40e-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: 98.45 E-value: 5.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTVAYD-DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV-----QKQVAYVEQ 77
Cdd:cd03254 5 FENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrkslRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 ---------RKDLDLNFPINVFDVVLtgtygklglfrdpgkqakaasrAALEQVALGDFERR-------QIGQ----LSG 137
Cdd:cd03254 85 dtflfsgtiMENIRLGRPNATDEEVI----------------------EAAKEAGAHDFIMKlpngydtVLGEnggnLSQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 138 GQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDaGKTIIVIHHDLNKVsQYFDDLVVMNHG-IVDYGP 216
Cdd:cd03254 143 GERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTI-KNADKILVLDDGkIIEEGT 220
|
....
gi 510996587 217 TDQV 220
Cdd:cd03254 221 HDEL 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-210 |
5.79e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 100.26 E-value: 5.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM----RAVQKQVAYVEQ 77
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpsraRHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RKDLDLNFPINVfDVVLTGTYgklglFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:PRK13537 88 FDNLDPDFTVRE-NLLVFGRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510996587 158 LDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-210 |
7.38e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.79 E-value: 7.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV---QKQVAYVEQR 78
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaeNRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 KDLdlnFP-INVFDVVLTGtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:PRK09452 95 YAL---FPhMTVFENVAFG----LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 158 LDEPFVGID------LQSEtaimaiMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:PRK09452 168 LDESLSALDyklrkqMQNE------LKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-230 |
8.73e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.52 E-value: 8.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV-QKQVAyveqRK 79
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIA----RM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 DLDLNF-------PINVFDVVLTGTYGKL------GLFRDPG---KQAKAASRAA--LEQVALGDFERRQIGQLSGGQLQ 141
Cdd:PRK11300 81 GVVRTFqhvrlfrEMTVIENLLVAQHQQLktglfsGLLKTPAfrrAESEALDRAAtwLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 142 RVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDA-GKTIIVIHHDLNKVSQYFDDLVVMNHG--IVDyGPTD 218
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGtpLAN-GTPE 239
|
250
....*....|..
gi 510996587 219 QVYNAQNIERAF 230
Cdd:PRK11300 240 EIRNNPDVIKAY 251
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-216 |
1.17e-24 |
|
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: 102.10 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY--DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK-----SMRAVQKQVAY 74
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHdladyTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRKDLdlnFPINVFDVVltgTYGklglfrDPGKQAKAASRAALEQVALGDFERR-------QIGQ----LSGGQLQRV 143
Cdd:TIGR02203 411 VSQDVVL---FNDTIANNI---AYG------RTEQADRAEIERALAAAYAQDFVDKlplgldtPIGEngvlLSGGQRQRL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510996587 144 FVARAIVQEAEIIILDEPFVGIDLQSETAIMA----IMKqwrdaGKTIIVIHHDLNKVsQYFDDLVVMNHG-IVDYGP 216
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAalerLMQ-----GRTTLVIAHRLSTI-EKADRIVVMDDGrIVERGT 550
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-220 |
1.29e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 98.19 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAI---LGLVK-AR-QGSVLYQGKSMRA-------VQ 69
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPgARvEGEILLDGEDIYDpdvdvveLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 70 KQVAYVEQRkdldLN-FPINVFDVVltgTYG-KLGLFRDPGKQAKAAsRAALEQVALGDfE-----RRQIGQLSGGQLQR 142
Cdd:COG1117 92 RRVGMVFQK----PNpFPKSIYDNV---AYGlRLHGIKSKSELDEIV-EESLRKAALWD-EvkdrlKKSALGLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 143 VFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDagK-TIIVIHHDLN---KVSQYfddLVVMNHG-IVDYGPT 217
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK--DyTIVIVTHNMQqaaRVSDY---TAFFYLGeLVEFGPT 237
|
...
gi 510996587 218 DQV 220
Cdd:COG1117 238 EQI 240
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-238 |
2.20e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.96 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPV-FTdvaVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV---QKQVAYVE 76
Cdd:PRK10771 1 MLKLTDITWLYHHLPMrFD---LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppsRRPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 QRKDLdlnFP-INVFDvvltgtygKLGLFRDPGKQAKAASRAALE----QVALGDFERRQIGQLSGGQLQRVFVARAIVQ 151
Cdd:PRK10771 78 QENNL---FShLTVAQ--------NIGLGLNPGLKLNAAQREKLHaiarQMGIEDLLARLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 152 EAEIIILDEPFVGID--LQSEtaIMAIMKQ-WRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIVDY-GPTDQVYNAQnie 227
Cdd:PRK10771 147 EQPILLLDEPFSALDpaLRQE--MLTLVSQvCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWdGPTDELLSGK--- 221
|
250
....*....|.
gi 510996587 228 rafsADLSAVL 238
Cdd:PRK10771 222 ----ASASALL 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-195 |
4.97e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 95.33 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRA--VQKQVAYVEQR 78
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpdVAEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 kdldlnfpiNVFDVVLT---------GTYGklglfrdpgkQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAI 149
Cdd:PRK13539 82 ---------NAMKPALTvaenlefwaAFLG----------GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510996587 150 VQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIV-IHHDLN 195
Cdd:PRK13539 143 VSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAaTHIPLG 189
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-212 |
7.32e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.84 E-value: 7.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDD-TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG-------KSMRAVQKQV 72
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 73 AYVEQRKDLDLnFPINVFDVVltgTYGKLGLfRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQE 152
Cdd:PRK13636 85 GMVFQDPDNQL-FSASVYQDV---SFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 153 AEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIV 212
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-222 |
7.98e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.19 E-value: 7.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV-----QKQVAYVE 76
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 Q----RKDLDLNFP-------INVFDVVLTGTYGKLGLfrdpgKQAKAASRAALEQVALGDFERRQIG---QLSGGQLQR 142
Cdd:PRK10619 86 QlrllRTRLTMVFQhfnlwshMTVLENVMEAPIQVLGL-----SKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 143 VFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIV-DYGPTDQVY 221
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIeEEGAPEQLF 240
|
.
gi 510996587 222 N 222
Cdd:PRK10619 241 G 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-222 |
8.47e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.26 E-value: 8.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAiLGLVKARQGSVLYQGK-------------SMRAV 68
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRveffnqniyerrvNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 69 QKQVAYVEQRKDLdlnFPINVFDVVLTGTygKLGLFRdPGKQAKAASRAALEQVALGDFERRQIGQ----LSGGQLQRVF 144
Cdd:PRK14258 87 RRQVSMVHPKPNL---FPMSVYDNVAYGV--KIVGWR-PKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 145 VARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGK-TIIVIHHDLNKVSQyFDDLVVMNHG-------IVDYGP 216
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSR-LSDFTAFFKGnenrigqLVEFGL 239
|
....*.
gi 510996587 217 TDQVYN 222
Cdd:PRK14258 240 TKKIFN 245
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.02e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 97.23 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDD-TP----VFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSV----LYQGKSMRAvQKQ 71
Cdd:PRK13631 21 ILRVKNLYCVFDEkQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNN-HEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 72 VAYVEQRKDLDLNFPINVFDVVLTgtYGKLGLFRDP-------------GKQAKAASRAA--LEQVALGD-FERRQIGQL 135
Cdd:PRK13631 100 ITNPYSKKIKNFKELRRRVSMVFQ--FPEYQLFKDTiekdimfgpvalgVKKSEAKKLAKfyLNKMGLDDsYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 136 SGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDY 214
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGkILKT 257
|
250
....*....|..
gi 510996587 215 GPTDQVYNAQNI 226
Cdd:PRK13631 258 GTPYEIFTDQHI 269
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-238 |
1.04e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 96.21 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY--DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-----RAVQKQVA 73
Cdd:PRK13632 7 MIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIskenlKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 74 YVEQRKDldlN--FPINVFDVVLTGTYGKlglfRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQ 151
Cdd:PRK13632 87 IIFQNPD---NqfIGATVEDDIAFGLENK----KVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 152 EAEIIILDEPFVGIDLQSETAIMAIMKQWRDAG-KTIIVIHHDLNKVSQYfDDLVVMNHG-IVDYG-PTDQVYNAQNIER 228
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAILA-DKVIVFSEGkLIAQGkPKEILNNKEILEK 238
|
250
....*....|....*
gi 510996587 229 A-----FSADLSAVL 238
Cdd:PRK13632 239 AkidspFIYKLSKKL 253
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-213 |
1.11e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.34 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYD---DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRA-----VQKQV 72
Cdd:PRK13650 4 IIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenvwdIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 73 AYVEQRKDldlnfpiNVF------DVVLTGTYGKlGLfrdPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVA 146
Cdd:PRK13650 84 GMVFQNPD-------NQFvgatveDDVAFGLENK-GI---PHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510996587 147 RAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDA-GKTIIVIHHDLNKVSqYFDDLVVMNHGIVD 213
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVE 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-222 |
1.21e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.27 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTVAYDD-TPVFT----DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG-------KSMRAVQKQ 71
Cdd:PRK13637 5 IENLTHIYMEgTPFEKkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 72 VAYV---------EQRKDLDLNF-PINvfdvvltgtygkLGLFRDpgkQAKAASRAALEQVALG--DFERRQIGQLSGGQ 139
Cdd:PRK13637 85 VGLVfqypeyqlfEETIEKDIAFgPIN------------LGLSEE---EIENRVKRAMNIVGLDyeDYKDKSPFELSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 140 LQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGK-TIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPT 217
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGkCELQGTP 229
|
....*
gi 510996587 218 DQVYN 222
Cdd:PRK13637 230 REVFK 234
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-228 |
1.24e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 95.18 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM--------------R 66
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLtgldeheiarlgigR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 67 AVQKQVAY----VEQRKDLDLNFPINVFDVvltgtygklgLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQR 142
Cdd:COG4674 90 KFQKPTVFeeltVFENLELALKGDRGVFAS----------LFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 143 VFVARAIVQEAEIIILDEPFVGIDlQSETA-----IMAImkqwrdAGK-TIIVIHHDLNKVSQYFDDLVVMNHGIV-DYG 215
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVAGMT-DAETErtaelLKSL------AGKhSVVVVEHDMEFVRQIARKVTVLHQGSVlAEG 232
|
250
....*....|...
gi 510996587 216 PTDQVynaQNIER 228
Cdd:COG4674 233 SLDEV---QADPR 242
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-210 |
1.40e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLT------VAYDDtpvftdvaVHFD--AGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR------ 66
Cdd:COG3845 5 ALELRGITkrfggvVANDD--------VSLTvrPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 67 AVQKQVAYVEQrkdldlNF----PINVFDVVLTGTYGKLGLFRDPgKQAKAASRAALEQVALG-DFERRqIGQLSGGQLQ 141
Cdd:COG3845 77 AIALGIGMVHQ------HFmlvpNLTVAENIVLGLEPTKGGRLDR-KAARARIRELSERYGLDvDPDAK-VEDLSVGEQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510996587 142 RVFVARAIVQEAEIIILDEPfvgidlqseTAI---------MAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:COG3845 149 RVEILKALYRGARILILDEP---------TAVltpqeadelFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-230 |
1.44e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.46 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQG----------SVLYQGKSMRAVQK 70
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 71 ---QVAYVEQRkdLDLNFPINVFDVVLTGTYGKLGLFRDP----GKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRV 143
Cdd:PRK09984 84 sraNTGYIFQQ--FNLVNRLSVLENVLIGALGSTPFWRTCfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 144 FVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIVDYGPTDQVYN 222
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFD 241
|
....*...
gi 510996587 223 AQNIERAF 230
Cdd:PRK09984 242 NERFDHLY 249
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-214 |
1.45e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 93.77 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYD------DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQ--GSVLYQGK--SMRAVQKQ 71
Cdd:cd03213 4 LSFRNLTVTVKsspsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRplDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 72 VAYVEQRkdldlnfpinvfDVVltgtYGKLGLfrdpgkqakaasRAALEQVAlgdferrQIGQLSGGQLQRVFVARAIVQ 151
Cdd:cd03213 84 IGYVPQD------------DIL----HPTLTV------------RETLMFAA-------KLRGLSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996587 152 EAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIV-IHHDLNKVSQYFDDLVVMNHGIVDY 214
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICsIHQPSSEIFELFDKLLLLSQGRVIY 192
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-223 |
1.79e-23 |
|
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: 98.22 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDD----TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGL----VKARQGSVLYQGKS-------- 64
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDllglsere 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 65 MRAVQ-KQVAYVEQRKDLDLNfPinVFdvvltgTYGK---------LGLfrdPGKQAKAASRAALEQVALGDFERRqIG- 133
Cdd:COG4172 86 LRRIRgNRIAMIFQEPMTSLN-P--LH------TIGKqiaevlrlhRGL---SGAAARARALELLERVGIPDPERR-LDa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 134 ---QLSGGQLQRVFVARAIVQEAEIIILDEPFVGID--LQSEtaIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVM 207
Cdd:COG4172 153 yphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtVQAQ--ILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVM 230
|
250
....*....|....*..
gi 510996587 208 NHG-IVDYGPTDQVYNA 223
Cdd:COG4172 231 RQGeIVEQGPTAELFAA 247
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-219 |
2.59e-23 |
|
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: 94.14 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTVAYD---DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQ-----KQVAYV 75
Cdd:cd03249 3 FKNVSFRYPsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlrwlrSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRKDLdlnFPINVFDVVltgtygKLGLFRDPGKQAKAASRAALEQ---VALGDFERRQIG----QLSGGQLQRVFVARA 148
Cdd:cd03249 83 SQEPVL---FDGTIAENI------RYGKPDATDEEVEEAAKKANIHdfiMSLPDGYDTLVGergsQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510996587 149 IVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRdAGKTIIVIHHDLNKVsQYFDDLVVMNHG-IVDYGPTDQ 219
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTI-RNADLIAVLQNGqVVEQGTHDE 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-228 |
3.07e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 94.00 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-------RAVQKQVA 73
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpkvdeRLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 74 YVEQRKDLdlnFP-INVFDVVLTGTYGKLGLFRdpgKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQE 152
Cdd:PRK09493 81 MVFQQFYL---FPhLTALENVMFGPLRVRGASK---EEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 153 AEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNIER 228
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGrIAEDGDPQVLIKNPPSQR 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
3.08e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.99 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTV-AYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKArQGSVLYQGKSMRAV-----QKQVAYV 75
Cdd:PRK11174 350 IEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELdpeswRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRKDLdlnFPINVFDVVLTGtygklglfrDPgkQA-KAASRAALEQVALGDFERRQ-------IGQ----LSGGQLQRV 143
Cdd:PRK11174 429 GQNPQL---PHGTLRDNVLLG---------NP--DAsDEQLQQALENAWVSEFLPLLpqgldtpIGDqaagLSVGQAQRL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 144 FVARAIVQEAEIIILDEPFVGIDLQSETAIM-AIMKQWRdaGKTIIVIHHDLNKVSQYfDDLVVMNHG-IVDYGPTDQVY 221
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLDAHSEQLVMqALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGqIVQQGDYAELS 571
|
....
gi 510996587 222 NAQN 225
Cdd:PRK11174 572 QAGG 575
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-238 |
5.30e-23 |
|
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: 95.56 E-value: 5.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLY---------QGKSMRAVQKQVAYVEQRKDLdlnFPinv 89
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdsrKGIFLPPEKRRIGYVFQEARL---FP--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 90 fdvvLTGTYGKL--GLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDL 167
Cdd:TIGR02142 89 ----HLSVRGNLryGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510996587 168 QSETAIMAIMKQWRDA-GKTIIVIHHDLNKVSQYFDDLVVMNHGIVD-YGPTDQVYNAQNIERAFSADLSAVL 238
Cdd:TIGR02142 165 PRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAaAGPIAEVWASPDLPWLAREDQGSLI 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-210 |
6.53e-23 |
|
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: 90.59 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLyQGKSMRavqkqVAYVEqrkdl 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-WGSTVK-----IGYFE----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 82 dlnfpinvfdvvltgtygklglfrdpgkqakaasraaleqvalgdferrqigQLSGGQLQRVFVARAIVQEAEIIILDEP 161
Cdd:cd03221 70 ----------------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510996587 162 FVGIDLQSETAIMAIMKQWRdagKTIIVIHHD---LNKVSqyfDDLVVMNHG 210
Cdd:cd03221 98 TNHLDLESIEALEEALKEYP---GTVILVSHDryfLDQVA---TKIIELEDG 143
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-227 |
8.68e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.30 E-value: 8.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAI-----LGLVKARQGSVLYQGKSMRAvqKQVAYV 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYS--PRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRKDLDL------NFPINVFDVVLTGtygklglFRDPGKQAKA----ASRAALEQVALGD-----FERRQIGqLSGGQL 140
Cdd:PRK14239 83 DLRKEIGMvfqqpnPFPMSIYENVVYG-------LRLKGIKDKQvldeAVEKSLKGASIWDevkdrLHDSALG-LSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 141 QRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAgKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQ 219
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGdLIEYNDTKQ 233
|
....*....
gi 510996587 220 VY-NAQNIE 227
Cdd:PRK14239 234 MFmNPKHKE 242
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-212 |
1.57e-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: 92.29 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 5 KNLTVAYDDT-PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQ-----KQVAYVEQr 78
Cdd:cd03253 4 ENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTldslrRAIGVVPQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 kdldlnfpinvfDVVLTGT-------YGKLGLFRDpgKQAKAASRAALEQ--VALGDFERRQIGQ----LSGGQLQRVFV 145
Cdd:cd03253 83 ------------DTVLFNDtigynirYGRPDATDE--EVIEAAKAAQIHDkiMRFPDGYDTIVGErglkLSGGEKQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 146 ARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRdAGKTIIVIHHDLNKVSQYfDDLVVMNHGIV 212
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVNA-DKIIVLKDGRI 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-210 |
1.76e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.62 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTvAYDDTPVfTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR------AVQKQVAYV-E 76
Cdd:PRK09700 268 VRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldAVKKGMAYItE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 QRKDLDL--NFPI--NVF---DVVLTGTYGKLGLFRDPGKQAKAASRAALEQVALGDFERrQIGQLSGGQLQRVFVARAI 149
Cdd:PRK09700 346 SRRDNGFfpNFSIaqNMAisrSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQ-NITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 150 VQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-220 |
2.08e-22 |
|
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: 95.49 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY--DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQ-----KQVAY 74
Cdd:TIGR01842 317 LSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDretfgKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRkdldlnfpINVFDVVLTGTYGKLGLFRDPGKQAKAASRAALEQVALG--DFERRQIGQ----LSGGQLQRVFVARA 148
Cdd:TIGR01842 397 LPQD--------VELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRlpDGYDTVIGPggatLSGGQRQRIALARA 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510996587 149 IVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQyFDDLVVMNHG-IVDYGPTDQV 220
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGC-VDKILVLQDGrIARFGERDEV 540
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-216 |
2.23e-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: 91.40 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDT--PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVqkqvayveQRK 79
Cdd:cd03244 3 IEFKNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI--------GLH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 DLDLNFPINVFDVVL-TGTygklglFR---DP-GKQAKAASRAALEQVALGDFERRQIGQL-----------SGGQLQRV 143
Cdd:cd03244 75 DLRSRISIIPQDPVLfSGT------IRsnlDPfGEYSDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996587 144 FVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRdAGKTIIVIHHDLNKVSQYfDDLVVMNHG-IVDYGP 216
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIREAF-KDCTVLTIAHRLDTIIDS-DRILVLDKGrVVEFDS 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-193 |
2.43e-22 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 95.00 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYqGKSMravqkQVAYVEQ-RKD 80
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-----KLAYVDQsRDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 81 LDLNfpINVFDVVLTGT-YGKLGLFRDPgkqakaaSRAALEQVAL-GDFERRQIGQLSGGQLQRVFVARAIVQEAEIIIL 158
Cdd:TIGR03719 397 LDPN--KTVWEEISGGLdIIKLGKREIP-------SRAYVGRFNFkGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
170 180 190
....*....|....*....|....*....|....*....
gi 510996587 159 DEPFVGIDLQS----ETAIMAImkqwrdAGkTIIVIHHD 193
Cdd:TIGR03719 468 DEPTNDLDVETlralEEALLNF------AG-CAVVISHD 499
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-215 |
2.54e-22 |
|
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: 91.20 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 27 GKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQ---------VAYVEQRKDLdlnFPinVFDVVLTGT 97
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlppqqrkIGLVFQQYAL---FP--HLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 98 YGklgLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIM 177
Cdd:cd03297 98 FG---LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 510996587 178 KQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIVDYG 215
Cdd:cd03297 175 KQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-210 |
3.01e-22 |
|
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: 91.38 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 5 KNLTVAY---DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQ-----KQVAYVE 76
Cdd:cd03248 15 QNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEhkylhSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 QRKDLdlnFPINVFDVVltgTYGKLGLFRDPGKQAKAASRAA--LEQVALG-DFERRQIG-QLSGGQLQRVFVARAIVQE 152
Cdd:cd03248 95 QEPVL---FARSLQDNI---AYGLQSCSFECVKEAAQKAHAHsfISELASGyDTEVGEKGsQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 510996587 153 AEIIILDEPFVGIDLQSETAIMAIMKQWRDAgKTIIVIHHDLNKVsQYFDDLVVMNHG 210
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTV-ERADQILVLDGG 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
2-212 |
4.14e-22 |
|
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: 90.69 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVhfDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV---QKQVAYVEQR 78
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFDLNV--ADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLapyQRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 KDLdlnFPinvfdvVLTgTYGKLGLFRDPGKQAKAASRAALEQVA----LGDFERRQIGQLSGGQLQRVFVARAIVQEAE 154
Cdd:TIGR01277 79 NNL---FA------HLT-VRQNIGLGLHPGLKLNAEQQEKVVDAAqqvgIADYLDRLPEQLSGGQRQRVALARCLVRPNP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 155 IIILDEPFVGIDLQSETAIMAIMKQWRDAGK-TIIVIHHDLNKVSQYFDDLVVMNHGIV 212
Cdd:TIGR01277 149 ILLLDEPFSALDPLLREEMLALVKQLCSERQrTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-166 |
4.27e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 90.86 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKS-------MRAvQKQVA 73
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlpmhKRA-RLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 74 YVEQ-----RKdldlnfpINVFDVVLtgtyGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARA 148
Cdd:COG1137 82 YLPQeasifRK-------LTVEDNIL----AVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170
....*....|....*...
gi 510996587 149 IVQEAEIIILDEPFVGID 166
Cdd:COG1137 151 LATNPKFILLDEPFAGVD 168
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-212 |
4.71e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 92.01 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 18 TDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLY---------QGKSMRAVQKQVAYV---------EQRK 79
Cdd:PRK13634 24 YDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkKNKKLKPLRKKVGIVfqfpehqlfEETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 DLDLNF-PINvFDVvltgtygklglfrdPGKQAKAASRAALEQVALG-DFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:PRK13634 104 EKDICFgPMN-FGV--------------SEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 158 LDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIV 212
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-212 |
4.78e-22 |
|
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: 90.39 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQ---KQVAYVEQR 78
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkdRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 KDLdlnFP-INVFDVVLTGtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:cd03301 81 YAL---YPhMTVYDNIAFG----LKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 158 LDEPFVGIDLQSETAIMA-IMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIV 212
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAeLKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-212 |
5.91e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.59 E-value: 5.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY-DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG------KSMRAVQKQVA 73
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 74 YVEQRKDLDLNFPINVFDVvltgTYGKLGLFRDPGKQAKAASRAaLEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEA 153
Cdd:PRK13644 81 IVFQNPETQFVGRTVEEDL----AFGPENLCLPPIEIRKRVDRA-LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 154 EIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVsQYFDDLVVMNHGIV 212
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKI 213
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-216 |
5.92e-22 |
|
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: 89.89 E-value: 5.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGL--VKARQGSVLYQGKSMravqkqvayveqrk 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDI-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 dldLNFPINVfdvvltgtYGKLGL---FRDPgkqakaasrAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEII 156
Cdd:cd03217 67 ---TDLPPEE--------RARLGIflaFQYP---------PEIPGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510996587 157 ILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHdLNKVSQYFD-DLV-VMNHG-IVDYGP 216
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH-YQRLLDYIKpDRVhVLYDGrIVKSGD 188
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-214 |
7.88e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 90.47 E-value: 7.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 11 YDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG----KSMRAVQKQVAYV-EQRKDLDLNF 85
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwKRRKKFLRRIGVVfGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 86 PinvfdvVLTGTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGI 165
Cdd:cd03267 111 P------VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510996587 166 DLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIVDY 214
Cdd:cd03267 185 DVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-223 |
1.22e-21 |
|
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: 93.21 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYddtPV----FTDVAVHFDA----------GKITGIIGPNGAGKSTLIKAILGLVKArQGSVLYQG----- 62
Cdd:COG4172 276 LEARDLKVWF---PIkrglFRRTVGHVKAvdgvsltlrrGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGqdldg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 63 ---KSMRAVQKQVAYVEQrkdlD----LNFPINVFDVVLTGtygkLGLFRDP--GKQAKAASRAALEQVAL-GDFERRQI 132
Cdd:COG4172 352 lsrRALRPLRRRMQVVFQ----DpfgsLSPRMTVGQIIAEG----LRVHGPGlsAAERRARVAEALEEVGLdPAARHRYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 133 GQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMK--QwRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRdlQ-REHGLAYLFISHDLAVVRALAHRVMVMKDG 502
|
250
....*....|....
gi 510996587 211 -IVDYGPTDQVYNA 223
Cdd:COG4172 503 kVVEQGPTEQVFDA 516
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-229 |
1.44e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 93.25 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 13 DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRA-----VQKQVAYVEQRKDLdlnFPI 87
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhhyLHRQVALVGQEPVL---FSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 88 NVFDVVltgTYGklgLFRDPGKQAKAASRAALEQVALGDFER---RQIG----QLSGGQLQRVFVARAIVQEAEIIILDE 160
Cdd:TIGR00958 570 SVRENI---AYG---LTDTPDEEIMAAAKAANAHDFIMEFPNgydTEVGekgsQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 161 PFVGIDLQSETAIMAIMKQwrdAGKTIIVIHHDLNKVSQYfDDLVVMNHG-IVDYGPTDQVYNAQNIERA 229
Cdd:TIGR00958 644 ATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTVERA-DQILVLKKGsVVEMGTHKQLMEDQGCYKH 709
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-223 |
2.30e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 89.37 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVaYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGL----VKARQGSVLYQGKSMRAVQ---KQVAY 74
Cdd:PRK10418 5 IELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVAPCAlrgRKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRkdldlnfPINVFDVVLTGTYGKLGLFRDPGKQAKAAS-RAALEQVALGDFER---RQIGQLSGGQLQRVFVARAIV 150
Cdd:PRK10418 84 IMQN-------PRSAFNPLHTMHTHARETCLALGKPADDATlTAALEAVGLENAARvlkLYPFEMSGGMLQRMMIALALL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 151 QEAEIIILDEPFVGIDLQSETAIMA-IMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNA 223
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDlLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGrIVEQGDVETLFNA 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-225 |
2.39e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.82 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVAYvEQRKD 80
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLY-TVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 81 LDLNFP-------INVFDVVltgTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEA 153
Cdd:PRK11831 86 MSMLFQsgalftdMNVFDNV---AYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996587 154 EIIILDEPFVGIDLQSETAIMAIMKQWRDA-GKTIIVIHHDLNKVSQYFD-DLVVMNHGIVDYGPTDQVYNAQN 225
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADhAYIVADKKIVAHGSAQALQANPD 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-240 |
2.74e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.05 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV---QKQVAYVEQ 77
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVppyQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RKDLdlnFPINVFDVVLTgtygkLGLFRDPGKQAKAASRAA--LEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEI 155
Cdd:PRK11607 99 SYAL---FPHMTVEQNIA-----FGLKQDKLPKAEIASRVNemLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 156 IILDEPFVGID------LQSEtaIMAIMKQwrdAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNIEr 228
Cdd:PRK11607 171 LLLDEPMGALDkklrdrMQLE--VVDILER---VGVTCVMVTHDQEEAMTMAGRIAIMNRGkFVQIGEPEEIYEHPTTR- 244
|
250
....*....|....
gi 510996587 229 aFSADL--SAVLFE 240
Cdd:PRK11607 245 -YSAEFigSVNVFE 257
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
3.18e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.81 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDD--TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR-----AVQKQVAY 74
Cdd:PRK11160 339 LTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdyseaALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRKDLdlnfpinvfdvvLTGTygklglFRDPGKQAKAAS-----RAALEQVALGDF-ERRQ-----IG----QLSGGQ 139
Cdd:PRK11160 419 VSQRVHL------------FSAT------LRDNLLLAAPNAsdealIEVLQQVGLEKLlEDDKglnawLGeggrQLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 140 LQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRdAGKTIIVIHHDLNKVSQyFDDLVVMNHG-IVDYGPTD 218
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQ-FDRICVMDNGqIIEQGTHQ 558
|
....*..
gi 510996587 219 QVYNAQN 225
Cdd:PRK11160 559 ELLAQQG 565
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-229 |
3.33e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.79 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSV---------LYQGKSMRAVQKQVAYVEQRKDLDLnFPINV 89
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvssTSKQKEIKPVRKKVGVVFQFPESQL-FEETV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 90 FDVVLTGTYGklglFRDPGKQAKAASRAALEQVALG-DFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQ 168
Cdd:PRK13643 103 LKDVAFGPQN----FGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510996587 169 SETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNIERA 229
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGhIISCGTPSDVFQEVDFLKA 240
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-228 |
3.57e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.04 E-value: 3.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSV------------LYQGKSM-RA 67
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarsLSQQKGLiRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 68 VQKQVAYVEQRKDLdlnFP-INVFDVVLTGtygKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVA 146
Cdd:PRK11264 83 LRQHVGFVFQNFNL---FPhRTVLENIIEG---PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 147 RAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQN 225
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGrIVEQGPAKALFADPQ 236
|
...
gi 510996587 226 IER 228
Cdd:PRK11264 237 QPR 239
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-215 |
3.59e-21 |
|
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: 87.85 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY--DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKS-----MRAVQKQVAY 74
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistipLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRKdldlnfpinvfdVVLTGTYgKLGLfrDP-GKQAKAASRAALEQVALGDferrqigQLSGGQLQRVFVARAIVQEA 153
Cdd:cd03369 87 IPQDP------------TLFSGTI-RSNL--DPfDEYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510996587 154 EIIILDEPFVGIDLQSETAIMAIMKQwRDAGKTIIVIHHDLNKVSQYfDDLVVMNHG-IVDYG 215
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIRE-EFTNSTILTIAHRLRTIIDY-DKILVMDAGeVKEYD 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-221 |
3.80e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.82 E-value: 3.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLV----KAR-QGSVLYQGKSMRavqkQVAYVE 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypEARvSGEVYLDGQDIF----KMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 QRKDLDLNFPI-------NVFDVVLTGTygKLGLFRDPGKQAKAASRAALEQVALGDFERRQI----GQLSGGQLQRVFV 145
Cdd:PRK14247 80 LRRRVQMVFQIpnpipnlSIFENVALGL--KLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapaGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 146 ARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAgKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVY 221
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGqIVEWGPTREVF 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-230 |
4.10e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.41 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-------RAvQKQVAY 74
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplhaRA-RRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRKDLDLNfpINVFDVVLtgtyGKLGLFRD-PGKQAKAASRAALEQVALGDFeRRQIGQ-LSGGQLQRVFVARAIVQE 152
Cdd:PRK10895 83 LPQEASIFRR--LSVYDNLM----AVLQIRDDlSAEQREDRANELMEEFHIEHL-RDSMGQsLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 153 AEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNIERAF 230
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGhLIAHGTPTEILQDEHVKRVY 234
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-217 |
4.32e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.98 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 16 VFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKS--------MRAVQKQVAYVEQRKDLDLNFPI 87
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlaklnraqRKAFRRDIQMVFQDSISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 88 NVFDVVLTGTYGKLGLfRDPGKQAKAasRAALEQVAL--GDFERRQiGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGI 165
Cdd:PRK10419 107 TVREIIREPLRHLLSL-DKAERLARA--SEMLRAVDLddSVLDKRP-PQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 510996587 166 DLQSETAIMAIMKQWRDAGKTIIV-IHHDLNKVSQYFDDLVVMNHG-IVDYGPT 217
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQFGTACLfITHDLRLVERFCQRVMVMDNGqIVETQPV 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
12-220 |
5.28e-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: 88.31 E-value: 5.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 12 DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV-----QKQVAYVEQRkdldlnfp 86
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdpawlRRQVGVVLQE-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 87 invfDVVLTGTYGKLGLFRDPG---KQAKAASRAA-----LEQVALGdFE----RRQIGqLSGGQLQRVFVARAIVQEAE 154
Cdd:cd03252 85 ----NVLFNRSIRDNIALADPGmsmERVIEAAKLAgahdfISELPEG-YDtivgEQGAG-LSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 155 IIILDEPFVGIDLQSETAIMAIMKQWRdAGKTIIVIHHDLNKVSQYfDDLVVMNHG-IVDYGPTDQV 220
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKNA-DRIIVMEKGrIVEQGSHDEL 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-222 |
5.49e-21 |
|
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: 87.98 E-value: 5.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-------RAvQKQVAY 74
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItklpmhkRA-RLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRKDL--DLNFPINVFDVvltgtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQE 152
Cdd:cd03218 80 LPQEASIfrKLTVEENILAV--------LEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 153 AEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYN 222
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGkVLAEGTPEEIAA 222
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-221 |
6.21e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 89.41 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 22 VHFD--AGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK--------SMRAVQKQVAYVEQrkdlD----LN--- 84
Cdd:COG4608 37 VSFDirRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQditglsgrELRPLRRRMQMVFQ----DpyasLNprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 85 -------FPINVFDVVltgtygklglfrdPGKQAKAASRAALEQVALG-DFERRQIGQLSGGQLQRVFVARAIVQEAEII 156
Cdd:COG4608 113 tvgdiiaEPLRIHGLA-------------SKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 157 ILDEPF----VGI---------DLQsetaimaimkqwRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVY 221
Cdd:COG4608 180 VCDEPVsaldVSIqaqvlnlleDLQ------------DELGLTYLFISHDLSVVRHISDRVAVMYLGkIVEIAPRDELY 246
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-219 |
1.56e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 90.16 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 3 SIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQ-----KQVAYVEQ 77
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldswrSRLAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RkdldlnfPINVFDVVLtgtyGKLGLFRdpgkqaKAASRAALEQVA-----------LGDFERRQIGQ----LSGGQLQR 142
Cdd:PRK10789 397 T-------PFLFSDTVA----NNIALGR------PDATQQEIEHVArlasvhddilrLPQGYDTEVGErgvmLSGGQKQR 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510996587 143 VFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDaGKTIIVIHHDLNKVSQYfDDLVVMNHG-IVDYGPTDQ 219
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTEA-SEILVMQHGhIAQRGNHDQ 535
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
22-221 |
2.27e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 22 VHFDAGKIT--GIIGPNGAGKSTLIKAILGLVKARQGSVLYQG-----KSMRAVQKQVAYVEQRKDLDLNFPINVFDVvl 94
Cdd:PRK13652 23 INFIAPRNSriAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkENIREVRKFVGLVFQNPDDQIFSPTVEQDI-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 95 tgTYGKLGLFRDPGKQAKAASrAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIM 174
Cdd:PRK13652 101 --AFGPINLGLDEETVAHRVS-SALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELI 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510996587 175 AIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVY 221
Cdd:PRK13652 178 DFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGrIVAYGTVEEIF 226
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-232 |
2.33e-20 |
|
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: 87.93 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 32 IIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV---QKQVAYVEQRKDLdlnFP-INVFDVVLTGtygkLGLFRDP 107
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVpphLRHINMVFQSYAL---FPhMTVEENVAFG----LKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 108 GKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGID------LQSETAIMAimkqwR 181
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrdqMQLELKTIQ-----E 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510996587 182 DAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNIEraFSA 232
Cdd:TIGR01187 149 QLGITFVFVTHDQEEAMTMSDRIAIMRKGkIAQIGTPEEIYEEPANL--FVA 198
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-212 |
3.16e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.73 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 5 KNLTVAYDDTPVFT--DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG-----KSMRAVQKQVAYVEQ 77
Cdd:PRK13648 11 KNVSFQYQSDASFTlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaitdDNFEKLRKHIGIVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RKDLDLNFPINVFDVVltgtygkLGL--FRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEI 155
Cdd:PRK13648 91 NPDNQFVGSIVKYDVA-------FGLenHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 510996587 156 IILDEPFVGIDLQSETAIMAIMKQWR-DAGKTIIVIHHDLNKVSQYfDDLVVMNHGIV 212
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAMEA-DHVIVMNKGTV 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-193 |
3.39e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.01 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY----DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKaILG-LVKARQGSVLYQGKSMRAV------- 68
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGcLDKPTSGTYRVAGQDVATLdadalaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 69 --QKQVAYVEQRKDLdLNFPINVFDVVLTGTYGKLGlfrdpGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVA 146
Cdd:PRK10535 83 lrREHFGFIFQRYHL-LSHLTAAQNVEVPAVYAGLE-----RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510996587 147 RAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHD 193
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
5.58e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 84.62 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR----AVQKQVAYVE 76
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdlcTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 QRKDLDLNFPIN---VFDVVLTGtyGKLGLfrdpgkqakaasRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEA 153
Cdd:PRK13540 81 HRSGINPYLTLRencLYDIHFSP--GAVGI------------TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 510996587 154 EIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHD---LNK 196
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQdlpLNK 192
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-191 |
1.13e-19 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 84.13 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQ--VAYVEQ- 77
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSrfMAYLGHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 ---RKDLD----LNFpinvfdvvLTGTYgklglfrdpGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIV 150
Cdd:PRK13543 91 pglKADLStlenLHF--------LCGLH---------GRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510996587 151 QEAEIIILDEPFVGIDLQSETAIMAIMK-QWRDAGKTIIVIH 191
Cdd:PRK13543 154 SPAPLWLLDEPYANLDLEGITLVNRMISaHLRGGGAALVTTH 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-223 |
1.18e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.15 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 6 NLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKA-----RQGSVLYQGKSM---RAV---QKQVAY 74
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnyRDVlefRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRKDldlNFPINVFDVVLTGTYGKLGLfrdPGKQAKAASRAALEQVALGDFERRQIG----QLSGGQLQRVFVARAIV 150
Cdd:PRK14271 106 LFQRPN---PFPMSIMDNVLAGVRAHKLV---PRKEFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996587 151 QEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAgKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNA 223
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGrLVEEGPTEQLFSS 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-223 |
1.23e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.45 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY-----------DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKArQGSVLYQG------- 62
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGqplhnln 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 63 -KSMRAVQKQVAYVEQRKDLDLNFPINVFDVVLTGtygklglFRDPGKQAKAASR-----AALEQVALgDFERRQ--IGQ 134
Cdd:PRK15134 354 rRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEG-------LRVHQPTLSAAQReqqviAVMEEVGL-DPETRHryPAE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 135 LSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGK-TIIVIHHDLNKVSQYFDDLVVMNHG-IV 212
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGeVV 505
|
250
....*....|.
gi 510996587 213 DYGPTDQVYNA 223
Cdd:PRK15134 506 EQGDCERVFAA 516
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-223 |
1.30e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY----DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGL-----VKARQGSVLYQGKSM------ 65
Cdd:PRK15134 5 LLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLlhaseq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 66 --RAVQ-KQVAYVEQRKDLDLNfPINVFDVVLtgtYGKLGLFRDPGKQAKAAS------RAALEQVA--LGDFERrqigQ 134
Cdd:PRK15134 85 tlRGVRgNKIAMIFQEPMVSLN-PLHTLEKQL---YEVLSLHRGMRREAARGEilncldRVGIRQAAkrLTDYPH----Q 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 135 LSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IV 212
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGrCV 236
|
250
....*....|.
gi 510996587 213 DYGPTDQVYNA 223
Cdd:PRK15134 237 EQNRAATLFSA 247
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-235 |
1.59e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.30 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG-----------KSMRAVQK 70
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 71 QVAYVEQRKDLdlnFP-INVFDVVLTGTYGKLGLFRDpgkQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAI 149
Cdd:PRK11124 83 NVGMVFQQYNL---WPhLTVQQNLIEAPCRVLGLSKD---QALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 150 VQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNieR 228
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGhIVEQGDASCFTQPQT--E 234
|
....*..
gi 510996587 229 AFSADLS 235
Cdd:PRK11124 235 AFKNYLS 241
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-223 |
1.75e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 84.50 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDD------TPVFTDVA-VHF--DAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK-------SM 65
Cdd:COG4167 5 LEVRNLSKTFKYrtglfrRQQFEAVKpVSFtlEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdyKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 66 RAvqKQVAYVEQRKDLDLNFPINV---FDVVLtgtygKLGLFRDPgKQAKAASRAALEQVAL-GDFERRQIGQLSGGQLQ 141
Cdd:COG4167 85 RC--KHIRMIFQDPNTSLNPRLNIgqiLEEPL-----RLNTDLTA-EEREERIFATLRLVGLlPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 142 RVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIM-KQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQ 219
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMlELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGeVVEYGKTAE 236
|
....
gi 510996587 220 VYNA 223
Cdd:COG4167 237 VFAN 240
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-221 |
2.74e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.41 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRA--VQKQVAYVEQRKDLDLNFPIN-VFD-VVL 94
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsKNKDIKQIRKKVGLVFQFPESqLFEeTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 95 TGTYGKLGLFRDPGKQAKAASRAALEQVALGD--FERRQIgQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETA 172
Cdd:PRK13649 105 KDVAFGPQNFGVSQEEAEALAREKLALVGISEslFEKNPF-ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510996587 173 IMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVY 221
Cdd:PRK13649 184 LMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGkLVLSGKPKDIF 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-241 |
2.74e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 84.47 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDT--PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLV---KARQGSVLYQG-----KSMRAVQKQ 71
Cdd:PRK13640 6 VEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGitltaKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 72 VAYVEQRKDldlnfpiNVFDVVLTGTYGKLGLFRD--PGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAI 149
Cdd:PRK13640 86 VGIVFQNPD-------NQFVGATVGDDVAFGLENRavPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 150 VQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYfDDLVVMNHG-IVDYGPTDQVYNaqNIE 227
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANMA-DQVLVLDDGkLLAQGSPVEIFS--KVE 235
|
250
....*....|....
gi 510996587 228 RAFSADLSAVLFEK 241
Cdd:PRK13640 236 MLKEIGLDIPFVYK 249
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-237 |
3.95e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 83.72 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKAR--------QGSVLYQGKSM------- 65
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLaaidapr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 66 ----RAVQKQVAyveQRKdldlnFPINVFDVVLTGTY------GKLGLfRDPGKQAKAASRAALEQVAlgdfeRRQIGQL 135
Cdd:PRK13547 81 larlRAVLPQAA---QPA-----FAFSAREIVLLGRYpharraGALTH-RDGEIAWQALALAGATALV-----GRDVTTL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 136 SGGQLQRVFVARAIVQ---------EAEIIILDEPFVGIDLQSETAIM----AIMKQWRDAGKTIIvihHDLNKVSQYFD 202
Cdd:PRK13547 147 SGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLdtvrRLARDWNLGVLAIV---HDPNLAARHAD 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 510996587 203 DLVVMNHG-IVDYGPTDQVYNAQNIERAFSADLSAV 237
Cdd:PRK13547 224 RIAMLADGaIVAHGAPADVLTPAHIARCYGFAVRLV 259
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-220 |
6.05e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.08 E-value: 6.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAyDDTPVftdVAVH---FD--AGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM------RAVQK 70
Cdd:COG3845 258 LEVENLSVR-DDRGV---PALKdvsLEvrAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglsprERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 71 QVAYV-EQR-KD-LDLNFPInVFDVVLT----GTYGKLGLFRdpGKQAKAASRAALEQ--VALGDfERRQIGQLSGGQLQ 141
Cdd:COG3845 334 GVAYIpEDRlGRgLVPDMSV-AENLILGryrrPPFSRGGFLD--RKAIRAFAEELIEEfdVRTPG-PDTPARSLSGGNQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 142 RVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQV 220
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGrIVGEVPAAEA 489
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-215 |
1.36e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.30 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYD--DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR-----AVQKQVAY 74
Cdd:PRK11176 342 IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdytlaSLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQrkdldlnfpiNVFdvvltgtygklgLFRD--PGKQAKAA----SRAALEQVA----LGDFERRQ-------IGQ--- 134
Cdd:PRK11176 422 VSQ----------NVH------------LFNDtiANNIAYARteqySREQIEEAArmayAMDFINKMdngldtvIGEngv 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 135 -LSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDaGKTIIVIHHDLNKVSQYfDDLVVMNHG-IV 212
Cdd:PRK11176 480 lLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTIEKA-DEILVVEDGeIV 557
|
...
gi 510996587 213 DYG 215
Cdd:PRK11176 558 ERG 560
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-226 |
1.63e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 82.36 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVAYVEQ-RKDLDL--NFP-INVFDVVL 94
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRlRKEIGLvfQFPeYQLFQETI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 95 TG--TYGKLGLFRDPGKQAKAASRAaLEQVALG-DFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSET 171
Cdd:PRK13645 109 EKdiAFGPVNLGENKQEAYKKVPEL-LKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 172 AIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNI 226
Cdd:PRK13645 188 DFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGkVISIGSPFEIFSNQEL 244
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-222 |
1.86e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.75 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGL----VKAR-QGSVLYQGKSMRA-------VQ 69
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndliPGFRvEGKVTFHGKNLYApdvdpveVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 70 KQVAYVEQRKDldlNFPINVFDVVLTGTygKLGLFRdpGKQAKAASRAaLEQVALGDFER---RQIGQ-LSGGQLQRVFV 145
Cdd:PRK14243 91 RRIGMVFQKPN---PFPKSIYDNIAYGA--RINGYK--GDMDELVERS-LRQAALWDEVKdklKQSGLsLSGGQQQRLCI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 146 ARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAgKTIIVIHHDLNKVSQYFDDLVVMN---------HG-IVDYG 215
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGyLVEFD 241
|
....*..
gi 510996587 216 PTDQVYN 222
Cdd:PRK14243 242 RTEKIFN 248
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-210 |
1.90e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 83.63 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 27 GKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK------SMRAVQKQVAYVEQrkDLDLNFPINVFDVVLTGTYGK 100
Cdd:PRK10982 24 HSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksSKEALENGISMVHQ--ELNLVLQRSVMDNMWLGRYPT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 101 LGLFRDPGKQAKaASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW 180
Cdd:PRK10982 102 KGMFVDQDKMYR-DTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL 180
|
170 180 190
....*....|....*....|....*....|
gi 510996587 181 RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:PRK10982 181 KERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-210 |
2.14e-18 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 80.97 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVAYVEQRKDLdlnFP-INVFDVVLTGT 97
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSL---LPwLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 98 YGKLGLFRDPGKQAkaASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGID------LQSEt 171
Cdd:TIGR01184 80 DRVLPDLSKSERRA--IVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDaltrgnLQEE- 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 510996587 172 aimaIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:TIGR01184 157 ----LMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-215 |
2.19e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.21 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG-----------KSMRAVQK 70
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpseKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 71 QVAYVEQRKDLdlnFP-INVFDVVLTGTYGKLGLFRdpgKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAI 149
Cdd:COG4161 83 KVGMVFQQYNL---WPhLTVMENLIEAPCKVLGLSK---EQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 150 VQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLN---KVSQYfddLVVMNHG-IVDYG 215
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEfarKVASQ---VVYMEKGrIIEQG 223
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-223 |
2.27e-18 |
|
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: 83.64 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 15 PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQ-----VAYVEQRKDLdlnFPINV 89
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlrqfINYLPQEPYI---FSGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 90 FDVVLTGTygKLGLFRDPGKQAK--AASRAALEQVALGDFER--RQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGI 165
Cdd:TIGR01193 565 LENLLLGA--KENVSQDEIWAACeiAEIKDDIENMPLGYQTElsEEGSSISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 166 DLQSETAIMAIMKQWRDagKTIIVIHHDLNkVSQYFDDLVVMNHG-IVDYGPTDQVYNA 223
Cdd:TIGR01193 643 DTITEKKIVNNLLNLQD--KTIIFVAHRLS-VAKQSDKIIVLDHGkIIEQGSHDELLDR 698
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-212 |
2.69e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.77 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 3 SIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV---QKQVAYVEQRK 79
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVppaERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 DLdlnFP-INVFDVVLTGTygKLglfrdpGKQAKAASRAALEQVA----LGDFERRQIGQLSGGQLQRVFVARAIVQEAE 154
Cdd:PRK11000 85 AL---YPhLSVAENMSFGL--KL------AGAKKEEINQRVNQVAevlqLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 155 IIILDEPFVGID--LQSETAImAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIV 212
Cdd:PRK11000 154 VFLLDEPLSNLDaaLRVQMRI-EISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-195 |
3.20e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVAYVEQRKDL 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 82 dlnFPI-NVFDVVLTGTYGKLglfrdpgkqaKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDE 160
Cdd:PRK11247 93 ---LPWkKVIDNVGLGLKGQW----------RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 510996587 161 PFVGIDlqsetAIMAI-MKQ-----WRDAGKTIIVIHHDLN 195
Cdd:PRK11247 160 PLGALD-----ALTRIeMQDlieslWQQHGFTVLLVTHDVS 195
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-224 |
3.39e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.23 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY-DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK-----SMRAVQKQVAYV 75
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRKdldlnfpinvfdVVLTGT-YGKLGLFRDPGKQAkaaSRAALEQVALGDFERR-----------QIGQLSGGQLQRV 143
Cdd:PRK10790 421 QQDP------------VVLADTfLANVTLGRDISEEQ---VWQALETVQLAELARSlpdglytplgeQGNNLSVGQKQLL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 144 FVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAgKTIIVIHHDLNKVSQYfDDLVVMNHG-IVDYGPTDQVYN 222
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVEA-DTILVLHRGqAVEQGTHQQLLA 563
|
..
gi 510996587 223 AQ 224
Cdd:PRK10790 564 AQ 565
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-228 |
5.65e-18 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 80.23 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR-----------AVQ 69
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvpADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 70 KQVAYVEQRkdLDLNF------------------PINVfdvvltgtygkLGLfrdPGKQAKAASRAALEQVALGDFERRQ 131
Cdd:COG4598 88 RQLQRIRTR--LGMVFqsfnlwshmtvlenvieaPVHV-----------LGR---PKAEAIERAEALLAKVGLADKRDAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 132 IGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGID--LQSEtaIMAIMKQWRDAGKTIIVIHHDLN---KVSqyfDDLVV 206
Cdd:COG4598 152 PAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDpeLVGE--VLKVMRDLAEEGRTMLVVTHEMGfarDVS---SHVVF 226
|
250 260
....*....|....*....|...
gi 510996587 207 MNHGIVD-YGPTDQVYNAQNIER 228
Cdd:COG4598 227 LHQGRIEeQGPPAEVFGNPKSER 249
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-161 |
6.10e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 82.47 E-value: 6.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 5 KNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYqGKSMravqkQVAYVEQ-RKDLDL 83
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-----KLAYVDQsRDALDP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 84 NfpINVFDVVLTGT-YGKLGLFRDPgkqakaaSRAaleqvALGDF------ERRQIGQLSGGQLQRVFVARAIVQEAEII 156
Cdd:PRK11819 402 N--KTVWEEISGGLdIIKVGNREIP-------SRA-----YVGRFnfkggdQQKKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
....*
gi 510996587 157 ILDEP 161
Cdd:PRK11819 468 LLDEP 472
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-225 |
8.01e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 81.30 E-value: 8.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM--RAVQKQ-VAYVEQR 78
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRdICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 KDLdlnFP-INVFDVVltgTYGkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:PRK11432 87 YAL---FPhMSLGENV---GYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510996587 158 LDEPFVGIDLQSETA----IMAIMKQWrdaGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQN 225
Cdd:PRK11432 160 FDEPLSNLDANLRRSmrekIRELQQQF---NITSLYVTHDQSEAFAVSDTVIVMNKGkIMQIGSPQELYRQPA 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-194 |
9.12e-18 |
|
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: 79.40 E-value: 9.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDT----PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-------RAV- 68
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldedaRARl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 69 -QKQVAYVEQrkdldlNFPI--------NVFdvvltgtygkLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQ 139
Cdd:COG4181 88 rARHVGFVFQ------SFQLlptltaleNVM----------LPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 140 LQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIM-KQWRDAGKTIIVIHHDL 194
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVLVTHDP 207
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-223 |
1.20e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.97 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKsmravqkqVAyveqrkdldlnFPINV---FDVVLT 95
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR--------VS-----------ALLELgagFHPELT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 96 G-----TYGK-LGLfrdpgkqAKAASRAALEQVA----LGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPF-VG 164
Cdd:COG1134 105 GreniyLNGRlLGL-------SRKEIDEKFDEIVefaeLGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLaVG 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 165 -IDLQsETAiMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNA 223
Cdd:COG1134 178 dAAFQ-KKC-LARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGrLVMDGDPEEVIAA 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-195 |
1.38e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.70 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDD----TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV-------- 68
Cdd:PRK11629 5 LLQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 69 -QKQVAYVEQRKDL--DLNFPINVFDVVLTGtygklglfrdpGKQAKAASRAALEQVALGDFERR---QIGQLSGGQLQR 142
Cdd:PRK11629 85 rNQKLGFIYQFHHLlpDFTALENVAMPLLIG-----------KKKPAEINSRALEMLAAVGLEHRanhRPSELSGGERQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 510996587 143 VFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLN 195
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-210 |
1.87e-17 |
|
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: 78.14 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 13 DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQ---------VAYVEQRKDLdl 83
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEatrsrnrysVAYAAQKPWL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 84 nfpinvfdvvLTGTYGKLGLFRDP-GKQA-KAASRAA-----LEQVALGDfeRRQIGQ----LSGGQLQRVFVARAIVQE 152
Cdd:cd03290 91 ----------LNATVEENITFGSPfNKQRyKAVTDACslqpdIDLLPFGD--QTEIGErginLSGGQRQRICVARALYQN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510996587 153 AEIIILDEPFVGIDLQSETAIM--AIMKQWRDAGKTIIVIHHDLnkvsQYF---DDLVVMNHG 210
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKL----QYLphaDWIIAMKDG 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-192 |
2.05e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.01 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVA-YDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLyqgksmRAVQKQVAYVEQRk 79
Cdd:COG4178 362 ALALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA------RPAGARVLFLPQR- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 dldlnfPinvfdvvltgtYGKLGLFRD-------PGKQAKAASRAALEQVALGDFERR--------QIgqLSGGQLQRVF 144
Cdd:COG4178 435 ------P-----------YLPLGTLREallypatAEAFSDAELREALEAVGLGHLAERldeeadwdQV--LSLGEQQRLA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510996587 145 VARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQwRDAGKTIIVIHH 192
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-210 |
2.56e-17 |
|
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: 80.60 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 27 GKITGIIGPNGAGKSTLIKAILGLVK-----------------ARQGSVLYQ------GKSMRAVQKqVAYVEQRKDldl 83
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKpnlgdydeepswdevlkRFRGTELQDyfkklaNGEIKVAHK-PQYVDLIPK--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 84 nfpinvfdvVLTGTYGKLgLfrdpgkqAKAASRAALEQVA----LGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILD 159
Cdd:COG1245 175 ---------VFKGTVREL-L-------EKVDERGKLDELAeklgLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510996587 160 EPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLnKVSQYFDDLVVMNHG 210
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL-AILDYLADYVHILYG 287
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-221 |
2.79e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 79.46 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYD----DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG--------KSMRAV 68
Cdd:PRK11153 1 MIELKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltalseKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 69 QKQVAYVEQRKDLdLNfPINVFDVV-----LTGTygklglfrdpgKQAKAASRAA--LEQVALGDFERRQIGQLSGGQLQ 141
Cdd:PRK11153 81 RRQIGMIFQHFNL-LS-SRTVFDNValpleLAGT-----------PKAEIKARVTelLELVGLSDKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 142 RVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQ 219
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGrLVEQGTVSE 227
|
..
gi 510996587 220 VY 221
Cdd:PRK11153 228 VF 229
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-192 |
3.77e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.80 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGL--VKARQGSVLYQGKSM-------RAvqkqv 72
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDIlelspdeRA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 73 ayveqRKDLDLNFP-------INVFDVVLTGtYGKLGLFRDPGKQAKAASRAALEQVALG-DFERRQIGQ-LSGGQLQRV 143
Cdd:COG0396 76 -----RAGIFLAFQypveipgVSVSNFLRTA-LNARRGEELSAREFLKLLKEKMKELGLDeDFLDRYVNEgFSGGEKKRN 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510996587 144 FVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHH 192
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-194 |
6.40e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 6.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 27 GKITGIIGPNGAGKSTLIKAILG-----------------LVKARQGSVLYQ------GKSMRAVQKqVAYVEQ-RKdld 82
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepswdeVLKRFRGTELQNyfkklyNGEIKVVHK-PQYVDLiPK--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 83 lnfpinvfdvVLTGTYGKLglfrdpgkQAKAASRAALEQVA----LGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIIL 158
Cdd:PRK13409 175 ----------VFKGKVREL--------LKKVDERGKLDEVVerlgLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*....
gi 510996587 159 DEPFVGIDL-QSETAIMAImkqwRD--AGKTIIVIHHDL 194
Cdd:PRK13409 237 DEPTSYLDIrQRLNVARLI----RElaEGKYVLVVEHDL 271
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-166 |
6.96e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 79.29 E-value: 6.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILG-----------LVKARQGSvlyqGKSMRAVQKQV 72
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGS----GETIWDIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 73 AYVEQRKDLDLNFPINVFDVVLTGTYGKLGLFRD-PGKQAKAASR--AAL---EQVALGDFERrqigqLSGGQLQRVFVA 146
Cdd:PRK10938 339 GYVSSSLHLDYRVSTSVRNVILSGFFDSIGIYQAvSDRQQKLAQQwlDILgidKRTADAPFHS-----LSWGQQRLALIV 413
|
170 180
....*....|....*....|
gi 510996587 147 RAIVQEAEIIILDEPFVGID 166
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLD 433
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-221 |
7.13e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 78.23 E-value: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY-----DDTPVfTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKAR---QGSVLYQGKS-------- 64
Cdd:PRK09473 12 LLDVKDLRVTFstpdgDVTAV-NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREilnlpeke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 65 ---MRAvqKQVAYVEQRKDLDLNFPINVFD-----VVLTGTYGKlglfrdpgKQAKAASRAALEQVALGDfERRQIG--- 133
Cdd:PRK09473 91 lnkLRA--EQISMIFQDPMTSLNPYMRVGEqlmevLMLHKGMSK--------AEAFEESVRMLDAVKMPE-ARKRMKmyp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 134 -QLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG- 210
Cdd:PRK09473 160 hEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAGr 239
|
250
....*....|.
gi 510996587 211 IVDYGPTDQVY 221
Cdd:PRK09473 240 TMEYGNARDVF 250
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
5-215 |
8.13e-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: 79.09 E-value: 8.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 5 KNLTVAYD-DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAV-----QKQVAYVEQr 78
Cdd:COG5265 361 ENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVtqaslRAAIGIVPQ- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 kdldlnfpinvfDVVLTGT-------YGKLGlfrdpgkqakaASRAALEQVA----LGDFERR-------QIGQ----LS 136
Cdd:COG5265 440 ------------DTVLFNDtiayniaYGRPD-----------ASEEEVEAAAraaqIHDFIESlpdgydtRVGErglkLS 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 137 GGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRdAGKTIIVIHHDLNKVsQYFDDLVVMNHG-IVDYG 215
Cdd:COG5265 497 GGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTI-VDADEILVLEAGrIVERG 574
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-212 |
8.67e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.84 E-value: 8.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM------RAVQKQVAY 74
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqtaKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 V-EQRKdldlnfpinVFD-VVLTGTYGKLGLFRDpgKQAKAASRAALEQVALGDFERR--QIGQLSGGQLQRVFVARAIV 150
Cdd:PRK11614 85 VpEGRR---------VFSrMTVEENLAMGGFFAE--RDQFQERIKWVYELFPRLHERRiqRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510996587 151 QEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIV 212
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
1.06e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.01 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQ------GSVLYQGKSMRAV-----Q 69
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIdaiklR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 70 KQVAYVEQRKDldlNFP-INVFDVVltgTYGKLGLFRDPGKQAKAASRAALEQVALG----DFERRQIGQLSGGQLQRVF 144
Cdd:PRK14246 90 KEVGMVFQQPN---PFPhLSIYDNI---AYPLKSHGIKEKREIKKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 145 VARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAgKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNA 223
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGeLVEWGSSNEIFTS 242
|
....
gi 510996587 224 QNIE 227
Cdd:PRK14246 243 PKNE 246
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-210 |
1.26e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.51 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTvayddTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQ------VAYV 75
Cdd:PRK10762 258 LKVDNLS-----GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 -EQRKDLDLNFPINVFD-VVLTGtygkLGLFRDPGKQAKAASraalEQVALGDFER----------RQIGQLSGGQLQRV 143
Cdd:PRK10762 333 sEDRKRDGLVLGMSVKEnMSLTA----LRYFSRAGGSLKHAD----EQQAVSDFIRlfniktpsmeQAIGLLSGGNQQKV 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 144 FVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-232 |
1.48e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 17 FTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRA------VQKQVAYV---EQRKDLDLNFPI 87
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlstaqrLARGLVYLpedRQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 88 --NVFDVvltgTYGKLGLFRDPGKQakaasRAALEQV--ALG---DFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDE 160
Cdd:PRK15439 359 awNVCAL----THNRRGFWIKPARE-----NAVLERYrrALNikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510996587 161 PFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIVDYGPTDQVYNAQNIER-AFSA 232
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRlAFGE 502
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-219 |
1.53e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKA---RQGSVLYQGKSMRAVQKQV--AYVEQRkdlDLNFP-INVFDV 92
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAisAYVQQD---DLFIPtLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 93 VLTGTYGKLGLfRDPGKQAKAASRAALEQVALGDFERRQIGQ------LSGGQLQRVFVARAIVQEAEIIILDEPFVGID 166
Cdd:TIGR00955 120 LMFQAHLRMPR-RVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 167 LQSETAIMAIMKQWRDAGKTIIV-IHHDLNKVSQYFDDLVVMNHGIVDY-GPTDQ 219
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILMAEGRVAYlGSPDQ 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-210 |
1.86e-16 |
|
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: 78.52 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTVAYDDT--PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK----SMRAVQKQVAYVEQ 77
Cdd:TIGR01257 931 VKNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 RKDLDLNFPINVFDVVLTGTYGKlglfrdPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGR------SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510996587 158 LDEPFVGIDLQSETAIMAIMKQWRdAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-217 |
2.48e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 76.66 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTVAYD-DTP----VFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLY------------------ 60
Cdd:PRK13651 5 VKNIVKIFNkKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkekekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 61 -----------QGKSMRAVQKQVAYVEQRKDLDLnFPINVFDVVLTG--TYGKlglfrdPGKQAKAASRAALEQVALG-D 126
Cdd:PRK13651 85 eklviqktrfkKIKKIKEIRRRVGVVFQFAEYQL-FEQTIEKDIIFGpvSMGV------SKEEAKKRAAKYIELVGLDeS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 127 FERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVV 206
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
250
....*....|..
gi 510996587 207 MNHG-IVDYGPT 217
Cdd:PRK13651 238 FKDGkIIKDGDT 249
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-221 |
2.76e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.65 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVK----AR-QGSVLYQGKSMRA-------VQ 69
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeARvEGEVRLFGRNIYSpdvdpieVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 70 KQVAYVEQRKDldlNFP-INVFDVVLTGTygKLGLFRDPGKQAKAASRAALEQVALGDFERRQI----GQLSGGQLQRVF 144
Cdd:PRK14267 85 REVGMVFQYPN---PFPhLTIYDNVAIGV--KLNGLVKSKKELDERVEWALKKAALWDEVKDRLndypSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510996587 145 VARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAgKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVY 221
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGkLIEVGPTRKVF 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-226 |
2.78e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.90 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYD---DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRA-----VQKQV 72
Cdd:PRK13642 4 ILEVENLVFKYEkesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenvwnLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 73 AYVEQRKDLDLnFPINVFDVVLTGTYGKlGLfrdPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQE 152
Cdd:PRK13642 84 GMVFQNPDNQF-VGATVEDDVAFGMENQ-GI---PREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 153 AEIIILDEPFVGIDLQSETAIMAIMKQWRDAGK-TIIVIHHDLNKVSQYfDDLVVMNHG--IVDYGPTDQVYNAQNI 226
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASS-DRILVMKAGeiIKEAAPSELFATSEDM 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-241 |
3.08e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVAYVEQRKDLDL---NFPINVFDVVLT 95
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMvfqSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 96 GTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIM- 174
Cdd:PRK10070 126 NTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQd 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510996587 175 AIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYN--AQNIERAF--SADLSAVLFEK 241
Cdd:PRK10070 206 ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGeVVQVGTPDEILNnpANDYVRTFfrGVDISQVFSAK 277
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-210 |
4.14e-16 |
|
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: 77.17 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVK--ARQGSVLYQGKSMRAV------QKQV 72
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASnirdteRAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 73 AYVEQRKDL--DLNFPINVF---DVVLTGtygklGLFRDPGKQAKAasRAALEQVALGDF-ERRQIGQLSGGQLQRVFVA 146
Cdd:TIGR02633 81 VIIHQELTLvpELSVAENIFlgnEITLPG-----GRMAYNAMYLRA--KNLLRELQLDADnVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996587 147 RAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-210 |
5.04e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.53 E-value: 5.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 20 VAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-RAVQKQVAYVEQR-----KDLDLNFPINVFDVV 93
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItRLKNREVPFLRRQigmifQDHHLLMDRTVYDNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 94 LTgtygKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAI 173
Cdd:PRK10908 101 AI----PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 510996587 174 MAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:PRK10908 177 LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-212 |
6.48e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.12 E-value: 6.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDD------TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG------KSMRAV 68
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 69 QKQVAYVEQRKDLDLNFPINVFDVvltgTYG--KLGLfrdPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVA 146
Cdd:PRK13633 84 RNKAGMVFQNPDNQIVATIVEEDV----AFGpeNLGI---PPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 147 RAIVQEAEIIILDEPFVGIDLQSETAIM-AIMKQWRDAGKTIIVIHHDLNKVSQYfDDLVVMNHGIV 212
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVnTIKELNKKYGITIILITHYMEEAVEA-DRIIVMDSGKV 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-192 |
9.12e-16 |
|
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: 72.19 E-value: 9.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY-DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVlyqgksMRAVQKQVAYVEQRkd 80
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI------GMPEGEDLLFLPQR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 81 ldlnfpinvfdvvltgTYGKLGLFRdpgkqakaasraalEQVAL--GDferrqigQLSGGQLQRVFVARAIVQEAEIIIL 158
Cdd:cd03223 73 ----------------PYLPLGTLR--------------EQLIYpwDD-------VLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....
gi 510996587 159 DEPFVGIDLQSETAIMAIMKqwrDAGKTIIVIHH 192
Cdd:cd03223 116 DEATSALDEESEDRLYQLLK---ELGITVISVGH 146
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-205 |
1.22e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.62 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 27 GKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKsmravqkqVAYVEQRkdLDLNFPINVFDVvLTGTYGKLGlfrD 106
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--------ISYKPQY--IKPDYDGTVEDL-LRSITDDLG---S 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 107 PGKQAKAASRAALEQValgdFERRqIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDL-QSETAIMAIMKQWRDAGK 185
Cdd:PRK13409 431 SYYKSEIIKPLQLERL----LDKN-VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeQRLAVAKAIRRIAEEREA 505
|
170 180
....*....|....*....|
gi 510996587 186 TIIVIHHDLnkvsqYFDDLV 205
Cdd:PRK13409 506 TALVVDHDI-----YMIDYI 520
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-210 |
2.40e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.56 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 26 AGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR------AVQKQVAYV-EQRKDLDLnFPI-NVFD---VVL 94
Cdd:PRK11288 278 AGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdAIRAGIMLCpEDRKAEGI-IPVhSVADninISA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 95 TGTYGKLGLFRDPGKQAKAASRAaLEQVALGDFERRQ-IGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAI 173
Cdd:PRK11288 357 RRHHLRAGCLINNRWEAENADRF-IRSLNIKTPSREQlIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEI 435
|
170 180 190
....*....|....*....|....*....|....*..
gi 510996587 174 MAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:PRK11288 436 YNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREG 472
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-219 |
2.84e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.38 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAydDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR------AVQKQVAY 74
Cdd:PRK10982 250 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnaneAINHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 V-EQRK------DLDLNFpiNVFDVVLTGTYGKLGLFRDpgKQAKAASRAALEQVALGD-FERRQIGQLSGGQLQRVFVA 146
Cdd:PRK10982 328 VtEERRstgiyaYLDIGF--NSLISNIRNYKNKVGLLDN--SRMKSDTQWVIDSMRVKTpGHRTQIGSLSGGNQQKVIIG 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 147 RAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG----IVDYGPTDQ 219
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGlvagIVDTKTTTQ 480
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-216 |
4.31e-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: 74.21 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKN--LTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGksmravqkQVAYVEQR- 78
Cdd:TIGR00957 637 ITVHNatFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------SVAYVPQQa 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 --KDLDLNFPInVFDVVLTGTYGKLGLfrdpgkQAkAASRAALEQVALGDfeRRQIGQ----LSGGQLQRVFVARAIVQE 152
Cdd:TIGR00957 709 wiQNDSLRENI-LFGKALNEKYYQQVL------EA-CALLPDLEILPSGD--RTEIGEkgvnLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 153 AEIIILDEPFVGIDLQSETAIM--AIMKQWRDAGKTIIVIHHDLNKVSQyFDDLVVMNHG-IVDYGP 216
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFehVIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGkISEMGS 844
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-210 |
6.31e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.42 E-value: 6.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVK--ARQGSVLYQGKSMRAV------QKQV 72
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASnirdteRAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 73 AYVEQRKDL--DLNFPINVFdvvLTGTYGKLGLFRDPGKQAKAasRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIV 150
Cdd:PRK13549 85 AIIHQELALvkELSVLENIF---LGNEITPGGIMDYDAMYLRA--QKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 151 QEAEIIILDEPFVGIDlQSETAI-MAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:PRK13549 160 KQARLLILDEPTASLT-ESETAVlLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-206 |
6.73e-15 |
|
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: 71.67 E-value: 6.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 24 FDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSmravqkqVAYVEQRKDLDlnFPINVFDVVltgtYGKL-G 102
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-------VSYKPQYIKAD--YEGTVRDLL----SSITkD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 103 LFRDPGKQAKAASRAALEQVAlgdfeRRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDlqSETAIMA---IMKQ 179
Cdd:cd03237 89 FYTHPYFKTEIAKPLQIEQIL-----DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRLMAskvIRRF 161
|
170 180
....*....|....*....|....*..
gi 510996587 180 WRDAGKTIIVIHHDLNKVSQYFDDLVV 206
Cdd:cd03237 162 AENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-205 |
8.80e-15 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 71.63 E-value: 8.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 27 GKITGIIGPNGAGKSTLIKAILGLVKARQGSvlYQG--------KSMRAVQKQvAYVEQRKDLDLNF---PINVfDVVLT 95
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDppdwdeilDEFRGSELQ-NYFTKLLEGDVKVivkPQYV-DLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 96 GTYGKLGLF----RDPGKQAKAASRAALEQVAlgdfeRRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSET 171
Cdd:cd03236 102 AVKGKVGELlkkkDERGKLDELVDQLELRHVL-----DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|....
gi 510996587 172 AIMAIMKQWRDAGKTIIVIHHDLnKVSQYFDDLV 205
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEHDL-AVLDYLSDYI 209
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-210 |
1.08e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 26 AGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-----RAVQKQ-VAYVEQRKDLDLNFPI--NVFdvvL--- 94
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpKSSQEAgIGIIHQELNLIPQLTIaeNIF---Lgre 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 95 -TGTYGKLGLfrdpgKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPfvgIDLQSET-- 171
Cdd:PRK10762 106 fVNRFGRIDW-----KKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP---TDALTDTet 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 510996587 172 -AIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:PRK10762 178 eSLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-210 |
1.10e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.99 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 27 GKITGIIGPNGAGKSTLIKAILGLVKAR--QGSVLYQ-GKSMRAVQKQVAYVEQRkdlDLNFPinvfDVVLTGTYGKLGL 103
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANnRKPTKQILKRTGFVTQD---DILYP----HLTVRETLVFCSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 104 FRDP---GKQAK-AASRAALEQVALGDFERRQIGQ-----LSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIM 174
Cdd:PLN03211 167 LRLPkslTKQEKiLVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190
....*....|....*....|....*....|....*..
gi 510996587 175 AIMKQWRDAGKTIIV-IHHDLNKVSQYFDDLVVMNHG 210
Cdd:PLN03211 247 LTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEG 283
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-210 |
2.15e-14 |
|
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: 69.77 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 15 PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKS------------MRAVQKQ-VAYVEQrkdl 81
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqaspreILALRRRtIGYVSQ---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 82 dlnFpINV------FDVVltgtygKLGLFRDPGKQAKAASRAAleqvALgdFERRQIGQ---------LSGGQLQRVFVA 146
Cdd:COG4778 101 ---F-LRViprvsaLDVV------AEPLLERGVDREEARARAR----EL--LARLNLPErlwdlppatFSGGEQQRVNIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996587 147 RAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-233 |
2.57e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 72.29 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 16 VFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQvayveqrkdlDLNFPINVF--DVV 93
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLH----------DLRFKITIIpqDPV 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 94 LTGtyGKLGLFRDP-GKQAKAASRAALEQVALGDFERRQIGQL-----------SGGQLQRVFVARAIVQEAEIIILDEP 161
Cdd:TIGR00957 1371 LFS--GSLRMNLDPfSQYSDEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996587 162 FVGIDLQSETAIMA-IMKQWRDAgkTIIVIHHDLNKVSQYfDDLVVMNHGIV-DYGPTDQVYNAQNIERAFSAD 233
Cdd:TIGR00957 1449 TAAVDLETDNLIQStIRTQFEDC--TVLTIAHRLNTIMDY-TRVIVLDKGEVaEFGAPSNLLQQRGIFYSMAKD 1519
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-193 |
3.61e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 16 VFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKqvayvEQRKDL---DLNFPINVFdv 92
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDE-----EARAKLrakHVGFVFQSF-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 93 VLTGTYGKL------GLFR-DPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGI 165
Cdd:PRK10584 98 MLIPTLNALenvelpALLRgESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180
....*....|....*....|....*....
gi 510996587 166 DLQSETAIMAIMKQW-RDAGKTIIVIHHD 193
Cdd:PRK10584 178 DRQTGDKIADLLFSLnREHGTTLILVTHD 206
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-210 |
4.76e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.71 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMR------AVQKQVAYV 75
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfasttaALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQrkDLDLNFPINVFDVVLTGTY-GKLGLFRdpGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAE 154
Cdd:PRK11288 85 YQ--ELHLVPEMTVAENLYLGQLpHKGGIVN--RRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 155 IIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-212 |
5.57e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.16 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYD---DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILG-LVKARQGSVLYQGksmravqkQVAYVEQ 77
Cdd:PLN03232 615 ISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRG--------SVAYVPQ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 rkdLDLNFPINVFDVVLTGTYgklglfRDPGKQAKAASRAALEQVA--LGDFERRQIGQ----LSGGQLQRVFVARAIVQ 151
Cdd:PLN03232 687 ---VSWIFNATVRENILFGSD------FESERYWRAIDVTALQHDLdlLPGRDLTEIGErgvnISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 152 EAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQyFDDLVVMNHGIV 212
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPL-MDRIILVSEGMI 817
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-222 |
8.18e-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: 70.22 E-value: 8.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKAR--QGSVLYQ------------------ 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 62 -----GKSM---------------RAVQKQVAYVEQRkdldlNFPINVFDVVLTGTYGKLGLFRDPGKQAKAASRAALEQ 121
Cdd:TIGR03269 81 pcpvcGGTLepeevdfwnlsdklrRRIRKRIAIMLQR-----TFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 122 VALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIM-AIMKQWRDAGKTIIVIHHDLNKVSQY 200
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHnALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|...
gi 510996587 201 FDDLVVMNHG-IVDYGPTDQVYN 222
Cdd:TIGR03269 236 SDKAIWLENGeIKEEGTPDEVVA 258
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-205 |
9.30e-14 |
|
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: 70.20 E-value: 9.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 27 GKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKsmravqkqVAYVEQRkdLDLNFPINVFDVvLTGTYGKLglFRD 106
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------ISYKPQY--ISPDYDGTVEEF-LRSANTDD--FGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 107 PGKQAKAASRAALEQValgdFERrQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDlqSETAIM---AIMKQWRDA 183
Cdd:COG1245 433 SYYKTEIIKPLGLEKL----LDK-NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLAvakAIRRFAENR 505
|
170 180
....*....|....*....|..
gi 510996587 184 GKTIIVIHHDLnkvsqYFDDLV 205
Cdd:COG1245 506 GKTAMVVDHDI-----YLIDYI 522
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-210 |
9.90e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.82 E-value: 9.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTV---AYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQ--GSVLYQGKSM------RAVQ 69
Cdd:NF040905 257 VFEVKNWTVyhpLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNisGTVFKDGKEVdvstvsDAID 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 70 KQVAYV-EQRKDLDLNFPINV-FDVVLTGtYGKL--GLFRDPGKQAKAAS--RAALEQVALGDFErrQIGQLSGGQLQRV 143
Cdd:NF040905 337 AGLAYVtEDRKGYGLNLIDDIkRNITLAN-LGKVsrRGVIDENEEIKVAEeyRKKMNIKTPSVFQ--KVGNLSGGNQQKV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 144 FVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:NF040905 414 VLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEG 480
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-215 |
1.05e-13 |
|
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: 67.94 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 16 VFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLyqgksmraVQKQVAYVeqrkdLDLNFPinvFDVVLT 95
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT--------VRGRVSSL-----LGLGGG---FNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 96 G---TYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPF-VGiDLQSET 171
Cdd:cd03220 101 GrenIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLaVG-DAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 510996587 172 AIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYG 215
Cdd:cd03220 180 KCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGkIRFDG 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-221 |
1.07e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 22 VHFD--AGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK---SMRAVQKQVAyveqRKDLDLNF--PINVFDVVL 94
Cdd:PRK10261 343 VSFDlwPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQAL----RRDIQFIFqdPYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 95 TGTYGKLGLFRDPG--KQAKAASRAA--LEQVAL-GDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQS 169
Cdd:PRK10261 419 TVGDSIMEPLRVHGllPGKAAAARVAwlLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 510996587 170 ETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVY 221
Cdd:PRK10261 499 RGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGqIVEIGPRRAVF 552
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-210 |
1.47e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTP---VFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKAR-QGSVLYQGKSMR------AVQK 70
Cdd:PRK13549 259 ILEVRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKirnpqqAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 71 QVAYV-EQRKDLDLnfpINVFDVVLTGTYGKLGLFRDPGKQAKAAsraalEQVALGDFERR----------QIGQLSGGQ 139
Cdd:PRK13549 339 GIAMVpEDRKRDGI---VPVMGVGKNITLAALDRFTGGSRIDDAA-----ELKTILESIQRlkvktaspelAIARLSGGN 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 140 LQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:PRK13549 411 QQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-166 |
1.56e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.77 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYD---DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQ-GSVLYQGKsmravqkqVAYVEQ 77
Cdd:PLN03130 615 ISIKNGYFSWDskaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT--------VAYVPQ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 rkdLDLNFPINVFDVVLtgtygkLGLFRDPGKQAKAASRAALEQ----VALGDFErrQIGQ----LSGGQLQRVFVARAI 149
Cdd:PLN03130 687 ---VSWIFNATVRDNIL------FGSPFDPERYERAIDVTALQHdldlLPGGDLT--EIGErgvnISGGQKQRVSMARAV 755
|
170
....*....|....*..
gi 510996587 150 VQEAEIIILDEPFVGID 166
Cdd:PLN03130 756 YSNSDVYIFDDPLSALD 772
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-232 |
1.66e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.38 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 3 SIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM------RAVQKQVAYVE 76
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadarhrRAVCPRIAYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 Q--RKDL--DLNFPINV-FdvvltgtYGKL-GLfrdpgkqaKAASRAA-----LEQVALGDFERRQIGQLSGGQLQRVFV 145
Cdd:NF033858 83 QglGKNLypTLSVFENLdF-------FGRLfGQ--------DAAERRRridelLRATGLAPFADRPAGKLSGGMKQKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 146 ARAIVQEAEIIILDEPFVGID-L---QSETAIMAIMKqwRDAGKTIIVihhdlnkVSQY------FDDLVVMNHG-IVDY 214
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDpLsrrQFWELIDRIRA--ERPGMSVLV-------ATAYmeeaerFDWLVAMDAGrVLAT 218
|
250 260
....*....|....*....|.
gi 510996587 215 GPTDQVY---NAQNIERAFSA 232
Cdd:NF033858 219 GTPAELLartGADTLEAAFIA 239
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-210 |
1.71e-13 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 66.58 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 18 TDVAVHFDAGKITGIIGPNGAGKSTLIKAILglvkarqgsvlyqgksmrAVQKQVAYVEQRKdldlnfpinVFDVVLTGT 97
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL------------------YASGKARLISFLP---------KFSRNKLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 98 YGKLGLFRDPGkqakaasraaLEQVALGdferRQIGQLSGGQLQRVFVARAIVQEAE--IIILDEPFVGIDLQSETAIMA 175
Cdd:cd03238 65 IDQLQFLIDVG----------LGYLTLG----QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE 130
|
170 180 190
....*....|....*....|....*....|....*
gi 510996587 176 IMKQWRDAGKTIIVIHHDLnKVSQYFDDLVVMNHG 210
Cdd:cd03238 131 VIKGLIDLGNTVILIEHNL-DVLSSADWIIDFGPG 164
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-192 |
2.11e-13 |
|
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: 67.29 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILG--LVKARQGSVLYQGKSMRAVQkqvayVEQRk 79
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELE-----PDER- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 dldlnfpinvfdvvltgtyGKLGLFRD-------PG-------KQAKAASRAALEQVALGDFE-RRQIGQL--------- 135
Cdd:TIGR01978 75 -------------------ARAGLFLAfqypeeiPGvsnleflRSALNARRSARGEEPLDLLDfEKLLKEKlalldmdee 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 136 ----------SGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHH 192
Cdd:TIGR01978 136 flnrsvnegfSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITH 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-217 |
2.36e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.77 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSmravqkQVAYVEQRKDL 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA------NIGYYAQDHAY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 82 DLNFPINVFD------------VVLTGTYGKLgLFR--DPGKQAKAasraaleqvalgdferrqigqLSGGQLQRVFVAR 147
Cdd:PRK15064 394 DFENDLTLFDwmsqwrqegddeQAVRGTLGRL-LFSqdDIKKSVKV---------------------LSGGEKGRMLFGK 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 148 AIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDagkTIIVIHHDLNKVSQYFDDLV-VMNHGIVDYGPT 217
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG---TLIFVSHDREFVSSLATRIIeITPDGVVDFSGT 519
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-199 |
2.57e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.05 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK-----SMRAVQKQVAYV 75
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRKDLdlnFPINVFDvVLTGTYGKLGLFRDPGKQAKAASRAALEQVALgdfeRRQIGQLSGGQLQRVFVARAIVQEAEI 155
Cdd:PRK10247 87 AQTPTL---FGDTVYD-NLIFPWQIRNQQPDPAIFLDDLERFALPDTIL----TKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 510996587 156 IILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQ 199
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINH 203
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-220 |
2.75e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.26 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKS-------------MRA 67
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyalseaeRRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 68 VQK-QVAYVEQ--RKDLDLNFPI--NVFDVVL-TGT--YGKLglfrdpgkqaKAASRAALEQVALgDFER--RQIGQLSG 137
Cdd:PRK11701 86 LLRtEWGFVHQhpRDGLRMQVSAggNIGERLMaVGArhYGDI----------RATAGDWLERVEI-DAARidDLPTTFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 138 GQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYG 215
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGrVVESG 234
|
....*
gi 510996587 216 PTDQV 220
Cdd:PRK11701 235 LTDQV 239
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-210 |
2.78e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.66 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVAY------ 74
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAqlgigi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRKDLdlnfpINVFDVVLTGTYGKLglfrdPGKQ---------AKAASRAA--LEQVALGDFERRQIGQLSGGQLQRV 143
Cdd:PRK09700 85 IYQELSV-----IDELTVLENLYIGRH-----LTKKvcgvniidwREMRVRAAmmLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 144 FVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-192 |
2.84e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILG--LVKARQGSVLYQGKS-------MR----- 66
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESildlepeERahlgi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 67 --AVQKQV-------------AYVEQRKDLDLNF--PINVFDVVLTgtygKLGLFrdpGKQAKAASRAALEQVALGDFER 129
Cdd:CHL00131 87 flAFQYPIeipgvsnadflrlAYNSKRKFQGLPEldPLEFLEIINE----KLKLV---GMDPSFLSRNVNEGFSGGEKKR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510996587 130 RQIGQLsggqlqrvfvaraIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHH 192
Cdd:CHL00131 160 NEILQM-------------ALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-210 |
3.55e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 68.31 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTP---VFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKAR-QGSVLYQGKSM------RAVQK 70
Cdd:TIGR02633 257 ILEARNLTCWDVINPhrkRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVdirnpaQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 71 QVAYV-EQRKD----LDLNFPINVFDVVLTgTYGKLGLFRDPGKQAkaASRAALEQVALGDFERR-QIGQLSGGQLQRVF 144
Cdd:TIGR02633 337 GIAMVpEDRKRhgivPILGVGKNITLSVLK-SFCFKMRIDAAAELQ--IIGSAIQRLKVKTASPFlPIGRLSGGNQQKAV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 145 VARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-223 |
4.81e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDD----TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQV---- 72
Cdd:PRK10261 12 VLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQViels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 73 ---------------AYVEQRKDLDLNFPINVFDVVLTGTYGKLGLFRDpgkQAKAASRAALEQVALGDFE---RRQIGQ 134
Cdd:PRK10261 92 eqsaaqmrhvrgadmAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASRE---EAMVEAKRMLDQVRIPEAQtilSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 135 LSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IV 212
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGeAV 248
|
250
....*....|.
gi 510996587 213 DYGPTDQVYNA 223
Cdd:PRK10261 249 ETGSVEQIFHA 259
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-222 |
1.12e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.44 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGS------VLY---QGKSMRAVQKQVAYVEQRKDLdlnFPinV 89
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRivlngrVLFdaeKGICLPPEKRRIGYVFQDARL---FP--H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 90 FDVVLTGTYGklglfrdpgkqAKAASRAALEQ-VALGDFE---RRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGI 165
Cdd:PRK11144 91 YKVRGNLRYG-----------MAKSMVAQFDKiVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510996587 166 DLQSETAIMAIMKQWRDAGKT-IIVIHHDLNKVSQYFDDLVVMNHGIVD-YGPTDQVYN 222
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKaFGPLEEVWA 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
27-220 |
1.28e-12 |
|
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: 66.75 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 27 GKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQ-----------GKSMRAVQKQ-VAYVEQRKDLdlnFPINVFDVVL 94
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpGPDGRGRAKRyIGILHQEYDL---YPHRTVLDNL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 95 TGTYGkLGLfrdPGKQAKAASRAALEQVALGDFERRQI-----GQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQS 169
Cdd:TIGR03269 387 TEAIG-LEL---PDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPIT 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510996587 170 ETAIM-AIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQV 220
Cdd:TIGR03269 463 KVDVThSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGkIVKIGDPEEI 515
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-213 |
1.49e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.49 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY-----DDTPVFTDVAVHFDAGK-ITgIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-------RA 67
Cdd:COG1101 1 MLELKNLSKTFnpgtvNEKRALDGLNLTIEEGDfVT-VIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 68 vqKQVAYVEQrkDldlnfPinvfdvvLTGTYG----------------KLGLFRDPGKQAKAASRAALEQVALGdFERR- 130
Cdd:COG1101 80 --KYIGRVFQ--D-----P-------MMGTAPsmtieenlalayrrgkRRGLRRGLTKKRRELFRELLATLGLG-LENRl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 131 --QIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVM 207
Cdd:COG1101 143 dtKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMM 222
|
....*...
gi 510996587 208 NHG--IVD 213
Cdd:COG1101 223 HEGriILD 230
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-234 |
1.49e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.73 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLyqgksmraVQKQVAYVEQRKdldlnfpinvfdVVLTGTY 98
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------AERSIAYVPQQA------------WIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 99 GKLGLFRDPGKQAKAAS-------RAALEQVAlGDFErRQIGQ----LSGGQLQRVFVARAIVQEAEIIILDEPFVGIDL 167
Cdd:PTZ00243 738 RGNILFFDEEDAARLADavrvsqlEADLAQLG-GGLE-TEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 168 QSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYfDDLVVMNHGIVDYGPTDQVYNAQNIERAFSADL 234
Cdd:PTZ00243 816 HVGERVVEECFLGALAGKTRVLATHQVHVVPRA-DYVVALGDGRVEFSGSSADFMRTSLYATLAAEL 881
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-205 |
1.76e-12 |
|
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: 66.50 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 3 SIKNLTVAYD-DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKArqgsvlYQGKSMRAVQKQVAYVEQRKDL 81
Cdd:TIGR03719 6 TMNRVSKVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------FNGEARPQPGIKVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 82 DLNfpINVFDVVLTGTYGKLGL----------FRDPGKQ--AKAASRAALEQV--ALG--DFERR--------------- 130
Cdd:TIGR03719 80 DPT--KTVRENVEEGVAEIKDAldrfneisakYAEPDADfdKLAAEQAELQEIidAADawDLDSQleiamdalrcppwda 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 131 QIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSetaiMAIMKQW-RDAGKTIIVIHHDlnkvsQYFDDLV 205
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHlQEYPGTVVAVTHD-----RYFLDNV 224
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-210 |
2.63e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 63.42 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLT----VAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLI-----KAILGLVKarqGSVLYQGKSMR-AVQKQ 71
Cdd:cd03232 4 LTWKNLNytvpVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLdvlagRKTAGVIT---GEILINGRPLDkNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 72 VAYVEQrkdLDLNFPinvfdvvltgtygklglfrdpgkqaKAASRAALEQVALgdferrqIGQLSGGQLQRVFVARAIVQ 151
Cdd:cd03232 81 TGYVEQ---QDVHSP-------------------------NLTVREALRFSAL-------LRGLSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 152 EAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIV-IHHDLNKVSQYFDDLVVMNHG 210
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCtIHQPSASIFEKFDRLLLLKRG 185
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-223 |
2.92e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 65.31 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDdTP-----VFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKAR----------QGSVLYQ---G 62
Cdd:COG4170 3 LLDIRNLTIEID-TPqgrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGIDLLKlspR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 63 KSMRAVQKQVAYVEQ--RKDLDLNFPI--NVFDVVLTGTYGklGLFRDPGKQAKAASRAALEQVALGDFERrqI-----G 133
Cdd:COG4170 82 ERRKIIGREIAMIFQepSSCLDPSAKIgdQLIEAIPSWTFK--GKWWQRFKWRKKRAIELLHRVGIKDHKD--ImnsypH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 134 QLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAI---MAIMKQWRdaGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIfrlLARLNQLQ--GTSILLISHDLESISQWADTITVLYCG 235
|
250
....*....|....
gi 510996587 211 -IVDYGPTDQVYNA 223
Cdd:COG4170 236 qTVESGPTEQILKS 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-210 |
4.21e-12 |
|
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: 65.42 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDT--PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM----RAVQKQVAY 74
Cdd:TIGR01257 1937 ILRLNELTKVYSGTssPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltniSDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQrkdldlnfpINVFDVVLTGT-----YGKL-GLfrdPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARA 148
Cdd:TIGR01257 2017 CPQ---------FDAIDDLLTGRehlylYARLrGV---PAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 149 IVQEAEIIILDEPFVGIDLQSE----TAIMAIMKQwrdaGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARrmlwNTIVSIIRE----GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-210 |
5.62e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 64.34 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 25 DAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGksMRAVQKQVAYVE-------QRKDL--DL----NFPIN--V 89
Cdd:COG4586 46 EPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVPFKRRKEFARrigvvfgQRSQLwwDLpaidSFRLLkaI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 90 FDVvltgtygklglfrdPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQS 169
Cdd:COG4586 124 YRI--------------PDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510996587 170 ETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG 210
Cdd:COG4586 190 KEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-216 |
6.62e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 6.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDD--TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYqgksmravqkqvayveqr 78
Cdd:COG2401 28 AIVLEAFGVELRVveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV------------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 kdldlNFPINVFDVVLTGtygklgLFRDPGKQAKAASRAALEQVALGD--FERRQIGQLSGGQLQRVFVARAIVQEAEII 156
Cdd:COG2401 90 -----DVPDNQFGREASL------IDAIGRKGDFKDAVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 157 ILDEPFVGIDLQSETAIMAIM-KQWRDAGKTIIVIHHDLNKVSQYFDDLVVmnhgIVDYGP 216
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLqKLARRAGITLVVATHHYDVIDDLQPDLLI----FVGYGG 215
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-195 |
1.42e-11 |
|
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: 60.84 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 22 VHFDAGKITGIIGPNGAGKSTLIKAIlGLVKARQGSVLYQGKsmravqkqvayveqrkdldlnfpinvfdvvltgtYGKL 101
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTILDAI-GLALGGAQSATRRRS----------------------------------GVKA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 102 GLFrdpgkqaKAASRAALEQValgdferrqIGQLSGGQLQRVFVArAIVQEAEI-----IILDEPFVGIDLQSETAIMAI 176
Cdd:cd03227 61 GCI-------VAAVSAELIFT---------RLQLSGGEKELSALA-LILALASLkprplYILDEIDRGLDPRDGQALAEA 123
|
170
....*....|....*....
gi 510996587 177 MKQWRDAGKTIIVIHHDLN 195
Cdd:cd03227 124 ILEHLVKGAQVIVITHLPE 142
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-219 |
1.46e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.44 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 6 NLTVAYDDT-PVFTDVAVHFDAGKITGIIGPNGAGKSTLIkAILGLVKARQ-GSVLYQGKSMRAV-----QKQVAYVEQR 78
Cdd:PRK13657 339 DVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVFDPQsGRILIDGTDIRTVtraslRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 KDLdlnFPINVFDVVLTGTYGKlglfrdpgkqAKAASRAALEQVALGDF-ERRQIG----------QLSGGQLQRVFVAR 147
Cdd:PRK13657 418 AGL---FNRSIEDNIRVGRPDA----------TDEEMRAAAERAQAHDFiERKPDGydtvvgergrQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 148 AIVQEAEIIILDEPFVGIDLQSET----AIMAIMKqwrdaGKTIIVIHHDLNKVSQYfDDLVVMNHG-IVDYGPTDQ 219
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAkvkaALDELMK-----GRTTFIIAHRLSTVRNA-DRILVFDNGrVVESGSFDE 555
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
25-222 |
2.70e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.29 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 25 DAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQG----KSMRAVQKQVayveqRKDLDLnfpinvfdvVLTGTYGK 100
Cdd:PRK11308 39 ERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdllKADPEAQKLL-----RQKIQI---------VFQNPYGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 101 LG-------LFRDP--------GKQAKAASRAALEQVAL-GDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVG 164
Cdd:PRK11308 105 LNprkkvgqILEEPllintslsAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 165 IDLQSETAIMAI-MKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYN 222
Cdd:PRK11308 185 LDVSVQAQVLNLmMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGrCVEKGTKEQIFN 244
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
2-193 |
4.63e-11 |
|
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: 60.36 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTPV-FTDVavhfDAGKITGIIGPNGAGKSTLIKAI-LGLV-KARQGSVLYQGKSMRAVQKQVAYVeqr 78
Cdd:cd03279 6 LELKNFGPFREEQVIdFTGL----DNNGLFLICGPTGAGKSTILDAItYALYgKTPRYGRQENLRSVFAPGEDTAEV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 kdlDLNFPINvfdvvltgtYGKLGLFRDPGKQAKAASRAA-LEQVALGDFERRQIGQLSGGQLQRVFVARAI-----VQE 152
Cdd:cd03279 79 ---SFTFQLG---------GKKYRVERSRGLDYDQFTRIVlLPQGEFDRFLARPVSTLSGGETFLASLSLALalsevLQN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 510996587 153 A-----EIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHD 193
Cdd:cd03279 147 RggarlEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHV 192
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-236 |
5.30e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM------RAVQKQVAY 74
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltpaKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQRKDLdlnFP-INVFDVVLtgtygkLGLFRDPGKQAKAASRAALEQVALgDFErRQIGQLSGGQLQRVFVARAIVQEA 153
Cdd:PRK15439 91 VPQEPLL---FPnLSVKENIL------FGLPKRQASMQKMKQLLAALGCQL-DLD-SSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 154 EIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQVYNAQNIE----R 228
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGtIALSGKTADLSTDDIIQaitpA 239
|
....*...
gi 510996587 229 AFSADLSA 236
Cdd:PRK15439 240 AREKSLSA 247
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-239 |
5.83e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.24 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY--DDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKArQGSVLYQGKSMRAVQKQvayvEQRK 79
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQ----TWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 DLDLnFPINVFdvVLTGTYGKlglFRDPGKQA------KAASRAALEQVALG-----DFERRQIGQ-LSGGQLQRVFVAR 147
Cdd:TIGR01271 1293 AFGV-IPQKVF--IFSGTFRK---NLDPYEQWsdeeiwKVAEEVGLKSVIEQfpdklDFVLVDGGYvLSNGHKQLMCLAR 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 148 AIVQEAEIIILDEPFVGIDLQSETAIMAIMKQwRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIVDYGPTDQVYN-AQNI 226
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNeTSLF 1445
|
250
....*....|...
gi 510996587 227 ERAFSADLSAVLF 239
Cdd:TIGR01271 1446 KQAMSAADRLKLF 1458
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
31-226 |
6.54e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.10 E-value: 6.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 31 GIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK-----SMRAVQKQVAYVEQRkdldlnfPInVFDvvltgtyGKLGLFR 105
Cdd:PTZ00243 1340 GIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGReigayGLRELRRQFSMIPQD-------PV-LFD-------GTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 106 DPGKQAKAASR-AALEQVAL---------GDFERRQIGQL--SGGQLQRVFVARAIVQEAE-IIILDEPFVGIDLQSETA 172
Cdd:PTZ00243 1405 DPFLEASSAEVwAALELVGLrervaseseGIDSRVLEGGSnySVGQRQLMCMARALLKKGSgFILMDEATANIDPALDRQ 1484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 173 IMA-IMKQWrdAGKTIIVIHHDLNKVSQYfDDLVVMNHGIV-DYG-PTDQVYNAQNI 226
Cdd:PTZ00243 1485 IQAtVMSAF--SAYTVITIAHRLHTVAQY-DKIIVMDHGAVaEMGsPRELVMNRQSI 1538
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-166 |
1.03e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 5 KNLTVAYDDtpvFTDV-AVHFD--AGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRA----VQKQVAYVEQ 77
Cdd:NF033858 270 RGLTMRFGD---FTAVdHVSFRirRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAgdiaTRRRVGYMSQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 ----------RKDLDLnfpinvfdvvltgtYGKlgLFRDPGKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVAR 147
Cdd:NF033858 347 afslygeltvRQNLEL--------------HAR--LFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAV 410
|
170
....*....|....*....
gi 510996587 148 AIVQEAEIIILDEPFVGID 166
Cdd:NF033858 411 AVIHKPELLILDEPTSGVD 429
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-192 |
2.20e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.03 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGL--VKARQGSVLYQGKSMRAVQKqvayvEQR 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSP-----EDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 KD----LDLNFPINVfdvvlTGTYGKLGLFRDPGKQAKAASRAALEQVALGDFERRQIGQL---------------SGGQ 139
Cdd:PRK09580 76 AGegifMAFQYPVEI-----PGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510996587 140 LQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHH 192
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-204 |
3.91e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVkarqgsVLYQGK-----------SMRAVQ 69
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGEL------PLLSGErqsqfshitrlSFEQLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 70 KQVAYVEQRKDLDL------NFPINVFDVVLTGTygklglfRDPGKQAKAAsraalEQVALGDFERRQIGQLSGGQLQRV 143
Cdd:PRK10938 77 KLVSDEWQRNNTDMlspgedDTGRTTAEIIQDEV-------KDPARCEQLA-----QQFGITALLDRRFKYLSTGETRKT 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 144 FVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIhhdLNKvsqyFDDL 204
Cdd:PRK10938 145 LLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV---LNR----FDEI 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-193 |
3.93e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMravqkqVAYVEQrkD 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI------VARLQQ--D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 81 LDLNFPINVFDVVLTG---------TYGKLG--LFRDPGKQ---AKAASRAALEQVALGDFERR------QIG------- 133
Cdd:PRK11147 75 PPRNVEGTVYDFVAEGieeqaeylkRYHDIShlVETDPSEKnlnELAKLQEQLDHHNLWQLENRinevlaQLGldpdaal 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996587 134 -QLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAgktIIVIHHD 193
Cdd:PRK11147 155 sSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGS---IIFISHD 212
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-223 |
4.81e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.60 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY-DDTPVFTDV---AVHFDAGKITGIIGPNGAGKSTLIKAILGLV----KARQGSVLYQGKSMRAVQKQv 72
Cdd:PRK11022 3 LLNVDKLSVHFgDESAPFRAVdriSYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 73 ayvEQRK----DLDLNF--PINVFDVVLTGTYGKLGLFR--DPGKQAKAASRAA--LEQVALGDFERR---QIGQLSGGQ 139
Cdd:PRK11022 82 ---ERRNlvgaEVAMIFqdPMTSLNPCYTVGFQIMEAIKvhQGGNKKTRRQRAIdlLNQVGIPDPASRldvYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 140 LQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPT 217
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGqVVETGKA 238
|
....*.
gi 510996587 218 DQVYNA 223
Cdd:PRK11022 239 HDIFRA 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-220 |
4.96e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 58.26 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAvqKQVAYVEQRKDLDLNFPIN---------- 88
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF--GDYSYRSQRIRMIFQDPSTslnprqrisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 89 VFDVVLtgtygKLGLFRDPGKQAKAASrAALEQVAL-GDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDL 167
Cdd:PRK15112 109 ILDFPL-----RLNTDLEPEQREKQII-ETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 168 QSETAIMAIMKQWRDA-GKTIIVIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQV 220
Cdd:PRK15112 183 SMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGeVVERGSTADV 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-173 |
6.09e-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: 59.15 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 14 TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSmrAVQKQVAYVeqrkdldlnFPINVFDVV 93
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRI--SFSPQTSWI---------MPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 94 LtgtygkLGLFRDPGKQAKAASRAALEQ--VALGDFERRQIGQ----LSGGQLQRVFVARAIVQEAEIIILDEPFVGIDL 167
Cdd:TIGR01271 508 I------FGLSYDEYRYTSVIKACQLEEdiALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
....*.
gi 510996587 168 QSETAI 173
Cdd:TIGR01271 582 VTEKEI 587
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-200 |
7.85e-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: 57.56 E-value: 7.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDD--TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKArQGSVLYQGKSMRAVQKQvayvEQRK 79
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQ----KWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 DLDLnFPINVFdvVLTGTYGKlglFRDP-GKQAKAASRAALEQVALGDFERRQIGQ-----------LSGGQLQRVFVAR 147
Cdd:cd03289 78 AFGV-IPQKVF--IFSGTFRK---NLDPyGKWSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 148 AIVQEAEIIILDEPFVGIDLQSETAIMAIMKQwRDAGKTIIVIHHDL--------------NKVSQY 200
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIeamlecqrflvieeNKVRQY 217
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
2-193 |
1.13e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 56.46 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDTpvftdvAVHFDAGkITGIIGPNGAGKSTLIKAIL----GLvKARQGSVLYQGKSMRAVQKQVAYVeq 77
Cdd:cd03240 4 LSIRNIRSFHERS------EIEFFSP-LTLIVGQNGAGKTTIIEALKyaltGE-LPPNSKGGAHDPKLIREGEVRAQV-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 78 rkdldlnfpinvfdvvltgtygKLGLFRDPGKQAKAA-SRAALEQVAL---GDFER---RQIGQLSGGQ------LQRVF 144
Cdd:cd03240 74 ----------------------KLAFENANGKKYTITrSLAILENVIFchqGESNWpllDMRGRCSGGEkvlaslIIRLA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510996587 145 VARAIVQEAEIIILDEPFVGIDLQS-ETAIMAIMK-QWRDAGKTIIVIHHD 193
Cdd:cd03240 132 LAETFGSNCGILALDEPTTNLDEENiEESLAEIIEeRKSQKNFQLIVITHD 182
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-212 |
1.55e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.16 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYD-DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGK---SMRAVQKQVAYVE 76
Cdd:PRK11650 3 GLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnELEPADRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 QRKDLdlnFP-INVFDVVltgTYG-KLglfRDPGKQ------AKAAsrAALEqvaLGDFERRQIGQLSGGQLQRVFVARA 148
Cdd:PRK11650 83 QNYAL---YPhMSVRENM---AYGlKI---RGMPKAeieervAEAA--RILE---LEPLLDRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 149 IVQEAEIIILDEPFVGIDLQSETAI-MAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIV 212
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVQMrLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
4-232 |
1.74e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.55 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKAR--QGSVLYQG--KSMRAVQKQVAYVEQRk 79
Cdd:PLN03140 883 MKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpKKQETFARISGYCEQN- 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 dlDLNFP-INVFDVVLTGTYgkLGLFRDPGKQAKAA-SRAALEQVALGDFERRQIG-----QLSGGQLQRVFVARAIVQE 152
Cdd:PLN03140 962 --DIHSPqVTVRESLIYSAF--LRLPKEVSKEEKMMfVDEVMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVAN 1037
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 153 AEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTII-VIHHDLNKVSQYFDDLVVMNHG--IVDYGPTDQvyNAQNIERA 229
Cdd:PLN03140 1038 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVcTIHQPSIDIFEAFDELLLMKRGgqVIYSGPLGR--NSHKIIEY 1115
|
...
gi 510996587 230 FSA 232
Cdd:PLN03140 1116 FEA 1118
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-173 |
1.87e-09 |
|
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: 56.79 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 14 TPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKsmravqkqVAYVEQrkdldlnfpinvFDVV 93
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------ISFSSQ------------FSWI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 94 LTGTYGK---LGLFRDPGKQAKAASRAALEQ--VALGDFERRQIGQ----LSGGQLQRVFVARAIVQEAEIIILDEPFVG 164
Cdd:cd03291 110 MPGTIKEniiFGVSYDEYRYKSVVKACQLEEdiTKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
....*....
gi 510996587 165 IDLQSETAI 173
Cdd:cd03291 190 LDVFTEKEI 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-215 |
1.89e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQ-----GKsMRavQKQVAYV 75
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGK-LR--QDQFAFE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 76 EQRkdldlnfpinVFDVVLTG-------------TYGKLGLFRDPGKQA-------------KAASRAALEQVALGDFER 129
Cdd:PRK15064 78 EFT----------VLDTVIMGhtelwevkqerdrIYALPEMSEEDGMKVadlevkfaemdgyTAEARAGELLLGVGIPEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 130 RQIGQLS----GGQLqRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQwRDAgkTIIVIHHD---LNKVSQYFD 202
Cdd:PRK15064 148 QHYGLMSevapGWKL-RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE-RNS--TMIIISHDrhfLNSVCTHMA 223
|
250
....*....|...
gi 510996587 203 DLvvmnhgivDYG 215
Cdd:PRK15064 224 DL--------DYG 228
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
130-216 |
2.68e-09 |
|
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: 55.73 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 130 RQIGQLSGGQLQRVFVARAIVQEAE--IIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDlnkvsqyfDDLVVM 207
Cdd:cd03270 133 RSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD--------EDTIRA 204
|
....*....
gi 510996587 208 NHGIVDYGP 216
Cdd:cd03270 205 ADHVIDIGP 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-220 |
2.83e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 26 AGKITGIIGPNGAGKSTLIKAIL----GLVKARQGSVLYQGKSMRAVQKQ----VAYVEQrkdLDLNFP-INVFDVVLTG 96
Cdd:TIGR00956 86 PGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHyrgdVVYNAE---TDVHFPhLTVGETLDFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 97 TygklgLFRDPG-------KQAKAASRAALEQVALG-----------DFERrqigQLSGGQLQRVFVARAIVQEAEIIIL 158
Cdd:TIGR00956 163 A-----RCKTPQnrpdgvsREEYAKHIADVYMATYGlshtrntkvgnDFVR----GVSGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510996587 159 DEPFVGIDlqSETAImaimkQWRDAGKTIIVIHHDLNKVSQY---------FDDLVVMNHG-IVDYGPTDQV 220
Cdd:TIGR00956 234 DNATRGLD--SATAL-----EFIRALKTSANILDTTPLVAIYqcsqdayelFDKVIVLYEGyQIYFGPADKA 298
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-209 |
3.27e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.96 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 13 DTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVL---------------YQGKSMRAV--------- 68
Cdd:PTZ00265 1180 NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfknehtndmtneqdYQGDEEQNVgmknvnefs 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 69 -QKQVAYVEQRK----------------DLDLNFPINVFDVVLTG------------TYGKLGLFRDPGKqaKAASRAAL 119
Cdd:PTZ00265 1260 lTKEGGSGEDSTvfknsgkilldgvdicDYNLKDLRNLFSIVSQEpmlfnmsiyeniKFGKEDATREDVK--RACKFAAI 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 120 EQV--ALGDFERRQIG----QLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRD-AGKTIIVIHH 192
Cdd:PTZ00265 1338 DEFieSLPNKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADKTIITIAH 1417
|
250
....*....|....*..
gi 510996587 193 DLNKVSQYfDDLVVMNH 209
Cdd:PTZ00265 1418 RIASIKRS-DKIVVFNN 1433
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-210 |
3.62e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDT-----PVftDVAVHfdAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAvQKQVAYve 76
Cdd:PRK10522 323 LELRNVTFAYQDNgfsvgPI--NLTIK--RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-EQPEDY-- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 qRKdldlnfpinVFDVVLTGTYgklgLF-RDPGKQAKAASRAA----LEQVALGD---FERRQIG--QLSGGQLQRVFVA 146
Cdd:PRK10522 396 -RK---------LFSAVFTDFH----LFdQLLGPEGKPANPALvekwLERLKMAHkleLEDGRISnlKLSKGQKKRLALL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510996587 147 RAIVQEAEIIILDEPFVGIDLQ-SETAIMAIMKQWRDAGKTIIVIHHDlnkvSQYF---DDLVVMNHG 210
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPHfRREFYQVLLPLLQEMGKTIFAISHD----DHYFihaDRLLEMRNG 525
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-212 |
6.58e-09 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 54.91 E-value: 6.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAYDDT--PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVayVEQRK 79
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT--LRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 DLDLNFPInVFDvvltgtyGKLGLFRDPGKQAKAASR-AALEQVALGDFERRQIGQL-----------SGGQLQRVFVAR 147
Cdd:cd03288 98 SIILQDPI-LFS-------GSIRFNLDPECKCTDDRLwEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLAR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510996587 148 AIVQEAEIIILDEPFVGIDLQSETAIM-AIMKQWRDagKTIIVIHHdlnKVSQYFD-DLV-VMNHGIV 212
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENILQkVVMTAFAD--RTVVTIAH---RVSTILDaDLVlVLSRGIL 232
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-191 |
9.75e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 53.72 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFtDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQ-VAYVEQrk 79
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPyCTYIGH-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 DLDLNFPINVFD--VVLTGTYGKLGLFrdpgkqakaasRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:PRK13541 78 NLGLKLEMTVFEnlKFWSEIYNSAETL-----------YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWL 146
|
170 180 190
....*....|....*....|....*....|....
gi 510996587 158 LDEpfVGIDLQSETaimaimkqwRDAGKTIIVIH 191
Cdd:PRK13541 147 LDE--VETNLSKEN---------RDLLNNLIVMK 169
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-171 |
1.05e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 32 IIGPNGAGKSTLIKAILGLVKARQGSVlYQGKSMravqkQVAYVEQ-RKDLDLNFPI--NVFDvvltgtygklglfrdpG 108
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKL-----EVAYFDQhRAELDPEKTVmdNLAE----------------G 407
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510996587 109 KQ---AKAASRAALEQvaLGDF------ERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPfvGIDLQSET 171
Cdd:PRK11147 408 KQevmVNGRPRHVLGY--LQDFlfhpkrAMTPVKALSGGERNRLLLARLFLKPSNLLILDEP--TNDLDVET 475
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-202 |
1.27e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 54.80 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTVAY---DDTPVFT----DVAVHfdAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQvAY 74
Cdd:COG4615 328 LELRGVTYRYpgeDGDEGFTlgpiDLTIR--RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNRE-AY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 75 VEQrkdldlnfpinvFDVVLTGTYgklgLFRD----PGKQAKAASRAALEQVALGD---FERRQIG--QLSGGQLQRVFV 145
Cdd:COG4615 405 RQL------------FSAVFSDFH----LFDRllglDGEADPARARELLERLELDHkvsVEDGRFSttDLSQGQRKRLAL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510996587 146 ARAIVQEAEIIILDE-------PFvgidlqsetaimaimKQW---------RDAGKTIIVIHHDlnkvSQYFD 202
Cdd:COG4615 469 LVALLEDRPILVFDEwaadqdpEF---------------RRVfytellpelKARGKTVIAISHD----DRYFD 522
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-161 |
1.29e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 3 SIKNLTVAYD-DTPVFTDVAVHFDAG-KItGIIGPNGAGKSTLIKAILGLVKArqgsvlYQGKSMRAVQKQVAYVEQRKD 80
Cdd:PRK11819 8 TMNRVSKVVPpKKQILKDISLSFFPGaKI-GVLGLNGAGKSTLLRIMAGVDKE------FEGEARPAPGIKVGYLPQEPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 81 LDLNFpiNVFDVVLTG---TYGKL-------GLFRDPG--------KQAKAasRAALEQVALGDFERR------------ 130
Cdd:PRK11819 81 LDPEK--TVRENVEEGvaeVKAALdrfneiyAAYAEPDadfdalaaEQGEL--QEIIDAADAWDLDSQleiamdalrcpp 156
|
170 180 190
....*....|....*....|....*....|....
gi 510996587 131 ---QIGQLSGGQLQRVFVARAIVQEAEIIILDEP 161
Cdd:PRK11819 157 wdaKVTKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-193 |
3.08e-08 |
|
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: 51.22 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 27 GKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYqgksmravqkqvayveqrkdLDLNfpinvfdvvltgtygklglfrd 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------IDGE---------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 107 pgkqakaASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAI------MKQW 180
Cdd:smart00382 40 -------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrllLLLK 112
|
170
....*....|...
gi 510996587 181 RDAGKTIIVIHHD 193
Cdd:smart00382 113 SEKNLTVILTTND 125
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-210 |
3.60e-08 |
|
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: 51.80 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 24 FDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSmravqkqVAYVEQRKDLdlnfpinvfdvvltgtygklgl 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT-------PVYKPQYIDL---------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 104 frdpgkqakaasraaleqvalgdferrqigqlSGGQLQRVFVARAIVQEAEIIILDEPFVGIDL-QSETAIMAIMKQWRD 182
Cdd:cd03222 73 --------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIeQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....*...
gi 510996587 183 AGKTIIVIHHDLnKVSQYFDDLVVMNHG 210
Cdd:cd03222 121 GKKTALVVEHDL-AVLDYLSDRIHVFEG 147
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-236 |
8.03e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 15 PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMravqKQVAYVEQRKDLDLnfpINVFDVVL 94
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV----AKFGLTDLRRVLSI---IPQSPVLF 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 95 TGTYgKLGLfrDPGKQAKAASR-AALEQVALGDFERR-------QIGQ----LSGGQLQRVFVARAIVQEAEIIILDEPF 162
Cdd:PLN03232 1323 SGTV-RFNI--DPFSEHNDADLwEALERAHIKDVIDRnpfgldaEVSEggenFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 163 VGIDLQSETAIM-AIMKQWRDAgkTIIVIHHDLNKVSQyFDDLVVMNHGivdygptdQVYNAQNIERAFSADLSA 236
Cdd:PLN03232 1400 ASVDVRTDSLIQrTIREEFKSC--TMLVIAHRLNTIID-CDKILVLSSG--------QVLEYDSPQELLSRDTSA 1463
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
118-216 |
9.49e-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: 51.46 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 118 ALEQVALGDFerrQIGQ----LSGGQLQRVFVARAIVQEAE---IIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVI 190
Cdd:cd03271 152 TLCDVGLGYI---KLGQpattLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVI 228
|
90 100
....*....|....*....|....*...
gi 510996587 191 HHDLN--KVSQYfddlvvmnhgIVDYGP 216
Cdd:cd03271 229 EHNLDviKCADW----------IIDLGP 246
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-234 |
1.19e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.73 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAY--DDTPV--FTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKA---------RQGSVLYQGKSMRA 67
Cdd:PRK15093 3 LLDIRNLTIEFktSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvtadrmRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 68 VQKQVA------YVEQRKDLDLNFPI--NVFDVVLTGTYGklGLFRDPGKQAKAASRAALEQVALGDFE---RRQIGQLS 136
Cdd:PRK15093 83 RRKLVGhnvsmiFQEPQSCLDPSERVgrQLMQNIPGWTYK--GRWWQRFGWRKRRAIELLHRVGIKDHKdamRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 137 GGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQW-RDAGKTIIVIHHDLNKVSQYFDDLVVMnhgivdyg 215
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVL-------- 232
|
250
....*....|....*....
gi 510996587 216 ptdqvYNAQNIERAFSADL 234
Cdd:PRK15093 233 -----YCGQTVETAPSKEL 246
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-212 |
2.24e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.28 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 15 PVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRavqkQVAYVEQRKDLDLnfpINVFDVVL 94
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS----KFGLMDLRKVLGI---IPQAPVLF 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 95 TGTYgKLGLfrDPGKQAKAASR-AALEQVALGDFERRQIGQL-----------SGGQLQRVFVARAIVQEAEIIILDEPF 162
Cdd:PLN03130 1326 SGTV-RFNL--DPFNEHNDADLwESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510996587 163 VGIDLQSEtAImaIMKQWRDAGK--TIIVIHHDLNKVSQYfDDLVVMNHGIV 212
Cdd:PLN03130 1403 AAVDVRTD-AL--IQKTIREEFKscTMLIIAHRLNTIIDC-DRILVLDAGRV 1450
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-216 |
3.61e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.60 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 130 RQIGQLSGGQLQRVFVARAIVQEAEII--ILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLNKVSqyFDDLvvm 207
Cdd:PRK00635 472 RALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMIS--LADR--- 546
|
....*....
gi 510996587 208 nhgIVDYGP 216
Cdd:PRK00635 547 ---IIDIGP 552
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-212 |
3.83e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPV-FTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQvayvEQRK 79
Cdd:PLN03073 508 IISFSDASFGYPGGPLlFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQ----HHVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 80 DLDLN----------FPiNVFDVVLTGTYGKLGLfrdpgkqakaasraaleqvaLGDFERRQIGQLSGGQLQRVFVARAI 149
Cdd:PLN03073 584 GLDLSsnpllymmrcFP-GVPEQKLRAHLGSFGV--------------------TGNLALQPMYTLSGGQKSRVAFAKIT 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510996587 150 VQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAgktIIVIHHDLNKVSQYFDDLVVMNHGIV 212
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG---VLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-227 |
4.31e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.27 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSM-----RAVQKQVAYVEqrkdldlnfpinvfDVV 93
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAliaisSGLNGQLTGIE--------------NIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 94 LTGTYgkLGLFRdpgKQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAI 173
Cdd:PRK13545 108 LKGLM--MGLTK---EKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 174 MAIMKQWRDAGKTIIVIHHDLNKVSQYFDDLVVMNHGIV-DYGPTDQV----------YNAQNIE 227
Cdd:PRK13545 183 LDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVkEYGDIKEVvdhydeflkkYNQMSVE 247
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-213 |
1.15e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 1 MLSIKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKARQGSV-LYQG-KSMRAVQKQVAYVeqR 78
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGiKLGYFAQHQLEFL--R 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 79 KDldlNFPINvfdvvltgtygklGLFRDPGKQAKAASRAALEQVAL-GDFERRQIGQLSGGQLQRVFVARAIVQEAEIII 157
Cdd:PRK10636 390 AD---ESPLQ-------------HLARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 158 LDEPFVGIDLQSETAIMAIMKQWRDAgktIIVIHHDLNKVSQYFDDLVVMNHGIVD 213
Cdd:PRK10636 454 LDEPTNHLDLDMRQALTEALIDFEGA---LVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-216 |
1.42e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 131 QIGQ----LSGGQLQRVFVARAIVQEAE---IIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLN--KVSQYf 201
Cdd:TIGR00630 822 RLGQpattLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDviKTADY- 900
|
90
....*....|....*
gi 510996587 202 ddlvvmnhgIVDYGP 216
Cdd:TIGR00630 901 ---------IIDLGP 906
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-199 |
1.58e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 19 DVAVHFDAGKITGIIGPNGAGKSTLIKAILGLVKA--RQGSVLYQG-----KSMRAVQKQ-VAYVEQRKDL--DLNFPIN 88
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGevcrfKDIRDSEALgIVIIHQELALipYLSIAEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 89 VFdvvLTGTYGKLGLFRDPGKQAKAasRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQ 168
Cdd:NF040905 99 IF---LGNERAKRGVIDWNETNRRA--RELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEE 173
|
170 180 190
....*....|....*....|....*....|.
gi 510996587 169 SETAIMAIMKQWRDAGKTIIVIHHDLNKVSQ 199
Cdd:NF040905 174 DSAALLDLLLELKAQGITSIIISHKLNEIRR 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-209 |
1.71e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 1.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510996587 134 QLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWR-DAGKTIIVIHHDLNKVsQYFDDLVVMNH 209
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTI-RYANTIFVLSN 654
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-192 |
1.96e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 4 IKNLTVAYDDTPVFTDVAVHFDAGKITGIIGPNGAGKSTLIK-----AILGLVKARQGSVLYQ---GKSMRAVQ------ 69
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGIPKNCQILHVEQevvGDDTTALQcvlntd 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 70 --------KQVAYVEQRKDLDLNFPI-------------NVFDVVLTGTYGKLGLFRDPGKQAKAAS-RAALEQVAlgDF 127
Cdd:PLN03073 260 iertqlleEEAQLVAQQRELEFETETgkgkgankdgvdkDAVSQRLEEIYKRLELIDAYTAEARAASiLAGLSFTP--EM 337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 128 ERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRdagKTIIVIHH 192
Cdd:PLN03073 338 QVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSH 399
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
130-193 |
4.39e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 4.39e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 130 RQIGQLSGGQLQRVFVARAIVQE--AEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHD 193
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD 549
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
26-215 |
4.74e-06 |
|
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: 46.10 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 26 AGKITGIIGPNGAGKSTLIKAILGLVKAR---QGSVLYQGKSM----RAVQKQVAYVEQRkdlDLNFPinvfdvVLTgty 98
Cdd:cd03233 32 PGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYkefaEKYPGEIIYVSEE---DVHFP------TLT--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 99 gklglfrdpgkqakaaSRAALEQVAL---GDFERrqigQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDlqSETA--I 173
Cdd:cd03233 100 ----------------VRETLDFALRckgNEFVR----GISGGERKRVSIAEALVSRASVLCWDNSTRGLD--SSTAleI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510996587 174 MAIMKQWRDAGKTIIVIhhdlnKVSQ-------YFDDLVVMNHG-IVDYG 215
Cdd:cd03233 158 LKCIRTMADVLKTTTFV-----SLYQasdeiydLFDKVLVLYEGrQIYYG 202
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
2-47 |
5.30e-06 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 46.58 E-value: 5.30e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 510996587 2 LSIKNLTVAYDDTpVFTDVAVHFDAGKITGIIGPNGAGKSTLIKAI 47
Cdd:COG1106 5 FSIENFRSFKDEL-TLSMVASGLRLLRVNLIYGANASGKSNLLEAL 49
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
109-220 |
8.20e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.27 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 109 KQAKAASRAALEQVALGDFERRQIGQLSGGQLQRVFVARAIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTII 188
Cdd:NF000106 119 KDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVL 198
|
90 100 110
....*....|....*....|....*....|...
gi 510996587 189 VIHHDLNKVSQYFDDLVVMNHG-IVDYGPTDQV 220
Cdd:NF000106 199 LTTQYMEEAEQLAHELTVIDRGrVIADGKVDEL 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-210 |
9.31e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 27 GKITGIIGPNGAGKSTLIKAILGLVKA---RQGSVLYQGKSMRA-VQKQVAYVEQRkdlDLNFP-INVFDVVLTGTYgkl 101
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSsFQRSIGYVQQQ---DLHLPtSTVRESLRFSAY--- 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 102 glFRDPGKQAKAASRAALEQV----ALGDFERRQIGQ----LSGGQLQRVFVARAIVQEAEIII-LDEPFVGIDLQSETA 172
Cdd:TIGR00956 863 --LRQPKSVSKSEKMEYVEEVikllEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWS 940
|
170 180 190
....*....|....*....|....*....|....*....
gi 510996587 173 IMAIMKQWRDAGKTII-VIHHDLNKVSQYFDDLVVMNHG 210
Cdd:TIGR00956 941 ICKLMRKLADHGQAILcTIHQPSAILFEEFDRLLLLQKG 979
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
17-67 |
1.05e-05 |
|
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: 44.76 E-value: 1.05e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 510996587 17 FTD-VAVHFDAGkITGIIGPNGAGKSTLIKAI---LGLVKArqgsvlyqgKSMRA 67
Cdd:cd03278 12 FADkTTIPFPPG-LTAIVGPNGSGKSNIIDAIrwvLGEQSA---------KSLRG 56
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
17-50 |
1.07e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 41.82 E-value: 1.07e-05
10 20 30
....*....|....*....|....*....|....
gi 510996587 17 FTDVAVHFDAGKITGIIGPNGAGKSTLIKAILGL 50
Cdd:pfam13555 12 FDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTL 45
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
17-47 |
2.09e-05 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 44.02 E-value: 2.09e-05
10 20 30
....*....|....*....|....*....|.
gi 510996587 17 FTDVAVHFDAGkITGIIGPNGAGKSTLIKAI 47
Cdd:pfam13476 9 FRDQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
32-192 |
3.29e-05 |
|
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: 44.74 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 32 IIGPNGAGKSTLIKAILGLVKarqgsvLYQGKSMRAVQKQVAYVEQRKdldlnfpinvfdvvltgtYGKLGLFRD----P 107
Cdd:TIGR00954 483 ICGPNGCGKSSLFRILGELWP------VYGGRLTKPAKGKLFYVPQRP------------------YMTLGTLRDqiiyP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 108 GK----QAKAASRAALEQ----VALGDFERRQIG---------QLSGGQLQRVFVARAIVQEAEIIILDE--PFVGIDLQ 168
Cdd:TIGR00954 539 DSsedmKRRGLSDKDLEQildnVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDEctSAVSVDVE 618
|
170 180
....*....|....*....|....
gi 510996587 169 SetaimAIMKQWRDAGKTIIVIHH 192
Cdd:TIGR00954 619 G-----YMYRLCREFGITLFSVSH 637
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
17-76 |
5.28e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 5.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 17 FTD-VAVHFDAGkITGIIGPNGAGKSTLIKAI---LGLVKARQ--GS----VLYQGKSMRAVQkQVAYVE 76
Cdd:TIGR02168 13 FADpTTINFDKG-ITGIVGPNGCGKSNIVDAIrwvLGEQSAKAlrGGkmedVIFNGSETRKPL-SLAEVE 80
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-194 |
5.93e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.69 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 2 LSIKNLTvAYDDTPVftdvaVHFDAGkITGIIGPNGAGKSTLIKAILGLVKARQGSVLYQGKSMRAVQKQVAYVE----- 76
Cdd:COG0419 5 LRLENFR-SYRDTET-----IDFDDG-LNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVElefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 77 -------QRKDLDLNFPIN---------VFDVVLTGTYGKLglfRDPGKQAKAASRAALEQVALGDFERRQI-------- 132
Cdd:COG0419 78 ggkryriERRQGEFAEFLEakpserkeaLKRLLGLEIYEEL---KERLKELEEALESALEELAELQKLKQEIlaqlsgld 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510996587 133 --GQLSGGQLQRVFVARAIVqeaeiIILDepFVGIDLQSETAIMAIMKQwrdagktIIVIHHDL 194
Cdd:COG0419 155 piETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEE-------LAIITHVI 204
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
24-60 |
8.68e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 42.65 E-value: 8.68e-05
10 20 30
....*....|....*....|....*....|....*..
gi 510996587 24 FDAGKITGIIGPNGAGKSTLIKAILGLvkaRQGSVLY 60
Cdd:COG4938 17 LELKPLTLLIGPNGSGKSTLIQALLLL---LQSNFIY 50
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
107-193 |
8.79e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 107 PGKQAKAASRAA---------LEQVALG----DferRQIGQLSGGQLQRVFVARAI------VqeaeIIILDEPFVGidL 167
Cdd:COG0178 448 TEREAEIAERILkeirsrlgfLVDVGLDyltlD---RSAGTLSGGEAQRIRLATQIgsglvgV----LYVLDEPSIG--L 518
|
90 100
....*....|....*....|....*...
gi 510996587 168 -QSETA-IMAIMKQWRDAGKTIIVIHHD 193
Cdd:COG0178 519 hQRDNDrLIETLKRLRDLGNTVIVVEHD 546
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
29-95 |
8.97e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 8.97e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996587 29 ITGIIGPNGAGKSTLIKAI---LGL-----VKARQGSVLYQGKSMRAVQKqvAYVE-QRKDLDLNFPINVFDVVLT 95
Cdd:pfam02463 25 FTAIVGPNGSGKSNILDAIlfvLGErsaksLRSERLSDLIHSKSGAFVNS--AEVEiTFDNEDHELPIDKEEVSIR 98
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-50 |
1.05e-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: 42.76 E-value: 1.05e-04
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
26-58 |
1.66e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 41.61 E-value: 1.66e-04
10 20 30
....*....|....*....|....*....|...
gi 510996587 26 AGKITGIIGPNGAGKSTLIKAILGLVKARQGSV 58
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
17-47 |
3.03e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.14 E-value: 3.03e-04
10 20 30
....*....|....*....|....*....|..
gi 510996587 17 FTDVAVHFDAG-KITGIIGPNGAGKSTLIKAI 47
Cdd:COG3950 14 FEDLEIDFDNPpRLTVLVGENGSGKTTLLEAI 45
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-204 |
3.36e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 119 LEQVALGdferRQIGQLSGGQLQRVFVAR---AIVQEAEIIILDEPFVGIDLQSETAIMAIMKQWRDAGKTIIVIHHDLN 195
Cdd:PRK00635 798 LDYLPLG----RPLSSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMH 873
|
90
....*....|.
gi 510996587 196 --KVSQYFDDL 204
Cdd:PRK00635 874 vvKVADYVLEL 884
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-47 |
3.46e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.14 E-value: 3.46e-04
10 20 30
....*....|....*....|....*....|.
gi 510996587 17 FTDVAVHFDaGKITGIIGPNGAGKSTLIKAI 47
Cdd:COG3593 14 IKDLSIELS-DDLTVLVGENNSGKSSILEAL 43
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
22-47 |
5.32e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.68 E-value: 5.32e-04
10 20
....*....|....*....|....*.
gi 510996587 22 VHFDAGKITGIIGPNGAGKSTLIKAI 47
Cdd:COG4637 16 LELPLGPLTVLIGANGSGKSNLLDAL 41
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
26-63 |
8.73e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 39.80 E-value: 8.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 510996587 26 AGKITGIIGPNGAGKSTLIKAILGLVKARQGSV---LYQGK 63
Cdd:PRK00098 163 AGKVTVLAGQSGVGKSTLLNALAPDLELKTGEIseaLGRGK 203
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
22-67 |
9.20e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 9.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 510996587 22 VHFDAGkITGIIGPNGAGKSTLIKAI---LGLVKArqgsvlyqgKSMRA 67
Cdd:COG1196 20 IPFEPG-ITAIVGPNGSGKSNIVDAIrwvLGEQSA---------KSLRG 58
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
131-216 |
1.13e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 131 QIGQ----LSGGQLQRVFVARAIVQEAE---IIILDEPFVG-----IDLqsetaIMAIMKQWRDAGKTIIVIHHDLN--K 196
Cdd:COG0178 819 KLGQpattLSGGEAQRVKLASELSKRSTgktLYILDEPTTGlhfhdIRK-----LLEVLHRLVDKGNTVVVIEHNLDviK 893
|
90 100
....*....|....*....|
gi 510996587 197 VSQYfddlvvmnhgIVDYGP 216
Cdd:COG0178 894 TADW----------IIDLGP 903
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
26-58 |
1.23e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 38.68 E-value: 1.23e-03
10 20 30
....*....|....*....|....*....|...
gi 510996587 26 AGKITGIIGPNGAGKSTLIKAILGLVKARQGSV 58
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEI 137
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
4-54 |
1.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 1.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 510996587 4 IKNLTVayDDTPVFTDVAVHFDAGkITGIIGPNGAGKSTLIKAILGLVKAR 54
Cdd:COG4717 3 IKELEI--YGFGKFRDRTIEFSPG-LNVIYGPNEAGKSTLLAFIRAMLLER 50
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
22-48 |
2.16e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 2.16e-03
10 20
....*....|....*....|....*..
gi 510996587 22 VHFDAGkITGIIGPNGAGKSTLIKAIL 48
Cdd:PRK03918 19 VEFDDG-INLIIGQNGSGKSSILEAIL 44
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
17-66 |
2.23e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 38.60 E-value: 2.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 510996587 17 FTDVAVHFDAGkITGIIGPNGAGKSTLIKAIlglvkarqgSVLYQGKSMR 66
Cdd:PRK00064 14 YEELDLELSPG-VNVLVGENGQGKTNLLEAI---------YLLAPGRSHR 53
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
32-50 |
4.27e-03 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 37.19 E-value: 4.27e-03
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
131-216 |
4.44e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.13 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996587 131 QIGQ----LSGGQLQRVFVARaivqeaE---------IIILDEPFVGI---DLQsetAIMAIMKQWRDAGKTIIVIHHDL 194
Cdd:PRK00349 823 KLGQpattLSGGEAQRVKLAK------ElskrstgktLYILDEPTTGLhfeDIR---KLLEVLHRLVDKGNTVVVIEHNL 893
|
90 100
....*....|....*....|....
gi 510996587 195 N--KVSQYfddlvvmnhgIVDYGP 216
Cdd:PRK00349 894 DviKTADW----------IIDLGP 907
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
17-66 |
5.13e-03 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 37.44 E-value: 5.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 510996587 17 FTDVAVHFDAGkITGIIGPNGAGKSTLIKAIlglvkarqgSVLYQGKSMR 66
Cdd:COG1195 13 YESLELEFSPG-INVLVGPNGQGKTNLLEAI---------YLLATGRSFR 52
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
16-47 |
7.11e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 37.30 E-value: 7.11e-03
10 20 30
....*....|....*....|....*....|..
gi 510996587 16 VFTDVavHFDAGKITGIIGPNGAGKSTLIKAI 47
Cdd:PHA02562 18 QPIEI--QLDKVKKTLITGKNGAGKSTMLEAL 47
|
|
| PRK12289 |
PRK12289 |
small ribosomal subunit biogenesis GTPase RsgA; |
26-58 |
9.57e-03 |
|
small ribosomal subunit biogenesis GTPase RsgA;
Pssm-ID: 237040 [Multi-domain] Cd Length: 352 Bit Score: 36.53 E-value: 9.57e-03
10 20 30
....*....|....*....|....*....|...
gi 510996587 26 AGKITGIIGPNGAGKSTLIKAILGLVKARQGSV 58
Cdd:PRK12289 171 RNKITVVAGPSGVGKSSLINRLIPDVELRVGKV 203
|
|
| |
