|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-251 |
3.94e-122 |
|
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: 347.80 E-value: 3.94e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVE 82
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANMRVRDVVRLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILL 162
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 163 DEPTNHLDIHHQMQLMQLISEL----PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWDVFRVKTKI 238
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLarerGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEARV 241
|
250
....*....|...
gi 445942648 239 EISPYHGKKHIHF 251
Cdd:COG1120 242 IEDPVTGRPLVLP 254
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
5-251 |
9.82e-89 |
|
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: 263.21 E-value: 9.82e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQH 84
Cdd:TIGR03873 4 LSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVEQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMTEANMRVRDVVRLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDE 164
Cdd:TIGR03873 84 SDTAVPLTVRDVVALGRIPHRSLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 165 PTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWDVFRVKTKIEIS 241
Cdd:TIGR03873 164 PTNHLDVRAQLETLALVRELAatgVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIRAVYGVDATVLTH 243
|
250
....*....|
gi 445942648 242 PYHGKKHIHF 251
Cdd:TIGR03873 244 PDTGRPIIAF 253
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-250 |
2.35e-88 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 262.36 E-value: 2.35e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVE 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANMRVRDVVRLGRIPHHSPfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQ------- 155
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHGSS----AAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 156 SPSEILLDEPTNHLDIHHQMQLMQLISEL---PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWDVF 232
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
250
....*....|....*...
gi 445942648 233 RVKTKIEISPYHGKKHIH 250
Cdd:COG4559 238 GADLRVLAHPEGGCPQVL 255
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-233 |
5.98e-82 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 246.22 E-value: 5.98e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVAC 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQHGMTEANMRVRDVVRLGRIPHhspfSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQ----- 155
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 156 -SPSEILLDEPTNHLDIHHQMQLMQLISEL----PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWD 230
Cdd:PRK13548 157 gPPRWLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRR 236
|
...
gi 445942648 231 VFR 233
Cdd:PRK13548 237 VYG 239
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-246 |
3.10e-79 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 239.15 E-value: 3.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVAC 80
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQHGMTEANMRVRDVVRLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEI 160
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 161 LLDEPTNHLDIHHQMQLMQLISELPV---TSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWDVFRVKTK 237
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
|
....*....
gi 445942648 238 IEISPYHGK 246
Cdd:PRK11231 241 IHPEPVSGT 249
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-217 |
2.71e-78 |
|
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: 233.87 E-value: 2.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQh 84
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 gmteanmrvrdvvrlgriphhspfsnwsaqddeaiaaALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDE 164
Cdd:cd03214 81 -------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 165 PTNHLDIHHQMQLMQLISEL----PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLarerGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-247 |
4.31e-72 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 220.73 E-value: 4.31e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVE 82
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANMRVRDVVRLGRIPHHSpfSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILL 162
Cdd:COG4604 82 QENHINSRLTVRELVAFGRFPYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 163 DEPTNHLDIHHQMQLMQLI----SELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWDVFrvKTKI 238
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLrrlaDELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIY--DTDI 237
|
....*....
gi 445942648 239 EISPYHGKK 247
Cdd:COG4604 238 EVEEIDGKR 246
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-245 |
5.93e-71 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 222.79 E-value: 5.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTEANMR 92
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 VRDVVRLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIH 172
Cdd:PRK09536 94 VRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 173 HQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWDVFRVKTKIEISPYHG 245
Cdd:PRK09536 174 HQVRTLELVRRLVddgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAVGTDPATG 249
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-233 |
3.78e-67 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 208.02 E-value: 3.78e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMakkqlARRVACVE 82
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEAN--MRVRDVVRLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQ--GwlSLSGGERQRVHIARALAQSPS 158
Cdd:COG1121 82 QRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRpiG--ELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 159 EILLDEPTNHLDIHHQMQLMQLISEL---PVTSIVAIHDLNHAAMFCDSLIVMQQGQIlASGTPEEILSEALLWDVFR 233
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELrreGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEVLTPENLSRAYG 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-245 |
1.86e-64 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 201.75 E-value: 1.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHG 85
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 MTEANMRVRDVVRLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEP 165
Cdd:PRK10253 91 TTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 166 TNHLDIHHQMQLMQLISELP----VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWDVFRVKTKIEIS 241
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNrekgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDD 250
|
....
gi 445942648 242 PYHG 245
Cdd:PRK10253 251 PVAG 254
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-227 |
1.64e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 190.66 E-value: 1.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKqLARRVACVE 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANMRVRDVVRL-GRIPHHSPfsnwsAQDDEAIAAALQRVAMLEKSEQ--GwlSLSGGERQRVHIARALAQSPSE 159
Cdd:COG1131 80 QEPALYPDLTVRENLRFfARLYGLPR-----KEARERIDELLELFGLTDAADRkvG--TLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 160 ILLDEPTNHLDIHHQMQLMQLISEL---PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEAL 227
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELaaeGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-226 |
7.26e-59 |
|
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: 186.93 E-value: 7.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTEAN 90
Cdd:COG1124 14 GGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYASLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 91 --MRVRDVVRLGRIPHHSPfsnwsaQDDEAIAAALQRVAMleksEQGWLS-----LSGGERQRVHIARALAQSPSEILLD 163
Cdd:COG1124 94 prHTVDRILAEPLRIHGLP------DREERIAELLEQVGL----PPSFLDryphqLSGGQRQRVAIARALILEPELLLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 164 EPTNHLDIHHQMQLMQLISEL----PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEA 226
Cdd:COG1124 164 EPTSALDVSVQAEILNLLKDLreerGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-217 |
8.11e-59 |
|
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: 185.43 E-value: 8.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKkqlarRVACVEQH 84
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-----RIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMTEANM--RVRDVVRLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILL 162
Cdd:cd03235 77 RSIDRDFpiSVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 163 DEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGqILASG 217
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRregMTILVVTHDLGLVLEYFDRVLLLNRT-VVASG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-228 |
3.07e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 185.26 E-value: 3.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 12 AGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLA---RRVACVEQHGMTE 88
Cdd:COG3638 13 PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrRRIGMIFQQFNLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 89 ANMRVRDVVRLGRIPHHSP----FSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDE 164
Cdd:COG3638 93 PRLSVLTNVLAGRLGRTSTwrslLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 165 PTNHLDIHHQMQLMQLI----SELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEiLSEALL 228
Cdd:COG3638 173 PVASLDPKTARQVMDLLrriaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE-LTDAVL 239
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-226 |
2.73e-57 |
|
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: 182.15 E-value: 2.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWK-AGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACV 81
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 82 ---------------------EQHGMTEANMRVRdvvrlgriphhspfsnwsaqddeaIAAALQRVAMLEKSEQGWLSLS 140
Cdd:COG1122 81 fqnpddqlfaptveedvafgpENLGLPREEIRER------------------------VEEALELVGLEHLADRPPHELS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 141 GGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:COG1122 137 GGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNkegKTVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
....*....
gi 445942648 218 TPEEILSEA 226
Cdd:COG1122 217 TPREVFSDY 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-224 |
3.03e-54 |
|
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: 182.41 E-value: 3.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAK---KQLARRVACVEQH--G 85
Cdd:COG1123 274 GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDpyS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 MTEANMRVRDVVRLG-RIPHHSPfsnwSAQDDEAIAAALQRVAmLEKSEQGWL--SLSGGERQRVHIARALAQSPSEILL 162
Cdd:COG1123 354 SLNPRMTVGDIIAEPlRLHGLLS----RAERRERVAELLERVG-LPPDLADRYphELSGGQRQRVAIARALALEPKLLIL 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 163 DEPTNHLDIHHQMQLMQLISEL---PVTSIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:COG1123 429 DEPTSALDVSVQAQILNLLRDLqreLGLTYLFIsHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-223 |
6.95e-54 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 177.26 E-value: 6.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQD--IARMAKKqlaRRV 78
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlfTNLPPRE---RRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 79 ACVEQHGMTEANMRVRDVVRLGriPHHSPFSNwsaqddeaiAAALQRVA-MLEKSEQGWLS------LSGGERQRVHIAR 151
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFG--LRVRPPSK---------AEIRARVEeLLELVQLEGLAdrypsqLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 152 ALAQSPSEILLDEPTNHLDIH--HQM--QLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEIL 223
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKvrKELrrWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-225 |
8.51e-54 |
|
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: 173.89 E-value: 8.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKqlARRVACV- 81
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE--ARRQIGVl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 82 -EQHGMTEaNMRVRDVVR-LGRIphhspFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSE 159
Cdd:COG4555 80 pDERGLYD-RLTVRENIRyFAEL-----YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 160 ILLDEPTNHLDIHHQMQLMQLISEL---PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-227 |
6.61e-52 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 168.90 E-value: 6.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 9 TWKAGKKVIvNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIA---RMAKKQLARRVACVEQHG 85
Cdd:cd03256 9 TYPNGKKAL-KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkGKALRQLRRQIGMIFQQF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 MTEANMRVRDVVRLGRIPHHSP----FSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEIL 161
Cdd:cd03256 88 NLIERLSVLENVLSGRLGRRSTwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 162 LDEPTNHLDIHHQMQLMQLI----SELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEAL 227
Cdd:cd03256 168 ADEPVASLDPASSRQVMDLLkrinREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVL 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-217 |
1.53e-51 |
|
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: 166.93 E-value: 1.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVACVEQHG 85
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 MTEANMRVRDVV----RLGRIPHhspfsnwsAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEIL 161
Cdd:cd03259 82 ALFPHLTVAENIafglKLRGVPK--------AEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 162 LDEPTNHLDIHHQMQLMQ----LISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:cd03259 154 LDEPLSALDAKLREELREelkeLQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-225 |
3.38e-51 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 174.95 E-value: 3.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 2 SICAENITWK-AGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVAC 80
Cdd:COG4988 336 SIELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQH----GMTeanmrVRDVVRLGRiPHHSpfsnwsaqdDEAIAAALQRVAMLE---KSEQGW--------LSLSGGERQ 145
Cdd:COG4988 416 VPQNpylfAGT-----IRENLRLGR-PDAS---------DEELEAALEAAGLDEfvaALPDGLdtplgeggRGLSGGQAQ 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 146 RVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELP--VTSIVAIHDLnHAAMFCDSLIVMQQGQILASGTPEEIL 223
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAkgRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELL 559
|
..
gi 445942648 224 SE 225
Cdd:COG4988 560 AK 561
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
3.83e-51 |
|
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: 176.95 E-value: 3.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 2 SICAENITWK--AGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVA 79
Cdd:COG2274 473 DIELENVSFRypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 80 CVEQHGM----TeanmrVRDVVRLGRiPHHspfsnwsaqDDEAIAAALQRVAMLEK------------SEQGwLSLSGGE 143
Cdd:COG2274 553 VVLQDVFlfsgT-----IRENITLGD-PDA---------TDEEIIEAARLAGLHDFiealpmgydtvvGEGG-SNLSGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 144 RQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISEL--PVTSIVAIHDLNHAAMfCDSLIVMQQGQILASGTPEE 221
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEE 695
|
...
gi 445942648 222 ILS 224
Cdd:COG2274 696 LLA 698
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-212 |
5.85e-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: 165.33 E-value: 5.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 9 TWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHgmTE 88
Cdd:cd03225 8 SYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQN--PD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 89 A---NMRVRDVVRLGRIPHHSPfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEP 165
Cdd:cd03225 86 DqffGPTVEEEVAFGLENLGLP----EEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 445942648 166 TNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQ 212
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKaegKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
16-224 |
2.53e-50 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 165.21 E-value: 2.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 16 VIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR-VACVEQHGMTEANMRVR 94
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIARTFQNPRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 95 DVVRLGRIPHHS--------PFSNWSAQDDEAIAAA---LQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLD 163
Cdd:COG0411 98 ENVLVAAHARLGrgllaallRLPRARREEREARERAeelLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 164 EPT---NHLDIHhqmQLMQLISELPVTSIVAI----HDLnHAAM-FCDSLIVMQQGQILASGTPEEILS 224
Cdd:COG0411 178 EPAaglNPEETE---ELAELIRRLRDERGITIllieHDM-DLVMgLADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-252 |
1.68e-49 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 162.70 E-value: 1.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 21 VSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRrPDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTEANMRVRDVVRLg 100
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLAL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 101 riphHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQ-----SPSE--ILLDEPTNHLDIHH 173
Cdd:COG4138 93 ----HQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptiNPEGqlLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 174 QMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWDVFRVktKIEISPYHGKKHIH 250
Cdd:COG4138 169 QAALDRLLRELCqqgITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGV--KFRRLEVEGHRWLI 246
|
..
gi 445942648 251 FI 252
Cdd:COG4138 247 PT 248
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-213 |
2.15e-49 |
|
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: 160.26 E-value: 2.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARmAKKQLARRVACVE 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANMRVRDVvrlgriphhspfsnwsaqddeaiaaalqrvamlekseqgwLSLSGGERQRVHIARALAQSPSEILL 162
Cdd:cd03230 80 EEPSLYENLTVREN----------------------------------------LKLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 445942648 163 DEPTNHLDIHHQMQLMQLISEL---PVTSIVAIHDLNHAAMFCDSLIVMQQGQI 213
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-222 |
2.60e-49 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 165.27 E-value: 2.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVACVEQHG 85
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGMVFQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 mteA---NMRVRDVV----RLGRIPhhspfsnwSAQDDEAIAAALQRVAM--LEK---SEqgwlsLSGGERQRVHIARAL 153
Cdd:COG3842 87 ---AlfpHLTVAENVafglRMRGVP--------KAEIRARVAELLELVGLegLADrypHQ-----LSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 154 AQSPSEILLDEPTNHLDIH--HQMQ--LMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKlrEEMReeLRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-223 |
4.18e-49 |
|
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: 169.56 E-value: 4.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 2 SICAENIT--WKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVA 79
Cdd:COG4987 333 SLELEDVSfrYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 80 CVEQH----GMTeanmrVRDVVRLGRiphhspfsnwSAQDDEAIAAALQRV---AMLEKSEQG---WL-----SLSGGER 144
Cdd:COG4987 413 VVPQRphlfDTT-----LRENLRLAR----------PDATDEELWAALERVglgDWLAALPDGldtWLgeggrRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 145 QRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPV--TSIVAIHDLNHAAMFcDSLIVMQQGQILASGTPEEI 222
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEEL 556
|
.
gi 445942648 223 L 223
Cdd:COG4987 557 L 557
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-232 |
1.01e-48 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 161.49 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHG 85
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 MTEANMRVRDVVRLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEP 165
Cdd:PRK10575 95 PAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 166 TNHLDIHHQMQLMQLISELP----VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWDVF 232
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSqergLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-222 |
1.21e-48 |
|
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: 160.58 E-value: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVAC 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQHGMTEANMRVRDVVRLG-RIPHHSpfSNWSAQDDEAIAAALQRVAMLEKSEQGWLS-LSGGERQRVHIARALAQSPS 158
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGlRVKPRS--ERPPEAEIRAKVHELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 159 EILLDEPTNHLD--IHHQMQ--LMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:cd03296 157 VLLLDEPFGALDakVRKELRrwLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-223 |
3.24e-48 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 159.37 E-value: 3.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITwKA-GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLA---RRV 78
Cdd:COG1127 6 IEVRNLT-KSfGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 79 ACVEQHGmteA---NMRVRDVV-----RLGRIPhhspfsnwsaqDDEAIAAALQRVAMLEKSEQGWL---SLSGGERQRV 147
Cdd:COG1127 85 GMLFQGG---AlfdSLTVFENVafplrEHTDLS-----------EAEIRELVLEKLELVGLPGAADKmpsELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 148 HIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISEL----PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEIL 223
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELrdelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-217 |
3.59e-48 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 158.82 E-value: 3.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLA---RRVACVEQHGMT 87
Cdd:cd03257 14 GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrKEIQMVFQDPMS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 EAN--MRVRDVVRLGrIPHHSPFSNwSAQDDEAIAAALQRVAMLEKseqgWLS-----LSGGERQRVHIARALAQSPSEI 160
Cdd:cd03257 94 SLNprMTIGEQIAEP-LRIHGKLSK-KEARKEAVLLLLVGVGLPEE----VLNrypheLSGGQRQRVAIARALALNPKLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 161 LLDEPTNHLDIHHQMQLMQLISELPV---TSIVAI-HDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:cd03257 168 IADEPTSALDVSVQAQILDLLKKLQEelgLTLLFItHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-224 |
5.22e-48 |
|
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: 158.75 E-value: 5.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR-VACVEQ 83
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 HGMTEANMRVRDVVRLGRIPHHSP---FSNWSAQDDEAIAAA---LQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSP 157
Cdd:cd03219 83 IPRLFPELTVLENVMVAAQARTGSgllLARARREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 158 SEILLDEPT---NHLDIHHQMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:cd03219 163 KLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-212 |
1.59e-47 |
|
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: 154.71 E-value: 1.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 4 CAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQ 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 hgmteanmrvrdvvrlgriphhspfsnwsaqddeaiaaalqrvamlekseqgwlsLSGGERQRVHIARALAQSPSEILLD 163
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 445942648 164 EPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQ 212
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAeegRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-213 |
1.10e-46 |
|
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: 154.57 E-value: 1.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENI--TWKAG--KKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLA----R 76
Cdd:cd03255 3 LKNLskTYGGGgeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafrrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 77 RVACVEQHGMTEANMRVRDVVRLGRIPHHSPfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQS 156
Cdd:cd03255 83 HIGFVFQSFNLLPDLTALENVELPLLLAGVP----KKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 157 PSEILLDEPTNHLDIHHQMQLMQLISELP----VTSIVAIHDLNhAAMFCDSLIVMQQGQI 213
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNkeagTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-222 |
1.36e-46 |
|
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: 154.97 E-value: 1.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQL---ARRVACVE 82
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANMRVRDVVRLgRIPHHSPFSNWsaQDDEAIAAALQRVAmLEKSEQGWLS-LSGGERQRVHIARALAQSPSEIL 161
Cdd:cd03261 84 QSGALFDSLTVFENVAF-PLREHTRLSEE--EIREIVLEKLEAVG-LRGAEDLYPAeLSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 162 LDEPTNHLDIHHQMQLMQLIS----ELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRslkkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-213 |
1.77e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.82 E-value: 1.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQh 84
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 gmtEANM---RVRDVVRLGRIPHHSPFsnwsaqDDEAIAAALQRV----AMLEKSEQgwlSLSGGERQRVHIARALAQSP 157
Cdd:COG4619 82 ---EPALwggTVRDNLPFPFQLRERKF------DRERALELLERLglppDILDKPVE---RLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 158 SEILLDEPTNHLDIHHQMQLMQLISELPV---TSIVAI-HDLNHAAMFCDSLIVMQQGQI 213
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAeegRAVLWVsHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-217 |
1.90e-46 |
|
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: 153.89 E-value: 1.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETvGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKqLARRVACVE 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANMRVRDVV----RLGRIPhhspfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPS 158
Cdd:cd03264 79 QEFGVYPNFTVREFLdyiaWLKGIP--------SKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 159 EILLDEPTNHLDIHHQMQLMQLISELPVTSIVAI--HDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILstHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-212 |
2.59e-46 |
|
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: 152.34 E-value: 2.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAK--KQLARRVACVEQ 83
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelPPLRRRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 HGMTEANMRVRDVVRLGriphhspfsnwsaqddeaiaaalqrvamlekseqgwlsLSGGERQRVHIARALAQSPSEILLD 163
Cdd:cd03229 84 DFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 445942648 164 EPTNHLD----IHHQMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQ 212
Cdd:cd03229 126 EPTSALDpitrREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
9-227 |
4.86e-46 |
|
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: 153.99 E-value: 4.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 9 TWKAGKKVIvNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKK---QLARRVACVEQHG 85
Cdd:TIGR02315 10 VYPNGKQAL-KNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrKLRRRIGMIFQHY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 MTEANMRVRDVVRLGRIPHHSP----FSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEIL 161
Cdd:TIGR02315 89 NLIERLTVLENVLHGRLGYKPTwrslLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLIL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 162 LDEPTNHLDIHHQMQLMQLI----SELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEAL 227
Cdd:TIGR02315 169 ADEPIASLDPKTSKQVMDYLkrinKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVL 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-224 |
1.03e-45 |
|
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: 159.68 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 7 NITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDA---GRVTLDGQDIARMAKKQLARRVACVEQ 83
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRRIGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 HGMTEANMR-----VRDVVRLGRIPHhspfsnwsAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPS 158
Cdd:COG1123 91 DPMTQLNPVtvgdqIAEALENLGLSR--------AEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 159 EILLDEPTNHLDIHHQMQLMQLISELPV---TSIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRergTTVLLItHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-222 |
2.94e-44 |
|
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: 148.87 E-value: 2.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLR-----RPDAGRVTLDGQDIA--RMAKKQLARR 77
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYdlDVDVLELRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 78 VACVEQHgmteAN---MRVRDVVRLGRIPHHSpfsNWSAQDDEAIAAALQRVAMLE--KSEQGWLSLSGGERQRVHIARA 152
Cdd:cd03260 83 VGMVFQK----PNpfpGSIYDNVAYGLRLHGI---KLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445942648 153 LAQSPSEILLDEPTNHLDIHHQMQLMQLISEL--PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-222 |
3.73e-44 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 152.15 E-value: 3.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 2 SICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVACV 81
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 82 EQ------HgMT-EANM----RVRDVvrlgriphhspfsnwsaqDDEAIAAALQRVA-MLE-------KSEQgwlsLSGG 142
Cdd:COG3839 81 FQsyalypH-MTvYENIafplKLRKV------------------PKAEIDRRVREAAeLLGledlldrKPKQ----LSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 143 ERQRVHIARALAQSPSEILLDEPTNHLDIH--HQM--QLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGT 218
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLDAKlrVEMraEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
....
gi 445942648 219 PEEI 222
Cdd:COG3839 218 PEEL 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-167 |
7.26e-44 |
|
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: 145.10 E-value: 7.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTEANMRVRDVV 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 98 RLGRIphhsPFSNWSAQDDEAIAAALQRVAMLEKSEQGWL----SLSGGERQRVHIARALAQSPSEILLDEPTN 167
Cdd:pfam00005 81 RLGLL----LKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
12-215 |
7.49e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 147.50 E-value: 7.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 12 AGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLA----RRVACVEQH--- 84
Cdd:COG1136 18 EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlrrRHIGFVFQFfnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 --GMTeanmrVRDVVRLGRIPHHSPfsnwSAQDDEAIAAALQRVAMLEK-----SEqgwlsLSGGERQRVHIARALAQSP 157
Cdd:COG1136 98 lpELT-----ALENVALPLLLAGVS----RKERRERARELLERVGLGDRldhrpSQ-----LSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445942648 158 SEILLDEPTNHLDIHHQMQLMQLISELP----VTSIVAIHDLNHAAMfCDSLIVMQQGQILA 215
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNrelgTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-222 |
1.16e-43 |
|
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: 147.38 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVACVEQHG 85
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 MTEANMRVRDVV----RLGRIPhhspfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEIL 161
Cdd:cd03300 82 ALFPHLTVFENIafglRLKKLP--------KAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 162 LDEPTNHLDI----HHQMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:cd03300 154 LDEPLGALDLklrkDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-230 |
1.23e-43 |
|
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: 147.38 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENIT--WKAGKKVIvNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQ 83
Cdd:cd03253 4 ENVTfaYDPGRPVL-KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 HgMTEANMRVRDVVRLGRiphhspfsnWSAQDDEAIAAAlqRVAMLEKS-------------EQGwLSLSGGERQRVHIA 150
Cdd:cd03253 83 D-TVLFNDTIGYNIRYGR---------PDATDEEVIEAA--KAAQIHDKimrfpdgydtivgERG-LKLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 151 RALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPV--TSIVAIHDLnHAAMFCDSLIVMQQGQILASGTPEEILSE--- 225
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAHRL-STIVNADKIIVLKDGRIVERGTHEELLAKggl 228
|
....*.
gi 445942648 226 -ALLWD 230
Cdd:cd03253 229 yAEMWK 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
13-224 |
1.06e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 145.14 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIArMAKKQLA---RRVACVEQH----- 84
Cdd:COG1126 12 GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINklrRKVGMVFQQfnlfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 ------GMTEANMRVRdvvrlgriphhspfsNWSAQDDEAIA-AALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSP 157
Cdd:COG1126 91 hltvleNVTLAPIKVK---------------KMSKAEAEERAmELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 158 SEILLDEPTNHLD---IHHQMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:COG1126 156 KVMLFDEPTSALDpelVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-225 |
2.37e-42 |
|
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: 145.09 E-value: 2.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQL----ARRVAC 80
Cdd:cd03294 27 KEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQHGMTEANMRVRDVVRLGRIPHHSPfsnwSAQDDEAIAAALQRVAmLEKSEQGWLS-LSGGERQRVHIARALAQSPSE 159
Cdd:cd03294 107 VFQSFALLPHRTVLENVAFGLEVQGVP----RAEREERAAEALELVG-LEGWEHKYPDeLSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 160 ILLDEPTNHLD--IHHQMQ--LMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:cd03294 182 LLMDEAFSALDplIRREMQdeLLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-225 |
4.03e-42 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 146.77 E-value: 4.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVAC 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQHGMTEANMRVRDVVRLG--RIPHHSPFSnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPS 158
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGltVLPRRERPN--AAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 159 EILLDEPTNHLDIHHQMQL----MQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELrrwlRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWRE 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-225 |
4.41e-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: 142.96 E-value: 4.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR-VACVEQHGMTEANM 91
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 92 RVRDVVRLGriphhspfsnWSAQDDEAIAAALQRV-----AMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPT 166
Cdd:cd03224 91 TVEENLLLG----------AYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 167 NHL------DIhhqMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:cd03224 161 EGLapkiveEI---FEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-212 |
9.77e-42 |
|
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: 140.60 E-value: 9.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENIT--WKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVAC 80
Cdd:cd03228 1 IEFKNVSfsYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQH----GMTeanmrVRDVVrlgriphhspfsnwsaqddeaiaaalqrvamlekseqgwlsLSGGERQRVHIARALAQS 156
Cdd:cd03228 81 VPQDpflfSGT-----IRENI-----------------------------------------LSGGQRQRIAIARALLRD 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 157 PSEILLDEPTNHLDIHHQMQLMQLISELP--VTSIVAIHDLnHAAMFCDSLIVMQQGQ 212
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALRALAkgKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-222 |
1.01e-41 |
|
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: 142.12 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKqLARRVACVE 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANMRVRD-VVRLGRIPHHSpfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEIL 161
Cdd:cd03265 80 QDLSVDDELTGWEnLYIHARLYGVP-----GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 162 LDEPTNHLDIHHQMQLMQLISEL----PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLkeefGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-223 |
1.93e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 149.16 E-value: 1.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQhgmtEA--- 89
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQ----DTflf 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 90 NMRVRDVVRLGRIphhspfsnwSAQDDEAIAAAlqRVAML----EKSEQGW--------LSLSGGERQRVHIARALAQSP 157
Cdd:COG1132 427 SGTIRENIRYGRP---------DATDEEVEEAA--KAAQAhefiEALPDGYdtvvgergVNLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 158 SEILLDEPTNHLDIHHQMQLMQLISELPV--TSIVAIHDLnHAAMFCDSLIVMQQGQILASGTPEEIL 223
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLMKgrTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEELL 562
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-239 |
2.58e-41 |
|
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: 141.76 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAG-RVTLDGQDIARMAKKQLARRVACV--E 82
Cdd:COG1119 7 RNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLVspA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANMRVRDVVR------LGRiphhspFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQS 156
Cdd:COG1119 87 LQLRFPRDETVLDVVLsgffdsIGL------YREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 157 PSEILLDEPTNHLDIHHQMQLMQLISEL---PVTSIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWDVF 232
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLaaeGAPTLVLVtHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEAF 240
|
....*..
gi 445942648 233 RVKTKIE 239
Cdd:COG1119 241 GLPVEVE 247
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
11-208 |
3.24e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.77 E-value: 3.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARmakkqLARRVACVEQhgmtEAN 90
Cdd:COG1116 20 GGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDRGVVFQ----EPA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 91 ----MRVRDVVRLG-RIPHHSPfsnwsAQDDEAIAAALQRVAmLEKSEQGWLS-LSGGERQRVHIARALAQSPSEILLDE 164
Cdd:COG1116 91 llpwLTVLDNVALGlELRGVPK-----AERRERARELLELVG-LAGFEDAYPHqLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 445942648 165 PTNHLDIH--HQMQ--LMQLISELPVTSIVAIHDLNHAAMFCDSLIVM 208
Cdd:COG1116 165 PFGALDALtrERLQdeLLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-225 |
1.62e-40 |
|
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: 138.76 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARmakkqLARRVACVEQHGMTEAN 90
Cdd:cd03293 13 GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDRGYVFQQDALLPW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 91 MRVRDVVRLG-RIPHHSPfsnwsAQDDEAIAAALQRVAmLEKSEQGWLS-LSGGERQRVHIARALAQSPSEILLDEPTNH 168
Cdd:cd03293 88 LTVLDNVALGlELQGVPK-----AEARERAEELLELVG-LSGFENAYPHqLSGGMRQRVALARALAVDPDVLLLDEPFSA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 169 LDIH--HQMQ--LMQLISELPVTSIVAIHDLNHAAMFCDSLIVMqqgqilaSGTPEEILSE 225
Cdd:cd03293 162 LDALtrEQLQeeLLDIWRETGKTVLLVTHDIDEAVFLADRVVVL-------SARPGRIVAE 215
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-237 |
4.68e-40 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 139.19 E-value: 4.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 15 KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAG-LRRPDA-------GRVTLDGQDIARMAKKQLARRVACVEQHGM 86
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 87 TEANMRVRDVVRLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQ---------SP 157
Cdd:PRK13547 94 PAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 158 SEILLDEPTNHLDIHHQMQLMQLISELP------VTSIVaiHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWDV 231
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLArdwnlgVLAIV--HDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARC 251
|
....*.
gi 445942648 232 FRVKTK 237
Cdd:PRK13547 252 YGFAVR 257
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-224 |
8.67e-40 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 137.47 E-value: 8.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRvac 80
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 veqhGMteanmrvrdvvrlGRIP-HHSPFSNWSAQDDeaIAAALQrvaMLEKSEQGW---------------------LS 138
Cdd:COG1137 79 ----GI-------------GYLPqEASIFRKLTVEDN--ILAVLE---LRKLSKKEReerleelleefgithlrkskaYS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 139 LSGGERQRVHIARALAQSPSEILLDEPTNHLD----------IHH--QMQLMQLISELPVTSIVAIhdlnhaamfCDSLI 206
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDpiavadiqkiIRHlkERGIGVLITDHNVRETLGI---------CDRAY 207
|
250
....*....|....*...
gi 445942648 207 VMQQGQILASGTPEEILS 224
Cdd:COG1137 208 IISEGKVLAEGTPEEILN 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-224 |
1.16e-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: 137.04 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR-VACVEQHGMTEANM 91
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 92 RVRDVVRLGRiphhspfsnWSAQDDEAIAAALQRVAML-----EKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPT 166
Cdd:COG0410 94 TVEENLLLGA---------YARRDRAEVRADLERVYELfprlkERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 167 NHL------DIhhqMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:COG0410 165 LGLapliveEI---FEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-199 |
1.58e-39 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 135.44 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGqdiarmakkqlARRVACVEQHGMTEANM--RVRD 95
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVPDSLplTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 96 VVRLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQM 175
Cdd:NF040873 77 LVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180
....*....|....*....|....*..
gi 445942648 176 QLMQLISEL---PVTSIVAIHDLNHAA 199
Cdd:NF040873 157 RIIALLAEEharGATVVVVTHDLELVR 183
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-223 |
1.70e-39 |
|
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: 136.52 E-value: 1.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRvacveqh 84
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GmteanmrvrdvvrLGRIPH-HSPFSNWSAQDDeaIAAALQrvaMLEKSEQGW---------------------LSLSGG 142
Cdd:cd03218 76 G-------------IGYLPQeASIFRKLTVEEN--ILAVLE---IRGLSKKEReekleelleefhithlrkskaSSLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 143 ERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPVTSI-VAIHDLNHAAMF--CDSLIVMQQGQILASGTP 219
Cdd:cd03218 138 ERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIgVLITDHNVRETLsiTDRAYIIYEGKVLAEGTP 217
|
....
gi 445942648 220 EEIL 223
Cdd:cd03218 218 EEIA 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-213 |
1.97e-39 |
|
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: 135.46 E-value: 1.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKV-IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARmakKQLARRVACVEQ 83
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 ---HGMTEANmrVRDVVRLGriphhspfSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEI 160
Cdd:cd03226 79 dvdYQLFTDS--VREELLLG--------LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 161 LLDEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQI 213
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAaqgKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-217 |
2.69e-39 |
|
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: 135.79 E-value: 2.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTEANmRVRDVV 97
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYG-TLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 98 RLGRiPHHspfsnwsaqDDEAIAAALQRVAM------------LEKSEQGwLSLSGGERQRVHIARALAQSPSEILLDEP 165
Cdd:cd03245 99 TLGA-PLA---------DDERILRAAELAGVtdfvnkhpngldLQIGERG-RGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 445942648 166 TNHLDIHHQMQLMQLISELPV--TSIVAIHDLNHAAMfCDSLIVMQQGQILASG 217
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDL-VDRIIVMDSGRIVADG 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-213 |
4.44e-39 |
|
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: 133.88 E-value: 4.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAG--KKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVAC 80
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VeqhgmteanmrvrdvvrlgriphhspfsnwsAQDDE----AIAAALqrvamlekseqgwlsLSGGERQRVHIARALAQS 156
Cdd:cd03246 81 L-------------------------------PQDDElfsgSIAENI---------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 157 PSEILLDEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMfCDSLIVMQQGQI 213
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-213 |
8.30e-39 |
|
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: 134.19 E-value: 8.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKK--QLARRVAC 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQHGMTEANMRVRDVVRLGRIPHHspfsNWSAQDDEAIA-AALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSE 159
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVK----GMSKAEAEERAlELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 160 ILLDEPTNHLD---IHHQMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQI 213
Cdd:cd03262 157 MLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-225 |
2.24e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 134.87 E-value: 2.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWK--AGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAK-KQLARRVACVE 82
Cdd:TIGR04520 4 ENVSFSypESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlWEIRKKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QH------GMTeanmrVRDVVRLG----RIPHhspfsnwsAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARA 152
Cdd:TIGR04520 84 QNpdnqfvGAT-----VEDDVAFGlenlGVPR--------EEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 153 LAQSPSEILLDEPTNHLDIHHQMQLMQLISEL----PVTsIVAI-HDLNHAAMfCDSLIVMQQGQILASGTPEEILSE 225
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLnkeeGIT-VISItHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-213 |
2.67e-38 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 133.15 E-value: 2.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVACVEQHG 85
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 MTEANMRVRDVVRLGRIPHHSPfsnwsaqdDEAIAAALQRVAMLEKSEQgWLS-----LSGGERQRVHIARALAQSPSEI 160
Cdd:cd03301 82 ALYPHMTVYDNIAFGLKLRKVP--------KDEIDERVREVAELLQIEH-LLDrkpkqLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 161 LLDEPTNHLD--IHHQM--QLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQI 213
Cdd:cd03301 153 LMDEPLSNLDakLRVQMraELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-225 |
2.68e-38 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 137.39 E-value: 2.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 7 NITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVACVEQHGM 86
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNTVFQSYA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 87 TEANMRVRDVV----RLGRIPHhspfsnwsAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILL 162
Cdd:PRK09452 97 LFPHMTVFENVafglRMQKTPA--------AEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 163 DEPTNHLD--IHHQMQ--LMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK09452 169 DESLSALDykLRKQMQneLKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-213 |
1.24e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.33 E-value: 1.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWK-AGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLA---RRV 78
Cdd:COG2884 2 IRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 79 ACVEQ-----HGMT-EAN----MRVrdvvrLGRIPhhspfsnwsAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVH 148
Cdd:COG2884 82 GVVFQdfrllPDRTvYENvalpLRV-----TGKSR---------KEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 149 IARALAQSPSEILLDEPTNHLDIHHQMQLMQL---ISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQI 213
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELleeINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-221 |
2.59e-37 |
|
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: 131.02 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 12 AGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLAR----RVACVEQHGMT 87
Cdd:COG4181 22 AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlrarHVGFVFQSFQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 EANMRVRDVVRLgriphhsPFSNWSAQDDEAIAAA-LQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPT 166
Cdd:COG4181 102 LPTLTALENVML-------PLELAGRRDARARARAlLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 167 NHLDIH---HQMQLM-QLISELPVTSIVAIHDLNHAAMfCDSLIVMQQGQILASGTPEE 221
Cdd:COG4181 175 GNLDAAtgeQIIDLLfELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
11-224 |
7.93e-37 |
|
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: 129.62 E-value: 7.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQL---ARRVACVEQHGMT 87
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIGMIFQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 EANMRVRDVVRLGRIPHHSPfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTN 167
Cdd:cd03258 94 LSSRTVFENVALPLEIAGVP----KAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 168 HLDIHHQMQLMQLIS----ELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:cd03258 170 ALDPETTQSILALLRdinrELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
10-214 |
1.24e-36 |
|
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: 130.31 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 10 WKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQ---LARRVACVEQ--H 84
Cdd:TIGR02769 19 GAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQdsP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMTEANMRVRDVVRlgriphhSPFSNW---SAQDDEAIAAALQRVAMLEKSEQGWL--SLSGGERQRVHIARALAQSPSE 159
Cdd:TIGR02769 99 SAVNPRMTVRQIIG-------EPLRHLtslDESEQKARIAELLDMVGLRSEDADKLprQLSGGQLQRINIARALAVKPKL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 160 ILLDEPTNHLDIHHQMQLMQLISELPV---TSIVAI-HDLNHAAMFCDSLIVMQQGQIL 214
Cdd:TIGR02769 172 IVLDEAVSNLDMVLQAVILELLRKLQQafgTAYLFItHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-222 |
1.27e-36 |
|
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: 128.78 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 9 TWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIaRMAKKQLARRVACVEQHGMTE 88
Cdd:cd03263 9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 89 ANMRVRDVVRL-GRIPHHSpfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTN 167
Cdd:cd03263 88 DELTVREHLRFyARLKGLP-----KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 168 HLDIHHQMQLMQLISEL-PVTSIV-AIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:cd03263 163 GLDPASRRAIWDLILEVrKGRSIIlTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-224 |
1.34e-36 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 129.32 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR-VACVEQ 83
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 HGMTEANMRVRDVVR--LGRIPHHSPfsnwsAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEIL 161
Cdd:TIGR04406 84 EASIFRKLTVEENIMavLEIRKDLDR-----AEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 162 LDEPTNHLDIHHQMQLMQLISELPVTSI-VAIHDLNHAAMF--CDSLIVMQQGQILASGTPEEILS 224
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDIKKIIKHLKERGIgVLITDHNVRETLdiCDRAYIISDGKVLAEGTPAEIVA 224
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-235 |
1.35e-36 |
|
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: 128.82 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 23 LRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQdiarmAKKQLARRVACVEQ-HGMT-EANMRVRDVVRLG 100
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQrHEFAwDFPISVAHTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 101 RIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQL 180
Cdd:TIGR03771 76 RTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 181 ISELP---VTSIVAIHDLNHAAMFCDSLIVMqQGQILASGTPEEILSEALLWDVFRVK 235
Cdd:TIGR03771 156 FIELAgagTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTFGVS 212
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-224 |
1.71e-36 |
|
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: 128.89 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKV--IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQ 83
Cdd:cd03251 4 KNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 -----HGMTEANMRvrdvvrlgriphhspFSNWSAQDDEAIAAALQRVAM--LEKSEQGW--------LSLSGGERQRVH 148
Cdd:cd03251 84 dvflfNDTVAENIA---------------YGRPGATREEVEEAARAANAHefIMELPEGYdtvigergVKLSGGQRQRIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 149 IARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPV--TSIVAIHDLN---HAamfcDSLIVMQQGQILASGTPEEIL 223
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLMKnrTTFVIAHRLStieNA----DRIVVLEDGKIVERGTHEELL 224
|
.
gi 445942648 224 S 224
Cdd:cd03251 225 A 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-224 |
1.85e-36 |
|
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: 132.15 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 20 NVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDG---QDIARmaKKQLA---RRVACVEQHGMTEANMRV 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSAR--GIFLPphrRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 94 RDVVRLGRipHHSPFSNWSAQDDEAIA----AAL--QRVAmlekseqgwlSLSGGERQRVHIARALAQSPSEILLDEPTN 167
Cdd:COG4148 95 RGNLLYGR--KRAPRAERRISFDEVVEllgiGHLldRRPA----------TLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 168 HLDIHHQMQLMQLISELP---------VTsivaiHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:COG4148 163 ALDLARKAEILPYLERLRdeldipilyVS-----HSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-227 |
2.28e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 130.94 E-value: 2.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRP---DAGRVTLDGQDIARMAKKQL----ARRVACVEQHGMTEAN 90
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELrkirGREIQMIFQDPMTSLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 91 --MRVRDVVRLGrIPHHSPFSnwSAQDDEAIAAALQRVAMLEKSE-------QgwlsLSGGERQRVHIARALAQSPSEIL 161
Cdd:COG0444 101 pvMTVGDQIAEP-LRIHGGLS--KAEARERAIELLERVGLPDPERrldryphE----LSGGMRQRVMIARALALEPKLLI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 162 LDEPTNHLDIHHQMQLMQLISEL---PVTSIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEILSEAL 227
Cdd:COG0444 174 ADEPTTALDVTIQAQILNLLKDLqreLGLAILFItHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPR 243
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-208 |
3.57e-36 |
|
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: 133.95 E-value: 3.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQH-GMTEANm 91
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHpFLFAGT- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 92 rVRDVVRLGRiphhspfsnwSAQDDEAIAAALQRVA---MLEKSEQGWLS--------LSGGERQRVHIARALAQSPSEI 160
Cdd:TIGR02857 412 -IAENIRLAR----------PDASDAEIREALERAGldeFVAALPQGLDTpigeggagLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 445942648 161 LLDEPTNHLDIHHQMQLMQLISELP--VTSIVAIHDLNHAAMfCDSLIVM 208
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEALRALAqgRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-228 |
5.65e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.98 E-value: 5.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENIT--WKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVAC 80
Cdd:PRK13635 6 IRVEHISfrYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQH------GMTeanmrVRDVVRLG----RIPHhspfsnwsaqDD--EAIAAALQRVAMLEKSEQGWLSLSGGERQRVH 148
Cdd:PRK13635 86 VFQNpdnqfvGAT-----VQDDVAFGleniGVPR----------EEmvERVDQALRQVGMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 149 IARALAQSPSEILLDEPTNHLDIHHQMQLM----QLISELPVTSIVAIHDLNHAAmFCDSLIVMQQGQILASGTPEEI-- 222
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLetvrQLKEQKGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTPEEIfk 229
|
....*.
gi 445942648 223 LSEALL 228
Cdd:PRK13635 230 SGHMLQ 235
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-217 |
1.52e-35 |
|
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: 125.79 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKqlARRVAC-VEQHGMTEaNM 91
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIGAlIEAPGFYP-NL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 92 RVRDVVRLGRIPHHSPfsnwsaqdDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDI 171
Cdd:cd03268 88 TARENLRLLARLLGIR--------KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 445942648 172 HHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:cd03268 160 DGIKELRELILSLRdqgITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-183 |
2.98e-35 |
|
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: 124.90 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARmAKKQLARRVAC 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQHGMTEANMRVRDVVRLgriphHSPFSNWSAqDDEAIAAALQRVAmLEKSEQGWLS-LSGGERQRVHIARALAQSPSE 159
Cdd:COG4133 80 LGHADGLKPELTVRENLRF-----WAALYGLRA-DREAIDEALEAVG-LAGLADLPVRqLSAGQKRRVALARLLLSPAPL 152
|
170 180
....*....|....*....|....
gi 445942648 160 ILLDEPTNHLDIHHQMQLMQLISE 183
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAA 176
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-223 |
3.85e-35 |
|
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: 125.49 E-value: 3.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWK-AGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQH 84
Cdd:cd03295 4 ENVTKRyGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMTEANMRVRDVVRLgrIPHhspFSNWS-AQDDEAIAAALQRVAMLEKSEQGWLS--LSGGERQRVHIARALAQSPSEIL 161
Cdd:cd03295 84 IGLFPHMTVEENIAL--VPK---LLKWPkEKIRERADELLALVGLDPAEFADRYPheLSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 162 LDEPTNHLD----IHHQMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEIL 223
Cdd:cd03295 159 MDEPFGALDpitrDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-224 |
4.29e-35 |
|
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: 125.14 E-value: 4.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITwKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVACVEQHG 85
Cdd:cd03299 4 ENLS-KDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 MTEANMRVRDVVRLGRIPHHSPFSNWSAQDDEaIAAALQRVAMLEKSEqgwLSLSGGERQRVHIARALAQSPSEILLDEP 165
Cdd:cd03299 81 ALFPHMTVYKNIAYGLKKRKVDKKEIERKVLE-IAEMLGIDHLLNRKP---ETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 166 TNHLDIHHQMQLMQLIS----ELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:cd03299 157 FSALDVRTKEKLREELKkirkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-213 |
4.49e-35 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 124.77 E-value: 4.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENI--TWKAGKK--VIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLA----R 76
Cdd:TIGR02211 4 CENLgkRYQEGKLdtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 77 RVACVEQ--HGMTEANMrvrdvvrLGRIPHHSPFSNWSAQDDEAIAAA-LQRVAMLEKSEQGWLSLSGGERQRVHIARAL 153
Cdd:TIGR02211 84 KLGFIYQfhHLLPDFTA-------LENVAMPLLIGKKSVKEAKERAYEmLEKVGLEHRINHRPSELSGGERQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 154 AQSPSEILLDEPTNHLDIHHQMQLMQLISELPVTS----IVAIHDLNHAAMFcDSLIVMQQGQI 213
Cdd:TIGR02211 157 VNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELntsfLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-223 |
4.52e-35 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 128.43 E-value: 4.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLA----RRVACVEQHGM 86
Cdd:TIGR01186 2 KTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELRevrrKKIGMVFQQFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 87 TEANMRVRDVVRLGriphhSPFSNWSAQDDEAIA-AALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEP 165
Cdd:TIGR01186 82 LFPHMTILQNTSLG-----PELLGWPEQERKEKAlELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445942648 166 TNHLD--IHHQMQ--LMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEIL 223
Cdd:TIGR01186 157 FSALDplIRDSMQdeLKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEIL 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-227 |
6.33e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 127.16 E-value: 6.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLA---RRVACVEQHGMTEAN--MR 92
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrRRMQMVFQDPYASLNprMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 VRDVVRLG-RIphHSPFSnwSAQDDEAIAAALQRVAmlekseqgwLS----------LSGGERQRVHIARALAQSPSEIL 161
Cdd:COG4608 114 VGDIIAEPlRI--HGLAS--KAERRERVAELLELVG---------LRpehadrypheFSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 162 LDEPTNHLDIHHQMQ----LMQLISELPVTSIVAIHDLN---HaamFCDSLIVMQQGQILASGTPEEILSEAL 227
Cdd:COG4608 181 CDEPVSALDVSIQAQvlnlLEDLQDELGLTYLFISHDLSvvrH---ISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-213 |
1.16e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 125.18 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLA---RRVACVEQHGMT 87
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafrRDIQMVFQDSIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 EANMRvRDVVRLGRIP-HHspFSNWSAQDDEAIAAALQRVAMLEKSEQGWL--SLSGGERQRVHIARALAQSPSEILLDE 164
Cdd:PRK10419 101 AVNPR-KTVREIIREPlRH--LLSLDKAERLARASEMLRAVDLDDSVLDKRppQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 445942648 165 PTNHLDIHHQMQLMQLISELPVTSIVAI----HDLNHAAMFCDSLIVMQQGQI 213
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTAClfitHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-217 |
2.47e-34 |
|
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: 122.79 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 20 NVSLRVPrGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQdIARMAKKQL-----ARRVACVEQHGMTEANMRVR 94
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKInlppqQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 95 DVVRLGrIPHHSPfsnwsAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQ 174
Cdd:cd03297 94 ENLAFG-LKRKRN-----REDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 445942648 175 MQLM----QLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:cd03297 168 LQLLpelkQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-224 |
2.52e-34 |
|
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: 129.03 E-value: 2.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRrPDAGRVTLDGQDIARMAKKQLA---RRVACVEQHGMTEAN--MR 92
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRplrRRMQVVFQDPFGSLSprMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 VRDVVRLGRIPHHSPFSnwSAQDDEAIAAALQRV----AMLEK--SEqgwlsLSGGERQRVHIARALAQSPSEILLDEPT 166
Cdd:COG4172 381 VGQIIAEGLRVHGPGLS--AAERRARVAEALEEVgldpAARHRypHE-----FSGGQRQRIAIARALILEPKLLVLDEPT 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445942648 167 NHLDIHHQMQLMQLISELPVT---SIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:COG4172 454 SALDVSVQAQILDLLRDLQREhglAYLFIsHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-171 |
3.80e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 128.26 E-value: 3.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQdiARMAKkqlarrvacVEQH 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG--LRIGY---------LPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMTEANMRVRDVVRLGriphHSPFSNWSAQDDEAIAA------ALQRVAMLE---KSEQGW------------L------ 137
Cdd:COG0488 70 PPLDDDLTVLDTVLDG----DAELRALEAELEELEAKlaepdeDLERLAELQeefEALGGWeaearaeeilsgLgfpeed 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 445942648 138 ------SLSGGERQRVHIARALAQSPSEILLDEPTNHLDI 171
Cdd:COG0488 146 ldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-234 |
6.45e-34 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 122.73 E-value: 6.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 21 VSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRrPDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTEANMRVRDVVRLg 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 101 riphHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEI-------LLDEPTNHLDIHH 173
Cdd:PRK03695 93 ----HQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 174 QMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWDVFRV 234
Cdd:PRK03695 169 QAALDRLLSELCqqgIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGV 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
8-232 |
6.49e-34 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 123.45 E-value: 6.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 8 ITWKAGKKVIvNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLarrVACVEQHGMT 87
Cdd:PRK15056 14 VTWRNGHTAL-RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 EAN--MRVRDVVRLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEP 165
Cdd:PRK15056 90 DWSfpVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 166 TNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDsLIVMQQGQILASGTPEEILSEALLWDVF 232
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRdegKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFTAENLELAF 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-222 |
6.62e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 125.22 E-value: 6.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 7 NITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVACVEQHGM 86
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 87 TEANMRVRDVVRLGRIPHHSPfsnwSAQDDEAIAAALQRVAmLEKSEQGWL-SLSGGERQRVHIARALAQSPSEILLDEP 165
Cdd:PRK11432 89 LFPHMSLGENVGYGLKMLGVP----KEERKQRVKEALELVD-LAGFEDRYVdQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 166 TNHLDIHHQMQLMQLISELP----VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQqqfnITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
18-222 |
7.68e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 125.33 E-value: 7.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVACVEQHGMTEANMRVRDVV 97
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQSYALFPHMTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 98 RLG----RIPhhspfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLD--I 171
Cdd:PRK11607 113 AFGlkqdKLP--------KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 445942648 172 HHQMQL--MQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:PRK11607 185 RDRMQLevVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-225 |
7.87e-34 |
|
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: 127.94 E-value: 7.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKA--GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVE 82
Cdd:COG4618 333 VENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QH-----GMTEANmrvrdVVRLGRIphhspfsnwsaqDDEAIAAALQRV---AMLEKSEQGW--------LSLSGGERQR 146
Cdd:COG4618 413 QDvelfdGTIAEN-----IARFGDA------------DPEKVVAAAKLAgvhEMILRLPDGYdtrigeggARLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 147 VHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISEL---PVTSIVAIHDLNHAAMfCDSLIVMQQGQILASGTPEEIL 223
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVL 554
|
..
gi 445942648 224 SE 225
Cdd:COG4618 555 AR 556
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-217 |
8.51e-34 |
|
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: 121.32 E-value: 8.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENIT--WKAGKKVI--VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARmAKKQLARRV 78
Cdd:cd03266 2 ITADALTkrFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 79 ACVEQHGMTEANMRVRDVVR-LGRIpHHSPFSNWSAQDDEaIAAALQRVAMLEKSEQGwlsLSGGERQRVHIARALAQSP 157
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEyFAGL-YGLKGDELTARLEE-LADRLGMEELLDRRVGG---FSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 158 SEILLDEPTNHLDIHHQMQLMQLISELPV---TSIVAIHDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
22-224 |
9.81e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 121.79 E-value: 9.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 22 SLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVACVEQHGMTEANMRVRDVVRLGR 101
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQENNLFPHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 102 iphhSPFSNWSAQDDEAIAAALQRV---AMLE-KSEQgwlsLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQL 177
Cdd:COG3840 97 ----RPGLKLTAEQRAQVEQALERVglaGLLDrLPGQ----LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 445942648 178 MQLISEL----PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:COG3840 169 LDLVDELcrerGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-213 |
1.41e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 126.72 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLdGQDIarmakkqlarRVACVEQH 84
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMT-EANMRVRDVVRLGRiphhspfsnwSAQDDEAIAAALQRvaMLEKSEQGWL---SLSGGERQRVHIARALAQSPSEI 160
Cdd:COG0488 387 QEElDPDKTVLDELRDGA----------PGGTEQEVRGYLGR--FLFSGDDAFKpvgVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 161 LLDEPTNHLDIHHQMQLMQLISELPVTSIVAIHDlnHAAM--FCDSLIVMQQGQI 213
Cdd:COG0488 455 LLDEPTNHLDIETLEALEEALDDFPGTVLLVSHD--RYFLdrVATRILEFEDGGV 507
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-224 |
1.80e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 123.65 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQL--ARR-VACVEQHgmt 87
Cdd:COG1135 14 KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraARRkIGMIFQH--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 eAN-MRVRDV---VRLgriphhsPF--SNWSAQDDEAIAAAL-QRVAMLEKSEQgWLS-LSGGERQRVHIARALAQSPSE 159
Cdd:COG1135 91 -FNlLSSRTVaenVAL-------PLeiAGVPKAEIRKRVAELlELVGLSDKADA-YPSqLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 160 ILLDEPTNHLD------IhhqMQLMQLI-SELPVTsIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:COG1135 162 LLCDEATSALDpettrsI---LDLLKDInRELGLT-IVLItHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-248 |
2.18e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 123.40 E-value: 2.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKkqLAR-RVA 79
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR--LARaRIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 80 CVEQHGMTEANMRVRD-VVRLGRiphhspFSNWSAQDDEAIAAALQRVAMLEKSEQGWLS-LSGGERQRVHIARALAQSP 157
Cdd:PRK13536 118 VVPQFDNLDLEFTVREnLLVFGR------YFGMSTREIEAVIPSLLEFARLESKADARVSdLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 158 SEILLDEPTNHLDIHHQMQLMQLISELPV---TSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWDVfrv 234
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLArgkTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQV--- 268
|
250
....*....|....
gi 445942648 235 ktkIEIspYHGKKH 248
Cdd:PRK13536 269 ---IEI--YGGDPH 277
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-222 |
3.87e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 121.75 E-value: 3.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARmakkQLARRVAcveqh 84
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIG----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMTE-----ANMRVRD-VVRLGRIPHHSPfsnwsAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPS 158
Cdd:COG4152 75 YLPEerglyPKMKVGEqLVYLARLKGLSK-----AEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 159 EILLDEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAakgTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-225 |
1.18e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.10 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWK--AGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQ 83
Cdd:PRK13632 11 ENVSFSypNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 H------GMTeanmrVRDVVRLG----RIPhhspfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARAL 153
Cdd:PRK13632 91 NpdnqfiGAT-----VEDDIAFGlenkKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 154 AQSPSEILLDEPTNHLDIHHQMQLMQLISELPVT---SIVAI-HDLNHaAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrkkTLISItHDMDE-AILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-217 |
1.71e-32 |
|
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: 117.27 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENIT------WKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRP--DAGRVTLDGQDIArmaKK 72
Cdd:cd03213 2 VTLSFRNLTvtvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLD---KR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 73 QLARRVACVEQHGMTEANMRVRDVVRlgriphhspfsnwsaqddeaIAAALQrvamlekseqgwlSLSGGERQRVHIARA 152
Cdd:cd03213 79 SFRKIIGYVPQDDILHPTLTVRETLM--------------------FAAKLR-------------GLSGGERKRVSIALE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 153 LAQSPSEILLDEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNhAAMF--CDSLIVMQQGQILASG 217
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdtgRTIICSIHQPS-SEIFelFDKLLLLSQGRVIYFG 194
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-234 |
2.08e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 120.30 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAkKQLARRVACVEQHG 85
Cdd:PRK13537 11 RNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGVVPQFD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 MTEANMRVRDVVRL-GRiphhspFSNWSAQDDEAIAAALQRVAMLE-KSEQGWLSLSGGERQRVHIARALAQSPSEILLD 163
Cdd:PRK13537 90 NLDPDFTVRENLLVfGR------YFGLSAAAARALVPPLLEFAKLEnKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 164 EPTNHLD--IHHQM--QLMQLISElPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWDVFRV 234
Cdd:PRK13537 164 EPTTGLDpqARHLMweRLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIEI 237
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-225 |
2.24e-32 |
|
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: 120.68 E-value: 2.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 33 LLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVACVEQ------HGMTEAN----MRVRDVVRlgri 102
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQsyalfpHMTVEENvafgLKMRKVPR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 103 phhspfsnwsAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLD--IHHQMQ--LM 178
Cdd:TIGR01187 75 ----------AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkkLRDQMQleLK 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 445942648 179 QLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
17-212 |
2.67e-32 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 117.35 E-value: 2.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLA---RRVACVEQHgmteanmrv 93
Cdd:TIGR02673 17 ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPllrRRIGVVFQD--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 94 rdvVRLgrIPHHSPFSN---------WSAQD-DEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLD 163
Cdd:TIGR02673 88 ---FRL--LPDRTVYENvalplevrgKKEREiQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 445942648 164 EPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQ 212
Cdd:TIGR02673 163 EPTGNLDPDLSERILDLLKRLNkrgTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-223 |
3.44e-32 |
|
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: 117.71 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIV-NNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQh 84
Cdd:cd03254 6 ENVNFSYDEKKPVlKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 gmtEA---NMRVRDVVRLGRiphhspfsnwSAQDDEAIAAALQRVAM---LEKSEQGWLS--------LSGGERQRVHIA 150
Cdd:cd03254 85 ---DTflfSGTIMENIRLGR----------PNATDEEVIEAAKEAGAhdfIMKLPNGYDTvlgenggnLSQGERQLLAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 151 RALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPV--TSIVAIHDLNhAAMFCDSLIVMQQGQILASGTPEEIL 223
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKgrTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-217 |
3.75e-32 |
|
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: 117.21 E-value: 3.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 22 SLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKqlARRVACVEQHGMTEANMRVRDVVRLGR 101
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 102 iphhSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLI 181
Cdd:cd03298 96 ----SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 445942648 182 SEL----PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:cd03298 172 LDLhaetKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-218 |
5.13e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 117.42 E-value: 5.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDG------QDIARMAKKQL 74
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 75 ARRVACVEQ-----------HGMTEANMRVRDVVRlgriphhspfsnwsaqdDEAIAAA---LQRVAMLEKSEQGWLSLS 140
Cdd:PRK11124 81 RRNVGMVFQqynlwphltvqQNLIEAPCRVLGLSK-----------------DQALARAeklLERLRLKPYADRFPLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 141 GGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAetgITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
.
gi 445942648 218 T 218
Cdd:PRK11124 224 D 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-216 |
7.78e-32 |
|
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: 114.83 E-value: 7.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIA-RMAKKQLARRVACV 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 82 EQhgmteanmrvrdvvrlgriphhspfsnwsaqddeaiaaalqrvamlekseqgwlsLSGGERQRVHIARALAQSPSEIL 161
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 162 LDEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILAS 216
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRaqgVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-225 |
1.08e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.49 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 16 VIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR--VACVEQHGMTEANM-R 92
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRktVGIVFQNPDDQLFApT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 VRDVVRLGRIphhspfsNWSAQDDEA---IAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHL 169
Cdd:PRK13639 96 VEEDVAFGPL-------NLGLSKEEVekrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 170 DIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK13639 169 DPMGASQIMKLLYDLNkegITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-224 |
1.47e-31 |
|
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: 121.33 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 12 AGKKVIVNNVSLRVPRGETVGLLGPNGCGKS----SLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLAR----RVACVEQ 83
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 HGMTEAN--MRVRD----VVRLgriphHSPFSnwSAQDDEAIAAALQRVAMLEKSEQgwLS-----LSGGERQRVHIARA 152
Cdd:COG4172 100 EPMTSLNplHTIGKqiaeVLRL-----HRGLS--GAAARARALELLERVGIPDPERR--LDayphqLSGGQRQRVMIAMA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 153 LAQSPsEILL-DEPTNHLDIHHQMQLMQLISELPV---TSIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:COG4172 171 LANEP-DLLIaDEPTTALDVTVQAQILDLLKDLQRelgMALLLItHDLGVVRRFADRVAVMRQGEIVEQGPTAELFA 246
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-226 |
2.07e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 116.77 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHgmtEANMRVRDVV 97
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQN---PDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 98 R----LGRIPHHSPFSNWSaqddEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHH 173
Cdd:PRK13648 102 KydvaFGLENHAVPYDEMH----RRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 174 QMQLMQLISELPVTSIVAI----HDLNHaAMFCDSLIVMQQGQILASGTPEEILSEA 226
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIisitHDLSE-AMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-194 |
2.59e-31 |
|
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: 114.81 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 19 NNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLA---RRVACVEQHGMTEANMRVRD 95
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVVFQDFRLLPDRNVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 96 VVRLG-RIPHHSPfsnwsAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQ 174
Cdd:cd03292 98 NVAFAlEVTGVPP-----REIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180
....*....|....*....|...
gi 445942648 175 ---MQLMQLISELPVTSIVAIHD 194
Cdd:cd03292 173 weiMNLLKKINKAGTTVVVATHA 195
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-224 |
4.71e-31 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 117.52 E-value: 4.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 21 VSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKK-QLA---RRVACVEQHGMTEANMRVRDV 96
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPpekRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 97 VRLGRIPHHSPFSNWSaqdDEAIAAALQRVAMLEKSEQgwlSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQ 176
Cdd:TIGR02142 96 LRYGMKRARPSERRIS---FERVIELLGIGHLLGRLPG---RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 445942648 177 LM----QLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:TIGR02142 170 ILpyleRLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-218 |
5.51e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 114.72 E-value: 5.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDG------QDIARMAKKQL 74
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 75 ARRVACVEQH-----------GMTEANMRVRDVVRlgriphhspfsnwsaqdDEAIAAA---LQRVAMLEKSEQGWLSLS 140
Cdd:COG4161 81 RQKVGMVFQQynlwphltvmeNLIEAPCKVLGLSK-----------------EQAREKAmklLARLRLTDKADRFPLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 141 GGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSqtgITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
.
gi 445942648 218 T 218
Cdd:COG4161 224 D 224
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
13-225 |
5.57e-31 |
|
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: 119.76 E-value: 5.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQH-----GMT 87
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDvelfpGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 EANmrvrdVVRLGRiphhspfsnwSAQDDEAIAAAlqRVA----MLEKSEQGW--------LSLSGGERQRVHIARALAQ 155
Cdd:TIGR01842 409 AEN-----IARFGE----------NADPEKIIEAA--KLAgvheLILRLPDGYdtvigpggATLSGGQRQRIALARALYG 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 156 SPSEILLDEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLnhAAMFC-DSLIVMQQGQILASGTPEEILSE 225
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITHRP--SLLGCvDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-212 |
7.27e-31 |
|
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: 111.39 E-value: 7.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGqdiarmakkqlARRVACVE 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QhgmteanmrvrdvvrlgriphhspfsnwsaqddeaiaaalqrvamlekseqgwlsLSGGERQRVHIARALAQSPSEILL 162
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 445942648 163 DEPTNHLDIHHQMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQ 212
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
9-228 |
9.77e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 115.28 E-value: 9.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 9 TWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDA---GRVTLDGQDIARMAKKQLARRVACVEQH- 84
Cdd:PRK13640 14 TYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREKVGIVFQNp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 -----GMTeanmrVRDVVRLGRIPHHSPFSnwsaQDDEAIAAALQRVAMLE--KSEQGwlSLSGGERQRVHIARALAQSP 157
Cdd:PRK13640 94 dnqfvGAT-----VGDDVAFGLENRAVPRP----EMIKIVRDVLADVGMLDyiDSEPA--NLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 158 SEILLDEPTNHLDIHHQMQLMQLISELP----VTSIVAIHDLNHAAMfCDSLIVMQQGQILASGTPEEILSEALL 228
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKkknnLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-206 |
1.04e-30 |
|
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: 113.09 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARM--AKKQLARR--VACV 81
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLnsKKASKFRRekLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 82 EQHGMTEANMRVRDVVRLGRIphhspFSNWSAQD-DEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEI 160
Cdd:TIGR03608 82 FQNFALIENETVEENLDLGLK-----YKKLSKKEkREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 445942648 161 LLDEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMfCDSLI 206
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNdegKTIIIVTHDPEVAKQ-ADRVI 204
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-225 |
1.18e-30 |
|
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: 113.79 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQhgmtEA---NMRV 93
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQ----EPvlfDGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 94 RDVVRLGRIPhhspfsnwsAQDDEAIAAALQR-----VAMLEKS------EQGwLSLSGGERQRVHIARALAQSPSEILL 162
Cdd:cd03249 94 AENIRYGKPD---------ATDEEVEEAAKKAnihdfIMSLPDGydtlvgERG-SQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 163 DEPTNHLDIHHQMQLMQLISELPV--TSIVAIHDLnHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAMKgrTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-224 |
5.27e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.11 E-value: 5.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 7 NITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDI-ARMAKKQLARRvacveqhg 85
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVnDPKVDERLIRQ-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 mtEANMRVRdvvRLGRIPHHSPFSN----------WSAQDDEAIAAAL-QRVAMLEKSEQGWLSLSGGERQRVHIARALA 154
Cdd:PRK09493 78 --EAGMVFQ---QFYLFPHLTALENvmfgplrvrgASKEEAEKQARELlAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 155 QSPSEILLDEPTNHLDI---HHQMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPelrHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-225 |
8.44e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 116.85 E-value: 8.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 19 NNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQhgmteanmRV----- 93
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQ--------RVhlfsa 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 94 --RDVVRLGrIPHhspfsnwsaQDDEAIAAALQRVAmLEK---SEQG---WL-----SLSGGERQRVHIARALAQSPSEI 160
Cdd:PRK11160 429 tlRDNLLLA-APN---------ASDEALIEVLQQVG-LEKlleDDKGlnaWLgeggrQLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 161 LLDEPTNHLDIHHQMQLMQLISELPV--TSIVAIHDLNHAAMFcDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELLAEHAQnkTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQ 563
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-217 |
1.72e-29 |
|
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: 110.06 E-value: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARrvaCVEQH 84
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGY---LPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMTEaNMRVRDVVR-LGRIpHHSPFSNWSAQDDEaiaaALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLD 163
Cdd:cd03269 80 GLYP-KMKVIDQLVyLAQL-KGLKKEEARRRIDE----WLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 164 EPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELAragKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-225 |
2.08e-29 |
|
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: 110.65 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENIT--WKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVAC 80
Cdd:cd03252 1 ITFEHVRfrYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQHGmTEANMRVRDVVRLGR--IPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGwLSLSGGERQRVHIARALAQSPS 158
Cdd:cd03252 81 VLQEN-VLFNRSIRDNIALADpgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQG-AGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 159 EILLDEPTNHLDI---HHQMQLMQLISElPVTSIVAIHDLNhAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:cd03252 159 ILIFDEATSALDYeseHAIMRNMHDICA-GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-229 |
5.06e-29 |
|
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: 114.53 E-value: 5.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQhgmteanmrvrDV 96
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQ-----------DT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 97 V----------RLGRiphhspfsnWSAQDDEAIAAAlqRVAML----EKSEQGW--------LSLSGGERQRVHIARALA 154
Cdd:COG5265 442 VlfndtiayniAYGR---------PDASEEEVEAAA--RAAQIhdfiESLPDGYdtrvgergLKLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 155 QSPSEILLDEPTNHLDIHHQMQLMQLISELPV--TSIVAIHDLN---HAamfcDSLIVMQQGQILASGTPEEILSE---- 225
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARgrTTLVIAHRLStivDA----DEILVLEAGRIVERGTHAELLAQggly 586
|
....
gi 445942648 226 ALLW 229
Cdd:COG5265 587 AQMW 590
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-222 |
5.58e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.96 E-value: 5.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 19 NNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQ-LARRVACVEQHGMTEANMRVRDVV 97
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNLSVAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 98 RLGRIPHHSPFSNWSAQDDEAiAAALQRV-------AMLEkseqgwlSLSGGERQRVHIARALAQSPSEILLDEPTNHLD 170
Cdd:COG1129 101 FLGREPRRGGLIDWRAMRRRA-RELLARLgldidpdTPVG-------DLSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 171 IHHQMQLMQLISELPV--TSIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:COG1129 173 EREVERLFRIIRRLKAqgVAIIYIsHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-170 |
2.75e-28 |
|
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: 112.45 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQhgmtEANM- 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQ----DAHLf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 92 --RVRDVVRLGRiphhspfsnwSAQDDEAIAAALQRV------AMLEKSEQGWL-----SLSGGERQRVHIARALAQSPS 158
Cdd:TIGR02868 422 dtTVRENLRLAR----------PDATDEELWAALERVgladwlRALPDGLDTVLgeggaRLSGGERQRLALARALLADAP 491
|
170
....*....|..
gi 445942648 159 EILLDEPTNHLD 170
Cdd:TIGR02868 492 ILLLDEPTEHLD 503
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-228 |
2.93e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.28 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 21 VSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTEA-NMRVRDVVRL 99
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPDDQVfSSTVWDDVAF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 100 GriphhsPFSNWSAQD--DEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQL 177
Cdd:PRK13647 104 G------PVNMGLDKDevERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 445942648 178 MQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALL 228
Cdd:PRK13647 178 MEILDRLHnqgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-225 |
3.00e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 107.67 E-value: 3.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR-VACVEQ 83
Cdd:PRK10895 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 HGMTEANMRVRD-VVRLGRIPHHSPfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILL 162
Cdd:PRK10895 86 EASIFRRLSVYDnLMAVLQIRDDLS----AEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 163 DEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRdsgLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-224 |
4.46e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 109.51 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENI--TWKAGKKVI--VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQL--ARR-V 78
Cdd:PRK11153 5 KNIskVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkARRqI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 79 ACVEQHGMTEANMRVRDVVRLgriphhsPF--SNWSAQDDEA-IAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQ 155
Cdd:PRK11153 85 GMIFQHFNLLSSRTVFDNVAL-------PLelAGTPKAEIKArVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 156 SPSEILLDEPTNHLDIHHQMQLMQLIS----ELPVTsIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKdinrELGLT-IVLItHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFS 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-217 |
4.99e-28 |
|
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: 106.59 E-value: 4.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 14 KKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDA---GRVTLDGQDiarMAKKQLARRVACVEQHGMTEAN 90
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQP---RKPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 91 MRVRDVVR---LGRIPHHSPFSNWSAQDDEAI--AAALQRVA-MLEKSeqgwlsLSGGERQRVHIARALAQSPSEILLDE 164
Cdd:cd03234 96 LTVRETLTytaILRLPRKSSDAIRKKRVEDVLlrDLALTRIGgNLVKG------ISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 165 PTNHLDIHHQMQLMQLISELPVTS---IVAIH----DLNHaaMFcDSLIVMQQGQILASG 217
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNrivILTIHqprsDLFR--LF-DRILLLSSGEIVYSG 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-217 |
7.83e-28 |
|
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: 106.26 E-value: 7.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 15 KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTEANMRVR 94
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 95 DVVRLGRIPHHSPFSNWSAQDDEaIAAALQRVAMLEKSEQgwlSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQ 174
Cdd:cd03267 114 DSFYLLAAIYDLPPARFKKRLDE-LSELLDLEELLDTPVR---QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 445942648 175 MQ----LMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:cd03267 190 ENirnfLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
13-219 |
1.37e-27 |
|
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: 105.27 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQH-----GMT 87
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDpvlfsGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 EANMrvrDvvrlgriphhsPFSNWSaqdDEAIAAALQRVAMLEKSEQ-----------GWLSLSGGERQRVHIARALAQS 156
Cdd:cd03244 95 RSNL---D-----------PFGEYS---DEELWQALERVGLKEFVESlpggldtvveeGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 157 PSEILLDEPTNHLDIHHQMQLMQLI-SELPVTSIVAI-HDLnHAAMFCDSLIVMQQGQILASGTP 219
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIrEAFKDCTVLTIaHRL-DTIIDSDRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-224 |
2.13e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 106.35 E-value: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 15 KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQH------GMTe 88
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNpdnqfvGAT- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 89 anmrVRDVVRLGR----IPHHspfsnwsaQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDE 164
Cdd:PRK13650 99 ----VEDDVAFGLenkgIPHE--------EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 165 PTNHLDIHHQMQLMQLISE------LPVTSIVaiHDLNHAAMfCDSLIVMQQGQILASGTPEEILS 224
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIKGirddyqMTVISIT--HDLDEVAL-SDRVLVMKNGQVESTSTPRELFS 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-240 |
2.55e-27 |
|
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: 104.86 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLArrvacVEQHGMTEANMRVRDVV 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV-----VFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 98 RLG--RIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQgwlsLSGGERQRVHIARALAQSPSEILLDEPTNHLDI---- 171
Cdd:TIGR01184 76 ALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrg 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 172 HHQMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGqilasgtPEEILSEALLWDVFRVKTKIEI 240
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG-------PAANIGQILEVPFPRPRDRLEV 213
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
21-198 |
2.58e-27 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 103.66 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 21 VSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR--VACVEQHGmteanmrvRDVVR 98
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRqrVGLVFQDP--------DDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 99 LGRIPHHSPFS--NWSAQDDEA---IAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHH 173
Cdd:TIGR01166 83 AADVDQDVAFGplNLGLSEAEVerrVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|....*...
gi 445942648 174 QMQLMQLISELP---VTSIVAIHDLNHA 198
Cdd:TIGR01166 163 REQMLAILRRLRaegMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-226 |
3.57e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.90 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENIT--WKAG---KKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIA--RMAKKQ 73
Cdd:PRK13637 1 MSIKIENLThiYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 74 LARRVACVEQHgmteanmrvrdvvrlgriPHHSPF------------SNWSAQDDEA---IAAALQRVA-----MLEKSE 133
Cdd:PRK13637 81 IRKKVGLVFQY------------------PEYQLFeetiekdiafgpINLGLSEEEIenrVKRAMNIVGldyedYKDKSP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 134 qgwLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISEL----PVTSIVAIHDLNHAAMFCDSLIVMQ 209
Cdd:PRK13637 143 ---FELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhkeyNMTIILVSHSMEDVAKLADRIIVMN 219
|
250
....*....|....*..
gi 445942648 210 QGQILASGTPEEILSEA 226
Cdd:PRK13637 220 KGKCELQGTPREVFKEV 236
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-224 |
5.97e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.61 E-value: 5.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRR--PDA---GRVTLDGQDIARMAKKQLARR 77
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 78 VACVEQHGMTEANMRVRDVVRLGriPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGW----LSLSGGERQRVHIARAL 153
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapaGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 154 AQSPSEILLDEPTNHLDIHHQMQLMQLISELP--VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKkdMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-226 |
7.19e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.10 E-value: 7.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 20 NVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAK----KQLARRVACVEQhgmteanmrvrd 95
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklKPLRKKVGIVFQ------------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 96 vvrlgrIPHHSPF------------SNWSAQDDEAIAAALQRVAM-------LEKSEqgwLSLSGGERQRVHIARALAQS 156
Cdd:PRK13634 93 ------FPEHQLFeetvekdicfgpMNFGVSEEDAKQKAREMIELvglpeelLARSP---FELSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 157 PSEILLDEPTNHLDIHHQMQLMQLISEL----PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEA 226
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLhkekGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
18-225 |
8.68e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.93 E-value: 8.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQ--DIARMAKKQLARRVACVEQ---HGMTEANmr 92
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQdpdNQLFSAS-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 VRDVVRLGRIphhspfsNWSAQDDEA---IAAALQR--VAMLEKSEQGWLSLsgGERQRVHIARALAQSPSEILLDEPTN 167
Cdd:PRK13636 100 VYQDVSFGAV-------NLKLPEDEVrkrVDNALKRtgIEHLKDKPTHCLSF--GQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445942648 168 HLD---IHHQMQLM-QLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK13636 171 GLDpmgVSEIMKLLvEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-222 |
9.95e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 103.96 E-value: 9.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGL--RRPDA---GRVTLDGQDIarMAKK----QLARRVACVEQ 83
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDI--YDPDvdvvELRRRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 HgmteAN---MRVRDVVRLG-RIPHHSPfsnwSAQDDEAIAAALQRVAM-------LEKSEqgwLSLSGGERQRVHIARA 152
Cdd:COG1117 100 K----PNpfpKSIYDNVAYGlRLHGIKS----KSELDEIVEESLRKAALwdevkdrLKKSA---LGLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445942648 153 LAQSPSEILLDEPTNHLDIHHQMQLMQLISELP--VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDPISTAKIEELILELKkdYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-222 |
1.50e-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: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 4 CAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR-VACVE 82
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANMRVRDVVRLGriphhspFSNWSAQDDEAIAAALQRVAMLE--KSEQGWLsLSGGERQRVHIARALAQSPSEI 160
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTG-------LAALPRRSRKIPDEIYELFPVLKemLGRRGGD-LSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 161 LLDEPTNHL------DIHHqmQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:TIGR03410 154 LLDEPTEGIqpsiikDIGR--VIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
18-222 |
2.06e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 103.15 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR-VACVEQHGMTEANMRVrdV 96
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgVVRTFQHVRLFREMTV--I 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 97 VRLGRIPHHSPFSNWSA----------QDDEAIAAA---LQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLD 163
Cdd:PRK11300 99 ENLLVAQHQQLKTGLFSgllktpafrrAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 164 EPTNHLDIHHQMQLMQLISEL----PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELrnehNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-194 |
2.20e-26 |
|
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: 106.94 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLdGQDIarmakkqlarRVACVE 82
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 Q-HGMTEANMRV-------RDVVRLG--RIPHHSPFS--NWSAQDDEaiaaalQRVAMlekseqgwlsLSGGERQRVHIA 150
Cdd:TIGR03719 392 QsRDALDPNKTVweeisggLDIIKLGkrEIPSRAYVGrfNFKGSDQQ------KKVGQ----------LSGGERNRVHLA 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 445942648 151 RALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPVTSIVAIHD 194
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHD 499
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
10-224 |
2.56e-26 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 102.99 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 10 WKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTEA 89
Cdd:COG4167 21 FRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDPNTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 90 NMRVRdvvrLGRIpHHSPFS---NWSAQD-DEAIAAALQRVAMLEksEQGWL---SLSGGERQRVHIARALAQSPSEILL 162
Cdd:COG4167 101 NPRLN----IGQI-LEEPLRlntDLTAEErEERIFATLRLVGLLP--EHANFyphMLSSGQKQRVALARALILQPKIIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 163 DEPTNHLDIHHQMQLMQLISELP----VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:COG4167 174 DEALAALDMSVRSQIINLMLELQeklgISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-213 |
3.04e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 102.83 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPD-----AGRVTL-DGQDIARMAKkQLARRVA 79
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSagellAGTAPLaEAREDTRLMF-QDARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 80 CveqhgmteanMRVRDVVRLGRIphhspfSNWSAQDDEAIAAalqrVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSE 159
Cdd:PRK11247 95 W----------KKVIDNVGLGLK------GQWRDAALQALAA----VGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 160 ILLDEPTNHLDIHHQMQLMQLISEL----PVTSIVAIHDLNHAAMFCDSLIVMQQGQI 213
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLwqqhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-223 |
4.09e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.20 E-value: 4.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWK-AGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQH 84
Cdd:PRK13657 338 DDVSFSyDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMTeANMRVRDVVRLGRIphhspfsnwSAQDDEAIAAALQRVAM--LEKSEQGW--------LSLSGGERQRVHIARALA 154
Cdd:PRK13657 418 AGL-FNRSIEDNIRVGRP---------DATDEEMRAAAERAQAHdfIERKPDGYdtvvgergRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 155 QSPSEILLDEPTNHLDIHHQMQLMQLISELP---VTSIVAiHDLN---HAamfcDSLIVMQQGQILASGTPEEIL 223
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMkgrTTFIIA-HRLStvrNA----DRILVFDNGRVVESGSFDELV 557
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-239 |
5.07e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 103.65 E-value: 5.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPD---AGRVTLDGQDIARMAKKQL----ARRVACVEQHGMTEAN 90
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELnklrAEQISMIFQDPMTSLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 91 --MRVRD----VVRLgriphHSPFSNWSA-------QDDEAIAAALQRVAMLEKseqgwlSLSGGERQRVHIARALAQSP 157
Cdd:PRK09473 112 pyMRVGEqlmeVLML-----HKGMSKAEAfeesvrmLDAVKMPEARKRMKMYPH------EFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 158 SEILLDEPTNHLDIHHQMQLMQLISELPV---TSIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEIL-------SEA 226
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKRefnTAIIMItHDLGVVAGICDKVLVMYAGRTMEYGNARDVFyqpshpySIG 260
|
250
....*....|...
gi 445942648 227 LLWDVFRVKTKIE 239
Cdd:PRK09473 261 LLNAVPRLDAEGE 273
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-176 |
7.01e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.86 E-value: 7.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAkkqlARRvACVEQHgmtEAN 90
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----ADR-GVVFQK---DAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 91 M---RVRDVV----RLGRIPHHspfsnwsaqDDEAIAAA-LQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILL 162
Cdd:COG4525 88 LpwlNVLDNVafglRLRGVPKA---------ERRARAEElLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
170
....*....|....*.
gi 445942648 163 DEPTNHLD--IHHQMQ 176
Cdd:COG4525 159 DEPFGALDalTREQMQ 174
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-224 |
7.06e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.56 E-value: 7.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSS----LLRVLAGlrrpdAGRVTLDGQDIARMAKKQL---ARRVACVEQHG 85
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 MTEANMR--VRDVVRLGRIPHHSPFSnwSAQDDEAIAAALQRVAMLEKSEQGWLS-LSGGERQRVHIARALAQSPSEILL 162
Cdd:PRK15134 372 NSSLNPRlnVLQIIEEGLRVHQPTLS--AAQREQQVIAVMEEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 163 DEPTNHLDIHHQMQLMQLISELPVTSIVAI----HDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLAYlfisHDLHVVRALCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-224 |
7.48e-26 |
|
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: 105.57 E-value: 7.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHgMTEANMRVRDVV 97
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQD-VVLFNDTIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 98 RLGRIPHHSpfsnwSAQDDEAIAAA--LQRVAMLEKS------EQGWLsLSGGERQRVHIARALAQSPSEILLDEPTNHL 169
Cdd:TIGR02203 427 AYGRTEQAD-----RAEIERALAAAyaQDFVDKLPLGldtpigENGVL-LSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 170 DIHHQMQLMQLISEL--PVTSIVAIHDLN---HAamfcDSLIVMQQGQILASGTPEEILS 224
Cdd:TIGR02203 501 DNESERLVQAALERLmqGRTTLVIAHRLStieKA----DRIVVMDDGRIVERGTHNELLA 556
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-224 |
1.18e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.96 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQL----ARRVACV 81
Cdd:PRK10070 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 82 EQHGMTEANMRVRDVVRLGRIPHHSPfsnwSAQDDEAIAAALQRVAmLEKSEQGWL-SLSGGERQRVHIARALAQSPSEI 160
Cdd:PRK10070 112 FQSFALMPHMTVLDNTAFGMELAGIN----AEERREKALDALRQVG-LENYAHSYPdELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 161 LLDEPTNHLD--IHHQMQ--LMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:PRK10070 187 LMDEAFSALDplIRTEMQdeLVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-209 |
2.97e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.40 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVE 82
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANMrVRDVVRLG-RIPHHSPfsnwsaqDDEAIAAALQRVA----MLEKSEQgwlSLSGGERQRVHIARALAQSP 157
Cdd:PRK10247 88 QTPTLFGDT-VYDNLIFPwQIRNQQP-------DPAIFLDDLERFAlpdtILTKNIA---ELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 158 SEILLDEPTNHLDIHHQMQLMQLISELPVTSIVAI----HD---LNHAamfcDSLIVMQ 209
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwvtHDkdeINHA----DKVITLQ 211
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
18-222 |
3.72e-25 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 103.82 E-value: 3.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQH-GMTeaNMRVRDV 96
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDaGLF--NRSIREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 97 VRLGRIphhspfsnwSAQDDEAIAAALQRVA--MLEKSEQGWLS--------LSGGERQRVHIARALAQSPSEILLDEPT 166
Cdd:TIGR01192 429 IRLGRE---------GATDEEVYEAAKAAAAhdFILKRSNGYDTlvgergnrLSGGERQRLAIARAILKNAPILVLDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 167 NHLDIHHQMQLMQLISELPV--TSIVAIHDLNhAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:TIGR01192 500 SALDVETEARVKNAIDALRKnrTTFIIAHRLS-TVRNADLVLFLDQGRLIEKGSFQEL 556
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-222 |
4.03e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 99.84 E-value: 4.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 7 NITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQL--AR-RVACVEQ 83
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytVRkRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 HGMTEANMRVRDVVRlgriphhspfsnWSAQDDEAIAAALQRVAMLEKSEQGWL---------SLSGGERQRVHIARALA 154
Cdd:PRK11831 92 SGALFTDMNVFDNVA------------YPLREHTQLPAPLLHSTVMMKLEAVGLrgaaklmpsELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445942648 155 QSPSEILLDEPTNHLDIHHQMQLMQLISELP----VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNsalgVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-225 |
4.11e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.26 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHgmteanmr 92
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQN-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 vrdvvrlgriPHHSPFSNWSAQD----------DEA-----IAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSP 157
Cdd:PRK13652 87 ----------PDDQIFSPTVEQDiafgpinlglDEEtvahrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445942648 158 SEILLDEPTNHLDIHHQMQLMQLISELPV----TSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-225 |
4.69e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 99.70 E-value: 4.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDA---GRVTLDGQDIARMAKkqLARRV-------ACVEQHGMT 87
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGR--LARDIrksrantGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 EANMRVRDVV---RLGRIPH-HSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLD 163
Cdd:PRK09984 98 VNRLSVLENVligALGSTPFwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 164 EPTNHLDIHHQMQLMQLISELP----VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINqndgITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNE 243
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-225 |
5.50e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.78 E-value: 5.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 15 KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVAcveqhGMTEAN---- 90
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKA-----GMVFQNpdnq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 91 ---MRVRDVVRLGriPHhspfsNWSAQDDEA---IAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDE 164
Cdd:PRK13633 98 ivaTIVEEDVAFG--PE-----NLGIPPEEIrerVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 165 PTNHLDIHHQMQLMQLISELP----VTSIVAIHDLNHAAMfCDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNkkygITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-213 |
1.45e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.23 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 15 KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQ-------HGMT 87
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQdpmmgtaPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 -EANMRV------RDVVRLGRiphhspfsnwSAQDDEAIAAALQRVAM-LE---KSEQGwlSLSGGERQRVHIARALAQS 156
Cdd:COG1101 99 iEENLALayrrgkRRGLRRGL----------TKKRRELFRELLATLGLgLEnrlDTKVG--LLSGGQRQALSLLMATLTK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 157 PSEILLDEPTNHLDIHHQMQLMQL----ISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQI 213
Cdd:COG1101 167 PKLLLLDEHTAALDPKTAALVLELtekiVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-219 |
1.62e-24 |
|
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: 96.71 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQH-----GMTEANM 91
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDptlfsGTIRSNL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 92 rvrdvvrlgriphhSPFSNWSaqdDEAIAAALqRVAmlekseQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDI 171
Cdd:cd03369 103 --------------DPFDEYS---DEEIYGAL-RVS------EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDY 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 445942648 172 HHQMQLMQLISEL--PVTSIVAIHDLnHAAMFCDSLIVMQQGQILASGTP 219
Cdd:cd03369 159 ATDALIQKTIREEftNSTILTIAHRL-RTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
9-222 |
2.08e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 99.53 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 9 TWKAGKKVIvNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVACVEQ----- 83
Cdd:PRK11650 12 SYDGKTQVI-KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVFQnyaly 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 -HgMT-EANM----RVRDVVRlgriphhspfsnwsAQDDEAIAAA---LQRVAMLE-KSEQgwlsLSGGERQRVHIARAL 153
Cdd:PRK11650 89 pH-MSvRENMayglKIRGMPK--------------AEIEERVAEAariLELEPLLDrKPRE----LSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 154 AQSPSEILLDEPTNHLD----IHHQMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDaklrVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-225 |
2.39e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 101.34 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQhgmteanmrvRDV 96
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQ----------EPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 97 VRLGRIPHHSPFSNWSAQDDEAIAAALQRVA--MLEKSEQGWLS--------LSGGERQRVHIARALAQSPSEILLDEPT 166
Cdd:TIGR00958 566 LFSGSVRENIAYGLTDTPDEEIMAAAKAANAhdFIMEFPNGYDTevgekgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 167 NHLDIHHQMQLMQLISELPVTSIVAIHDLnHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:TIGR00958 646 SALDAECEQLLQESRSRASRTVLLIAHRL-STVERADQILVLKKGSVVEMGTHKQLMED 703
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-224 |
2.65e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 97.73 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMA----------KKQLA---RRVA 79
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgqlkvadKNQLRllrTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 80 CVEQHGMTEANMRVRDVVRlgriphHSPFSNWSAQDDEAIAAA---LQRVAMLEKSEQGW-LSLSGGERQRVHIARALAQ 155
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENVM------EAPIQVLGLSKQEARERAvkyLAKVGIDERAQGKYpVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445942648 156 SPSEILLDEPTNHLD---IHHQMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:PRK10619 170 EPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-225 |
2.69e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.89 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENI--TWKAG---KKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAK---- 71
Cdd:PRK13649 1 MGINLQNVsyTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 72 KQLARRVACVEQHGMTE--ANMRVRDVVrlgriphHSPfSNWSAQDDEAIAAALQRVAMLEKSE----QGWLSLSGGERQ 145
Cdd:PRK13649 81 KQIRKKVGLVFQFPESQlfEETVLKDVA-------FGP-QNFGVSQEEAEALAREKLALVGISEslfeKNPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 146 RVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISEL---PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhqsGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
...
gi 445942648 223 LSE 225
Cdd:PRK13649 233 FQD 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-226 |
2.84e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.86 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNN---VSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVE 82
Cdd:PRK13642 8 ENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTE-ANMRVRDVVRLGRIPHHSPFSNWSAQDDEAIAAalqrVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEIL 161
Cdd:PRK13642 88 QNPDNQfVGATVEDDVAFGMENQGIPREEMIKRVDEALLA----VNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 162 LDEPTNHLDIHHQMQLMQLISELP----VTSIVAIHDLNHAAMfCDSLIVMQQGQILASGTPEEILSEA 226
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKekyqLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATS 231
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-213 |
3.30e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 96.08 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 22 SLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVACVEQHGMTEANMRVRDVVRLGR 101
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 102 iphhSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLI 181
Cdd:TIGR01277 96 ----HPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 445942648 182 SEL----PVTSIVAIHDLNHAAMFCDSLIVMQQGQI 213
Cdd:TIGR01277 172 KQLcserQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-212 |
4.11e-24 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 96.35 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQ----DIARMAKKQLA--RR--VACVEQHgmtea 89
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPREILalRRrtIGYVSQF----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 90 nMRV------RDVVRlgriphhSPFSNWSAQDDEAIAAALQRVAMLEKSEQGW-LS---LSGGERQRVHIARALAQSPSE 159
Cdd:COG4778 102 -LRViprvsaLDVVA-------EPLLERGVDREEARARARELLARLNLPERLWdLPpatFSGGEQQRVNIARGFIADPPL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 160 ILLDEPTNHLDIHHQMQLMQLISELPV--TSIVAI-HDLNHAAMFCDSLIVMQQGQ 212
Cdd:COG4778 174 LLLDEPTASLDAANRAVVVELIEEAKArgTAIIGIfHDEEVREAVADRVVDVTPFS 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-213 |
4.34e-24 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 96.10 E-value: 4.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQ---LARRVACVEQHGMTEA 89
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 90 NMRVRDVVRLGRIphhspFSNWSAQD-DEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNH 168
Cdd:PRK10908 93 DRTVYDNVAIPLI-----IAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 445942648 169 LDIHHQMQLMQLISE---LPVTSIVAIHDLNHAAMFCDSLIVMQQGQI 213
Cdd:PRK10908 168 LDDALSEGILRLFEEfnrVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-221 |
5.20e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.10 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITwKAGKKVIVN-NVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIA----RMAkkqLARRVAC 80
Cdd:COG3845 9 RGIT-KRFGGVVANdDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirspRDA---IALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQHGMTEANMRVRDVVRLGRIPHHSPFSNWsaqddeaiAAALQRVAmlEKSEQGWL---------SLSGGERQRVHIAR 151
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGLEPTKGGRLDR--------KAARARIR--ELSERYGLdvdpdakveDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 152 ALAQSPsEIL-LDEPTNHLDIHHQMQLMQLISELpV---TSIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEE 221
Cdd:COG3845 155 ALYRGA-RILiLDEPTAVLTPQEADELFEILRRL-AaegKSIIFItHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2-170 |
7.48e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 95.24 E-value: 7.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 2 SICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDA---GRVTLDGQDIARMAkkQLARRV 78
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALP--AEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 79 ACVEQHGMTEANMRVRDVVRLGrIPHHSPfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPS 158
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFA-LPPTIG----RAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170
....*....|..
gi 445942648 159 EILLDEPTNHLD 170
Cdd:COG4136 154 ALLLDEPFSKLD 165
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
1.04e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.53 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 2 SICAEN-ITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRrPDAGRVTLDGQDIARMAKKQLARRVAC 80
Cdd:PRK11174 349 TIEAEDlEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQ-----HGMteanmrVRDVVRLGRIphhspfsnwsAQDDEAIAAALQR------VAMLEK------SEQGwLSLSGGE 143
Cdd:PRK11174 428 VGQnpqlpHGT------LRDNVLLGNP----------DASDEQLQQALENawvsefLPLLPQgldtpiGDQA-AGLSVGQ 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 144 RQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELP--VTSIVAIHDLNHAAMfCDSLIVMQQGQILASGTPEE 221
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASrrQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAE 569
|
....
gi 445942648 222 ILSE 225
Cdd:PRK11174 570 LSQA 573
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-220 |
1.87e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 95.18 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVtldgqdiarmaKKQLARRVACVE 82
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEAN--------MRVRDVVRlgriphhspfsnwsaqdDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALA 154
Cdd:PRK09544 74 QKLYLDTTlpltvnrfLRLRPGTK-----------------KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 155 QSPSEILLDEPTNHLDIHHQMQLMQLIS----ELPVTSIVAIHDLNHAAMFCDSLIVMQQgQILASGTPE 220
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDqlrrELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPE 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-217 |
2.16e-23 |
|
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: 93.15 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 7 NITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARmAKKQLARRVACVEQHgm 86
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD-LEKALSSLISVLNQR-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 87 teanmrvrdvvrlgriPH---HSPFSNWSAQddeaiaaalqrvamlekseqgwlsLSGGERQRVHIARALAQSPSEILLD 163
Cdd:cd03247 84 ----------------PYlfdTTLRNNLGRR------------------------FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 164 EPTNHLDIHHQMQLMQLI-SELPVTSIVAI-HDLNHAAMFcDSLIVMQQGQILASG 217
Cdd:cd03247 124 EPTVGLDPITERQLLSLIfEVLKDKTLIWItHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-192 |
2.97e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.96 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 15 KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTL-DGQDIARMAKK----------QLARrvacveq 83
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPQRpylplgtlreALLY------- 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 hgmteanmrvrdvvrlgriPHHSpfsnwSAQDDEAIAAALQRV------AMLEKsEQGWLS-LSGGERQRVHIARALAQS 156
Cdd:COG4178 449 -------------------PATA-----EAFSDAELREALEAVglghlaERLDE-EADWDQvLSLGEQQRLAFARLLLHK 503
|
170 180 190
....*....|....*....|....*....|....*..
gi 445942648 157 PSEILLDEPTNHLDIHHQMQLMQLI-SELPVTSIVAI 192
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLrEELPGTTVISV 540
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-225 |
3.50e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.38 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGqdiarmakkqlarRVAC-VE-QHGMtE 88
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVSAlLElGAGF-H 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 89 ANMRVRDVVRL-GRIPHHSPfsnwsaqddEAIAAALQRVAmlEKSEqgwL---------SLSGGERQRVHIARALAQSPs 158
Cdd:COG1134 101 PELTGRENIYLnGRLLGLSR---------KEIDEKFDEIV--EFAE---LgdfidqpvkTYSSGMRARLAFAVATAVDP- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 159 EILL-DEPTNHLDIHHQMQLMQLISEL---PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:COG1134 166 DILLvDEVLAVGDAAFQKKCLARIRELresGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-211 |
3.87e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.38 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAkkqlARRvACVEQH 84
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AER-GVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 gmtEANMRVRDVV-------RLGRIPhhspfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSP 157
Cdd:PRK11248 79 ---EGLLPWRNVQdnvafglQLAGVE--------KMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 158 SEILLDEPTNHLD--IHHQMQ--LMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQG 211
Cdd:PRK11248 148 QLLLLDEPFGALDafTREQMQtlLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-217 |
4.65e-23 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 93.37 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAkkqlarrvacvEQHGMtEAN 90
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG-----------LGGGF-NPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 91 MRVRDVVRL-GRIphhspfSNWSAQDDEAIAAALQRVAMLEKS-EQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNH 168
Cdd:cd03220 99 LTGRENIYLnGRL------LGLSRKEIDEKIDEIIEFSELGDFiDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 445942648 169 LDIHHQMQLMQLISEL---PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:cd03220 173 GDAAFQEKCQRRLRELlkqGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-225 |
4.77e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.90 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITW-----KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDI----ARMAK 71
Cdd:PRK13641 1 MSIKFENVDYiyspgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 72 KQLARRVACVEQHGMTE--ANMRVRDVvrlgripHHSPfSNWSAQDDEAIAAALQ---RVA----MLEKSEqgwLSLSGG 142
Cdd:PRK13641 81 KKLRKKVSLVFQFPEAQlfENTVLKDV-------EFGP-KNFGFSEDEAKEKALKwlkKVGlsedLISKSP---FELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 143 ERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPV---TSIVAIHDLNHAAMFCDSLIVMQQGQILASGTP 219
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP 229
|
....*.
gi 445942648 220 EEILSE 225
Cdd:PRK13641 230 KEIFSD 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
1.02e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.28 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MS-ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDI--ARMAKKQLARR 77
Cdd:PRK11264 1 MSaIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 78 VACVEQHGMTEANMRVrdvvrlgrIPHHSPFSNW--------SAQDDEAIAAA---LQRVAMLEKSEQGWLSLSGGERQR 146
Cdd:PRK11264 81 RQLRQHVGFVFQNFNL--------FPHRTVLENIiegpvivkGEPKEEATARArelLAKVGLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 147 VHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPV---TSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEIL 223
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQekrTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
..
gi 445942648 224 SE 225
Cdd:PRK11264 233 AD 234
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-222 |
1.18e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.10 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 2 SICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQdiaRMAKKQLARR-VAC 80
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNDVPPAERgVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQhgmteanmrvrdvvRLGRIPHHSPFSNWS-------------AQDDEAIAAALQRVAMLEKSEQgwlSLSGGERQRV 147
Cdd:PRK11000 80 VFQ--------------SYALYPHLSVAENMSfglklagakkeeiNQRVNQVAEVLQLAHLLDRKPK---ALSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 148 HIARALAQSPSEILLDEPTNHLD--IHHQM--QLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:PRK11000 143 AIGRTLVAEPSVFLLDEPLSNLDaaLRVQMriEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-198 |
1.22e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 92.57 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARM---AKKQLA-RRVACVEQ-HGMTEANM 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRnQKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 92 RVRDVVRLGRIPHHSPfsnwsAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDI 171
Cdd:PRK11629 104 ALENVAMPLLIGKKKP-----AEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180 190
....*....|....*....|....*....|.
gi 445942648 172 HHQMQLMQLISELPVTS----IVAIHDLNHA 198
Cdd:PRK11629 179 RNADSIFQLLGELNRLQgtafLVVTHDLQLA 209
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-213 |
1.75e-22 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 90.95 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGkkviVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARmakkqlarrvacveqh 84
Cdd:cd03215 7 VRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR---------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 gmteanMRVRDVVRLG--RIP----HHSPFSNWSAQDDEAIAAalqrvamlekseqgwlSLSGGERQRVHIARALAQSPS 158
Cdd:cd03215 67 ------RSPRDAIRAGiaYVPedrkREGLVLDLSVAENIALSS----------------LLSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 159 EILLDEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQI 213
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
10-222 |
2.03e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 94.00 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 10 WKAGKKV-IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQL--ARR-VACVEQHG 85
Cdd:PRK15079 28 WQPPKTLkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWraVRSdIQMIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 MTEANMRvrdvVRLGRI---PHHSPFSNWSAQD-DEAIAAALQRVAMLEK------SEqgwlsLSGGERQRVHIARALAQ 155
Cdd:PRK15079 108 LASLNPR----MTIGEIiaePLRTYHPKLSRQEvKDRVKAMMLKVGLLPNlinrypHE-----FSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 156 SPSEILLDEPTNHLDIHHQMQ----LMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQvvnlLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-183 |
2.11e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.09 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDI----ARMAKKQLAR 76
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIddpdVAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 77 RVACveqhgmtEANMRVRDVVRLgriphhspfsnWSA---QDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARAL 153
Cdd:PRK13539 81 RNAM-------KPALTVAENLEF-----------WAAflgGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLL 142
|
170 180 190
....*....|....*....|....*....|.
gi 445942648 154 AqSPSEI-LLDEPTNHLDIHHQMQLMQLISE 183
Cdd:PRK13539 143 V-SNRPIwILDEPTAALDAAAVALFAELIRA 172
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-216 |
2.11e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 95.36 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 20 NVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIA-RMAKKQLARRVACVEQHGMTEANMRVRDVVR 98
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELHLVPEMTVAENLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 99 LGRIPHHSPFSNWSAQDDEAiAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLM 178
Cdd:PRK11288 102 LGQLPHKGGIVNRRLLNYEA-REQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLF 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 445942648 179 QLISELPVTSIVAI---HDLNHAAMFCDSLIVMQQGQILAS 216
Cdd:PRK11288 181 RVIRELRAEGRVILyvsHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-203 |
2.95e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.15 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLR-------VLAGLRRpdAGRVTLDGQDI--ARMAKKQLA 75
Cdd:PRK14243 13 TENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLyaPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 76 RRVACVEQhgmtEAN---MRVRDVVRLG-RIphhspfSNWSAQDDEAIAAALQRVAMLE----KSEQGWLSLSGGERQRV 147
Cdd:PRK14243 91 RRIGMVFQ----KPNpfpKSIYDNIAYGaRI------NGYKGDMDELVERSLRQAALWDevkdKLKQSGLSLSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 148 HIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELP--VTSIVAIHDLNHAAMFCD 203
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKeqYTIIIVTHNMQQAARVSD 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-171 |
4.41e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 94.80 E-value: 4.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTL--------------------- 61
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvklayvdqsrdaldpnkt 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 62 ------DGQDIARMAKKQLARRVACveqhgmteanmrvrdvvrlgriphhSPFsNWSAQDDEaiaaalQRVAMlekseqg 135
Cdd:PRK11819 405 vweeisGGLDIIKVGNREIPSRAYV-------------------------GRF-NFKGGDQQ------KKVGV------- 445
|
170 180 190
....*....|....*....|....*....|....*.
gi 445942648 136 wlsLSGGERQRVHIARALAQSPSEILLDEPTNHLDI 171
Cdd:PRK11819 446 ---LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-225 |
5.10e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.10 E-value: 5.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 20 NVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAK----KQLARRVACVEQHGMTE--ANMRV 93
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKPVRKKVGVVFQFPESQlfEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 94 RDVVrlgriphHSPfSNWSAQDDEAIAAALQRVAMLEKSEQGW----LSLSGGERQRVHIARALAQSPSEILLDEPTNHL 169
Cdd:PRK13643 104 KDVA-------FGP-QNFGIPKEKAEKIAAEKLEMVGLADEFWekspFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 170 DIHHQMQLMQL---ISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK13643 176 DPKARIEMMQLfesIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-224 |
5.43e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.26 E-value: 5.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 15 KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQ------DIARMAKKQLARRVACVEQHGMTE 88
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 89 ANMRVRDVVRLgriphhsPFSNWSAQDDEAIAA----ALQRVAMLEKSEQGWLS----LSGGERQRVHIARALAQSPSEI 160
Cdd:PRK14246 103 PHLSIYDNIAY-------PLKSHGIKEKREIKKiveeCLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 161 LLDEPTNHLDIHHQMQLMQLISELP--VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKneIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-225 |
5.53e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.76 E-value: 5.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKAGK-----KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAK---- 71
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 72 KQLARRVACVEQhgMTEANMrVRDVVRlgRIPHHSPfSNWSAQDDEAIAAALQRVAMLEKS----EQGWLSLSGGERQRV 147
Cdd:PRK13646 81 RPVRKRIGMVFQ--FPESQL-FEDTVE--REIIFGP-KNFKMNLDEVKNYAHRLLMDLGFSrdvmSQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 148 HIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPV----TSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEIL 223
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdenkTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
..
gi 445942648 224 SE 225
Cdd:PRK13646 235 KD 236
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-224 |
5.74e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 92.72 E-value: 5.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIA---RMAKKQLARRVACVEQHGMTEANMR-- 92
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPYGSLNPRkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 VRDVV--------RLGRiphhspfsnwsAQDDEAIAAALQRVAMleKSEQGWL---SLSGGERQRVHIARALAQSPSEIL 161
Cdd:PRK11308 111 VGQILeepllintSLSA-----------AERREKALAMMAKVGL--RPEHYDRyphMFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 162 LDEPTNHLDIHHQMQ----LMQLISELPvTSIVAI-HDLN---HAAmfcDSLIVMQQGQILASGTPEEILS 224
Cdd:PRK11308 178 ADEPVSALDVSVQAQvlnlMMDLQQELG-LSYVFIsHDLSvveHIA---DEVMVMYLGRCVEKGTKEQIFN 244
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
11-221 |
8.00e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.96 E-value: 8.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPD---AGRVTLDGQdiaRMAKKQLARRVACVEQHGMT 87
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM---PIDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 EANMRVRD------VVRLGRiphhspfSNWSAQDDEAIAAALQRVAMLE------KSEQGWLSLSGGERQRVHIARALAQ 155
Cdd:TIGR00955 111 IPTLTVREhlmfqaHLRMPR-------RVTKKEKRERVDEVLQALGLRKcantriGVPGRVKGLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 156 SPSEILLDEPTNHLD---IHHQMQLMQLISELPVTSIVAIHDLNhAAMFC--DSLIVMQQGQILASGTPEE 221
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDsfmAYSVVQVLKGLAQKGKTIICTIHQPS-SELFElfDKIILMAEGRVAYLGSPDQ 253
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-231 |
9.13e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.20 E-value: 9.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR-VACVEQHGMTEANMR-VRD 95
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKlVGIVFQNPETQFVGRtVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 96 VVRLGRIPHHSPFSNWSAQDDEAIAaalqRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQM 175
Cdd:PRK13644 98 DLAFGPENLCLPPIEIRKRVDRALA----EIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 176 QLMQLISEL---PVTSIVAIHDLN--HAAmfcDSLIVMQQGQILASGTPEEILSEALLWDV 231
Cdd:PRK13644 174 AVLERIKKLhekGKTIVYITHNLEelHDA---DRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-207 |
1.24e-21 |
|
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: 90.16 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 27 RGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAkkqlarrvacveQHGMTEANMRVRDVVRlGRIPHHS 106
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP------------QYIKADYEGTVRDLLS-SITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 107 PFSNWSAQddeaIAAALQRVAMLeksEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPV 186
Cdd:cd03237 91 THPYFKTE----IAKPLQIEQIL---DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180
....*....|....*....|....*
gi 445942648 187 ----TSIVAIHDLNHAAMFCDSLIV 207
Cdd:cd03237 164 nnekTAFVVEHDIIMIDYLADRLIV 188
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-228 |
1.35e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.05 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 21 VSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR--VACVE---QHGMTeANMRVRD 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgiMLCPEdrkAEGII-PVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 96 VVRLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKS---EQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIH 172
Cdd:PRK11288 351 NINISARRHHLRAGCLINNRWEAENADRFIRSLNIKTpsrEQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVG 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 173 HQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQIL-----ASGTPEEILSEALL 228
Cdd:PRK11288 431 AKHEIYNVIYELAaqgVAVLFVSSDLPEVLGVADRIVVMREGRIAgelarEQATERQALSLALP 494
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-222 |
1.46e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 93.27 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDI-AR-MAKKqlaRRVac 80
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdAGdIATR---RRV-- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 veqhG-MTEA-----NMRVRDVV----RLGRIPhhspfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIA 150
Cdd:NF033858 342 ----GyMSQAfslygELTVRQNLelhaRLFHLP--------AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLA 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 151 RALAQSPsEIL-LDEPTNHLDIHHQMQLMQLISELP----VTSIVAIHDLNHAAMfCDSLIVMQQGQILASGTPEEI 222
Cdd:NF033858 410 VAVIHKP-ELLiLDEPTSGVDPVARDMFWRLLIELSredgVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-223 |
1.57e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.99 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQ-----DIARMAKKQ---LAR 76
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAErrrLLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 77 -RVACVEQHGMTEANMRVR---DVV-RL--------GRIphHSPFSNWsaqddeaiaaaLQRVAM-LEKSEQGWLSLSGG 142
Cdd:PRK11701 89 tEWGFVHQHPRDGLRMQVSaggNIGeRLmavgarhyGDI--RATAGDW-----------LERVEIdAARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 143 ERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLM----QLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGT 218
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLdllrGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGL 235
|
....*
gi 445942648 219 PEEIL 223
Cdd:PRK11701 236 TDQVL 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-222 |
6.13e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.24 E-value: 6.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVI-VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR-VACV-- 81
Cdd:COG3845 261 ENLSVRDDRGVPaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIpe 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 82 EQHGM-TEANMRVRDVVRLGRIpHHSPFSNWSAQDDEAIAA-ALQRVAMLE-KSEQGWL---SLSGGERQRVHIARALAQ 155
Cdd:COG3845 341 DRLGRgLVPDMSVAENLILGRY-RRPPFSRGGFLDRKAIRAfAEELIEEFDvRTPGPDTparSLSGGNQQKVILARELSR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 156 SPSEILLDEPTNHLDIH-----HQmQLMQ---------LISElpvtsivaihDLNHAAMFCDSLIVMQQGQILASGTPEE 221
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGaiefiHQ-RLLElrdagaavlLISE----------DLDEILALSDRIAVMYEGRIVGEVPAAE 488
|
.
gi 445942648 222 I 222
Cdd:COG3845 489 A 489
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-223 |
6.72e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 87.20 E-value: 6.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLR--RPDAGRVTLDGQDIARMAKKQLARR------ 77
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLgiflaf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 78 VACVEQHGMTEANMrVRDVvrlgriphhspfsnwsaqdDEaiaaalqrvamlekseqgwlSLSGGERQRVHIARALAQSP 157
Cdd:cd03217 84 QYPPEIPGVKNADF-LRYV-------------------NE--------------------GFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 158 SEILLDEPTNHLDIHHQMQLMQLISEL--PVTSIVAI-H-----DLNHAamfcDSLIVMQQGQILASGTPEEIL 223
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLreEGKSVLIItHyqrllDYIKP----DRVHVLYDGRIVKSGDKELAL 193
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-225 |
7.33e-21 |
|
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: 91.02 E-value: 7.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRV-TLDGQDIARMAKKQLARRVACVEQHGMTEAnmrvrdv 96
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDMTKPGPDGRGRAKRYIGILHQ------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 97 vRLGRIPHHSPFSNWSAQ------DDEAIAAA---LQRVAMLEKSEQGWL-----SLSGGERQRVHIARALAQSPSEILL 162
Cdd:TIGR03269 373 -EYDLYPHRTVLDNLTEAiglelpDELARMKAvitLKMVGFDEEKAEEILdkypdELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 163 DEPTNHLDIHHQMQLMQLI----SELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSIlkarEEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-182 |
1.07e-20 |
|
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: 86.78 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMaKKQLARRVACVEQH 84
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ-RDSIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMTEANMRVRDVVRLGRIPHhspfsnwsaqDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDE 164
Cdd:cd03231 82 PGIKTTLSVLENLRFWHADH----------SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170
....*....|....*...
gi 445942648 165 PTNHLDIHHQMQLMQLIS 182
Cdd:cd03231 152 PTTALDKAGVARFAEAMA 169
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-213 |
1.07e-20 |
|
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: 87.14 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTEANmRVRDV 96
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 97 VRLGRIphhspfsnwSAQDDEAIAAA-----------LQRVAMLEKSEQGWLsLSGGERQRVHIARALAQSPSEILLDEP 165
Cdd:cd03248 108 IAYGLQ---------SCSFECVKEAAqkahahsfiseLASGYDTEVGEKGSQ-LSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 445942648 166 TNHLDIHHQMQLMQLISELPV--TSIVAIHDLN---HAamfcDSLIVMQQGQI 213
Cdd:cd03248 178 TSALDAESEQQVQQALYDWPErrTVLVIAHRLStveRA----DQILVLDGGRI 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-183 |
4.20e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 85.24 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARmakkqlarrvaCVEQH 84
Cdd:PRK13538 4 ARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----------QRDEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GmteanmrvRDVVRLGripHH-------SPFSN--WSA-----QDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIA 150
Cdd:PRK13538 73 H--------QDLLYLG---HQpgiktelTALENlrFYQrlhgpGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALA 141
|
170 180 190
....*....|....*....|....*....|....
gi 445942648 151 RaLAQSPSEI-LLDEPTNHLDIHHQMQLMQLISE 183
Cdd:PRK13538 142 R-LWLTRAPLwILDEPFTAIDKQGVARLEALLAQ 174
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
13-227 |
4.54e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 87.27 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPD----AGRVTLDGQDIARMAKKQ----LARRVACVEQH 84
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRErrkiIGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMTEANmrvrDVVRLGR-----IPHHS---PFSNWSAQDDEAIAAALQRVAMleKSEQGWLS-----LSGGERQRVHIAR 151
Cdd:COG4170 98 PSSCLD----PSAKIGDqlieaIPSWTfkgKWWQRFKWRKKRAIELLHRVGI--KDHKDIMNsypheLTEGECQKVMIAM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 152 ALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPV---TSIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEILSEAL 227
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqgTSILLIsHDLESISQWADTITVLYCGQTVESGPTEQILKSPH 251
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-212 |
5.05e-20 |
|
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: 84.83 E-value: 5.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 7 NITWKAGK---KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGqdiarmakkqlarRVACVEQ 83
Cdd:cd03250 7 SFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 hgmtEA---NMRVRDVVRLGriphhSPFsnwsaqD----DEAI-AAALQR-VAMLEK------SEQGwLSLSGGERQRVH 148
Cdd:cd03250 74 ----EPwiqNGTIRENILFG-----KPF------DeeryEKVIkACALEPdLEILPDgdlteiGEKG-INLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 149 IARALAQSPSEILLDEPTNHLDIHHQMQLMQ--LISEL--PVTSIVAIHDLnHAAMFCDSLIVMQQGQ 212
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLlnNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-230 |
5.57e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.21 E-value: 5.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQ--DIARMAKKQLARRVACVEQHgmTEANMRVR 94
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD--PEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 95 DvvrlgrIPHHSPFS--NWSAQDDEA---IAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHL 169
Cdd:PRK13638 94 D------IDSDIAFSlrNLGVPEAEItrrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 170 DIHHQMQLMQLISELPVTS---IVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLWD 230
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGnhvIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAME 231
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-225 |
5.91e-20 |
|
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: 88.64 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 2 SICAENITWKAG-KKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVAC 80
Cdd:TIGR01193 473 DIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQHGMTEANmRVRDVVRLGRIPHHSPFSNWSAQDDEAIAAALQRVAM---LEKSEQGWlSLSGGERQRVHIARALAqSP 157
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLgyqTELSEEGS-SISGGQKQRIALARALL-TD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 158 SEIL-LDEPTNHLD-IHHQMQLMQLISELPVTSIVAIHDLNHAAMfCDSLIVMQQGQILASGTPEEILSE 225
Cdd:TIGR01193 630 SKVLiLDESTSNLDtITEKKIVNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-213 |
6.64e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 85.22 E-value: 6.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQ----LARRVACVEQHGMTEANMR 92
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 VRDVVRLGRIPHHSPfsnwSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIH 172
Cdd:PRK10584 105 ALENVELPALLRGES----SRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 445942648 173 HQMQLMQLISEL----PVTSIVAIHDLNHAAMfCDSLIVMQQGQI 213
Cdd:PRK10584 181 TGDKIADLLFSLnrehGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-224 |
7.03e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.02 E-value: 7.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 22 SLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQlaRRVACVEQHGMTEANMRVRDVVRLGR 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 102 iphhSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLI 181
Cdd:PRK10771 97 ----NPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 445942648 182 SEL----PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:PRK10771 173 SQVcqerQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-223 |
7.27e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.68 E-value: 7.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARmAKKQLARRVACVeqhgmteanM--R--- 92
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVV---------FgqRsql 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 -----VRDVVRLGR----IPhhspfsnwsaqdDEAIAAALQR-VAMLEKSE-------QgwLSLsgGERQRVHIARALAQ 155
Cdd:COG4586 108 wwdlpAIDSFRLLKaiyrIP------------DAEYKKRLDElVELLDLGElldtpvrQ--LSL--GQRMRCELAAALLH 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445942648 156 SPSEILLDEPTNHLDIHHQMQLMQLISEL----PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEIL 223
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYnrerGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELK 243
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-222 |
8.43e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.99 E-value: 8.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKS----SLLRVL--AG---------LRRPDAGRVTLDGQDIARMAKKQLARrVACVE 82
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGglvqcdkmlLRRRSRQVIELSEQSAAQMRHVRGAD-MAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANmrvrDVVRLGRIPHHSPFSNWSAQDDEAIAAALQrvaMLEK----SEQGWLS-----LSGGERQRVHIARAL 153
Cdd:PRK10261 111 QEPMTSLN----PVFTVGEQIAESIRLHQGASREEAMVEAKR---MLDQvripEAQTILSryphqLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 154 AQSPSEILLDEPTNHLDIHHQMQLMQLIS----ELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-223 |
9.94e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 85.28 E-value: 9.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 2 SICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGL--RRPDA---GRVTLDGQDI--ARMAKKQL 74
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRLFGRNIysPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 75 ARRVACVEQHGMTEANMRVRDVVRLGRipHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGW----LSLSGGERQRVHIA 150
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGV--KLNGLVKSKKELDERVEWALKKAALWDEVKDRLndypSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 151 RALAQSPSEILLDEPTNHLDIHHQMQLMQLISELP--VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEIL 223
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKkeYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-199 |
1.14e-19 |
|
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: 87.68 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLrrpdagrvtldGQDIARMAKKQLARRVACVEQHGMTEANMR 92
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFNGEARPQPGIKVGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 VRDVVRLG--RIPH--------HSPFSNWSAQDDEAIA--AALQ---------------RVAM----LEKSEQGWLSLSG 141
Cdd:TIGR03719 85 VRENVEEGvaEIKDaldrfneiSAKYAEPDADFDKLAAeqAELQeiidaadawdldsqlEIAMdalrCPPWDADVTKLSG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 142 GERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPVTSIVAIHD---LNHAA 199
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDryfLDNVA 225
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-223 |
1.82e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.10 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIA-RMAKKQLARRVACVEQh 84
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdARHRRAVCPRIAYMPQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GmteanmrvrdvvrLGR--IPHHSPFSN---------WSAQDDEaiaaalQRVAMLEKSeQGWLS--------LSGGERQ 145
Cdd:NF033858 84 G-------------LGKnlYPTLSVFENldffgrlfgQDAAERR------RRIDELLRA-TGLAPfadrpagkLSGGMKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 146 RVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISEL----PVTS-IVAIHDLNHAAMFcDSLIVMQQGQILASGTPE 220
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIraerPGMSvLVATAYMEEAERF-DWLVAMDAGRVLATGTPA 222
|
...
gi 445942648 221 EIL 223
Cdd:NF033858 223 ELL 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-225 |
2.07e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.00 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 19 NNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQH----GMTEANMrvr 94
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNvhlfNDTIANN--- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 95 dvVRLGRIPHHSpfsnwsaqDDEAIAAALQRVAM--LEKSEQGW--------LSLSGGERQRVHIARALAQSPSEILLDE 164
Cdd:PRK11176 437 --IAYARTEQYS--------REQIEEAARMAYAMdfINKMDNGLdtvigengVLLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 165 PTNHLDIHHQMQLMQLISELPV--TSIVAIHDLNHAAMfCDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK11176 507 ATSALDTESERAIQAALDELQKnrTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQ 568
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-224 |
2.44e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 86.95 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 10 WKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQhgmteA 89
Cdd:PLN03232 1244 YRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQ-----S 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 90 NMRVRDVVRLGRIP--HHSPFSNWSAQDDEAIAAALQRVAMLEKSE--QGWLSLSGGERQRVHIARALAQSPSEILLDEP 165
Cdd:PLN03232 1319 PVLFSGTVRFNIDPfsEHNDADLWEALERAHIKDVIDRNPFGLDAEvsEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 166 TNHLDIHHQMQLMQLISE--LPVTSIVAIHDLNhAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIREefKSCTMLVIAHRLN-TIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-207 |
6.52e-19 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 85.61 E-value: 6.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 27 RGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDgqdiARMAKKqlarrvacvEQHGMTEANMRVRDVVRlGRIPHHS 106
Cdd:COG1245 365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----LKISYK---------PQYISPDYDGTVEEFLR-SANTDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 107 PFSNWSAQddeaIAAALQRVAMLEKSEQgwlSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISEL-- 184
Cdd:COG1245 431 GSSYYKTE----IIKPLGLEKLLDKNVK---DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFae 503
|
170 180
....*....|....*....|....*
gi 445942648 185 --PVTSIVAIHDLNHAAMFCDSLIV 207
Cdd:COG1245 504 nrGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-189 |
7.13e-19 |
|
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: 80.66 E-value: 7.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 15 KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQdiarmakkqlaRRVACVEQHG-MTEANMRv 93
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLLFLPQRPyLPLGTLR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 94 rdvvrlgriphhspfsnwsaqddEAIAAALQRVamlekseqgwlsLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHH 173
Cdd:cd03223 82 -----------------------EQLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170
....*....|....*.
gi 445942648 174 QMQLMQLISELPVTSI 189
Cdd:cd03223 127 EDRLYQLLKELGITVI 142
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-220 |
8.75e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.42 E-value: 8.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGlrRPD----AGRVTLDGQDIARMAKKQLARRvacv 81
Cdd:COG0396 4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG--HPKyevtSGSILLDGEDILELSPDERARA---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 82 eqhGM-------TE-ANMRVRDVVRLGRiphhspfsnwSAQDDEAIAAALQRVAMLEKSEQGWLS-----------LSGG 142
Cdd:COG0396 78 ---GIflafqypVEiPGVSVSNFLRTAL----------NARRGEELSAREFLKLLKEKMKELGLDedfldryvnegFSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 143 ERQRVHIARALAQSPSEILLDEPTNHLDIhhqmQLMQLISEL------PVTSIVAI-HD---LNHAAmfCDSLIVMQQGQ 212
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDI----DALRIVAEGvnklrsPDRGILIItHYqriLDYIK--PDFVHVLVDGR 218
|
....*...
gi 445942648 213 ILASGTPE 220
Cdd:COG0396 219 IVKSGGKE 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3-222 |
9.23e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.44 E-value: 9.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAgKKVIVNNVSLRVPRGETVGLLGPNGCGKS----SLLRVL-AGLRRPdAGRVTLDGQDIARMAKKqlARR 77
Cdd:PRK10418 5 IELRNIALQA-AQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQT-AGRVLLDGKPVAPCALR--GRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 78 VACVEQHGMTEAN----MR--VRDVVR-LGRIPhhspfsnwsaqDDEAIAAAL--------QRVAMLEKSEqgwlsLSGG 142
Cdd:PRK10418 81 IATIMQNPRSAFNplhtMHthARETCLaLGKPA-----------DDATLTAALeavglenaARVLKLYPFE-----MSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 143 ERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPVTS----IVAIHDLNHAAMFCDSLIVMQQGQILASGT 218
Cdd:PRK10418 145 MLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRalgmLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
....
gi 445942648 219 PEEI 222
Cdd:PRK10418 225 VETL 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-207 |
9.62e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.86 E-value: 9.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 27 RGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDgqdiarmakkqlaRRVACVEQHGMTEANMRVRDVvrLGRIPhhS 106
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------------LKISYKPQYIKPDYDGTVEDL--LRSIT--D 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 107 PF-SNWSAQDdeaIAAALQRVAMLEKSEQGwlsLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQ----LMQLI 181
Cdd:PRK13409 427 DLgSSYYKSE---IIKPLQLERLLDKNVKD---LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAvakaIRRIA 500
|
170 180
....*....|....*....|....*.
gi 445942648 182 SELPVTSIVAIHDLNHAAMFCDSLIV 207
Cdd:PRK13409 501 EEREATALVVDHDIYMIDYISDRLMV 526
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-228 |
1.12e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.68 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGkkviVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQ-LARRVACVeq 83
Cdd:COG1129 259 VEGLSVGGV----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYV-- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 hgmTE--------ANMRVRDVVRLGRIPHHSPFSNWSAQDDEAIAAALqrVAMLE-KS---EQGWLSLSGGERQRVHIAR 151
Cdd:COG1129 333 ---PEdrkgeglvLDLSIRENITLASLDRLSRGGLLDRRRERALAEEY--IKRLRiKTpspEQPVGNLSGGNQQKVVLAK 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 152 ALAQSPSEILLDEPT------NHLDIHHQM-QLMQ------LIS-ELPvtSIVAIhdlnhaamfCDSLIVMQQGQILASG 217
Cdd:COG1129 408 WLATDPKVLILDEPTrgidvgAKAEIYRLIrELAAegkaviVISsELP--ELLGL---------SDRILVMREGRIVGEL 476
|
250
....*....|.
gi 445942648 218 TPEEILSEALL 228
Cdd:COG1129 477 DREEATEEAIM 487
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-224 |
1.87e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.46 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR-VACVEQH 84
Cdd:PRK11614 9 DKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAIVPEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMTEANMRVRDVVRLGriphhsPFSNWSAQDDEAIAAALQRVAML-EKSEQGWLSLSGGERQRVHIARALAQSPSEILLD 163
Cdd:PRK11614 89 RRVFSRMTVEENLAMG------GFFAERDQFQERIKWVYELFPRLhERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 164 EPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLReqgMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-183 |
2.09e-18 |
|
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: 80.48 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAkKQLARRVACVEQH 84
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMTEANMRVRDVVRLgriphhspFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDE 164
Cdd:TIGR01189 82 PGLKPELSALENLHF--------WAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170
....*....|....*....
gi 445942648 165 PTNHLDIHHQMQLMQLISE 183
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRA 172
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-211 |
2.41e-18 |
|
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: 79.98 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 2 SICAENITW----KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGlrRPDAGRVT----LDGQDIarmaKKQ 73
Cdd:cd03232 3 VLTWKNLNYtvpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITgeilINGRPL----DKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 74 LARRVACVEQHGMTEANMRVRDVVRlgriphhspFSnwsaqddeaiaAALQrvamlekseqgwlSLSGGERQRVHIARAL 153
Cdd:cd03232 77 FQRSTGYVEQQDVHSPNLTVREALR---------FS-----------ALLR-------------GLSVEQRKRLTIGVEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 154 AQSPSEILLDEPTNHLDIHHQMQLMQLISELPVT--SIV-AIHDLNHA--AMFcDSLIVMQQG 211
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSgqAILcTIHQPSASifEKF-DRLLLLKRG 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-225 |
2.64e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 7 NITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLrRPDA---GRVTLDGQDI-ARMAKKQLARRVACVE 82
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEELqASNIRDTERAGIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANMRVRDVVRLGRIPHHSPFSNWSAQDDEAiAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILL 162
Cdd:PRK13549 89 QELALVKELSVLENIFLGNEITPGGIMDYDAMYLRA-QKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 163 DEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASgTPEEILSE 225
Cdd:PRK13549 168 DEPTASLTESETAVLLDIIRDLKahgIACIYISHKLNEVKAISDTICVIRDGRHIGT-RPAAGMTE 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-224 |
3.70e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 83.31 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLR--RPDAGRV--------------------- 59
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 60 -------TLDGQDI-----ARMAKKQLARRVACVEQHgmTEA---NMRVRDVVRlgRIPHHSPFSNwsaqdDEAIAAALQ 124
Cdd:TIGR03269 81 pcpvcggTLEPEEVdfwnlSDKLRRRIRKRIAIMLQR--TFAlygDDTVLDNVL--EALEEIGYEG-----KEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 125 RVAMLEKSEQGW---LSLSGGERQRVHIARALAQSPSEILLDEPTNHLD-----IHHQMqLMQLISELPVTSIVAIHDLN 196
Cdd:TIGR03269 152 LIEMVQLSHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtakLVHNA-LEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*...
gi 445942648 197 HAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-221 |
3.76e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.23 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLA--RRvacvEQHGMTeanmrvr 94
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlRR----EHFGFI------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 95 dVVRLGRIPHHSPFSNWS----------AQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDE 164
Cdd:PRK10535 92 -FQRYHLLSHLTAAQNVEvpavyaglerKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 165 PTNHLDIHHQMQLMQLISELPV---TSIVAIHDLNHAAMfCDSLIVMQQGQILASGTPEE 221
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDrghTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQE 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-222 |
3.89e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.23 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 20 NVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKK--------------QLAR-----RVAC 80
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclppekrrigyvfQDARlfphyKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 VEQHGMTEAnMRVR--DVVRLGRIPHHspfsnwsaqddeaiaaaLQRVAMlekseqgwlSLSGGERQRVHIARALAQSPS 158
Cdd:PRK11144 96 NLRYGMAKS-MVAQfdKIVALLGIEPL-----------------LDRYPG---------SLSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 159 EILLDEPTNHLDIHHQMQLMQLISELPVTSIVAI----HDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELLPYLERLAREINIPIlyvsHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-224 |
5.50e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 5.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 2 SICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDA-----GRVTLDGQDI--ARMAKKQL 74
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 75 ARRVACVeqhgMTEAN---MRVRDVVRLG-RIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIA 150
Cdd:PRK14258 87 RRQVSMV----HPKPNlfpMSVYDNVAYGvKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 151 RALAQSPSEILLDEPTNHLD------IHHQMQLMQLISELpvTSIVAIHDLNHAAMFCDSLIVMQQ-----GQILASGTP 219
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDpiasmkVESLIQSLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLT 240
|
....*
gi 445942648 220 EEILS 224
Cdd:PRK14258 241 KKIFN 245
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
6-220 |
7.25e-18 |
|
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: 80.00 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGlrRPD----AGRVTLDGQDIARMAKKQLARR---- 77
Cdd:TIGR01978 4 KDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDLLELEPDERARAglfl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 78 --VACVEQHGMTeANMRVRDV---VRLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKS-EQGWlslSGGERQRVHIAR 151
Cdd:TIGR01978 82 afQYPEEIPGVS-NLEFLRSAlnaRRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSvNEGF---SGGEKKRNEILQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 152 ALAQSPSEILLDEPTNHLDIHHQMQLMQLISEL--PVTSIVAI-HD---LNHAAMfcDSLIVMQQGQILASGTPE 220
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDIDALKIVAEGINRLrePDRSFLIItHYqrlLNYIKP--DYVHVLLDGRIVKSGDVE 230
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-196 |
1.02e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 81.86 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLD-GQDIARMAKKQLArrvacV 81
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQFA-----F 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 82 EQhgmteanMRVRDVVRLGriphHSPFsnWSA-QDDEAIAAALQ-------RVAMLE-----------KSEQGWLSLSGG 142
Cdd:PRK15064 77 EE-------FTVLDTVIMG----HTEL--WEVkQERDRIYALPEmseedgmKVADLEvkfaemdgytaEARAGELLLGVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 143 --ERQ--------------RVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPVTSIVAIHD---LN 196
Cdd:PRK15064 144 ipEEQhyglmsevapgwklRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDrhfLN 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
1.15e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.52 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKAGKKV-----IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAK---- 71
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 72 --------------------KQLARRVACVEQ---HGMTEANMRvRDVVrlgriphHSPFSnWSAQDDEAIAAALQRVAM 128
Cdd:PRK13651 81 ekvleklviqktrfkkikkiKEIRRRVGVVFQfaeYQLFEQTIE-KDII-------FGPVS-MGVSKEEAKKRAAKYIEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 129 -------LEKSEqgwLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPV---TSIVAIHDLNHA 198
Cdd:PRK13651 152 vgldesyLQRSP---FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqgkTIILVTHDLDNV 228
|
250 260
....*....|....*....|....*..
gi 445942648 199 AMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK13651 229 LEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-212 |
1.25e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.68 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKS-SLLRVLAGLRRPDA----GRVTLDGQDIARMAKKQL----ARRVACVEQHGMT 87
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLLHASEQTLrgvrGNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 EAN------MRVRDVVRLgriphHSPFSNWSAQDDeaIAAALQRVAMLEKSEQgwLS-----LSGGERQRVHIARALAQS 156
Cdd:PRK15134 104 SLNplhtleKQLYEVLSL-----HRGMRREAARGE--ILNCLDRVGIRQAAKR--LTdyphqLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 157 PSEILLDEPTNHLDIHHQMQLMQLISELPV---TSIVAI-HDLNHAAMFCDSLIVMQQGQ 212
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQelnMGLLFItHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-227 |
1.49e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.45 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTEANMRVRdVV 97
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTSLNPRQR-IS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 98 RLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGW-LSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQ 176
Cdd:PRK15112 108 QILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYpHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 177 LMQLISELPVT-SIVAIHDLNHAAMF---CDSLIVMQQGQILASGTPEEILSEAL 227
Cdd:PRK15112 188 LINLMLELQEKqGISYIYVTQHLGMMkhiSDQVLVMHQGEVVERGSTADVLASPL 242
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-211 |
1.62e-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: 78.53 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 9 TWKAGKKVIvNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR----VACVEQH 84
Cdd:cd03290 9 SWGSGLATL-SNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMTeANMRVRDVVRLGriphhSPFSNwsaQDDEAI--AAALQ-RVAML------EKSEQGwLSLSGGERQRVHIARALAQ 155
Cdd:cd03290 88 PWL-LNATVEENITFG-----SPFNK---QRYKAVtdACSLQpDIDLLpfgdqtEIGERG-INLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 156 SPSEILLDEPTNHLDIH---HQMQ--LMQLISELPVTSIVAIHDLN---HAamfcDSLIVMQQG 211
Cdd:cd03290 158 NTNIVFLDDPFSALDIHlsdHLMQegILKFLQDDKRTLVLVTHKLQylpHA----DWIIAMKDG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-228 |
2.04e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR-VACV 81
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 82 EQHGMTEANMRVRDVVRLGRIPHHS----PFSNWSAQDDEAiAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSP 157
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKvcgvNIIDWREMRVRA-AMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 158 SEILLDEPTNHLDIHHQMQLMQLISELPV--TSIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALL 228
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKegTAIVYIsHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIV 238
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-199 |
3.13e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.55 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLdgqdiarmakkQLARRVACVEQHGMTEANMR 92
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-----------APGIKVGYLPQEPQLDPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 VRDVV------------RLGRIphHSPFSNWSAQDDEAIA--AALQ---------------RVAM----LEKSEQGWLSL 139
Cdd:PRK11819 87 VRENVeegvaevkaaldRFNEI--YAAYAEPDADFDALAAeqGELQeiidaadawdldsqlEIAMdalrCPPWDAKVTKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 140 SGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPVTsIVAI-HD---LNHAA 199
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGT-VVAVtHDryfLDNVA 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-242 |
5.62e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.74 E-value: 5.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 16 VIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLdgQDIARMAKKQLARRVACVEQHGMTEANMRVRD 95
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELITNPYSKKIKNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 96 VVRLGRIPHHSPFSNWSAQD-------------DEAIAAALQRVAM------LEKSEQGwlsLSGGERQRVHIARALAQS 156
Cdd:PRK13631 118 VSMVFQFPEYQLFKDTIEKDimfgpvalgvkksEAKKLAKFYLNKMglddsyLERSPFG---LSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 157 PSEILLDEPTNHLDIHHQMQLMQLISELPV---TSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEallwDVFR 233
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTD----QHII 270
|
....*....
gi 445942648 234 VKTKIEISP 242
Cdd:PRK13631 271 NSTSIQVPR 279
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-170 |
1.10e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.74 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVL--AGLRRPD---AGRVTLDGQDI--ARMAKKQLARRVACVEQhg 85
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQ-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 mtEAN---MRVRDVVRLG-RIPhhspfsnwSAQD----DEAIAAALQRVAMLEKSE----QGWLSLSGGERQRVHIARAL 153
Cdd:PRK14239 94 --QPNpfpMSIYENVVYGlRLK--------GIKDkqvlDEAVEKSLKGASIWDEVKdrlhDSALGLSGGQQQRVCIARVL 163
|
170
....*....|....*..
gi 445942648 154 AQSPSEILLDEPTNHLD 170
Cdd:PRK14239 164 ATSPKIILLDEPTSALD 180
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-225 |
1.11e-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: 78.71 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 7 NITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLrRPDA---GRVTLDGQDI-ARMAKKQLARRVACVE 82
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLkASNIRDTERAGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANMRVRDVVRLG-RIPHHSPFSNWSA--QDDEAIAAALQRVAMLEKSEQGwlSLSGGERQRVHIARALAQSPSE 159
Cdd:TIGR02633 85 QELTLVPELSVAENIFLGnEITLPGGRMAYNAmyLRAKNLLRELQLDADNVTRPVG--DYGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 160 ILLDEPTNHLDIHHQMQLMQLISELPVTSIVAI---HDLNHAAMFCDSLIVMQQGQILASgTPEEILSE 225
Cdd:TIGR02633 163 LILDEPSSSLTEKETEILLDIIRDLKAHGVACVyisHKLNEVKAVCDTICVIRDGQHVAT-KDMSTMSE 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-223 |
2.43e-16 |
|
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: 78.45 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 9 TWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQdiarmakkqlarrVACVEQHGMTE 88
Cdd:TIGR00957 645 TWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 89 aNMRVRDVVRLGriphHSPFSNWSAQDDEAiAAALQRVAML------EKSEQGwLSLSGGERQRVHIARALAQSPSEILL 162
Cdd:TIGR00957 712 -NDSLRENILFG----KALNEKYYQQVLEA-CALLPDLEILpsgdrtEIGEKG-VNLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 163 DEPTNHLDIHHQMQLMQ-LISELPV----TSIVAIHDLNHAAMfCDSLIVMQQGQILASGTPEEIL 223
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIFEhVIGPEGVlknkTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELL 849
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
18-225 |
2.51e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 77.09 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKS-SLLRVLAGLRRPdaGRVT-----LDGQDIARMAKKQlaRR------VACVEQHG 85
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaekleFNGQDLQRISEKE--RRnlvgaeVAMIFQDP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 86 MTEAN---------MRVRDVVRLGriphhspfsNWSAQDDEAIAAaLQRVAMLEKSEQgwLS-----LSGGERQRVHIAR 151
Cdd:PRK11022 99 MTSLNpcytvgfqiMEAIKVHQGG---------NKKTRRQRAIDL-LNQVGIPDPASR--LDvyphqLSGGMSQRVMIAM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 152 ALAQSPSEILLDEPTNHLDIHHQMQLMQLISELP----VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDVTIQAQIIELLLELQqkenMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRA 244
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-242 |
2.73e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.59 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKV-----IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDI-ARMAK----K 72
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKikevK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 73 QLARRVACVEQhgMTEANM---RVRDVVRLGRIphhspfsNWSAQDDEA---IAAALQRVAMLEK-SEQGWLSLSGGERQ 145
Cdd:PRK13645 87 RLRKEIGLVFQ--FPEYQLfqeTIEKDIAFGPV-------NLGENKQEAykkVPELLKLVQLPEDyVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 146 RVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPVTS----IVAIHDLNHAAMFCDSLIVMQQGQILASGTPEE 221
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYkkriIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFE 237
|
250 260
....*....|....*....|.
gi 445942648 222 ILSEALLWdvfrvkTKIEISP 242
Cdd:PRK13645 238 IFSNQELL------TKIEIDP 252
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
14-224 |
4.58e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.23 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 14 KKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPD--AGRVTLDGQDIArmakKQLARRVACVEQHGMTEANM 91
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT----KQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 92 RVRDV---VRLGRIPhhspfSNWSAQDDEAIAAALQRVAMLEKSEQGWLS------LSGGERQRVHIARALAQSPSEILL 162
Cdd:PLN03211 156 TVRETlvfCSLLRLP-----KSLTKQEKILVAESVISELGLTKCENTIIGnsfirgISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 163 DEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAA--MFcDSLIVMQQGQILASGTPEEILS 224
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAqkgKTIVTSMHQPSSRVyqMF-DSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-228 |
5.78e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 19 NNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKK--QLA------RRVACVEQHGMTEAN 90
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssQEAgigiihQELNLIPQLTIAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 91 MRVRDVV-RLGRIphhspfsNWSAQDDEAiAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHL 169
Cdd:PRK10762 101 FLGREFVnRFGRI-------DWKKMYAEA-DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445942648 170 DIHHQMQLMQLISELPVTS--IVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALL 228
Cdd:PRK10762 173 TDTETESLFRVIRELKSQGrgIVYIsHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLI 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-222 |
5.99e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 20 NVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARR--VACVE---QHGM-TEANMRv 93
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARglVYLPEdrqSSGLyLDAPLA- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 94 RDVVRLgriPHHSPfSNWsaQDDEAIAAALQRV--AM---LEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNH 168
Cdd:PRK15439 360 WNVCAL---THNRR-GFW--IKPARENAVLERYrrALnikFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 169 LDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAaqnVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-193 |
8.90e-16 |
|
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: 76.33 E-value: 8.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 16 VIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGL--------------------RRPDAGRVTLDGQDIARMAKKQLA 75
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrltkpakgklfyvpQRPYMTLGTLRDQIIYPDSSEDMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 76 RRvacveqhGMTEANM-RVRDVVRLGRIphhspfsnwsaqddeaiaaaLQRVAMLEkSEQGWLS-LSGGERQRVHIARAL 153
Cdd:TIGR00954 546 RR-------GLSDKDLeQILDNVQLTHI--------------------LEREGGWS-AVQDWMDvLSGGEKQRIAMARLF 597
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 445942648 154 AQSPSEILLDEPTNHLDIHHQMQLMQLISELPVTSIVAIH 193
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-194 |
1.66e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 75.37 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVtldgqdiaRMAKKQlarRVACVEQH 84
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--------HCGTKL---EVAYFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 gmtEANM----RVRDVVRLGR-------IPHHspfsnwsaqddeaIAAALQ------RVAMLEKSeqgwlSLSGGERQRV 147
Cdd:PRK11147 391 ---RAELdpekTVMDNLAEGKqevmvngRPRH-------------VLGYLQdflfhpKRAMTPVK-----ALSGGERNRL 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 445942648 148 HIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPVTSIVAIHD 194
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
15-225 |
1.87e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.52 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 15 KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTEANmRVR 94
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLAD-TFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 95 DVVRLGRiphhspfsnwsAQDDEAIAAALQRV--AMLEKS----------EQGwLSLSGGERQRVHIARALAQSPSEILL 162
Cdd:PRK10790 433 ANVTLGR-----------DISEEQVWQALETVqlAELARSlpdglytplgEQG-NNLSVGQKQLLALARVLVQTPQILIL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 163 DEPTNHLDIHHQM---QLMQLISElPVTSIVAIHDLNhAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:PRK10790 501 DEATANIDSGTEQaiqQALAAVRE-HTTLVVIAHRLS-TIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-224 |
1.99e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.98 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 2 SICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVL-------AGLRRpdAGRVTLDGQDIARMAKK-Q 73
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRY--SGDVLLGGRSIFNYRDVlE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 74 LARRVACVEQHGmTEANMRVRDVVRLGRIPHH-SPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARA 152
Cdd:PRK14271 99 FRRRVGMLFQRP-NPFPMSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 153 LAQSPSEILLDEPTNHLDIHHQMQLMQLISELP--VTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAdrLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-224 |
2.19e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.54 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQhgmteANMRVRDV 96
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQ-----APVLFSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 97 VRLGRIP--HHSPFSNWSAQDDEAIAAALQRVAM---LEKSEQGwLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDI 171
Cdd:PLN03130 1329 VRFNLDPfnEHNDADLWESLERAHLKDVIRRNSLgldAEVSEAG-ENFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 172 HHQMQLMQLISE--LPVTSIVAIHDLNhAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:PLN03130 1408 RTDALIQKTIREefKSCTMLIIAHRLN-TIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-217 |
1.37e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.97 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLA---RRVACVEQHGMTEANMR-- 92
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalrRDIQFIFQDPYASLDPRqt 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 ----VRDVVRLgriphHSPFSNWSAQddEAIAAALQRVAMleKSEQGWL---SLSGGERQRVHIARALAQSPSEILLDEP 165
Cdd:PRK10261 420 vgdsIMEPLRV-----HGLLPGKAAA--ARVAWLLERVGL--LPEHAWRyphEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 166 TNHLDIHHQMQLMQLI----SELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASG 217
Cdd:PRK10261 491 VSALDVSIRGQIINLLldlqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-217 |
2.20e-14 |
|
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: 69.60 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDA---GRVTLDGQDIARMaKKQLARRVACVEQHGMT 87
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEF-AEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 EANMRVRDVVRLgriphhspfsnwsaqddeaiAAALQRVAMLEKseqgwlsLSGGERQRVHIARALAQSPSEILLDEPTN 167
Cdd:cd03233 95 FPTLTVRETLDF--------------------ALRCKGNEFVRG-------ISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 168 HLD---IHHQMQLMQLIS-ELPVTSIVAIHDLNHA--AMFcDSLIVMQQGQILASG 217
Cdd:cd03233 148 GLDsstALEILKCIRTMAdVLKTTTFVSLYQASDEiyDLF-DKVLVLYEGRQIYYG 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-228 |
5.17e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.85 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENItWKAGKKVIV-NNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARM--AK-KQLArrV 78
Cdd:PRK15439 12 LCARSI-SKQYSGVEVlKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpAKaHQLG--I 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 79 ACVEQHGMTEANMRVRDVVrLGRIPHHspfsnwsaqddeaiAAALQRVAMLEKSEQGWLSLSG-------GERQRVHIAR 151
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENI-LFGLPKR--------------QASMQKMKQLLAALGCQLDLDSsagslevADRQIVEILR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 152 ALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPVTS--IVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALL 228
Cdd:PRK15439 154 GLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGvgIVFIsHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDII 233
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-171 |
6.28e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 70.69 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTL-DGQDIARMAKKqlarrvacveq 83
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWsENANIGYYAQD----------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 hgmteanmrvrdvvrlgripHHSPFSN------WSAQ------DDEAIAAALQRvaML------EKSEQgwlSLSGGERQ 145
Cdd:PRK15064 391 --------------------HAYDFENdltlfdWMSQwrqegdDEQAVRGTLGR--LLfsqddiKKSVK---VLSGGEKG 445
|
170 180
....*....|....*....|....*.
gi 445942648 146 RVHIARALAQSPSEILLDEPTNHLDI 171
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDM 471
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-216 |
9.08e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.14 E-value: 9.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIA-RMAKKQLARRVACVEQhgmtEANM----R 92
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQ----ELNLvlqrS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 VRDVVRLGRIPHHSPFSNWSA--QDDEAIAAALQrVAMLEKSEQGWLSLSggERQRVHIARALAQSPSEILLDEPTNHLD 170
Cdd:PRK10982 90 VMDNMWLGRYPTKGMFVDQDKmyRDTKAIFDELD-IDIDPRAKVATLSVS--QMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 445942648 171 IHHQMQLMQLISELPVT--SIVAI-HDLNHAAMFCDSLIVMQQGQILAS 216
Cdd:PRK10982 167 EKEVNHLFTIIRKLKERgcGIVYIsHKMEEIFQLCDEITILRDGQWIAT 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-219 |
9.84e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.43 E-value: 9.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENIT--WKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIarmakkqlarrvac 80
Cdd:TIGR01257 929 VCVKNLVkiFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-------------- 994
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 81 veqhgmtEANMrvrDVVR--LGRIPHHSP-FSNWSAQD-------------DEA---IAAALQRVAMLEKSEQGWLSLSG 141
Cdd:TIGR01257 995 -------ETNL---DAVRqsLGMCPQHNIlFHHLTVAEhilfyaqlkgrswEEAqleMEAMLEDTGLHHKRNEEAQDLSG 1064
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 142 GERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPV--TSIVAIHDLNHAAMFCDSLIVMQQGQILASGTP 219
Cdd:TIGR01257 1065 GMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSgrTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-227 |
9.89e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 9.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENITWKAGKKVivNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMA-----KKQLA---- 75
Cdd:PRK09700 268 VRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavKKGMAyite 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 76 -RRVACVEQHGMTEANMRVRDVVRLGR------IPHHSpfsnwsaqdDEAIAAALQRVAMLEKS---EQGWLSLSGGERQ 145
Cdd:PRK09700 346 sRRDNGFFPNFSIAQNMAISRSLKDGGykgamgLFHEV---------DEQRTAENQRELLALKChsvNQNITELSGGNQQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 146 RVHIARALAQSPSEILLDEPTNHLDIHHQMQ---LMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQI------LAS 216
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEiykVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLtqiltnRDD 496
|
250
....*....|.
gi 445942648 217 GTPEEILSEAL 227
Cdd:PRK09700 497 MSEEEIMAWAL 507
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
18-213 |
1.41e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.62 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIA---RMAKKQLARRVacveqhgmteanmrVR 94
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaeqPEDYRKLFSAV--------------FT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 95 DVVRLGRIPHHSPFsnwsAQDDEAIAAALQRVAMLEK-SEQGW----LSLSGGERQRVHIARALAQSPSEILLDEPTNHL 169
Cdd:PRK10522 405 DFHLFDQLLGPEGK----PANPALVEKWLERLKMAHKlELEDGrisnLKLSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 445942648 170 DIHHQ----MQLMQLISELPVTsIVAI-HDlNHAAMFCDSLIVMQQGQI 213
Cdd:PRK10522 481 DPHFRrefyQVLLPLLQEMGKT-IFAIsHD-DHYFIHADRLLEMRNGQL 527
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-208 |
1.79e-13 |
|
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: 68.16 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 23 LRVPR-GETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVT-----------LDGQDIARMAKKQLARRVACVeqhgmtean 90
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQNYFTKLLEGDVKVI--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 91 MRVRDVVRLGRIPHHSPFSNWSAQDD----EAIAAALQRVAMLEKSEQgwlSLSGGERQRVHIARALAQSPSEILLDEPT 166
Cdd:cd03236 91 VKPQYVDLIPKAVKGKVGELLKKKDErgklDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 445942648 167 NHLDIHHQMQLMQLISEL--PVTSIVAI-HDLNHAAMFCDSLIVM 208
Cdd:cd03236 168 SYLDIKQRLNAARLIRELaeDDNYVLVVeHDLAVLDYLSDYIHCL 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-228 |
2.37e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDI-ARMAKKQLARRVACVEQH----GMTeANMR 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEDrkrdGLV-LGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 VRDVVRLGRIPHhspFSNWSAQ---DDEAIAAA-------LQRVAMleksEQGWLSLSGGERQRVHIARALAQSPSEILL 162
Cdd:PRK10762 347 VKENMSLTALRY---FSRAGGSlkhADEQQAVSdfirlfnIKTPSM----EQAIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 163 DEPTNHLDIHHQMQLMQLISELPVT--SIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALL 228
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQFKAEglSIILVsSEMPEVLGMSDRILVMHEGRISGEFTREQATQEKLM 488
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-213 |
3.07e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 68.66 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTL-DGQDIARMAKKQLA--RRVACVE 82
Cdd:PRK10636 316 EKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLEflRADESPL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QH----GMTEANMRVRDVvrLGriphhspfsNWSAQDDEaiaaalqrvaMLEKSEQgwlsLSGGERQRVHIARALAQSPS 158
Cdd:PRK10636 396 QHlarlAPQELEQKLRDY--LG---------GFGFQGDK----------VTEETRR----FSGGEKARLVLALIVWQRPN 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 159 EILLDEPTNHLDIHHQMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQI 213
Cdd:PRK10636 451 LLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-216 |
3.36e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 68.73 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLA-----GLRR------------------------ 53
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIPKncqilhveqevvgddttalqcvln 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 54 PDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTEANMRVRDVV--RLGRIPHHSPFSN-WSAQDDEA-IAAALQRVAML 129
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVsqRLEEIYKRLELIDaYTAEARAAsILAGLSFTPEM 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 130 EKSEQGwlSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPVTSIVaihdLNHAAMFCDSL---I 206
Cdd:PLN03073 338 QVKATK--TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIV----VSHAREFLNTVvtdI 411
|
250
....*....|
gi 445942648 207 VMQQGQILAS 216
Cdd:PLN03073 412 LHLHGQKLVT 421
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-171 |
3.60e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.44 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 20 NVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDG--------QD----------------IARMAKK--- 72
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqQDpprnvegtvydfvaegIEEQAEYlkr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 73 --QLARRVACVEQHGMTEANMRVRDVvrlgrIPHHSpfsNWsaQDDEAIAAALQRvamLEKSEQGWLS-LSGGERQRVHI 149
Cdd:PRK11147 101 yhDISHLVETDPSEKNLNELAKLQEQ-----LDHHN---LW--QLENRINEVLAQ---LGLDPDAALSsLSGGWLRKAAL 167
|
170 180
....*....|....*....|..
gi 445942648 150 ARALAQSPSEILLDEPTNHLDI 171
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDI 189
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-194 |
4.46e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 68.27 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQ-DIARMAKKQLARRVACVE-------QH 84
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPALPQPALEyvidgdrEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 GMTEANMRVRDVVRLGR-IPH-HSPFSNWSAQDDEAIAAALQRVAML--EKSEQGWLSLSGGERQRVHIARALAQSPSEI 160
Cdd:PRK10636 92 RQLEAQLHDANERNDGHaIATiHGKLDAIDAWTIRSRAASLLHGLGFsnEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190
....*....|....*....|....*....|....
gi 445942648 161 LLDEPTNHLDIHHQMQLMQLISELPVTSIVAIHD 194
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHD 205
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-224 |
8.03e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 66.75 E-value: 8.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLR----RPDAGRVTLDGQDIARMAKKQLARRVAcveqHGMT----EA 89
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRERRKLVG----HNVSmifqEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 90 NMRVRDVVRLGR-----IPHHSPFSNW----SAQDDEAIAAaLQRVAMleKSEQGWLS-----LSGGERQRVHIARALAQ 155
Cdd:PRK15093 99 QSCLDPSERVGRqlmqnIPGWTYKGRWwqrfGWRKRRAIEL-LHRVGI--KDHKDAMRsfpyeLTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 156 SPSEILLDEPTNHLDIHHQMQLMQLISELPV---TSIVAI-HDLNHAAMFCDSLIVMQQGQILASGTPEEILS 224
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnnTTILLIsHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-195 |
1.38e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 22 SLRVPR-GETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDG--------------QD-IARMAKKQL--ARRVACVEQ 83
Cdd:PRK13409 92 GLPIPKeGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdevlkrfrgtelQNyFKKLYNGEIkvVHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 -----HGmteanmRVRDVVRlgriphhspfsnwsaQDDEA-----IAAALQRVAMLEKSEQgwlSLSGGERQRVHIARAL 153
Cdd:PRK13409 172 ipkvfKG------KVRELLK---------------KVDERgkldeVVERLGLENILDRDIS---ELSGGELQRVAIAAAL 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 445942648 154 AQSPSEILLDEPTNHLDIHHQMQLMQLISELPVTSIVAI--HDL 195
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVveHDL 271
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-222 |
1.57e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.11 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 10 WKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLrvLAGLRRPD--AGRVTLDGQDIARMAKKQLARRVACVEQHGMT 87
Cdd:PTZ00243 1318 YREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLL--LTFMRMVEvcGGEIRVNGREIGAYGLRELRRQFSMIPQDPVL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 eANMRVRDVVrlgriphhSPFSNWSAqddEAIAAALQRVAMLEK--SE---------QGWLSLSGGERQRVHIARALAQS 156
Cdd:PTZ00243 1396 -FDGTVRQNV--------DPFLEASS---AEVWAALELVGLRERvaSEsegidsrvlEGGSNYSVGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 157 PSE-ILLDEPTNHLD--IHHQMQ--LMQLISELPVTSIVaiHDLnHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:PTZ00243 1464 GSGfILMDEATANIDpaLDRQIQatVMSAFSAYTVITIA--HRL-HTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-195 |
2.41e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.96 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 22 SLRVPR-GETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDG--------------QD-IARMAKKQLarRVACVEQH- 84
Cdd:COG1245 92 GLPVPKkGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPswdevlkrfrgtelQDyFKKLANGEI--KVAHKPQYv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 --------GmteanmRVRDVvrLGRIphhspfsnwsaqdDEA-----IAAALQRVAMLEKSEQgwlSLSGGERQRVHIAR 151
Cdd:COG1245 170 dlipkvfkG------TVREL--LEKV-------------DERgkldeLAEKLGLENILDRDIS---ELSGGELQRVAIAA 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 445942648 152 ALAQSPSEILLDEPTNHLDIHHQMQLMQLISEL--PVTSIVAI-HDL 195
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDIYQRLNVARLIRELaeEGKYVLVVeHDL 272
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-227 |
2.49e-12 |
|
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: 66.00 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPD-AGRVTLDGQDIA-RMAKKQLARRVACV----EQHGMTeANM 91
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAGIAMVpedrKRHGIV-PIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 92 RVRDVVRLGRIphhSPFSNWSAQDDEA----IAAALQRVAMleKSEQGWL---SLSGGERQRVHIARALAQSPSEILLDE 164
Cdd:TIGR02633 355 GVGKNITLSVL---KSFCFKMRIDAAAelqiIGSAIQRLKV--KTASPFLpigRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 165 PTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILASG-----TPEEILSEAL 227
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAqegVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFvnhalTQEQVLAAAL 500
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-209 |
4.41e-12 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 62.59 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 25 VPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIArmAKKQlarrvacveqhgmteanmrvrdvvrlgriph 104
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV--YKPQ------------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 105 hspfsnwsaqddeaiaaalqrvamlekseqgWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQ----LMQL 180
Cdd:cd03222 69 -------------------------------YIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNaaraIRRL 117
|
170 180
....*....|....*....|....*....
gi 445942648 181 ISELPVTSIVAIHDLNHAAMFCDSLIVMQ 209
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-170 |
5.95e-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: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 7 NITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAG--LRRPDAGRVTLDGQDIArmakkqlarrvacveqh 84
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFG----------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 85 gmteanmrvRDVVRLGRIPHHSPFsnwsaqddeaiAAALQRVAMLEKSE-QGWLS----LSGGERQRVHIARALAQSPSE 159
Cdd:COG2401 98 ---------REASLIDAIGRKGDF-----------KDAVELLNAVGLSDaVLWLRrfkeLSTGQKFRFRLALLLAERPKL 157
|
170
....*....|.
gi 445942648 160 ILLDEPTNHLD 170
Cdd:COG2401 158 LVIDEFCSHLD 168
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-225 |
9.02e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.58 E-value: 9.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 8 ITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQ---- 83
Cdd:TIGR00957 1292 LRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQdpvl 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 -HGMTEANMrvrdvvrlgriphhSPFSNWSaqdDEAIAAALQrVAMLE------------KSEQGWLSLSGGERQRVHIA 150
Cdd:TIGR00957 1372 fSGSLRMNL--------------DPFSQYS---DEEVWWALE-LAHLKtfvsalpdkldhECAEGGENLSVGQRQLVCLA 1433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 151 RALAQSPSEILLDEPTNHLDIHHQMQLMQLI-SELPVTSIVAI-HDLNhAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:TIGR00957 1434 RALLRKTKILVLDEATAAVDLETDNLIQSTIrTQFEDCTVLTIaHRLN-TIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-229 |
1.04e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.37 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKA-GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDA-GRVTLDGqdiarmakkqlarRV 78
Cdd:PLN03130 615 ISIKNGYFSWDSkAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRG-------------TV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 79 ACVEQHGMTeANMRVRDVVRLGriphhSPFSnwSAQDDEAI-AAALQR-VAML------EKSEQGwLSLSGGERQRVHIA 150
Cdd:PLN03130 682 AYVPQVSWI-FNATVRDNILFG-----SPFD--PERYERAIdVTALQHdLDLLpggdltEIGERG-VNISGGQKQRVSMA 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 151 RALAQSPSEILLDEPTNHLDIHHQMQLMQ--LISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALL 228
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPL 832
|
.
gi 445942648 229 W 229
Cdd:PLN03130 833 F 833
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-171 |
1.78e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.79 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 3 ICAENITWKAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKkqlARRVACVE 82
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR---SRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 83 QHGMTEANMRVRDVVRL-----GRIPHHSPFSnwsaqddeaiaaALQRVAMLEKSEQGWLSLSGGERQRVHIARaLAQSP 157
Cdd:PRK13543 89 HLPGLKADLSTLENLHFlcglhGRRAKQMPGS------------ALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSP 155
|
170
....*....|....*
gi 445942648 158 SEI-LLDEPTNHLDI 171
Cdd:PRK13543 156 APLwLLDEPYANLDL 170
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-66 |
2.86e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 62.89 E-value: 2.86e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 445942648 21 VSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDI 66
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-227 |
3.12e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 5 AENIT-W---KAGKKvIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRrPDA--GRVTLDGQDIA-RMAKKQLARR 77
Cdd:PRK13549 262 VRNLTaWdpvNPHIK-RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGEIFIDGKPVKiRNPQQAIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 78 VACV----EQHGMTEAnMRVRDVVRLGRIPHhspFSNWSAQDDEA----IAAALQRVAMLEKS-EQGWLSLSGGERQRVH 148
Cdd:PRK13549 340 IAMVpedrKRDGIVPV-MGVGKNITLAALDR---FTGGSRIDDAAelktILESIQRLKVKTASpELAIARLSGGNQQKAV 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 149 IARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQILAS-----GTPE 220
Cdd:PRK13549 416 LAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVqqgVAIIVISSELPEVLGLSDRVLVMHEGKLKGDlinhnLTQE 495
|
....*..
gi 445942648 221 EILSEAL 227
Cdd:PRK13549 496 QVMEAAL 502
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-227 |
3.83e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 22 SLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTE--------ANMRV 93
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDmlspgeddTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 94 RDVVRLGripHHSPfsnwsaQDDEAIAAALQRVAMLEKSeqgWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHH 173
Cdd:PRK10938 103 AEIIQDE---VKDP------ARCEQLAQQFGITALLDRR---FKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 174 QMQLMQLISELPVTSIVAIHDLNHaamFCDSLIVMQQGQILA------SGTPEEILSEAL 227
Cdd:PRK10938 171 RQQLAELLASLHQSGITLVLVLNR---FDEIPDFVQFAGVLAdctlaeTGEREEILQQAL 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-229 |
4.31e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 1 MSICAENITWKAG-KKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAG-LRRPDAGRVTLDGQdiarmakkqlarrV 78
Cdd:PLN03232 615 ISIKNGYFSWDSKtSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS-------------V 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 79 ACVEQHGMTeANMRVRDVVRLGRipHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQG--WLSLSGGERQRVHIARALAQS 156
Cdd:PLN03232 682 AYVPQVSWI-FNATVRENILFGS--DFESERYWRAIDVTALQHDLDLLPGRDLTEIGerGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 157 PSEILLDEPTNHLDIH--HQMQLMQLISELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEALLW 229
Cdd:PLN03232 759 SDIYIFDDPLSALDAHvaHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLF 833
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-244 |
1.17e-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: 61.46 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 6 ENITWK--AGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDaGRVTLDGQDIARMAKKQLARRVACVEQ 83
Cdd:TIGR01271 1221 QGLTAKytEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 H-----GMTEANMrvrdvvrlgriphhSPFSNWSAQDDEAIAAALQRVAMLEKS--------EQGWLSLSGGERQRVHIA 150
Cdd:TIGR01271 1300 KvfifsGTFRKNL--------------DPYEQWSDEEIWKVAEEVGLKSVIEQFpdkldfvlVDGGYVLSNGHKQLMCLA 1365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 151 RALAQSPSEILLDEPTNHLD-IHHQM---QLMQLISElpVTSIVAIHDLnHAAMFCDSLIVMQQGQILASGTPEEILSEA 226
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDpVTLQIirkTLKQSFSN--CTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLLNET 1442
|
250
....*....|....*....
gi 445942648 227 -LLWDVFRVKTKIEISPYH 244
Cdd:TIGR01271 1443 sLFKQAMSAADRLKLFPLH 1461
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-248 |
1.31e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.03 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTldgqdiaRMAKKqlarRVACVEQHGMTEANMR 92
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-------RSAKV----RMAVFSQHHVDGLDLS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 VRDVVRLGRIPHHSPfsnwsaqdDEAIAAALQRVAMLEK-SEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDI 171
Cdd:PLN03073 589 SNPLLYMMRCFPGVP--------EQKLRAHLGSFGVTGNlALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 172 HHQMQLMQLIselpvtsivaihdlnhaAMFCDSLIVMQQGQILASGTPEEilsealLWdvfrVKTKIEISPYHGKKH 248
Cdd:PLN03073 661 DAVEALIQGL-----------------VLFQGGVLMVSHDEHLISGSVDE------LW----VVSEGKVTPFHGTFH 710
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
15-184 |
1.41e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 15 KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIAR---MAKKQ-------------LARRV 78
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlcTYQKQlcfvghrsginpyLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 79 ACVEQHGMTEANMRVRDVVRLGRIPHHSPFsnwsaqddeaiAAALqrvamlekseqgwlsLSGGERQRVHIARALAQSPS 158
Cdd:PRK13540 94 NCLYDIHFSPGAVGITELCRLFSLEHLIDY-----------PCGL---------------LSSGQKRQVALLRLWMSKAK 147
|
170 180
....*....|....*....|....*.
gi 445942648 159 EILLDEPTNHLDihhQMQLMQLISEL 184
Cdd:PRK13540 148 LWLLDEPLVALD---ELSLLTIITKI 170
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-226 |
1.63e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.50 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 15 KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARRVACVEQHGMTEANMrVR 94
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDT-VA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 95 DVVRLGRiphhspfsnwsaqdDEAIAAALQRVAML----------------EKSEQGwLSLSGGERQRVHIARALAQSPS 158
Cdd:PRK10789 407 NNIALGR--------------PDATQQEIEHVARLasvhddilrlpqgydtEVGERG-VMLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 159 EILLDEPTNHLDIHHQMQLMQLISEL--PVTSIVAIHDLNhAAMFCDSLIVMQQGQILASGTPEEILSEA 226
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWgeGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-227 |
2.60e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.18 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 15 KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVtldgqdiarmakkQLARRVACVEQHG--MT----- 87
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAwiMNatvrg 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 -------EANMRVRDVVRLGRIphhspfsnwsaqddEAIAAALQRVAMLEKSEQGwLSLSGGERQRVHIARALAQSPSEI 160
Cdd:PTZ00243 740 nilffdeEDAARLADAVRVSQL--------------EADLAQLGGGLETEIGEKG-VNLSGGQKARVSLARAVYANRDVY 804
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 161 LLDEPTNHLDIHHQMQLMQ--LISELP-VTSIVAIHDLnHAAMFCDSLIVMQQGQILASGTPEEILSEAL 227
Cdd:PTZ00243 805 LLDDPLSALDAHVGERVVEecFLGALAgKTRVLATHQV-HVVPRADYVVALGDGRVEFSGSSADFMRTSL 873
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-225 |
2.87e-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: 60.31 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGqdiarmakkqlarRVACVEQ------------- 83
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQtswimpgtikdni 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 -HGMTEANMRVRDVVRLGRIphhspfsnwsaQDDEAIAAALQRVAMLEkseqGWLSLSGGERQRVHIARALAQSPSEILL 162
Cdd:TIGR01271 508 iFGLSYDEYRYTSVIKACQL-----------EEDIALFPEKDKTVLGE----GGITLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 163 DEPTNHLDIHHQMQLMQ-LISELPV--TSIVAIHDLNHAAMfCDSLIVMQQGQILASGTPEEILSE 225
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFEsCLCKLMSnkTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAK 637
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-220 |
8.47e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGlrRPD----AGRVTLDGQDIARMAKKQLARR---VAC---VEQHGM 86
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAHLgifLAFqypIEIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 87 TEAnmrvrDVVRLGRIPHHSpFSNWSAQDD----EAIAAALQRVAMleksEQGWLS------LSGGERQRVHIARaLAQS 156
Cdd:CHL00131 100 SNA-----DFLRLAYNSKRK-FQGLPELDPleflEIINEKLKLVGM----DPSFLSrnvnegFSGGEKKRNEILQ-MALL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445942648 157 PSEI-LLDEPTNHLDIHHQMQLMQLISEL--PVTSIVAIhdlNHAAMFCDSLI-----VMQQGQILASGTPE 220
Cdd:CHL00131 169 DSELaILDETDSGLDIDALKIIAEGINKLmtSENSIILI---THYQRLLDYIKpdyvhVMQNGKIIKTGDAE 237
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-225 |
9.10e-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: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDaGRVTLDGQDIARMAKKQLARRVACVEQH-----GMT 87
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKvfifsGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 EANMrvrdvvrlgriphhSPFSNWSaqdDEAIAAALQRVAMLEKSEQ-----------GWLSLSGGERQRVHIARALAQS 156
Cdd:cd03289 94 RKNL--------------DPYGKWS---DEEIWKVAEEVGLKSVIEQfpgqldfvlvdGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 157 PSEILLDEPTNHLD-IHHQM---QLMQLISElpVTSIVAIHDLnHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:cd03289 157 AKILLLDEPSAHLDpITYQVirkTLKQAFAD--CTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
15-225 |
1.56e-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: 56.84 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 15 KVIVNNVSLRVPRGETVGLLGPNGCGKSSLlrVLAGLRRPDA--GRVTLDGQDIARMAKKQLARRVACVEQHGMTEANmr 92
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIfdGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSG-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 93 vrdVVRLGRIPHHSpfsnwsAQDD---EAIAAAlqRVAMLEKSEQGWL---------SLSGGERQRVHIARALAQSPSEI 160
Cdd:cd03288 110 ---SIRFNLDPECK------CTDDrlwEALEIA--QLKNMVKSLPGGLdavvteggeNFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942648 161 LLDEPTNHLDIHHQMQLMQLI-SELPVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSE 225
Cdd:cd03288 179 IMDEATASIDMATENILQKVVmTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-211 |
2.37e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 11 KAGKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGlrRPDAGRVTlDGQDIARMAKKQ--LARRVACVEQHGMTE 88
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVIT-GGDRLVNGRPLDssFQRSIGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 89 ANMRVRDVVRLG---RIPHHSPFSNWSAQDDEAIaaalqRVAMLEKSEQGWLSLSGG-----ERQRVHIARALAQSPSEI 160
Cdd:TIGR00956 849 PTSTVRESLRFSaylRQPKSVSKSEKMEYVEEVI-----KLLEMESYADAVVGVPGEglnveQRKRLTIGVELVAKPKLL 923
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 161 L-LDEPTNHLDIHHQMQLMQLISELPVT--SIV-AIHDLNhAAMFC--DSLIVMQQG 211
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKLADHgqAILcTIHQPS-AILFEefDRLLLLQKG 979
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-225 |
2.44e-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: 56.40 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGqdiarmakkqlarRVACVEQ------------- 83
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQfswimpgtikeni 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 -HGMTEANMRVRDVVRLGRIphHSPFSNWSAQDDEAIAaalqrvamlekseQGWLSLSGGERQRVHIARALAQSPSEILL 162
Cdd:cd03291 119 iFGVSYDEYRYKSVVKACQL--EEDITKFPEKDNTVLG-------------EGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445942648 163 DEPTNHLDIHHQMQ--------LMQLISELPVTSivAIHDLNHAamfcDSLIVMQQGQILASGTPEEILSE 225
Cdd:cd03291 184 DSPFGYLDVFTEKEifescvckLMANKTRILVTS--KMEHLKKA----DKILILHEGSSYFYGTFSELQSL 248
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
138-219 |
8.73e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.54 E-value: 8.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 138 SLSGGERQRVHIARALA-QSPSEIL--LDEPTNHL---DIHHQMQLMQLISELPVTSIVAIHDLnHAAMFCDSLIVM--- 208
Cdd:cd03271 169 TLSGGEAQRIKLAKELSkRSTGKTLyiLDEPTTGLhfhDVKKLLEVLQRLVDKGNTVVVIEHNL-DVIKCADWIIDLgpe 247
|
90
....*....|....
gi 445942648 209 ---QQGQILASGTP 219
Cdd:cd03271 248 ggdGGGQVVASGTP 261
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-229 |
1.48e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIA-RMAKKQLARRVACVeqhgmTEANmRVRDV 96
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnHNANEAINHGFALV-----TEER-RSTGI 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 97 VRLGRIPHHSPFSN-------WSAQDDEAIAAALQRV--AMLEK--SEQGWL-SLSGGERQRVHIARALAQSPSEILLDE 164
Cdd:PRK10982 338 YAYLDIGFNSLISNirnyknkVGLLDNSRMKSDTQWVidSMRVKtpGHRTQIgSLSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942648 165 PTNHLDIHHQMQLMQLISELPVTS---IVAIHDLNHAAMFCDSLIVMQQGQI-----LASGTPEEILSEALLW 229
Cdd:PRK10982 418 PTRGIDVGAKFEIYQLIAELAKKDkgiIIISSEMPELLGITDRILVMSNGLVagivdTKTTTQNEILRLASLH 490
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-212 |
2.18e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 19 NNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLrRPDA---GRVTLDGQ-----DIarmaKKQLARRVACVEQHGMTEAN 90
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDGEvcrfkDI----RDSEALGIVIIHQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 91 MRVRDVVRLGRIPHHSPFSNWSAQDDEAiAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLD 170
Cdd:NF040905 93 LSIAENIFLGNERAKRGVIDWNETNRRA-RELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 445942648 171 IHHQMQLMQLISELP---VTSIVAIHDLNHAAMFCDSLIVMQQGQ 212
Cdd:NF040905 172 EEDSAALLDLLLELKaqgITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-242 |
2.83e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.25 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIArMAKKQLARRVACVEQHGMTEANMRVRD-- 95
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISDVHQNMGYCPQFDAIDDLLTGREhl 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 96 --VVRLGRIPHHS--PFSNWSAQDdEAIAAALQRVAMlekseqgwlSLSGGERQRVHIARALAQSPSEILLDEPTNHLDI 171
Cdd:TIGR01257 2034 ylYARLRGVPAEEieKVANWSIQS-LGLSLYADRLAG---------TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942648 172 HHQMQL----MQLISELPVTsIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEILSEalLWDVFRVKTKIEiSP 242
Cdd:TIGR01257 2104 QARRMLwntiVSIIREGRAV-VLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK--FGDGYIVTMKIK-SP 2174
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
13-222 |
3.35e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.59 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCG--KSSLLRVLAGlrrPDAGRVTLdgQDIARMAKKQLARRVACVE---QHGMT 87
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPW--RF*TWCANRRALRRTIG*HrpvR*GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 88 EANMRVRDVVRLGRiphhspFSNWSAQDDEAIA-AALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPT 166
Cdd:NF000106 99 ESFSGRENLYMIGR------*LDLSRKDARARAdELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 167 NHLDIHHQMQLMQLISEL---PVTSIVAIHDLNHAAMFCDSLIVMQQGQILASGTPEEI 222
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMvrdGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
10-63 |
5.05e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.36 E-value: 5.05e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 10 WKAGKKVI---VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDG 63
Cdd:PRK13545 29 FRSKDGEYhyaLNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-224 |
6.91e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 55 DAGRVTLDGQDIARMAKKQLARRVACVEQHGMTeANMRVRDVVRLGR-------IPHHSPFsnwsAQDDEAIAAALQR-- 125
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFGKedatredVKRACKF----AAIDEFIESLPNKyd 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 126 --VAMLEKSeqgwlsLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELPVTSIVAIHDLNH---AAM 200
Cdd:PTZ00265 1350 tnVGPYGKS------LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHriaSIK 1423
|
170 180
....*....|....*....|....*....
gi 445942648 201 FCDSLIVMQQGQ-----ILASGTPEEILS 224
Cdd:PTZ00265 1424 RSDKIVVFNNPDrtgsfVQAHGTHEELLS 1452
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
139-222 |
1.33e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 51.95 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 139 LSGGERQRVHIARALAQSPSE---ILLDEPTNHL---DIHHqmqLMQLISELpVT---SIVAI-HDLN--HAAmfcDSLI 206
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTGktlYILDEPTTGLhfhDIRK---LLEVLHRL-VDkgnTVVVIeHNLDviKTA---DWII 899
|
90 100
....*....|....*....|..
gi 445942648 207 VM------QQGQILASGTPEEI 222
Cdd:COG0178 900 DLgpeggdGGGEIVAEGTPEEV 921
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-222 |
1.56e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.94 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 138 SLSGGERQRVHIARAL---AQSPSEILLDEPTNHL---DIHHQMQLMQLISELPVTSIVAIHDLnHAAMFCDSLIVM--- 208
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfdDIKKLLEVLQRLVDKGNTVVVIEHNL-DVIKTADYIIDLgpe 907
|
90
....*....|....*..
gi 445942648 209 ---QQGQILASGTPEEI 222
Cdd:TIGR00630 908 ggdGGGTVVASGTPEEV 924
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-233 |
2.04e-07 |
|
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: 49.29 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 27 RGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRvtldgqdiarmakkqlarrvacveqhgmteanmrvrdVVRLgriphhs 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG-------------------------------------VIYI------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 107 pfsnwsaqDDEAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELpv 186
Cdd:smart00382 37 --------DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELR-- 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 445942648 187 tsivaihdlnhaamFCDSLIVMQQGQILASGTPEEILSEALLWDVFR 233
Cdd:smart00382 107 --------------LLLLLKSEKNLTVILTTNDEKDLGPALLRRRFD 139
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-224 |
3.24e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.98 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 138 SLSGGERQRVHIARAL---AQSPSEILLDEPTNHL---DIHHQMQLMQLISELPVTSIVAIHDLnHAAMFCDSLIVM--- 208
Cdd:PRK00635 809 SLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYVLELgpe 887
|
90
....*....|....*....
gi 445942648 209 ---QQGQILASGTPEEILS 224
Cdd:PRK00635 888 ggnLGGYLLASCSPEELIH 906
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-217 |
6.44e-07 |
|
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: 48.09 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLlrVLAGLRRPDAGRVTLDGQDIAR---MAKKQLARRVAcveqhgmteanmrvr 94
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKARLISFLPKFSRnklIFIDQLQFLID--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 95 dvVRLGRIPHHSPFSnwsaqddeaiaaalqrvamlekseqgwlSLSGGERQRVHIARALAQSP--SEILLDEPTNHLdih 172
Cdd:cd03238 74 --VGLGYLTLGQKLS----------------------------TLSGGELQRVKLASELFSEPpgTLFILDEPSTGL--- 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 173 HQMQLMQLISELP------VTSIVAIHDLnhaAMFC--DSLIVM------QQGQILASG 217
Cdd:cd03238 121 HQQDINQLLEVIKglidlgNTVILIEHNL---DVLSsaDWIIDFgpgsgkSGGKVVFSG 176
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
15-171 |
1.48e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.86 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 15 KVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLR--RPDAGRVTLDGQDIARMAKKQLARRVAC------VEQHGM 86
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFmafqypVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 87 TEANMRVRDVVRLGRIPHHSPFSNWSAQD--DEAIAAALQRVAMLEKSEQgwLSLSGGERQRVHIARALAQSPSEILLDE 164
Cdd:PRK09580 94 SNQFFLQTALNAVRSYRGQEPLDRFDFQDlmEEKIALLKMPEDLLTRSVN--VGFSGGEKKRNDILQMAVLEPELCILDE 171
|
....*..
gi 445942648 165 PTNHLDI 171
Cdd:PRK09580 172 SDSGLDI 178
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
139-222 |
2.04e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.53 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 139 LSGGERQRVHIARALAQSP---SEILLDEPTNHL---DIHHQMQLMQLISELPVTSIVAIHDL----NhaamfCDSLIVM 208
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDIRKLLEVLHRLVDKGNTVVVIEHNLdvikT-----ADWIIDL 905
|
90 100
....*....|....*....|
gi 445942648 209 ------QQGQILASGTPEEI 222
Cdd:PRK00349 906 gpeggdGGGEIVATGTPEEV 925
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-170 |
2.10e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 13 GKKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGlRRPD--AGRVTLDGQ---------DIAR-----MAKKQLAR 76
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgySNDLTLFGRrrgsgetiwDIKKhigyvSSSLHLDY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 77 RVACveqhgmteanmRVRDVVRLGripHHSPFSNWSAQDDEAIAAALQRVAML----EKSEQGWLSLSGGERQRVHIARA 152
Cdd:PRK10938 350 RVST-----------SVRNVILSG---FFDSIGIYQAVSDRQQKLAQQWLDILgidkRTADAPFHSLSWGQQRLALIVRA 415
|
170
....*....|....*...
gi 445942648 153 LAQSPSEILLDEPTNHLD 170
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLD 433
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-191 |
2.18e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 17 IVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTL-DGQDIARMAKKQLARRVACVEQHGM--------- 86
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLlfsnsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 87 ------------------------TEANMRVRDVVRLGRIPHHSPFS-------------NWSAQDDEAIAAALQRV--- 126
Cdd:PTZ00265 480 ikyslyslkdlealsnyynedgndSQENKNKRNSCRAKCAGDLNDMSnttdsneliemrkNYQTIKDSEVVDVSKKVlih 559
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445942648 127 ----AMLEKSE----QGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLISELP-----VTSIVA 191
Cdd:PTZ00265 560 dfvsALPDKYEtlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnenrITIIIA 637
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-217 |
2.25e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 14 KKVIVNNVSLRVPRGETVGLLGPNGCGKSSLLRVLA----GLRRPDAGRVTLDGQDIARMaKKQLARRVACVEQHGMTEA 89
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 90 NMRVRD----VVRLgRIPHHSPfsnwSAQDDEAIAAALQRVAMlekSEQGwLS--------------LSGGERQRVHIAR 151
Cdd:TIGR00956 152 HLTVGEtldfAARC-KTPQNRP----DGVSREEYAKHIADVYM---ATYG-LShtrntkvgndfvrgVSGGERKRVSIAE 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445942648 152 ALAQSPSEILLDEPTNHLDIHHQMQ----LMQLISELPVTSIVAIHDLNHAA--MFcDSLIVMQQGQILASG 217
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEfiraLKTSANILDTTPLVAIYQCSQDAyeLF-DKVIVLYEGYQIYFG 293
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-240 |
2.95e-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: 48.09 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 138 SLSGGERQRVHIARALAQSPSEIL--LDEPTNHLdihHQMQLMQLISELPV------TSIVAIHD---LNHAamfcDSLI 206
Cdd:TIGR00630 488 TLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGL---HQRDNRRLINTLKRlrdlgnTLIVVEHDedtIRAA----DYVI 560
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 445942648 207 VM------QQGQILASGTPEEIL--SEALLWDVFRVKTKIEI 240
Cdd:TIGR00630 561 DIgpgageHGGEVVASGTPEEILanPDSLTGQYLSGRKKIEV 602
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-181 |
1.19e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 35 GPNGCGKSSLLRVLAGLRRPDAGRVTLDGQDIARMAKKQLARrvacVEQHGMTEANMRVRDVVRLgriphhspfsnWSAQ 114
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTY----IGHNLGLKLEMTVFENLKF-----------WSEI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445942648 115 DD--EAIAAALQRVAMLEKSEQGWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLI 181
Cdd:PRK13541 98 YNsaETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
35-188 |
1.30e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.62 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 35 GPNGCGKSSLLR----VLAGlrrpDAGRVTLDGQDIARMAKKQ---------------LARRVACVEQHGMTEANMRVRD 95
Cdd:COG0419 30 GPNGAGKSTILEairyALYG----KARSRSKLRSDLINVGSEEasvelefehggkryrIERRQGEFAEFLEAKPSERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 96 VVRLGRIPHHSPFSNWSAQDDEAIAAALQRVAMLEKSEQGWLS----------LSGGERQRVHIARALaqspsEILLDep 165
Cdd:COG0419 106 LKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAqlsgldpietLSGGERLRLALADLL-----SLILD-- 178
|
170 180
....*....|....*....|...
gi 445942648 166 TNHLDIHHQMQLMQLISELPVTS 188
Cdd:COG0419 179 FGSLDEERLERLLDALEELAIIT 201
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
117-240 |
2.02e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.59 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 117 EAIAAALQRVAMLEKSEQGWLS-------LSGGERQRVHIARALAQSPSEI--LLDEPTNHL---DIHHQMQLMQLISEL 184
Cdd:PRK00635 448 EVLQGLKSRLSILIDLGLPYLTperalatLSGGEQERTALAKHLGAELIGItyILDEPSIGLhpqDTHKLINVIKKLRDQ 527
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942648 185 PVTSIVAIHDlNHAAMFCDSLIVMQQ------GQILASGTPEEIL--SEALLWDVFRVKTKIEI 240
Cdd:PRK00635 528 GNTVLLVEHD-EQMISLADRIIDIGPgagifgGEVLFNGSPREFLakSDSLTAKYLRQELTIPI 590
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
28-218 |
6.31e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 28 GETVGLLGPNGCGKSSLLRVLAGlrRPDAGRVTLDGQdIARMAKKQ--LARRVACVEQHGMTEANMRVRDVVRLG---RI 102
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-ISGFPKKQetFARISGYCEQNDIHSPQVTVRESLIYSaflRL 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 103 PHHSpfsnwSAQDDEAIAAALQRVAMLEKSEQ------GWLSLSGGERQRVHIARALAQSPSEILLDEPTNHLDIHHQMQ 176
Cdd:PLN03140 983 PKEV-----SKEEKMMFVDEVMELVELDNLKDaivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1057
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 445942648 177 LMQLIS---ELPVTSIVAIH----DLNHAAmfcDSLIVMQQ-GQILASGT 218
Cdd:PLN03140 1058 VMRTVRntvDTGRTVVCTIHqpsiDIFEAF---DELLLMKRgGQVIYSGP 1104
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
139-201 |
3.52e-04 |
|
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: 40.04 E-value: 3.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 139 LSGGERQRVHIARALA----QSPSEILLDEPTNHLDIHHQMQLMQLISELPV---TSIVAIHDLNHAAMF 201
Cdd:cd03227 78 LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVkgaQVIVITHLPELAELA 147
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-224 |
4.51e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 134 QGWLSLSGGERQRVHIARALAQSPSE---ILLDEPTNHLDIHHQMQLMQLISELPVT--SIVAI-HD---LNHAamfcDS 204
Cdd:PRK00635 1695 QNLSSLSLSEKIAIKIAKFLYLPPKHptlFLLDEIATSLDNQQKSALLVQLRTLVSLghSVIYIdHDpalLKQA----DY 1770
|
90 100
....*....|....*....|....*.
gi 445942648 205 LIVM------QQGQILASGTPEEILS 224
Cdd:PRK00635 1771 LIEMgpgsgkTGGKILFSGPPKDISA 1796
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-64 |
6.83e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 6.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 445942648 18 VNNVSLRVPRGETVGLLGPNGCGKSSLLRVLAGLRRPDAGRVTLDGQ 64
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE 86
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
14-184 |
1.02e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.60 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 14 KKVIVNN------VSLRVPRGETVgLLGPNGCGKSSLLRVLAGLRRPDAGRvTLDGQD---------------------- 65
Cdd:COG3593 4 EKIKIKNfrsikdLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSR-KFDEEDfylgddpdlpeieieltfgsll 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 66 -------IARMAKKQLARRVACVEQH---GMTEANMRVRDVVRLGRIPHHSPFSNwSAQDDEAIAAALQrvAMLEKSEQG 135
Cdd:COG3593 82 srllrllLKEEDKEELEEALEELNEElkeALKALNELLSEYLKELLDGLDLELEL-SLDELEDLLKSLS--LRIEDGKEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 445942648 136 WLSLSG-GERQRVHIA--RALAQSPSE-----ILLDEPTNHLDIHHQMQLMQLISEL 184
Cdd:COG3593 159 PLDRLGsGFQRLILLAllSALAELKRApanpiLLIEEPEAHLHPQAQRRLLKLLKEL 215
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
134-181 |
2.83e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.73 E-value: 2.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 445942648 134 QGWLSLSGGERQ------RVHIARALAQSPSEILLDEPTNHLDIHHQMQLMQLI 181
Cdd:PRK01156 797 EGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDII 850
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
20-193 |
3.34e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.06 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 20 NVSLRVPRGETVgLLGPNGCGKSSLLRVLA-GLRRPDAGRVTLDGQDIARMAKKQLARRVACV---------------EQ 83
Cdd:COG3950 18 EIDFDNPPRLTV-LVGENGSGKTTLLEAIAlALSGLLSRLDDVKFRKLLIRNGEFGDSAKLILyygtsrllldgplkkLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 84 HGMTEANMRVRDVVR-LGRIPHHSPFSNW--------SAQDDEAIAAALQRV-----AMLE-------KSEQGWL----- 137
Cdd:COG3950 97 RLKEEYFSRLDGYDSlLDEDSNLREFLEWlreyledlENKLSDELDEKLEAVrealnKLLPdfkdiriDRDPGRLvildk 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 138 --------SLSGGERQRV----HIARALAQSPSE----------ILLDEPTNHLDIHHQMQLMQ-LISELP-VTSIVAIH 193
Cdd:COG3950 177 ngeelplnQLSDGERSLLalvgDLARRLAELNPAlenplegegiVLIDEIDLHLHPKWQRRILPdLRKIFPnIQFIVTTH 256
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
25-127 |
4.29e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 37.36 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942648 25 VPRGETVGLLGPNGCGKSSLLRVLA-----------GLRRPDAGRVTL----DGQDiarmakkQLARRVACVEQHGMTEA 89
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLAaavatgkpwlgGPRVPEQGKVLYvsaeGPAD-------ELRRRLRAAGADLDLPA 102
|
90 100 110
....*....|....*....|....*....|....*...
gi 445942648 90 NMRVRDVVRLGRIPHHSPFSNWSAQDDEAIAAALQRVA 127
Cdd:pfam13481 103 RLLFLSLVESLPLFFLDRGGPLLDADVDALEAALEEVE 140
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
138-194 |
5.51e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 37.24 E-value: 5.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445942648 138 SLSGGERQRVHIARALAQSPSEIL--LDEPTNHL---DIHHQMQLMQLISELPVTSIVAIHD 194
Cdd:cd03270 137 TLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLhprDNDRLIETLKRLRDLGNTVLVVEHD 198
|
|
| |
