|
Name |
Accession |
Description |
Interval |
E-value |
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-252 |
0e+00 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 498.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSIL 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVADLVAFGRYPYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 161 EPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEALKDIYDMDINVH 240
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEVE 240
|
250
....*....|..
gi 351592836 241 EIGGHRVSLFYD 252
Cdd:COG4604 241 EIDGKRICVYFR 252
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-250 |
4.60e-104 |
|
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: 301.96 E-value: 4.60e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSIL 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVADLVAFGRYPYSK--GRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGlfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 159 LDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEALKDIYDMDIN 238
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
250
....*....|....
gi 351592836 239 V--HEIGGHRVSLF 250
Cdd:COG1120 241 VieDPVTGRPLVLP 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-240 |
4.59e-86 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 256.48 E-value: 4.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSIL 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQdNHMTAR-LTVADLVAFGRYPYSK--GRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYV 157
Cdd:PRK11231 82 PQ-HHLTPEgITVRELVAYGRSPWLSlwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 158 LLDEPLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEALKDIYDMDI 237
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEA 239
|
...
gi 351592836 238 NVH 240
Cdd:PRK11231 240 EIH 242
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-218 |
3.63e-70 |
|
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: 213.07 E-value: 3.63e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 11 YGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQdnhmtarl 90
Cdd:cd03214 9 YGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 tvadlvafgrypyskgrltiedkahidqSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKH 170
Cdd:cd03214 81 ----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 351592836 171 AMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:cd03214 133 QIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-241 |
1.68e-66 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 206.55 E-value: 1.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSIL 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVADLVAFGRYPYSKGRltIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQ------DT 154
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPHGLSR--AEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 155 DYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEALKDIYD 234
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYG 239
|
....*..
gi 351592836 235 MDINVHE 241
Cdd:PRK13548 240 ADVLVQP 246
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-245 |
1.23e-62 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 196.88 E-value: 1.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSIL 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVADLVAFGRYPYskGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQ---DTD-- 155
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPH--GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwePVDgg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 156 --YVLLDEPLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEALKDIY 233
Cdd:COG4559 159 prWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
250
....*....|....
gi 351592836 234 DMDINV--HEIGGH 245
Cdd:COG4559 238 GADLRVlaHPEGGC 251
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-241 |
9.09e-62 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 194.15 E-value: 9.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 11 YGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIvsrLLGM---DAGSVTVDGLDVSNTPSDV--LARRLSIlrqDNH 85
Cdd:COG1121 16 YGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKA---ILGLlppTSGTVRLFGKPPRRARRRIgyVPQRAEV---DWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 86 MtaRLTVADLVAFGRYPYSK--GRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPL 163
Cdd:COG1121 90 F--PITVRDVVLMGRYGRRGlfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 164 NNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMkNGRVIRHGTKNDIITPEALKDIYDMDINVHE 241
Cdd:COG1121 168 AGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRAYGGPVALLA 243
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-251 |
3.61e-60 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 190.77 E-value: 3.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 20 VSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARLTVADLVAFG 99
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 100 RYPY--SKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKL 177
Cdd:PRK10575 110 RYPWhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAL 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 178 MQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEALKDIYD--MDINVHEIGGHRVSLFY 251
Cdd:PRK10575 190 VHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGipMGILPHPAGAAPVSFVY 265
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-235 |
1.43e-57 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 184.03 E-value: 1.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 11 YGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARL 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 TVADLVAFGRYPYSK--GRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDM 168
Cdd:PRK10253 97 TVQELVARGRYPHQPlfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 169 KHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEALKDIYDM 235
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGL 243
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-218 |
1.06e-55 |
|
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: 177.73 E-value: 1.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 11 YGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDV--LARRLSILRqdnhmTA 88
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIgyVPQRRSIDR-----DF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 89 RLTVADLVAFGRYPYSK--GRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNL 166
Cdd:cd03235 84 PISVRDVVLMGLYGHKGlfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 351592836 167 DMKHAMGMMKLMQRAcHELGKTVVLVLHDINFASWYSDYIIAMkNGRVIRHG 218
Cdd:cd03235 164 DPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-245 |
3.87e-53 |
|
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: 171.96 E-value: 3.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLaRRLSIL 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVADLVAFgrypYSK--GRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:COG4555 80 PDERGLYDRLTVRENIRY----FAElyGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 159 LDEPLNNLDMKHAMGMMKLMqRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEALKDIYdmDIN 238
Cdd:COG4555 156 LDEPTNGLDVMARRLLREIL-RALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLE--DAF 232
|
....*..
gi 351592836 239 VHEIGGH 245
Cdd:COG4555 233 VALIGSE 239
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-218 |
5.87e-53 |
|
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: 170.39 E-value: 5.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPsdVLARRLSILRQDNH 85
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP--PERRNIGMVFQDYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 86 MTARLTVADLVAFGRYPYSKGRLTIEDKAHidQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNN 165
Cdd:cd03259 83 LFPHLTVAENIAFGLKLRGVPKAEIRARVR--ELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 351592836 166 LDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-233 |
3.89e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 169.09 E-value: 3.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLaRRLSILR 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 QDNHMTARLTVAD-LVAFGRYpysKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:COG1131 80 QEPALYPDLTVREnLRFFARL---YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351592836 161 EPLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITpEALKDIY 233
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA-RLLEDVF 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-213 |
9.94e-51 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 164.95 E-value: 9.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQD-NHMTARL 90
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNpDDQFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 TVADLVAFGryPYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKH 170
Cdd:cd03225 92 TVEEEVAFG--LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 351592836 171 AMGMMKLMQRAcHELGKTVVLVLHDINFASWYSDYIIAMKNGR 213
Cdd:cd03225 170 RRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-231 |
1.38e-50 |
|
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: 164.81 E-value: 1.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 9 KYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQD-NHMT 87
Cdd:COG1122 9 SYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNpDDQL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 88 ARLTVADLVAFGryPYSKGrLTIED-KAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNL 166
Cdd:COG1122 89 FAPTVEEDVAFG--PENLG-LPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 167 DMKHAMGMMKLMQRAcHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT-PEALKD 231
Cdd:COG1122 166 DPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSdYELLEE 230
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
8-236 |
9.09e-49 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 160.99 E-value: 9.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLA---RRLSILRQDN 84
Cdd:COG3638 10 KRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrRRIGMIFQQF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 HMTARLTVADLVAFGRYPYSK------GRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:COG3638 90 NLVPRLSVLTNVLAGRLGRTStwrsllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLIL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 159 LDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDiITPEALKDIYDMD 236
Cdd:COG3638 170 ADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE-LTDAVLREIYGGE 246
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-234 |
2.46e-48 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 164.24 E-value: 2.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSIL 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVADLVAFGRYPYSK--GRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSrfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 159 LDEPLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEALKDIYD 234
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFD 237
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-233 |
5.71e-47 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 156.19 E-value: 5.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLA---RRLSILRQDN 84
Cdd:cd03256 8 KTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQIGMIFQQF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 HMTARLTVADLVAFGRYPYSK------GRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:cd03256 88 NLIERLSVLENVLSGRLGRRStwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 159 LDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDiITPEALKDIY 233
Cdd:cd03256 168 ADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVLDEIY 241
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-232 |
1.14e-46 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 154.91 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIelPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDvlARRLSIL 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPLRFDLTI--AAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVADLVAFGRYPysKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRP--GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 161 EPLNNLD--MKHamGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDII---TPEALKDI 232
Cdd:COG3840 155 EPFSALDpaLRQ--EMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLdgePPPALAAY 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
2.59e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.05 E-value: 2.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYG----ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARr 76
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 77 lsiLR--------QDNHMTARLTVADLVAFGRYPysKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAM 148
Cdd:COG1136 83 ---LRrrhigfvfQFFNLLPELTALENVALPLLL--AGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 149 VLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASwYSDYIIAMKNGRVIR 216
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
5.82e-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: 152.64 E-value: 5.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYG----ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLA--- 74
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 75 -RRLSILRQDNHMTARLTVADLVAFGRYPYSKGRLTIEDKAHidQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQD 153
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAE--ELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 154 TDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASwYSDYIIAMKNGRV 214
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-234 |
9.38e-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: 153.22 E-value: 9.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGE-TAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVL---ARR 76
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 77 LSILRQDNHMTARLTVADLVAFGRYPYSK------GRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVL 150
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKPtwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 151 CQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDiITPEALK 230
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE-LDDEVLR 239
|
....
gi 351592836 231 DIYD 234
Cdd:TIGR02315 240 HIYG 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-228 |
2.06e-44 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 149.51 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 4 TSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRlSILR-- 81
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARL-GIGRtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 QDNHMTARLTVADLV-----AFGRYPYSKGRLTIEDKAH---IDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQD 153
Cdd:cd03219 82 QIPRLFPELTVLENVmvaaqARTGSGLLLARARREEREArerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 154 TDYVLLDEPLNNLDMKHAMGMMKLMQRAcHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEA 228
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-200 |
5.34e-43 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 144.30 E-value: 5.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 11 YGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvsntpsdvlARRLSILRQDNHMTARL 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 --TVADLVAFGRYPY--SKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNL 166
Cdd:NF040873 71 plTVRDLVAMGRWARrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|....
gi 351592836 167 DMKHAMGMMKLMQRACHElGKTVVLVLHDINFAS 200
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-225 |
4.75e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 149.67 E-value: 4.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYY-----GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDV---LARRL 77
Cdd:COG1123 265 NLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreLRRRV 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 78 SILRQD-NHM-TARLTVADLVAFGryPYSKGRLTIED-KAHIDQSIAYLNLD-DLRDRFLDELSGGQRQRAFVAMVLCQD 153
Cdd:COG1123 345 QMVFQDpYSSlNPRMTVGDIIAEP--LRLHGLLSRAErRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALALE 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 154 TDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT 225
Cdd:COG1123 423 PKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-232 |
8.38e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 149.28 E-value: 8.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLL---GMDAGSVTVDGLDVSNTPSDVLARRLSILRQDnHMTA 88
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLDGRDLLELSEALRGRRIGMVFQD-PMTQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 89 --RLTVADLVAFGRYPYSKGRLTIEDKAhiDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNL 166
Cdd:COG1123 96 lnPVTVGDQIAEALENLGLSRAEARARV--LELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTAL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 167 DMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT-PEALKDI 232
Cdd:COG1123 174 DVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAaPQALAAV 240
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
2.76e-41 |
|
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: 141.71 E-value: 2.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRlSIL 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL-GIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 R--QDNHMTARLTVADLVAFGRYPYSKGRLTI----------EDKAHIDQS---IAYLNLDDLRDRFLDELSGGQRQRAF 145
Cdd:COG0411 83 RtfQNPRLFPELTVLENVLVAAHARLGRGLLAallrlprarrEEREARERAeelLERVGLADRADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 146 VAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT 225
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRA 242
|
....*...
gi 351592836 226 PEALKDIY 233
Cdd:COG0411 243 DPRVIEAY 250
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
7-218 |
1.36e-40 |
|
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: 138.78 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 7 IKKYYGETAVVDDVSIelPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVsnTPSDVLARRLSILRQDNHM 86
Cdd:cd03298 6 IRFSYGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV--TAAPPADRPVSMLFQENNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 87 TARLTVADLVAFGRYPysKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNL 166
Cdd:cd03298 82 FAHLTVEQNVGLGLSP--GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 351592836 167 DMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:cd03298 160 DPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-228 |
1.52e-40 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 139.74 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 7 IKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQD--- 83
Cdd:cd03295 7 TKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQigl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 84 -NHMTARLTVADLVAFGRYPyskgRLTIEDKAhiDQSIAYLNLDD--LRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:cd03295 87 fPHMTVEENIALVPKLLKWP----KEKIRERA--DELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 161 EPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEA 228
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-223 |
2.03e-40 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 139.55 E-value: 2.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGE----TAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARR 76
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 77 LSILRQDnHMTA---RLTVADLVAfgrYPY-SKGRLTIEDKahIDQSIAYLNLD-DLRDRFLDELSGGQRQRAFVAMVLC 151
Cdd:COG1124 81 VQMVFQD-PYASlhpRHTVDRILA---EPLrIHGLPDREER--IAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 152 QDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
2.55e-40 |
|
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: 136.93 E-value: 2.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLA--RRLSI 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQDNHMTARLTVADLVAFGrypyskgrltiedkahidqsiaylnlddlrdrfldeLSGGQRQRAFVAMVLCQDTDYVLL 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 351592836 160 DEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGR 213
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-216 |
2.67e-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: 138.37 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYG----ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvsnTPSDVLARRL 77
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 78 SILRQDNHMTARLTVADLVAFGryPYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYV 157
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALG--LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 158 LLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKN--GRVIR 216
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-223 |
7.21e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 140.62 E-value: 7.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDvlARRLSILRQD-- 83
Cdd:COG3842 10 NVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMVFQDya 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 84 --NHMTarltVADLVAFG----RYPyskgRLTIEDKAhiDQSIAYLNLDDLRDRFLDELSGGQRQRafVAM--------- 148
Cdd:COG3842 88 lfPHLT----VAENVAFGlrmrGVP----KAEIRARV--AELLELVGLEGLADRYPHQLSGGQQQR--VALaralapepr 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 149 VLcqdtdyvLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:COG3842 156 VL-------LLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
9.01e-38 |
|
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: 130.21 E-value: 9.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLaRRLSILR 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 QDNHMTARLTVADlvafgrypyskgrltiedkahidqsiaylNLDdlrdrfldeLSGGQRQRAFVAMVLCQDTDYVLLDE 161
Cdd:cd03230 80 EEPSLYENLTVRE-----------------------------NLK---------LSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 351592836 162 PLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGRV 214
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-213 |
4.10e-37 |
|
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: 128.13 E-value: 4.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQdn 84
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 hmtarltvadlvafgrypyskgrltiedkahidqsiaylnlddlrdrfldeLSGGQRQRAFVAMVLCQDTDYVLLDEPLN 164
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 351592836 165 NLDMKHAMGMMKLMQRAChELGKTVVLVLHDINFASWYSDYIIAMKNGR 213
Cdd:cd00267 110 GLDPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-246 |
8.49e-37 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 129.96 E-value: 8.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 29 ITSIIGPNGAGKSTMLSIVSRLLGmDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARLTVADLVAFGRYPyskgrl 108
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLALHQPA------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 109 tIEDKAHIDQSIAY----LNLDDLRDRFLDELSGGQRQRAFVAMVLCQ-------DTDYVLLDEPLNNLDMKHAMGMMKL 177
Cdd:COG4138 97 -GASSEAVEQLLAQlaeaLGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 178 MQRAChELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEALKDIYDMDINVHEIGGHR 246
Cdd:COG4138 176 LRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLEVEGHR 243
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
9.28e-37 |
|
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: 128.75 E-value: 9.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVlARRLSIL 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVADLVAFgrypYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:COG4133 81 GHADGLKPELTVRENLRF----WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 351592836 161 EPLNNLDmKHAMGM-MKLMQRACHElGKTVVLVLHD 195
Cdd:COG4133 157 EPFTALD-AAGVALlAELIAAHLAR-GGAVLLTTHQ 190
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-230 |
1.17e-36 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 129.03 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVlARRLSILR 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREV-RRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 Q----DNHMTARltvADLVAFGR-YPYSKGRLtiedKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDY 156
Cdd:cd03265 80 QdlsvDDELTGW---ENLYIHARlYGVPGAER----RERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 157 VLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGtkndiiTPEALK 230
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG------TPEELK 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-218 |
2.95e-36 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 128.01 E-value: 2.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYY----GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSD---VLARRL 77
Cdd:cd03257 5 KNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRRKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 78 SILRQD--NHMTARLTVADLVAFgryPYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLD----ELSGGQRQRAFVAMVLC 151
Cdd:cd03257 85 QMVFQDpmSSLNPRMTIGEQIAE---PLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNryphELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 152 QDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
3.21e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 128.67 E-value: 3.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYY----GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVlarr 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 77 lSILRQDnhmtARL----TVADLVAFGryPYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQ 152
Cdd:COG1116 83 -GVVFQE----PALlpwlTVLDNVALG--LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 153 DTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKN--GRVIR 216
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-238 |
9.48e-36 |
|
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: 126.97 E-value: 9.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDvlARRLSILRQDN 84
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 HMTARLTVADLVAFGRYPYSKGRLTIedKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLN 164
Cdd:cd03300 82 ALFPHLTVFENIAFGLRLKKLPKAEI--KERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 165 NLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGtkndiiTPEalkDIYDMDIN 238
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG------TPE---EIYEEPAN 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-223 |
1.62e-35 |
|
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: 126.68 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPsdVLARRLSILR 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP--VQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 QDNHMTARLTVADLVAFGRypYSKGRLTIEDKAHIDQSIAYL----NLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYV 157
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGL--RVKPRSERPPEAEIRAKVHELlklvQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 158 LLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-225 |
2.30e-35 |
|
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: 126.08 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVS-NTPSD--VLARRLSILR 81
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISgLSEAElyRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 QDNHMTARLTVADLVAFGRYPYSK-GRLTIEDKAHidQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:cd03261 84 QSGALFDSLTVFENVAFPLREHTRlSEEEIREIVL--EKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 161 EPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT 225
Cdd:cd03261 162 EPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-223 |
2.88e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 128.73 E-value: 2.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDV-SNTPsdVLARRLSIL 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLP--PRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDN----HMTarltVADLVAFG--RYPYSKGRltIEDKAHidQSIAYLNLDDLRDRFLDELSGGQRQRafVAM--VLCQ 152
Cdd:COG1118 81 FQHYalfpHMT----VAENIAFGlrVRPPSKAE--IRARVE--ELLELVQLEGLADRYPSQLSGGQRQR--VALarALAV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 153 DTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-234 |
2.94e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 128.65 E-value: 2.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPsdVLARRLSIL 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP--PKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQD----NHMTarltVADLVAFGrypyskgrLTI--EDKAHIDQSIAY----LNLDDLRDRFLDELSGGQRQRafVAM-- 148
Cdd:COG3839 81 FQSyalyPHMT----VYENIAFP--------LKLrkVPKAEIDRRVREaaelLGLEDLLDRKPKQLSGGQRQR--VALgr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 149 VLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGtkndiiTPEa 228
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVG------TPE- 219
|
....*.
gi 351592836 229 lkDIYD 234
Cdd:COG3839 220 --ELYD 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-224 |
3.19e-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: 125.53 E-value: 3.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGETaVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDvlARRLSILRQDNH 85
Cdd:cd03299 5 NLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 86 MTARLTVADLVAFGRYPYSKGRLTIEDKahIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNN 165
Cdd:cd03299 82 LFPHMTVYKNIAYGLKKRKVDKKEIERK--VLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 166 LDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDII 224
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-219 |
3.26e-35 |
|
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: 131.80 E-value: 3.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTAr 89
Cdd:COG4988 346 YPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFA- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 90 LTVADLVAFGRYPYSKGRL-TIEDKAHIDQSIAYLNlDDLrDRFLDE----LSGGQRQRAFVAMVLCQDTDYVLLDEPLN 164
Cdd:COG4988 425 GTIRENLRLGRPDASDEELeAALEAAGLDEFVAALP-DGL-DTPLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 165 NLDMKHAMGMMKLMQRACHelGKTVVLVLHDINFASWYsDYIIAMKNGRVIRHGT 219
Cdd:COG4988 503 HLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDDGRIVEQGT 554
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-223 |
3.40e-35 |
|
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: 125.37 E-value: 3.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 4 TSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGM-----DAGSVTVDGLDVSNTPSDVLA--RR 76
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLElrRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 77 LSILRQDNHMTaRLTVADLVAFG-RYPYSKGRLTIEDKAHIDQSIAYLnLDDLRDR-FLDELSGGQRQRAFVAMVLCQDT 154
Cdd:cd03260 83 VGMVFQKPNPF-PGSIYDNVAYGlRLHGIKLKEELDERVEEALRKAAL-WDEVKDRlHALGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 155 DYVLLDEPLNNLDMKHAMGMMKLMQRACHELgkTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-164 |
1.02e-34 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 121.60 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 17 VDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARLTVADLV 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 97 AFGRYPysKGRLTIEDKAHIDQSIAYLNLDDLRDRFLD----ELSGGQRQRAFVAMVLCQDTDYVLLDEPLN 164
Cdd:pfam00005 81 RLGLLL--KGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-214 |
2.44e-34 |
|
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: 122.66 E-value: 2.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 26 ARG-ITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSdvLARRLSILRQDNHMTARLTVADLVAFGRYPYS 104
Cdd:TIGR01277 22 ADGeIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP--YQRPVSMLFQENNLFAHLTVRQNIGLGLHPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 105 KgrLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHE 184
Cdd:TIGR01277 100 K--LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|
gi 351592836 185 LGKTVVLVLHDINFASWYSDYIIAMKNGRV 214
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
13-232 |
6.38e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 123.33 E-value: 6.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARrlsiLRQD--------N 84
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKD----LRKKvglvfqfpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 HMTARLTVADLVAFG--RYPYSKGRltIEDKAhidqsIAYLNLDDLRDRFLD----ELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:TIGR04521 93 HQLFEETVYKDIAFGpkNLGLSEEE--AEERV-----KEALELVGLDEEYLErspfELSGGQMRRVAIAGVLAMEPEVLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 159 LDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT-PEALKDI 232
Cdd:TIGR04521 166 LDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSdVDELEKI 240
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-243 |
7.19e-34 |
|
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: 122.50 E-value: 7.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVS-----------RLLGMDAGSVTVD------GLdVSNTpsdv 72
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgdlpptygndvRLFGERRGGEDVWelrkriGL-VSPA---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 73 LARRLsilrqdnhmTARLTVADLVA------FGRYPyskgRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFV 146
Cdd:COG1119 87 LQLRF---------PRDETVLDVVLsgffdsIGLYR----EPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 147 AMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDInfaswysDYIIA-------MKNGRVIRHGT 219
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHV-------EEIPPgithvllLKDGRVVAAGP 226
|
250 260
....*....|....*....|....
gi 351592836 220 KNDIITPEALKDIYDMDINVHEIG 243
Cdd:COG1119 227 KEEVLTSENLSEAFGLPVEVERRD 250
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-220 |
1.12e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 121.31 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLA---RRLSILRQDN 84
Cdd:COG2884 9 KRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRRIGVVFQDF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 HMTARLTVADLVAFGrypyskgrLTI------EDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:COG2884 89 RLLPDRTVYENVALP--------LRVtgksrkEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 159 LDEPLNNLDMKHAMGMMKLMQRAcHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTK 220
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-219 |
1.51e-33 |
|
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: 121.00 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARR-LSILRQD 83
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 84 NHMTARLTVADLVAFGRYPYSKGRltieDKAHIDQSIAYL-NLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEP 162
Cdd:cd03224 84 RRIFPELTVEENLLLGAYARRRAK----RKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 163 LNNLDMKHAMGMMKLMQRAChELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGT 219
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
1.66e-33 |
|
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: 120.55 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYY----GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLaRR 76
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR-RR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 77 LSILRQDNHMTARLTV-ADLVAFGRYPYSKGRltiEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTD 155
Cdd:cd03266 80 LGFVSDSTGLYDRLTArENLEYFAGLYGLKGD---ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351592836 156 YVLLDEPLNNLDMKHAMGMMKLMQRAChELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
3.36e-33 |
|
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: 119.61 E-value: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPArGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPsDVLARRLSILR 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 QDNHMTARLTVADLVAfgrypYS---KGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:cd03264 79 QEFGVYPNFTVREFLD-----YIawlKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 159 LDEPLNNLDMKHAMGMMKLMQrachELGKTVVLVL--HDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLS----ELGEDRIVILstHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-225 |
5.46e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 119.71 E-value: 5.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLArrlsiL 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINK-----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQD-----------NHMTAR--LTVADLVAFGRypySKgrltieDKAHiDQSIAYLN---LDDLRDRFLDELSGGQRQRa 144
Cdd:COG1126 76 RRKvgmvfqqfnlfPHLTVLenVTLAPIKVKKM---SK------AEAE-ERAMELLErvgLADKADAYPAQLSGGQQQR- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 145 fVAMV--LCQDTDYVLLDEPLNNLD--MKHamGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTK 220
Cdd:COG1126 145 -VAIAraLAMEPKVMLFDEPTSALDpeLVG--EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPP 220
|
....*
gi 351592836 221 NDIIT 225
Cdd:COG1126 221 EEFFE 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-223 |
5.61e-33 |
|
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: 119.70 E-value: 5.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLA---RRL 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 78 SILRQ-----DNhmtarLTVADLVAFG-RYPYSKGRLTIEDKAhiDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLC 151
Cdd:COG1127 85 GMLFQggalfDS-----LTVFENVAFPlREHTDLSEAEIRELV--LEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 152 QDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-214 |
1.16e-32 |
|
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: 118.51 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNT-PSDvlaRRLSIL 80
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLpPKD---RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVADLVAFGRypyskgRLTIEDKAHIDQSI----AYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDY 156
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGL------KLRKVPKDEIDERVrevaELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 157 VLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRV 214
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-215 |
3.03e-32 |
|
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: 116.97 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 9 KYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvSNTPSDVLARRLSILRQD-NHMT 87
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQDvDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 88 ARLTVADLVAFGRYPYSKGRLTIEdkahidQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLD 167
Cdd:cd03226 85 FTDSVREELLLGLKELDAGNEQAE------TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 351592836 168 MKHAMGMMKLMqRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVI 215
Cdd:cd03226 159 YKNMERVGELI-RELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-246 |
3.58e-32 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 118.78 E-value: 3.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 15 AVVDDVSIELPARGITSIIGPNGAGKSTML-SIVSRLLGMDA-------GSVTVDGLDVSNTPSDVLARRLSILRQDNHM 86
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 87 TARLTVADLVAFGRYPYSK--GRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQ---------DTD 155
Cdd:PRK13547 95 AFAFSAREIVLLGRYPHARraGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 156 YVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEALKDIYDM 235
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCYGF 254
|
250
....*....|.
gi 351592836 236 DINVHEIGGHR 246
Cdd:PRK13547 255 AVRLVDAGDGV 265
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
7.02e-32 |
|
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: 116.09 E-value: 7.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDV--LARRLSI 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQDNHMTARLTVADLVAFGryP-YSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLA--PiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 159 LDEPLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGRV 214
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-224 |
1.63e-31 |
|
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: 115.76 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETA----VVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVL--- 73
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 74 ARRLSILRQDNHMTARLTVADLVAfgrYPYskgRLTIEDKAHIDQSIAYL----NLDDLRDRFLDELSGGQRQRAFVAMV 149
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVA---LPL---EIAGVPKAEIEERVLELlelvGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 150 LCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDII 224
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-219 |
1.00e-30 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 113.37 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYG--ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLaRRLSI 79
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR-QSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQDNHMTARLTVADLVAFgrypYS--KGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYV 157
Cdd:cd03263 80 CPQFDALFDELTVREHLRF----YArlKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 158 LLDEPLNNLD--MKHAMGMMKLMQRAchelGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGT 219
Cdd:cd03263 156 LLDEPTSGLDpaSRRAIWDLILEVRK----GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGS 215
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-233 |
1.07e-30 |
|
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: 113.92 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARR-LSI 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQDNHMTARLTVAD---LVAFGRypyskgrltiEDKAHIDQSIAYL-----NLDDLRDRFLDELSGGQRQRAFVAMVLC 151
Cdd:COG0410 83 VPEGRRIFPSLTVEEnllLGAYAR----------RDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 152 QDTDYVLLDEPLnnldmkhaMG----MMKLMQRACHEL---GKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDII 224
Cdd:COG0410 153 SRPKLLLLDEPS--------LGlaplIVEEIFEIIRRLnreGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
....*....
gi 351592836 225 TPEALKDIY 233
Cdd:COG0410 225 ADPEVREAY 233
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-225 |
1.09e-30 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 115.57 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGE-TAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSI 79
Cdd:COG1125 1 MIEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQDN----HMTarltVADLVAFgrYPyskgRLTIEDKAHIDQSIAYL----NLD--DLRDRFLDELSGGQRQRAFVAMV 149
Cdd:COG1125 81 VIQQIglfpHMT----VAENIAT--VP----RLLGWDKERIRARVDELlelvGLDpeEYRDRYPHELSGGQQQRVGVARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 150 LCQDTDYVLLDEPLNNLD---MKHAMGMMKLMQRachELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT 225
Cdd:COG1125 151 LAADPPILLMDEPFGALDpitREQLQDELLRLQR---ELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILA 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
11-214 |
1.15e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.99 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 11 YGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARl 90
Cdd:COG4619 10 VGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGG- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 TVADLVAFGrYPYSKGRLtieDKAHIDQSIAYLNLD-DLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMK 169
Cdd:COG4619 89 TVRDNLPFP-FQLRERKF---DRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 351592836 170 HAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRV 214
Cdd:COG4619 165 NTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-228 |
4.40e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 111.98 E-value: 4.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 32 IIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSdvlARR-LSILRQDNHMTARLTVADLVAFGRYPyskG-RLT 109
Cdd:PRK10771 30 ILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP---SRRpVSMLFQENNLFSHLTVAQNIGLGLNP---GlKLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 110 IEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTV 189
Cdd:PRK10771 104 AAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTL 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 351592836 190 VLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEA 228
Cdd:PRK10771 184 LMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-225 |
5.71e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.11 E-value: 5.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLS-- 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 79 -ILRQDN---HMTArltvADLVAFG-RYPYSKGRLTIEDKAHidQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQD 153
Cdd:PRK09493 81 mVFQQFYlfpHLTA----LENVMFGpLRVRGASKEEAEKQAR--ELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 154 TDYVLLDEPLNNLD--MKHAmgMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT 225
Cdd:PRK09493 155 PKLMLFDEPTSALDpeLRHE--VLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-219 |
8.36e-30 |
|
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: 116.79 E-value: 8.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHmtarL- 90
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPH----Lf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 --TVADLVAFGRypyskGRLTIE------DKAHIDQSIAylNLDDLRDRFLDE----LSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:COG4987 422 dtTLRENLRLAR-----PDATDEelwaalERVGLGDWLA--ALPDGLDTWLGEggrrLSGGERRRLALARALLRDAPILL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 159 LDEPLNNLDMKHAMGMMKLMQRACHelGKTVVLVLHDINFASWYsDYIIAMKNGRVIRHGT 219
Cdd:COG4987 495 LDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVLEDGRIVEQGT 552
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-246 |
1.18e-29 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 111.56 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 20 VSIELPARGITSIIGPNGAGKSTMLSIVSRLLgMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARLTVADLVAFG 99
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 100 RYPyskGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQ-------DTDYVLLDEPLNNLDMKHAM 172
Cdd:PRK03695 94 QPD---KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 173 GMMKLMQRAChELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEALKDIYDMDINVHEIGGHR 246
Cdd:PRK03695 171 ALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLDVEGHP 243
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
10-209 |
2.11e-29 |
|
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: 115.46 E-value: 2.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTAR 89
Cdd:TIGR02857 331 YPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 90 lTVADLVAFGRyPYSKGRLTIE--DKAHIDQSIAylNLDDLRDRFLDE----LSGGQRQRAFVAMVLCQDTDYVLLDEPL 163
Cdd:TIGR02857 411 -TIAENIRLAR-PDASDAEIREalERAGLDEFVA--ALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 351592836 164 NNLDMKHAMGMMKLMQRACHelGKTVVLVLHDINFASWYsDYIIAM 209
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-225 |
2.51e-29 |
|
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: 112.89 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 19 DVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDG---LDvSNTPSDVLA--RRLSILRQDNHMTARLTVA 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQD-SARGIFLPPhrRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 94 DLVAFGRypysKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRafVAMV--LCQDTDYVLLDEPLNNLDMKHA 171
Cdd:COG4148 96 GNLLYGR----KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQR--VAIGraLLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 351592836 172 MGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT 225
Cdd:COG4148 170 AEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-224 |
2.72e-29 |
|
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: 115.70 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARlT 91
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSG-T 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 92 VADLVAFGRYPYSKGRLtIE--DKAHIDQSIAylNLDDLRDRFLDE----LSGGQRQRAFVAMVLCQDTDYVLLDEPLNN 165
Cdd:COG2274 565 IRENITLGDPDATDEEI-IEaaRLAGLHDFIE--ALPMGYDTVVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 166 LDMKHAMGMMKLMQRACHelGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDII 224
Cdd:COG2274 642 LDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELL 697
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
10-220 |
3.33e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.98 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQD-NHMTA 88
Cdd:PRK13647 14 YKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpDDQVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 89 RLTVADLVAFGryPYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDM 168
Cdd:PRK13647 94 SSTVWDDVAFG--PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 351592836 169 KHAMGMMKLMQRaCHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTK 220
Cdd:PRK13647 172 RGQETLMEILDR-LHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-251 |
5.32e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 112.10 E-value: 5.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNtpsdVLA--RRLSI 79
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR----LHArdRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQDNHMTARLTVADLVAFGrypyskgrLTI------EDKAHIDQSIAYL----NLDDLRDRFLDELSGGQRQRAFVAMV 149
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFG--------LTVlprrerPNAAAIKAKVTQLlemvQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 150 LCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDII-TP-- 226
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWrEPat 230
|
250 260 270
....*....|....*....|....*....|...
gi 351592836 227 ----EALKDIYDMDINVH----EIGGHRVSLFY 251
Cdd:PRK10851 231 rfvlEFMGEVNRLQGTIRggqfHVGAHRWPLGY 263
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-225 |
6.67e-29 |
|
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: 110.04 E-value: 6.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 7 IKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTP----SDVLARRLSILRQ 82
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelRELRRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 83 DNHMTARLTVADLVAFGRYPYSKGRLTIEDKAhiDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEP 162
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERA--AEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351592836 163 LNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT 225
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-218 |
7.50e-29 |
|
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: 108.54 E-value: 7.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 19 DVSIELPArGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDG---LDVS---NTPSDvlARRLSILRQDNHMTARLTV 92
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRkkiNLPPQ--QRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 93 ADLVAFGrypySKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAM 172
Cdd:cd03297 93 RENLAFG----LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 351592836 173 GMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-233 |
1.72e-28 |
|
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: 108.01 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARR-LSIL 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVAD--LVAFGRYPYSKGRLTIEdkahIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:cd03218 81 PQEASIFRKLTVEEniLAVLEIRGLSKKEREEK----LEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 159 LDEPLNNLDMKhamgmmklmqrACHELgKTVVLVLHDINFASWYSD-------------YIIamKNGRVIRHGTKNDIIT 225
Cdd:cd03218 157 LDEPFAGVDPI-----------AVQDI-QKIIKILKDRGIGVLITDhnvretlsitdraYII--YEGKVLAEGTPEEIAA 222
|
....*...
gi 351592836 226 PEALKDIY 233
Cdd:cd03218 223 NELVRKVY 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-215 |
2.57e-28 |
|
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: 106.92 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNtPSDVLARRLSILR 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 QD---NHMTARltvADLVAfgrypysKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:cd03268 80 APgfyPNLTAR---ENLRL-------LARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 159 LDEPLNNLDmkhAMGMMKLMQ--RACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVI 215
Cdd:cd03268 150 LDEPTNGLD---PDGIKELREliLSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-225 |
3.07e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.69 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMD-----AGSVTVDGLDVSNTPSDVLARR 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 77 LSILRQDNHMTARLTVADLVAFG----RYPYSKGRLtiedKAHIDQSIAYLNL-DDLRDRfLD----ELSGGQRQRAFVA 147
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGlklnRLVKSKKEL----QERVRWALEKAQLwDEVKDR-LDapagKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 148 MVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQrachELGK--TVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT 225
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFL----ELKKdmTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-214 |
4.52e-28 |
|
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: 106.34 E-value: 4.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLA---RRLSILRQDN 84
Cdd:cd03292 8 KTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVVFQDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 HMTARLTVADLVAFG-RYPYSKGRLTIEDKAhidqsiAYLNLDDLRDR---FLDELSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:cd03292 88 RLLPDRNVYENVAFAlEVTGVPPREIRKRVP------AALELVGLSHKhraLPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 351592836 161 EPLNNLDMKHAMGMMKLMQRAcHELGKTVVLVLHDINFASWYSDYIIAMKNGRV 214
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-218 |
6.77e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 105.83 E-value: 6.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvsnTPSDVLAR-RLSILRQDN 84
Cdd:cd03269 5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-----KPLDIAARnRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 HMTARLTVAD-LVAFGRYpysKGrLTIEDKAH-IDQSIAYLNLDDLRDRFLDELSGGQRQRA-FVAMVLcQDTDYVLLDE 161
Cdd:cd03269 80 GLYPKMKVIDqLVYLAQL---KG-LKKEEARRrIDEWLERLELSEYANKRVEELSKGNQQKVqFIAAVI-HDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 162 PLNNLDMKHAMGMMKLMqRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:cd03269 155 PFSGLDPVNVELLKDVI-RELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-213 |
1.06e-27 |
|
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: 104.00 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMtarlt 91
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFL----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 92 vadlvaFGRypyskgrlTIEDkahidqsiaylNLddlrdrfldeLSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHA 171
Cdd:cd03228 88 ------FSG--------TIRE-----------NI----------LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 351592836 172 MGMMKLMQRACHelGKTVVLVLHDINFASwYSDYIIAMKNGR 213
Cdd:cd03228 133 ALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
7-223 |
1.68e-27 |
|
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: 107.89 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 7 IKKYYGETAVvdDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDG--LDVSNTPSDVLA--RRLSILRQ 82
Cdd:TIGR02142 5 FSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtLFDSRKGIFLPPekRRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 83 DNHMTARLTVADLVafgRYPYSKGRLTiEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEP 162
Cdd:TIGR02142 83 EARLFPHLSVRGNL---RYGMKRARPS-ERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 163 LNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-223 |
2.54e-27 |
|
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: 107.19 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 32 IIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVlaRRLSILRQDNHMTARLTVADLVAFGRYPYSKGRLTIe 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 112 dKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVL 191
Cdd:TIGR01187 78 -KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180 190
....*....|....*....|....*....|..
gi 351592836 192 VLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-223 |
5.23e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.96 E-value: 5.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDvlARRLSILRQDN 84
Cdd:PRK09452 18 RGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 HMTARLTVADLVAFG-RYpysKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPL 163
Cdd:PRK09452 96 ALFPHMTVFENVAFGlRM---QKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351592836 164 NNLDMKHAMGM---MKLMQRachELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:PRK09452 173 SALDYKLRKQMqneLKALQR---KLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
8-213 |
1.07e-26 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 102.71 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLA---RRLSILRQDN 84
Cdd:TIGR02673 9 KAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPllrRRIGVVFQDF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 HMTARLTVADLVAFGRYPYSKGRLTIEDKAHidQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLN 164
Cdd:TIGR02673 89 RLLPDRTVYENVALPLEVRGKKEREIQRRVG--AALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 351592836 165 NLDMKHAMGMMKLMQRAcHELGKTVVLVLHDINFASWYSDYIIAMKNGR 213
Cdd:TIGR02673 167 NLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-215 |
1.24e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.63 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYG-----ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLAR 75
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 76 RLSILRQDNHM-TA-RLTVAD--LVAFGR---YPYSKGrLTIEDKAHIDQSIAYLNLdDLRDRfLDE----LSGGQRQRA 144
Cdd:COG1101 81 YIGRVFQDPMMgTApSMTIEEnlALAYRRgkrRGLRRG-LTKKRRELFRELLATLGL-GLENR-LDTkvglLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 145 FVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVI 215
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-223 |
1.48e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 104.42 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvsnTPSDVLARRLsI- 79
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-----EPLDPEDRRR-Ig 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 -------LRQdnhmtaRLTVAD-LVAFGRYpysKGRltieDKAHIDQSIAY----LNLDDLRDRFLDELSGGQRQRA-FV 146
Cdd:COG4152 75 ylpeergLYP------KMKVGEqLVYLARL---KGL----SKAEAKRRADEwlerLGLGDRANKKVEELSKGNQQKVqLI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 147 AMVLCqDTDYVLLDEPLNNLDmKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:COG4152 142 AALLH-DPELLILDEPFSGLD-PVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-219 |
3.86e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 106.40 E-value: 3.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTAR 89
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 90 lTVADLVAFGRYPYSKGRLtIE--DKAHIDQSIAylNLDDLRDRFLDE----LSGGQRQR-AFvAMVLCQDTDYVLLDEP 162
Cdd:COG1132 429 -TIRENIRYGRPDATDEEV-EEaaKAAQAHEFIE--ALPDGYDTVVGErgvnLSGGQRQRiAI-ARALLKDPPILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 163 LNNLDMKHAmgmmKLMQRACHEL--GKTVVLV---LHDINFAswysDYIIAMKNGRVIRHGT 219
Cdd:COG1132 504 TSALDTETE----ALIQEALERLmkGRTTIVIahrLSTIRNA----DRILVLDDGRIVEQGT 557
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-223 |
3.93e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 104.42 E-value: 3.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 7 IKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVsnTPSDVLARRLSILRQDNHM 86
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV--THRSIQQRDICMVFQSYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 87 TARLTVADLVAFGRYpySKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNL 166
Cdd:PRK11432 90 FPHMSLGENVGYGLK--MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 167 D--MKHAM--GMMKLMQRacheLGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:PRK11432 168 DanLRRSMreKIRELQQQ----FNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-196 |
9.07e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.48 E-value: 9.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSnTPSdvlARRlSILRQDNHMTARLT 91
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT-GPG---ADR-GVVFQKDALLPWLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 92 VADLVAFG-RYpysKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDmkh 170
Cdd:COG4525 93 VLDNVAFGlRL---RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD--- 166
|
170 180
....*....|....*....|....*....
gi 351592836 171 AMG---MMKLMQRACHELGKTVVLVLHDI 196
Cdd:COG4525 167 ALTreqMQELLLDVWQRTGKGVFLITHSV 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
13-237 |
1.13e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.61 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQ--DNHMTArL 90
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQnpDNQFIG-A 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 TVADLVAFG----RYPYSKGRLTIEDKAHIdqsiayLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNL 166
Cdd:PRK13632 100 TVEDDIAFGlenkKVPPKKMKDIIDDLAKK------VGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 167 DMKHAMGMMKLMQRACHELGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDIITPEALKDIYDMDI 237
Cdd:PRK13632 174 DPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILEKAKIDS 243
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-233 |
1.29e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 100.74 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARR-LSIL 80
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVAD-LVAFGRYPYSKGRLTIEDKAhiDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLL 159
Cdd:PRK10895 84 PQEASIFRRLSVYDnLMAVLQIRDDLSAEQREDRA--NELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 160 DEPLNNLDMKHAMGMMKLMQRaCHELGKTVVLVLHDI--NFASWYSDYIIAmkNGRVIRHGTKNDIITPEALKDIY 233
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVreTLAVCERAYIVS--QGHLIAHGTPTEILQDEHVKRVY 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-195 |
1.52e-25 |
|
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: 104.36 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTAR 89
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 90 lTVADLVAFGRypyskGRLTIEDkahIDQSIAYLNLDDLRDRFLD-----------ELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:TIGR02868 424 -TVRENLRLAR-----PDATDEE---LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 351592836 159 LDEPLNNLDMKHAMGMMKLMQRAchELGKTVVLVLHD 195
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-232 |
2.34e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 100.86 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 19 DVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDvlaRRLSILRQD--------NHMTARL 90
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKN---KKLKPLRKKvgivfqfpEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 TVADLVAFGryPYSKGRLTIEDKAHIDQSIAYLNLD-DLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMK 169
Cdd:PRK13634 102 TVEKDICFG--PMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 170 HAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT-PEALKDI 232
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAdPDELEAI 243
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-224 |
2.48e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.83 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTmlsIVSRLLGM---DAGSVTVDGLDVsntPSDV-LAR-RLSI 79
Cdd:PRK13536 45 AGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKST---IARMILGMtspDAGKITVLGVPV---PARArLARaRIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQDNHMTARLTV-ADLVAFGRYPYSKGRltiEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:PRK13536 119 VPQFDNLDLEFTVrENLLVFGRYFGMSTR---EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 159 LDEPLNNLDmKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDII 224
Cdd:PRK13536 196 LDEPTTGLD-PHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-199 |
2.60e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.16 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNtPSdvlARRlSIL 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PG---AER-GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVADLVAFGRYPYSKGRLTIEDKAHidQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAH--QMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 351592836 161 EPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFA 199
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-227 |
3.67e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 99.32 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDG--LDVSNTPSD----VLARRLS 78
Cdd:COG4161 6 KNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDFSQKPSEkairLLRQKVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 79 ILRQDNHMTARLTVAD-LVAfgrYPYSKGRLTIED-KAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDY 156
Cdd:COG4161 86 MVFQQYNLWPHLTVMEnLIE---APCKVLGLSKEQaREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 157 VLLDEPLNNLDMKHAMGMMKLMqRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPE 227
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEII-RELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQPQ 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-225 |
4.18e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 101.31 E-value: 4.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYY----GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSdvlaRR 76
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSE----RE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 77 LSILRQD--------NHMTARlTVADLVAFgryPyskgrLTIE--DKAHIDQSIAYL----NLDDLRDRFLDELSGGQRQ 142
Cdd:COG1135 77 LRAARRKigmifqhfNLLSSR-TVAENVAL---P-----LEIAgvPKAEIRKRVAELlelvGLSDKADAYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 143 RAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDInfaswysDYI--IA-----MKNGRVI 215
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEM-------DVVrrICdrvavLENGRIV 220
|
250
....*....|
gi 351592836 216 RHGTKNDIIT 225
Cdd:COG1135 221 EQGPVLDVFA 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-227 |
6.12e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.93 E-value: 6.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDG--LDVSNTPSDVLARRLS- 78
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSDKAIRELRr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 79 ----ILRQDN---HMTAR--LTVADLVAFGrypYSKGrltiEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMV 149
Cdd:PRK11124 83 nvgmVFQQYNlwpHLTVQqnLIEAPCRVLG---LSKD----QALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 150 LCQDTDYVLLDEPLNNLDMKHAMGMMKLMqRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPE 227
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSII-RELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQPQ 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
10-229 |
2.43e-24 |
|
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: 96.92 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQD----NH 85
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDtvlfND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 86 mtarlTVADLVAFGRYPYSKgrltiED------KAHIDQSIayLNLDDLRDRFLDE----LSGGQRQRAFVAMVLCQDTD 155
Cdd:cd03253 90 -----TIGYNIRYGRPDATD-----EEvieaakAAQIHDKI--MRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 156 YVLLDEPLNNLDMKHAMGMMKLMQRACHelGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDIITPEAL 229
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIV-NADKIIVLKDGRIVERGTHEELLAKGGL 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-162 |
4.92e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.25 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELpARG-ITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARR--- 76
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEV-NQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 77 -L----SILRqdnhmtaRLTVAD---LVAFGRYPYSKGRltiedKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAM 148
Cdd:COG1137 82 yLpqeaSIFR-------KLTVEDnilAVLELRKLSKKER-----EERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170
....*....|....
gi 351592836 149 VLCQDTDYVLLDEP 162
Cdd:COG1137 150 ALATNPKFILLDEP 163
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-224 |
7.76e-24 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 95.76 E-value: 7.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARlTV 92
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFND-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 93 ADLVAFGRYPYSKGRltIEDKAHIDQSIAYL-NLDDLRDRFLDE----LSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLD 167
Cdd:cd03251 93 AENIAYGRPGATREE--VEEAARAANAHEFImELPEGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 168 MKHAMgmmkLMQRACHEL--GKTVVLVLH---DINFAswysDYIIAMKNGRVIRHGTKNDII 224
Cdd:cd03251 171 TESER----LVQAALERLmkNRTTFVIAHrlsTIENA----DRIVVLEDGKIVERGTHEELL 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-223 |
1.43e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 95.85 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 17 VDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVS-NTPSDVlARRLSILRQ--DNHMTARlTVA 93
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeETVWDV-RRQVGMVFQnpDNQFVGA-TVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 94 DLVAFGRYPYSKGRLTIEDKahIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMG 173
Cdd:PRK13635 101 DDVAFGLENIGVPREEMVER--VDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 351592836 174 MMKLMQRACHELGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:PRK13635 179 VLETVRQLKEQKGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-218 |
2.01e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 95.29 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDA-----GSVTVDGLDVSNTPSDVLA-- 74
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIEvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 75 RRLSILRQDNHMTARLTVADLVAFGrypySKGRLTIEDKAHIDQSIAY-----LNLDDLRDRFLD---ELSGGQRQRAFV 146
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIG----VKLNGLVKSKKELDERVEWalkkaALWDEVKDRLNDypsNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 147 AMVLCQDTDYVLLDEPLNNLDmkhAMGMMKLmQRACHELGK--TVVLVLHDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANID---PVGTAKI-EELLFELKKeyTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
9-219 |
2.50e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.68 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 9 KYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDG--LDVSNTPSDVLARRLSILRQD-NH 85
Cdd:PRK13636 14 NYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDpDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 86 MTARLTVADLVAFGryPYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNN 165
Cdd:PRK13636 94 QLFSASVYQDVSFG--AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 351592836 166 LDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGT 219
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
11-197 |
2.71e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 93.70 E-value: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 11 YGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDA---GSVTVDGLDVSNTPsdVLARRLSILRQDNHMT 87
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALP--AEQRRIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 88 ARLTVADLVAFGrYPYSKGRLtiEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLD 167
Cdd:COG4136 89 PHLSVGENLAFA-LPPTIGRA--QRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190
....*....|....*....|....*....|
gi 351592836 168 MKHAMGMMKLMQRACHELGKTVVLVLHDIN 197
Cdd:COG4136 166 AALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-214 |
3.98e-23 |
|
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: 93.57 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGE----TAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLA----RRL 77
Cdd:TIGR02211 6 NLGKRYQEgkldTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnKKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 78 SILRQDNHMTARLTVADLVAFgryPYSKGRLTIEDKAHIDQSI-AYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDY 156
Cdd:TIGR02211 86 GFIYQFHHLLPDFTALENVAM---PLLIGKKSVKEAKERAYEMlEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 157 VLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASwYSDYIIAMKNGRV 214
Cdd:TIGR02211 163 VLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAK-KLDRVLEMKDGQL 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-227 |
5.21e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.87 E-value: 5.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIvsrLLGM---DAGSVTVDGLDVsntPSDV-LAR-RLSIL 80
Cdd:PRK13537 12 NVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRM---LLGLthpDAGSISLCGEPV---PSRArHARqRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVAD-LVAFGRYpysKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLL 159
Cdd:PRK13537 86 PQFDNLDPDFTVREnLLVFGRY---FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 160 DEPLNNLD--MKHAM--GMMKLMQRachelGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPE 227
Cdd:PRK13537 163 DEPTTGLDpqARHLMweRLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
10-229 |
6.00e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.48 E-value: 6.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQD-NHMTA 88
Cdd:PRK13652 13 YSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNpDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 89 RLTVADLVAFGryPYSKGrLTIEDKAH-IDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLD 167
Cdd:PRK13652 93 SPTVEQDIAFG--PINLG-LDEETVAHrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 168 MKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEAL 229
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-223 |
6.32e-23 |
|
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: 93.36 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARR-LSILRQD 83
Cdd:TIGR03410 4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVPQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 84 NHMTARLTVAD--LVAFGRYPYSKgrltiedkAHIDQSIAYL--NLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLL 159
Cdd:TIGR03410 84 REIFPRLTVEEnlLTGLAALPRRS--------RKIPDEIYELfpVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 160 DEPLNnldmkhamGM----MKLMQRACHEL----GKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:TIGR03410 156 DEPTE--------GIqpsiIKDIGRVIRRLraegGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
10-219 |
6.96e-23 |
|
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: 93.06 E-value: 6.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTAR 89
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 90 lTVADLVAFGRyPYSKGRLTIE--DKAHIDQSIayLNLDDLRDRFLDE----LSGGQRQRAFVAMVLCQDTDYVLLDEPL 163
Cdd:cd03254 92 -TIMENIRLGR-PNATDEEVIEaaKEAGAHDFI--MKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 164 NNLDMKhamgMMKLMQRACHEL--GKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGT 219
Cdd:cd03254 168 SNIDTE----TEKLIQEALEKLmkGRTSIIIAHRLSTIK-NADKILVLDDGKIIEEGT 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-252 |
7.96e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.42 E-value: 7.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 19 DVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDV----LARRLSILRQ--DNHMTARLTV 92
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQfpESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 93 ADlVAFGryPYSKGrLTIEDKAHIdqSIAYLNLDDLRDRFLD----ELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDM 168
Cdd:PRK13643 104 KD-VAFG--PQNFG-IPKEKAEKI--AAEKLEMVGLADEFWEkspfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 169 KHAMGMMKLMQrACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITpealkdiyDMD-INVHEIGGHRV 247
Cdd:PRK13643 178 KARIEMMQLFE-SIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ--------EVDfLKAHELGVPKA 248
|
....*
gi 351592836 248 SLFYD 252
Cdd:PRK13643 249 THFAD 253
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
13-233 |
8.73e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.13 E-value: 8.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDG----LDVSNTPSDVLARRLSILRQdnHMTA 88
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKKLRKKVSLVFQ--FPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 89 RL---TVADLVAFGryPYSKGrlTIEDKAHIdQSIAYLNLDDLRDRFLD----ELSGGQRQRAFVAMVLCQDTDYVLLDE 161
Cdd:PRK13641 97 QLfenTVLKDVEFG--PKNFG--FSEDEAKE-KALKWLKKVGLSEDLISkspfELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 162 PLNNLDMKHAMGMMKLM---QRACHelgkTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT-PEALKDIY 233
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFkdyQKAGH----TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSdKEWLKKHY 243
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-223 |
1.57e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 92.72 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 7 IKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDG------------LDVSNTPSDVLA 74
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqLKVADKNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 75 R-RLSILRQDNHMTARLTVADLVAfgRYPYSKGRLTIEDKAhiDQSIAYLN---LDD-LRDRFLDELSGGQRQRAFVAMV 149
Cdd:PRK10619 91 RtRLTMVFQHFNLWSHMTVLENVM--EAPIQVLGLSKQEAR--ERAVKYLAkvgIDErAQGKYPVHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 150 LCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
4.42e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.06 E-value: 4.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIK-KYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARR--L 77
Cdd:PRK13639 1 ILETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRktV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 78 SILRQ--DNHMTARlTVADLVAFGryPYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTD 155
Cdd:PRK13639 81 GIVFQnpDDQLFAP-TVEEDVAFG--PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351592836 156 YVLLDEPLNNLDMKHAMGMMKLMqracHELGK---TVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT 225
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLL----YDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-223 |
4.68e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.11 E-value: 4.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 19 DVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSD----VLARRLSILRQ--DNHMTARlTV 92
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQIRKKVGLVFQfpESQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 93 ADLVAFGryPYSKGRLTIEDKAHIDQSIAYLNLD-DLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHA 171
Cdd:PRK13649 104 LKDVAFG--PQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 351592836 172 MGMMKLMQRaCHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:PRK13649 182 KELMTLFKK-LHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
12-230 |
5.73e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 91.48 E-value: 5.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVvDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLarrLSILRQDNHM--TAR 89
Cdd:PRK15056 19 GHTAL-RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEVdwSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 90 LTVADLVAFGRYPYSK--GRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLD 167
Cdd:PRK15056 95 VLVEDVVMMGRYGHMGwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351592836 168 MKHAMGMMKLMqRACHELGKTVVLVLHDINFASWYSDYIIAMKnGRVIRHGTKNDIITPEALK 230
Cdd:PRK15056 175 VKTEARIISLL-RELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLE 235
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
9-230 |
6.94e-22 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 94.16 E-value: 6.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 9 KYYG-ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDnhmt 87
Cdd:TIGR03375 472 AYPGqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQD---- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 88 ARL---TVADLVAFGRyPYskgrltIEDKAhIDQSIAYLNLDDLR-------DRFLDE----LSGGQRQRAFVAMVLCQD 153
Cdd:TIGR03375 548 PRLfygTLRDNIALGA-PY------ADDEE-ILRAAELAGVTEFVrrhpdglDMQIGErgrsLSGGQRQAVALARALLRD 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 154 TDYVLLDEPLNNLDMKHAMGMMKLMQRACHelGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDIItpEALK 230
Cdd:TIGR03375 620 PPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQVL--EALR 691
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-225 |
1.11e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.49 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVD------GLDVSNTPSDVLARRLSILRQD 83
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 84 NHMTARLTVADLVAfgrYPY-SKGrltIEDKAHI----DQSIAYLNL-DDLRDRF---LDELSGGQRQRAFVAMVLCQDT 154
Cdd:PRK14246 99 PNPFPHLSIYDNIA---YPLkSHG---IKEKREIkkivEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 155 DYVLLDEPLNNLDMKHAMGMMKLMQRACHELgkTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT 225
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
13-232 |
1.41e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.53 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTpSDV--LARRLSILRQ--DNHMTA 88
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE-ENLwdIRNKAGMVFQnpDNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 89 RLTVADlVAFGryPYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDM 168
Cdd:PRK13633 101 TIVEED-VAFG--PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 169 KHAMGMMKLMQRACHELGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDIITP-EALKDI 232
Cdd:PRK13633 178 SGRREVVNTIKELNKKYGITIILITHYMEEAV-EADRIIVMDSGKVVMEGTPKEIFKEvEMMKKI 241
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-214 |
2.31e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.74 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLsivsRLLGmdagsvtvdGLDvsnTPS--DVLARR--LSILR 81
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLL----RLLA---------GLE---TPSagELLAGTapLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 QDNHMT---ARL----TVADLVAFGRypysKGRLtiEDKAHidQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDT 154
Cdd:PRK11247 81 EDTRLMfqdARLlpwkKVIDNVGLGL----KGQW--RDAAL--QALAAVGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 155 DYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRV 214
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-218 |
2.62e-21 |
|
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: 88.80 E-value: 2.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARlTV 92
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYG-TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 93 ADLVAFGRyPYSKGRLTIE--DKAHIDQSIAylNLDDLRDRFLDE----LSGGQRQRAFVAMVLCQDTDYVLLDEPLNNL 166
Cdd:cd03245 95 RDNITLGA-PLADDERILRaaELAGVTDFVN--KHPNGLDLQIGErgrgLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 351592836 167 DMkhaMGMMKLMQRACHEL-GKTVVLVLHDINFASwYSDYIIAMKNGRVIRHG 218
Cdd:cd03245 172 DM---NSEERLKERLRQLLgDKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-225 |
2.68e-21 |
|
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: 90.50 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYY----GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLL---GMDAGSVTVDGLDVSNTPSDVL----A 74
Cdd:COG0444 6 NLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKELrkirG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 75 RRLSILRQDNhMTA---RLTVADLVAFG---RYPYSKgrltiedKAHIDQSIAYLNLDDLRD--RFLD----ELSGGQRQ 142
Cdd:COG0444 86 REIQMIFQDP-MTSlnpVMTVGDQIAEPlriHGGLSK-------AEARERAIELLERVGLPDpeRRLDryphELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 143 RAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKND 222
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
...
gi 351592836 223 IIT 225
Cdd:COG0444 238 LFE 240
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-235 |
2.91e-21 |
|
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: 88.75 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 22 IELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvsnTPSDVLARRLSILRQDNHMT--ARLTVADLVAFG 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG-----ASPGKGWRHIGYVPQRHEFAwdFPISVAHTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 100 RY----PYSKGRltIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMM 175
Cdd:TIGR03771 76 RTghigWLRRPC--VADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 176 KLMQRACHElGKTVVLVLHDINFASWYSDYIIAMkNGRVIRHGTKNDIITPEALKDIYDM 235
Cdd:TIGR03771 154 ELFIELAGA-GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTFGV 211
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-225 |
3.04e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 89.33 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLgmD-------AGSVTVDGLDVSNTPSDV--LARRLSIL 80
Cdd:COG1117 20 YYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMN--DlipgarvEGEILLDGEDIYDPDVDVveLRRRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQ----------DNhmtarltvadlVAFGryPyskgRLT-IEDKAHIDQSI------AYLnLDDLRDRfLDE----LSGG 139
Cdd:COG1117 98 FQkpnpfpksiyDN-----------VAYG--L----RLHgIKSKSELDEIVeeslrkAAL-WDEVKDR-LKKsalgLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 140 QRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMqracHELGK--TVVLVLHDINFASWYSDYIIAMKNGRVIRH 217
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELI----LELKKdyTIVIVTHNMQQAARVSDYTAFFYLGELVEF 234
|
....*...
gi 351592836 218 GTKNDIIT 225
Cdd:COG1117 235 GPTEQIFT 242
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-219 |
3.96e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 88.64 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 17 VDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLArRLSILR--QdnhmTAR----L 90
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIA-RLGIGRkfQ----KPTvfeeL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 TVAD--LVAFGRY--PYS--KGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPln 164
Cdd:COG4674 101 TVFEnlELALKGDrgVFAslFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEP-- 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351592836 165 nldmkhAMGMM--------KLMQRACHElgKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGT 219
Cdd:COG4674 179 ------VAGMTdaetertaELLKSLAGK--HSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-212 |
4.52e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 88.29 E-value: 4.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 17 VDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSD--VLARRLSILRQdnhMTARLTVAD 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmVVFQNYSLLPW---LTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 95 LVAFGRYPYSKGrltiEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGM 174
Cdd:TIGR01184 78 AVDRVLPDLSKS----ERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 351592836 175 MKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNG 212
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-218 |
5.32e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 88.83 E-value: 5.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDvsNTPSDVLA------RRLS- 78
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD--GQLRDLYAlseaerRRLLr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 79 ----ILRQDNHMTARLTVA-------DLVAFGRYPYSKGRLTIED---KAHIDQSiaylNLDDLRDRFldelSGGQRQRA 144
Cdd:PRK11701 89 tewgFVHQHPRDGLRMQVSaggnigeRLMAVGARHYGDIRATAGDwleRVEIDAA----RIDDLPTTF----SGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 145 FVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-218 |
5.75e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 88.16 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMT 87
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 88 ARLTVADLVAFGRYPYSkgrltIED---KAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLN 164
Cdd:cd03267 108 WDLPVIDSFYLLAAIYD-----LPParfKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 351592836 165 NLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-215 |
6.64e-21 |
|
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: 85.94 E-value: 6.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVS-NTPSDvlARRLSIlrqd 83
Cdd:cd03216 4 RGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRD--ARRAGI---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 84 nhmtarltvadlvafgrypyskgrltiedkAHIDQsiaylnlddlrdrfldeLSGGQRQRAFVAMVLCQDTDYVLLDEPL 163
Cdd:cd03216 78 ------------------------------AMVYQ-----------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 351592836 164 NNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGRVI 215
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-231 |
6.70e-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: 88.23 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 29 ITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLArrlsilrqDNHMTARLTVADLVA-FGRYPYSKGR 107
Cdd:cd03237 27 VIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKA--------DYEGTVRDLLSSITKdFYTHPYFKTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 108 LtiedkahidqsIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGK 187
Cdd:cd03237 99 I-----------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 351592836 188 TVVLVLHDINFASWYSDYIIAMkNGRVIRHGTKNdiiTPEALKD 231
Cdd:cd03237 168 TAFVVEHDIIMIDYLADRLIVF-EGEPSVNGVAN---PPQSLRS 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-219 |
7.28e-21 |
|
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: 91.61 E-value: 7.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 11 YGETAVvDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSnTPSDVLARRLSILRQDNHMTARL 90
Cdd:TIGR01257 941 SGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 TVADLVAFgrYPYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKH 170
Cdd:TIGR01257 1019 TVAEHILF--YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 351592836 171 AMGMMKLMQRacHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGT 219
Cdd:TIGR01257 1097 RRSIWDLLLK--YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
9-229 |
1.01e-20 |
|
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: 87.54 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 9 KYYGETAVV-DDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMT 87
Cdd:cd03252 9 RYKPDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 88 ARlTVADLVAFGRYPYSKGRltIEDKAHIDQSIAY-LNLDDLRDRFLDE----LSGGQRQRAFVAMVLCQDTDYVLLDEP 162
Cdd:cd03252 89 NR-SIRDNIALADPGMSMER--VIEAAKLAGAHDFiSELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 163 LNNLDMKHAMGMMKLMQRACHelGKTVVLVLHDINfASWYSDYIIAMKNGRVIRHGTKNDIITPEAL 229
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAENGL 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-224 |
1.63e-20 |
|
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: 90.16 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARlTV 92
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 93 ADLVAFGRypyskgrLTIEDKAHIDQSIAYLNLDDLRDRfLDE------------LSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:TIGR02203 423 ANNIAYGR-------TEQADRAEIERALAAAYAQDFVDK-LPLgldtpigengvlLSGGQRQRLAIARALLKDAPILILD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 161 EPLNNLDMKHAmgmmKLMQRACHEL--GKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDII 224
Cdd:TIGR02203 495 EATSALDNESE----RLVQAALERLmqGRTTLVIAHRLSTIE-KADRIVVMDDGRIVERGTHNELL 555
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-214 |
2.01e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 88.93 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNT-PSDvlaRRLSILRQDN 84
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVpPAE---RGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 HMTARLTVADLVAFGRypyskgRLTIEDKAHIDQSI----AYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:PRK11000 85 ALYPHLSVAENMSFGL------KLAGAKKEEINQRVnqvaEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 161 EPLNNLDMKHAMGM----MKLMQRacheLGKTVVLVLHDINFASWYSDYIIAMKNGRV 214
Cdd:PRK11000 159 EPLSNLDAALRVQMrieiSRLHKR----LGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
13-229 |
2.24e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.48 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVsnTPSDV--LARRLSILRQ--DNHMTA 88
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL--TEENVwdIRHKIGMVFQnpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 89 RlTVADLVAFGRYpySKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDM 168
Cdd:PRK13650 97 A-TVEDDVAFGLE--NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 169 KHAMGMMKLMQRACHELGKTVVLVLHDINFASwYSDYIIAMKNGRVirhgtkNDIITPEAL 229
Cdd:PRK13650 174 EGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV------ESTSTPREL 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-228 |
2.30e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.94 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 17 VDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPS----DVLARRLSILRQDNHMTARLTV 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrEVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 93 ADLVAFGRypYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAM 172
Cdd:PRK10070 124 LDNTAFGM--ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 173 GMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEA 228
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-225 |
2.49e-20 |
|
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: 89.71 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARlT 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 92 VADLVA-FGRYPYSKGRLTIEDKAHIDQSIayLNLDDLRDRFLDE----LSGGQRQRAFVAMVLCQDTDYVLLDEPLNNL 166
Cdd:TIGR01842 408 VAENIArFGENADPEKIIEAAKLAGVHELI--LRLPDGYDTVIGPggatLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 167 DMKHAMGMMKLMQRAcHELGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDIIT 225
Cdd:TIGR01842 486 DEEGEQALANAIKAL-KARGITVVVITHRPSLLG-CVDKILVLQDGRIARFGERDEVLA 542
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-223 |
3.42e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.35 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETAVvDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSdvLARRLSILRQDNHMT 87
Cdd:PRK11607 27 KSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQSYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 88 ARLTVADLVAFGrypYSKGRLT-IEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNL 166
Cdd:PRK11607 104 PHMTVEQNIAFG---LKQDKLPkAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 167 DMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:PRK11607 181 DKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-232 |
4.00e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.78 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGS---VTVDGLDV-SNTPSDVlARRLSILRQ--DNHM 86
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLtAKTVWDI-REKVGIVFQnpDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 87 TARlTVADLVAFG----RYPYSKgRLTIedkahIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEP 162
Cdd:PRK13640 98 VGA-TVGDDVAFGlenrAVPRPE-MIKI-----VRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 163 LNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDIIT-PEALKDI 232
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSkVEMLKEI 240
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-223 |
4.07e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.55 E-value: 4.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYY----GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPsdvlARR 76
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALS----EKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 77 LSILRQD--------NHMTARlTVADLVAFgryPyskgrLTIE--DKAHIDQSIAYL----NLDDLRDRFLDELSGGQRQ 142
Cdd:PRK11153 77 LRKARRQigmifqhfNLLSSR-TVFDNVAL---P-----LELAgtPKAEIKARVTELlelvGLSDKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 143 RAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKND 222
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
.
gi 351592836 223 I 223
Cdd:PRK11153 228 V 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-225 |
4.80e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.54 E-value: 4.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELpARG-ITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVS-NTPSDVLARRLSILRQ 82
Cdd:COG1129 8 RGISKSFGGVKALDGVSLEL-RPGeVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQAAGIAIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 83 DNHMTARLTVADLVAFGRYPYSKGRltIEDKAHIDQS---IAYLNLD-DLRDRfLDELSGGQRQrafvaMV-----LCQD 153
Cdd:COG1129 87 ELNLVPNLSVAENIFLGREPRRGGL--IDWRAMRRRArelLARLGLDiDPDTP-VGDLSVAQQQ-----LVeiaraLSRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 154 TDYVLLDEPLNNLDMKHAMGMMKLMQRAChELGKTVVLVLHDIN--FAswYSDYIIAMKNGRVIRHG-----TKNDIIT 225
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLK-AQGVAIIYISHRLDevFE--IADRVTVLRDGRLVGTGpvaelTEDELVR 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
9-238 |
6.51e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 85.96 E-value: 6.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 9 KYYGETA-VVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQ--DNH 85
Cdd:PRK13648 16 QYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQnpDNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 86 MTARlTVADLVAFG----RYPYskgrltieDKAH--IDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLL 159
Cdd:PRK13648 96 FVGS-IVKYDVAFGlenhAVPY--------DEMHrrVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 160 DEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDIITP-EALKDI-----Y 233
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM-EADHVIVMNKGTVYKEGTPTEIFDHaEELTRIgldlpF 245
|
....*
gi 351592836 234 DMDIN 238
Cdd:PRK13648 246 PIKIN 250
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-229 |
1.12e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.83 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVsntPSDV--------LARRLSI 79
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI---PANLkkikevkrLRKEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQ-DNHMTARLTVADLVAFGryPYSKGrltiEDKAHIDQSIA-YLNLDDLRDRFLD----ELSGGQRQRAFVAMVLCQD 153
Cdd:PRK13645 95 VFQfPEYQLFQETIEKDIAFG--PVNLG----ENKQEAYKKVPeLLKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 154 TDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEAL 229
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-223 |
1.17e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 84.85 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNH 85
Cdd:COG4598 13 DLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVPADRRQLQR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 86 MTARL-------------TVADLVAFGryP-YSKGRltieDKAH-IDQSIAYLN---LDDLRDRFLDELSGGQRQRAFVA 147
Cdd:COG4598 93 IRTRLgmvfqsfnlwshmTVLENVIEA--PvHVLGR----PKAEaIERAEALLAkvgLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 148 MVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMqRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVM-RDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-218 |
1.48e-19 |
|
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: 83.13 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNtpsdvlarrlsilrqdnhmtARLTV 92
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD--------------------LEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 93 ADLVAFgrypyskgrltiedkahIDQSIaYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAM 172
Cdd:cd03247 74 SSLISV-----------------LNQRP-YLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 351592836 173 GMMKLMqrACHELGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHG 218
Cdd:cd03247 136 QLLSLI--FEVLKDKTLIWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-227 |
1.91e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.44 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMD-----AGSVTVDGLDVSNTPSDVLARRLSI---LR 81
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTVDLRKEIgmvFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 QDNHMTarLTVADLVAFGRypyskgRLT-IEDKAHIDQ----SIAYLNL-DDLRDRFLDE---LSGGQRQRAFVAMVLCQ 152
Cdd:PRK14239 94 QPNPFP--MSIYENVVYGL------RLKgIKDKQVLDEavekSLKGASIwDEVKDRLHDSalgLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 153 DTDYVLLDEPLNNLDMKHAmGMmklMQRACHELGK--TVVLVLHDINFASWYSDYIIAMKNGRVIRHG-TKNDIITPE 227
Cdd:PRK14239 166 SPKIILLDEPTSALDPISA-GK---IEETLLGLKDdyTMLLVTRSMQQASRISDRTGFFLDGDLIEYNdTKQMFMNPK 239
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
8-223 |
2.08e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 85.67 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSN-TPSDvlaRRLSILRQdN-- 84
Cdd:PRK11650 11 KSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElEPAD---RDIAMVFQ-Nya 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 ---HMTarltVADLVAFGRypysKGRLTieDKAHIDQSIAY----LNLDDLRDRFLDELSGGQRQRafVAM--VLCQDTD 155
Cdd:PRK11650 87 lypHMS----VRENMAYGL----KIRGM--PKAEIEERVAEaariLELEPLLDRKPRELSGGQRQR--VAMgrAIVREPA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 156 YVLLDEPLNNLDMKHAMGM---MKLMQRachELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVQMrleIQRLHR---RLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-232 |
2.26e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 84.71 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTP---SDVLARRLSILRQDNHMTAR 89
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSDIRKKVGLVFQYPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 90 LTVADLVAFGRYPYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMK 169
Cdd:PRK13637 99 ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 170 HAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITP-EALKDI 232
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEvETLESI 242
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-232 |
3.15e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.75 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYG-----ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSV----------TVDGLDVS 66
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 67 NTPSDVLAR-RLSILRQDNHMTARL--------------TVADLVAFGryPYSKGrltIEDKAHIDQSIAYLNLDDLRDR 131
Cdd:PRK13651 83 VLEKLVIQKtRFKKIKKIKEIRRRVgvvfqfaeyqlfeqTIEKDIIFG--PVSMG---VSKEEAKKRAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 132 FLD----ELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRaCHELGKTVVLVLHDINFASWYSDYII 207
Cdd:PRK13651 158 YLQrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDN-LNKQGKTIILVTHDLDNVLEWTKRTI 236
|
250 260
....*....|....*....|....*
gi 351592836 208 AMKNGRVIRHGTkndiiTPEALKDI 232
Cdd:PRK13651 237 FFKDGKIIKDGD-----TYDILSDN 256
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
10-232 |
3.40e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.27 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNtPSDVLARR--LSILRQ--DNH 85
Cdd:PRK13644 11 YPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGD-FSKLQGIRklVGIVFQnpETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 86 MTARlTVADLVAFGryPYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNN 165
Cdd:PRK13644 90 FVGR-TVEEDLAFG--PENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 166 LDMKHAMGMMKLMQRaCHELGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDIITPEALKDI 232
Cdd:PRK13644 167 LDPDSGIAVLERIKK-LHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-168 |
5.62e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.50 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 4 TSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVdgldvsntPSDVlarRLSILRQD 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGL---RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 84 NHMTARLTVADLVAFGRYPYSKgrlTIEDKAHIDQSIAYLN-----LDDLRDRF-------------------------- 132
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRA---LEAELEELEAKLAEPDedlerLAELQEEFealggweaearaeeilsglgfpeedl 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 351592836 133 ---LDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDM 168
Cdd:COG0488 147 drpVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
9-229 |
6.98e-19 |
|
type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain] Cd Length: 694 Bit Score: 85.56 E-value: 6.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 9 KYYGETAVV-DDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMT 87
Cdd:TIGR01846 464 RYAPDSPEVlSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLF 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 88 ARlTVADLVAFGRyPyskgRLTIEDKAHIDQ-SIAYLNLDDLRDRF---LDE----LSGGQRQRAFVAMVLCQDTDYVLL 159
Cdd:TIGR01846 544 SR-SIRDNIALCN-P----GAPFEHVIHAAKlAGAHDFISELPQGYnteVGEkganLSGGQRQRIAIARALVGNPRILIF 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 160 DEPLNNLDMKHAMGMMKLMQRACHelGKTVVLVLHDINfASWYSDYIIAMKNGRVIRHGTKNDIITPEAL 229
Cdd:TIGR01846 618 DEATSALDYESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELLALQGL 684
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-215 |
1.00e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 81.93 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 3 ITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLL---GMDAGSVTVDGLDVSntpSDVLARRLSI 79
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRK---PDQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQDNHMTARLTVADLVAF-----GRYPYSKGRLTIEDKahiDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDT 154
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYtailrLPRKSSDAIRKKRVE---DVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 155 DYVLLDEPLNNLDMKHAMGMMKLMQRACHElGKTVVLVLH----DInFASWysDYIIAMKNGRVI 215
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHqprsDL-FRLF--DRILLLSSGEIV 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-219 |
1.11e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 7 IKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVT-VDGLDVSNTPSDVLARRLSILR---- 81
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGShIELLGRTVQREGRLARDIRKSRantg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 ---QDNHMTARLTVADLV---AFGRYPYSKGRL---TIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQ 152
Cdd:PRK09984 90 yifQQFNLVNRLSVLENVligALGSTPFWRTCFswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 153 DTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGT 219
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-223 |
1.14e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.24 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYY--------GETAV---VDDVSIELpARGIT-SIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTP 69
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgRTVGVvkaVDGVSFDI-RRGETlGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 70 SDVLA---RRLSILRQD-----NhmtARLTVADLVAFGrypyskgrL---TIEDKAHIDQSIAYLnLD------DLRDRF 132
Cdd:COG4608 87 GRELRplrRRMQMVFQDpyaslN---PRMTVGDIIAEP--------LrihGLASKAERRERVAEL-LElvglrpEHADRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 133 LDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDM---KHAMGMMKLMQRachELGKTVVLVLHDINFASWYSDYIIAM 209
Cdd:COG4608 155 PHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVsiqAQVLNLLEDLQD---ELGLTYLFISHDLSVVRHISDRVAVM 231
|
250
....*....|....
gi 351592836 210 KNGRVIRHGTKNDI 223
Cdd:COG4608 232 YLGKIVEIAPRDEL 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
13-252 |
1.16e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.91 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARrlsilrqdnhmTARLTV 92
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIR-----------PVRKRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 93 AdlVAFgRYPYSKgrlTIEDKahIDQSIAY------LNLDDLRDRFLD-----------------ELSGGQRQRAFVAMV 149
Cdd:PRK13646 88 G--MVF-QFPESQ---LFEDT--VEREIIFgpknfkMNLDEVKNYAHRllmdlgfsrdvmsqspfQMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 150 LCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITpeAL 229
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK--DK 237
|
250 260
....*....|....*....|...
gi 351592836 230 KDIYDMDINVHEIgghrVSLFYD 252
Cdd:PRK13646 238 KKLADWHIGLPEI----VQLQYD 256
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-224 |
1.37e-18 |
|
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: 84.41 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLsivsRLL-GM---DAGSVTVDGLDVSNTPSDVLARRLSILRQDnhmt 87
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA----RLLvGVwppTAGSVRLDGADLSQWDREELGRHIGYLPQD---- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 88 ARL---TVADLVAfgRYPYSKGRLTIE--DKAHIDQSIayLNLDDLRDRFLDE----LSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:COG4618 415 VELfdgTIAENIA--RFGDADPEKVVAaaKLAGVHEMI--LRLPDGYDTRIGEggarLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 159 LDEPLNNLDmkhAMGMMKLMQ--RACHELGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDII 224
Cdd:COG4618 491 LDEPNSNLD---DEGEAALAAaiRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
3-212 |
1.47e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 81.22 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 3 ITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSV---TVDGLDVSNTPSDVLARRLSI 79
Cdd:cd03290 3 VTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQDNHMTARLTVADLVAFGRyPYSKGRL-TIEDKAHIDQSIAYLNLDD---LRDRFLDeLSGGQRQRAFVAMVLCQDTD 155
Cdd:cd03290 83 YAAQKPWLLNATVEENITFGS-PFNKQRYkAVTDACSLQPDIDLLPFGDqteIGERGIN-LSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 156 YVLLDEPLNNLDM---KHAM--GMMKLMQrachELGKTVVLVLHDINFASwYSDYIIAMKNG 212
Cdd:cd03290 161 IVFLDDPFSALDIhlsDHLMqeGILKFLQ----DDKRTLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-221 |
1.84e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.75 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 4 TSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGM-----DAGSVTVDGLDVSNTPSDVLA--RR 76
Cdd:PRK14243 13 TENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDVDPVEvrRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 77 LSILRQDNHMTARlTVADLVAFG-RYPYSKGRLTIEDKAHIDQSIAYlnlDDLRDRFLDE---LSGGQRQRAFVAMVLCQ 152
Cdd:PRK14243 93 IGMVFQKPNPFPK-SIYDNIAYGaRINGYKGDMDELVERSLRQAALW---DEVKDKLKQSglsLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 153 DTDYVLLDEPLNNLDMKHAMGMMKLMqracHELGK--TVVLVLHDINFASWYSDYiIAMKNGRVIRHGTKN 221
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELM----HELKEqyTIIIVTHNMQQAARVSDM-TAFFNVELTEGGGRY 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-223 |
1.91e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.98 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDG--LDVSNTPSDVLARRLS 78
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 79 ILRQDNHMTARLTVADL-VAFGRypYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYV 157
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSdIAFSL--RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 158 LLDEPLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-218 |
2.01e-18 |
|
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: 80.29 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVS-RLLGM-DAGSVTVDGldvSNTPSDVLARRLSILRQDNHMTAR 89
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLgVSGEVLING---RPLDKRSFRKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 90 LTVadlvafgrypyskgRLTIEDKAHIDQsiaylnlddlrdrfldeLSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMK 169
Cdd:cd03213 97 LTV--------------RETLMFAAKLRG-----------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 351592836 170 HAMGMMKLMQRACHElGKTVVLVLH-----DINFAswysDYIIAMKNGRVIRHG 218
Cdd:cd03213 146 SALQVMSLLRRLADT-GRTIICSIHqpsseIFELF----DKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
13-229 |
2.05e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 82.59 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDglDVSNTPSDVLARRLSILRQ---DNHMTAR 89
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG--DIYIGDKKNNHELITNPYSkkiKNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 90 LTVADLVAFGRYPYSKGrlTIED------------KAHIDQSIA-YLNLDDLRDRFLD----ELSGGQRQRAFVAMVLCQ 152
Cdd:PRK13631 116 RRVSMVFQFPEYQLFKD--TIEKdimfgpvalgvkKSEAKKLAKfYLNKMGLDDSYLErspfGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 153 DTDYVLLDEPLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEAL 229
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-219 |
2.28e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 81.74 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvSNTPSdvLAR--------RLSILRQD 83
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG---ENIPA--MSRsrlytvrkRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 84 NHMTARLTVADLVAF-----GRYPYSKGRLTIEDKahidqsIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:PRK11831 93 GALFTDMNVFDNVAYplrehTQLPAPLLHSTVMMK------LEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 159 LDEPLNNLDmKHAMG-MMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGT 219
Cdd:PRK11831 167 FDEPFVGQD-PITMGvLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGS 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-215 |
2.34e-18 |
|
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: 81.78 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 4 TSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSN-TPSDVLA--RRLSIL 80
Cdd:TIGR02769 14 TGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQlDRKQRRAfrRDVQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNH--MTARLTVADLVafgRYPYSkgRLTIEDKAHIDQSIAY-LNLDDLRDRFLD----ELSGGQRQRAFVAMVLCQD 153
Cdd:TIGR02769 94 FQDSPsaVNPRMTVRQII---GEPLR--HLTSLDESEQKARIAElLDMVGLRSEDADklprQLSGGQLQRINIARALAVK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 154 TDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVI 215
Cdd:TIGR02769 169 PKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-233 |
2.56e-18 |
|
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: 81.05 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 16 VVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARlTVADL 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDG-TIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 96 VAFGRYPyskgrLTIED------KAHIDQSIAylnldDLRDRFLDE-------LSGGQRQRAFVAMVLCQDTDYVLLDEP 162
Cdd:cd03249 97 IRYGKPD-----ATDEEveeaakKANIHDFIM-----SLPDGYDTLvgergsqLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351592836 163 LNNLDMKHAmgmmKLMQRACHEL--GKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDIItpeALKDIY 233
Cdd:cd03249 167 TSALDAESE----KLVQEALDRAmkGRTTIVIAHRLSTIR-NADLIAVLQNGQVVEQGTHDELM---AQKGVY 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-206 |
4.98e-18 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 82.68 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTV-------------DGLDVSNT 68
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayvdqsrDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 69 PSDVLARRLSILRQDNH-MTARLTVadlvafGRYPYSKGrltiedkahiDQSiaylnlddlrdRFLDELSGGQRQRAFVA 147
Cdd:TIGR03719 403 VWEEISGGLDIIKLGKReIPSRAYV------GRFNFKGS----------DQQ-----------KKVGQLSGGERNRVHLA 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 148 MVLCQDTDYVLLDEPLNNLDMKhamgMMKLMQRACHELGKTVVLVLHDinfaSWYSDYI 206
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVE----TLRALEEALLNFAGCAVVISHD----RWFLDRI 506
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-225 |
5.02e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.85 E-value: 5.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDaGSVTVDGlDVSNTPSDVLARRLSI--LRQDNHMT 87
Cdd:PRK14258 16 YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEG-RVEFFNQNIYERRVNLnrLRRQVSMV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 88 AR------LTVADLVAFG-RYPYSKGRLTIEDKahIDQSIAYLNL-DDLRDRFLD---ELSGGQRQRAFVAMVLCQDTDY 156
Cdd:PRK14258 94 HPkpnlfpMSVYDNVAYGvKIVGWRPKLEIDDI--VESALKDADLwDEIKHKIHKsalDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 157 VLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKN-----GRVIRHGTKNDIIT 225
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFN 245
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
9-232 |
9.44e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.14 E-value: 9.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 9 KYYGETAV--VDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQ--DN 84
Cdd:PRK13642 13 KYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQnpDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 HMTARlTVADLVAFGRYpySKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLN 164
Cdd:PRK13642 93 QFVGA-TVEDDVAFGME--NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 165 NLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDII-TPEALKDI 232
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAPSELFaTSEDMVEI 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-229 |
1.21e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.61 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVS-NTPSDvlARRLSI--LRQ 82
Cdd:COG3845 10 GITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRD--AIALGIgmVHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 83 dnHMT--ARLTVADLVAFGRYPYSKGRLtieDKAHIDQSIAYL----NLD-DLrDRFLDELSGGQRQRAFVAMVLCQDTD 155
Cdd:COG3845 88 --HFMlvPNLTVAENIVLGLEPTKGGRL---DRKAARARIRELseryGLDvDP-DAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 156 YVLLDEPLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDiITPEAL 229
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE-TSEEEL 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-214 |
1.67e-17 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 78.67 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARlTV 92
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 93 ADLVAFGRYPYSKGRLT-IEDKAHIDQSIAYLNL--DDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMK 169
Cdd:cd03248 105 QDNIAYGLQSCSFECVKeAAQKAHAHSFISELASgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 351592836 170 HAMGMMKLMQrACHElGKTVVLVLHDINFASwYSDYIIAMKNGRV 214
Cdd:cd03248 185 SEQQVQQALY-DWPE-RRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-216 |
1.73e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.31 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYY----GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLA--RR-- 76
Cdd:PRK10535 8 KDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlRReh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 77 LSILRQDNHMTARLTVADLVAFGRYPYSKGRLTIEDKAHidQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDY 156
Cdd:PRK10535 88 FGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQ--ELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 157 VLLDEPLNNLDMKHAMGMMKLMQRAChELGKTVVLVLHDINFASwYSDYIIAMKNGRVIR 216
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAA-QAERVIEIRDGEIVR 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-215 |
2.16e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTV-------------DGLDVSN 67
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgetvkigyfdqhqEELDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 68 TPSDVLARrlsILRQDNHMTARLTVADlvaFGRYPyskgrltiedkAHIDQSIAylnlddlrdrfldELSGGQRQRAFVA 147
Cdd:COG0488 395 TVLDELRD---GAPGGTEQEVRGYLGR---FLFSG-----------DDAFKPVG-------------VLSGGEKARLALA 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 148 MVLCQDTDYVLLDEPLNNLDMKhamgMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVI 215
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIE----TLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-219 |
8.42e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.78 E-value: 8.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 9 KYYGE----TAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLA----RRLSIL 80
Cdd:PRK11629 13 KRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVADLVAFGRYPYSKGRLTIEDKAHidQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRAL--EMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 161 EPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYiIAMKNGRVIRHGT 219
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDGRLTAELS 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-207 |
8.54e-17 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 79.06 E-value: 8.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 32 IIGPNGAGKSTMLSIVSRLLGMDAGSVTVDgLDVSNTPSdvlarrlsILRQDNHMTarltVADLVafgrypyskgRLTIE 111
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISYKPQ--------YISPDYDGT----VEEFL----------RSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 112 DKahIDQSIAY------LNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHEL 185
Cdd:COG1245 428 DD--FGSSYYKteiikpLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENR 505
|
170 180
....*....|....*....|..
gi 351592836 186 GKTVVLVLHDINFASWYSDYII 207
Cdd:COG1245 506 GKTAMVVDHDIYLIDYISDRLM 527
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
7-218 |
1.33e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.99 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 7 IKKYYGETAVvdDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDV-LA---RRLSILRQ 82
Cdd:PRK11144 6 FKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIcLPpekRRIGYVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 83 DnhmtARLtvadlvafgrYP-YS-KGRLTI----EDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDY 156
Cdd:PRK11144 84 D----ARL----------FPhYKvRGNLRYgmakSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 157 VLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-194 |
1.48e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.61 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTpSDVLARRLSILRQDNHMTARLT 91
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ-RDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 92 VADLVAFGRypyskgrlTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDmkhA 171
Cdd:cd03231 90 VLENLRFWH--------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD---K 158
|
170 180
....*....|....*....|....*
gi 351592836 172 MGMMKLMQR-ACH-ELGKTVVLVLH 194
Cdd:cd03231 159 AGVARFAEAmAGHcARGGMVVLTTH 183
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-224 |
1.55e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 78.52 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARlTV 92
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFND-TI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 93 ADLVAFGRYP-YSkgRLTIEDKAHIDQSIAYLN-LDDLRDRFLDE----LSGGQRQRAFVAMVLCQDTDYVLLDEPLNNL 166
Cdd:PRK11176 434 ANNIAYARTEqYS--REQIEEAARMAYAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 167 DMKHAmgmmKLMQRACHELGK--TVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDII 224
Cdd:PRK11176 512 DTESE----RAIQAALDELQKnrTSLVIAHRLSTIE-KADEILVVEDGEIVERGTHAELL 566
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-214 |
2.45e-16 |
|
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: 74.17 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARlT 91
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSG-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 92 VADLVafgrypyskgrltiedkahidqsiaylnlddlrdrfldeLSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMK-- 169
Cdd:cd03246 92 IAENI---------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEge 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 351592836 170 ----HAMGMMKLMqrachelGKTVVLVLHDINFASwYSDYIIAMKNGRV 214
Cdd:cd03246 133 ralnQAIAALKAA-------GATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-223 |
2.62e-16 |
|
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: 77.80 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETAVVDDVSIELPaRGIT-SIIGPNGAGKSTM-LSIVsRLLGmDAGSVTVDGLDVSNTPSDVLA---RRLSILRQ 82
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLR-RGETlGLVGESGSGKSTLgLALL-RLIP-SEGEIRFDGQDLDGLSRRALRplrRRMQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 83 D--NHMTARLTVADLVAFGrypyskgrLTI----EDKAHIDQSIAYL----NLD-DLRDRFLDELSGGQRQRAFVA--MV 149
Cdd:COG4172 370 DpfGSLSPRMTVGQIIAEG--------LRVhgpgLSAAERRARVAEAleevGLDpAARHRYPHEFSGGQRQRIAIAraLI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 150 LcqDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:COG4172 442 L--EPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-223 |
3.41e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.41 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRlSILR--Q 82
Cdd:PRK11300 9 SGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVRtfQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 83 DNHMTARLTVAD--LVAFGRY---PYSKGRLTI------EDKAhIDQSIAYL---NLDDLRDRFLDELSGGQRQRAFVAM 148
Cdd:PRK11300 88 HVRLFREMTVIEnlLVAQHQQlktGLFSGLLKTpafrraESEA-LDRAATWLervGLLEHANRQAGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 149 VLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-224 |
3.77e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.15 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYY-----GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTV----DGLDVSNTPSD 71
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 72 VLARR---LSILRQDNHMTARLTVADLV--AFG-RYPYSKGRLtiedKAHIDQSIAYLNLDDLR---DRFLDELSGGQRQ 142
Cdd:TIGR03269 359 GRGRAkryIGILHQEYDLYPHRTVLDNLteAIGlELPDELARM----KAVITLKMVGFDEEKAEeilDKYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 143 RAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKND 222
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
..
gi 351592836 223 II 224
Cdd:TIGR03269 515 IV 516
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-194 |
4.66e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvSNTPSDVLARRLSILRQDNHMTARLT 91
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 92 VADLVAFGRYPYSKGRLTIEDkahidqSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDmKHA 171
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIAA------ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD-AAA 162
|
170 180
....*....|....*....|....*
gi 351592836 172 MGMMK-LMQRacH-ELGKTVVLVLH 194
Cdd:PRK13539 163 VALFAeLIRA--HlAQGGIVIAATH 185
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-207 |
4.89e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.16 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 32 IIGPNGAGKSTMLSIVSRLLGMDAGSVTVDgLDVSNTPSDVLArrlsilrqDNHMTarltVADLVAfgrypyskgrlTIE 111
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKPQYIKP--------DYDGT----VEDLLR-----------SIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 112 DKahIDQSIAY------LNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHEL 185
Cdd:PRK13409 426 DD--LGSSYYKseiikpLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER 503
|
170 180
....*....|....*....|..
gi 351592836 186 GKTVVLVLHDINFASWYSDYII 207
Cdd:PRK13409 504 EATALVVDHDIYMIDYISDRLM 525
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-213 |
7.32e-16 |
|
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: 73.66 E-value: 7.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 16 VVDDVSIELPARGITSIIGPNGAGKSTMLSIvsrLLG-MDA--GSVTVDGLD--VSNTPSdvlarrlsilrqdnHMTArl 90
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSA---LLGeLEKlsGSVSVPGSIayVSQEPW--------------IQNG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 TVADLVAFGrYPYSKGRL--TIEDKAhIDQSIAYLNLDDLrdrflDE-------LSGGQRQRAFVAMVLCQDTDYVLLDE 161
Cdd:cd03250 81 TIRENILFG-KPFDEERYekVIKACA-LEPDLEILPDGDL-----TEigekginLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 162 PLNNLD-------MKHA-MGMMKlmqracheLGKTVVLVLHDINFAsWYSDYIIAMKNGR 213
Cdd:cd03250 154 PLSAVDahvgrhiFENCiLGLLL--------NNKTRILVTHQLQLL-PHADQIVVLDNGR 204
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-215 |
7.39e-16 |
|
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: 74.01 E-value: 7.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETA----VVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSD----V 72
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDararL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 73 LARRLSILRQDNHMTARLTVADLVAfgrypyskgrLTIEDKAHID---QSIAYLN---LDDLRDRFLDELSGGQRQ---- 142
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVM----------LPLELAGRRDaraRARALLErvgLGHRLDHYPAQLSGGEQQrval 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 143 -RAFVAmvlcqDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASwYSDYIIAMKNGRVI 215
Cdd:COG4181 158 aRAFAT-----EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLV 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-219 |
8.45e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.42 E-value: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 20 VSIELPARGITSIIGPNGAGKSTMLSIvsrLLGMDA--GSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARlTVADLVA 97
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNA---LLGFLPyqGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG-TLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 98 FGRYPYSKGRL-TIEDKAHIDQSIAYLN--LD-DLRDRFLDeLSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMG 173
Cdd:PRK11174 445 LGNPDASDEQLqQALENAWVSEFLPLLPqgLDtPIGDQAAG-LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 351592836 174 MMKLMQRACHelGKTVVLVLHDINF-ASWysDYIIAMKNGRVIRHGT 219
Cdd:PRK11174 524 VMQALNAASR--RQTTLMVTHQLEDlAQW--DQIWVMQDGQIVQQGD 566
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-210 |
1.02e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.45 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLL--GMDAGSVTVDgldvsntpsdvlarrlsilrqDNHMTARL 90
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP---------------------DNQFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 TVADlvAFGRypyskgrltiedKAHIDQSIAYLNLDDLRDRFL-----DELSGGQRQRAFVAMVLCQDTDYVLLDEPLNN 165
Cdd:COG2401 101 SLID--AIGR------------KGDFKDAVELLNAVGLSDAVLwlrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 351592836 166 LDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMK 210
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFV 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-206 |
1.46e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 75.59 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 25 PARG-ITSIIGPNGAGKSTMLSIVSRLLGMDAGsvtvdglDVSNTPS--DVLAR-RLSILRqdNHMTA----RLTVA--- 93
Cdd:COG1245 96 PKKGkVTGILGPNGIGKSTALKILSGELKPNLG-------DYDEEPSwdEVLKRfRGTELQ--DYFKKlangEIKVAhkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 94 ---DLVAfgryPYSKGRL-----TIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNN 165
Cdd:COG1245 167 qyvDLIP----KVFKGTVrelleKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 351592836 166 LDMKHAMGMMKLMQRAChELGKTVVLVLHDINFASWYSDYI 206
Cdd:COG1245 243 LDIYQRLNVARLIRELA-EEGKYVLVVEHDLAILDYLADYV 282
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-167 |
1.95e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.16 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTV-------------DGLDVSNT 68
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvklayvdqsrDALDPNKT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 69 PSDVLARRLSILRQDNH-MTARLTVAdlvAFGrypySKGRltiedkahiDQSiaylnlddlrdRFLDELSGGQRQRAFVA 147
Cdd:PRK11819 405 VWEEISGGLDIIKVGNReIPSRAYVG---RFN----FKGG---------DQQ-----------KKVGVLSGGERNRLHLA 457
|
170 180
....*....|....*....|
gi 351592836 148 MVLCQDTDYVLLDEPLNNLD 167
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLD 477
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
2.12e-15 |
|
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: 70.94 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVdgldvsntpsdvlarrlsilr 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 qdnhmtarltvadlvafgrypyskgrltiedkaHIDQSIAYLnlddlrdrflDELSGGQRQRAFVAMVLCQDTDYVLLDE 161
Cdd:cd03221 60 ---------------------------------GSTVKIGYF----------EQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 351592836 162 PLNNLDMKHAmgmmKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGR 213
Cdd:cd03221 97 PTNHLDLESI----EALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-225 |
2.31e-15 |
|
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: 75.11 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKS-TMLSIVsRLL----GMDAGSVTVDGLDVSNTPSDVLAR----RLSILRQ 82
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLpdpaAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 83 DNhMTArLTvadlvafgryPYskgrLTIED--------------KAHIDQSIAYLNLDDLRD--RFLD----ELSGGQRQ 142
Cdd:COG4172 100 EP-MTS-LN----------PL----HTIGKqiaevlrlhrglsgAAARARALELLERVGIPDpeRRLDayphQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 143 RAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKND 222
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
...
gi 351592836 223 IIT 225
Cdd:COG4172 244 LFA 246
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-233 |
2.38e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.99 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARR-LSI 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQDNHMTARLTVADLVAFGRYpyskgrltIEDKAHIDQSIA-----YLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDT 154
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGF--------FAERDQFQERIKwvyelFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 155 DYVLLDEPLNNLDMKHAMGMMKLMQRaCHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPEALKDIY 233
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQ-LREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-219 |
3.23e-15 |
|
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: 72.14 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 16 VVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHM---TARltv 92
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLfsgTIR--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 93 ADLVAFGRYPYSKGRLTIED---KAHIDQSIAYLNLDDLRDRflDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMK 169
Cdd:cd03244 96 SNLDPFGEYSDEELWQALERvglKEFVESLPGGLDTVVEEGG--ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 351592836 170 HAMGMMKLMQRACHelGKTVVLVLHDINfASWYSDYIIAMKNGRVIRHGT 219
Cdd:cd03244 174 TDALIQKTIREAFK--DCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-218 |
4.16e-15 |
|
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: 71.79 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvsnTPSDVLARRLSIlrqDNHMT 87
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----RVSSLLGLGGGF---NPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 88 ARltvaDLVAF-GRYpysKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQR-AFvAMVLCQDTDYVLLDEPLNN 165
Cdd:cd03220 101 GR----ENIYLnGRL---LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARlAF-AIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 166 LD---MKHAMGMMKLMQRAchelGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:cd03220 173 GDaafQEKCQRRLRELLKQ----GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-218 |
4.63e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.48 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 7 IKKYYGETaVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDV-SNTPSDVLARRLSILRQD-- 83
Cdd:PRK11264 10 VKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIRQLRQHvg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 84 ------NHMTARlTVADLVAFGryPY-SKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDY 156
Cdd:PRK11264 89 fvfqnfNLFPHR-TVLENIIEG--PViVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 157 VLLDEPLNNLDmKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:PRK11264 166 ILFDEPTSALD-PELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-214 |
5.86e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.44 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVS---NTPSDVLARRLSILRQDN 84
Cdd:PRK10908 9 KAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlkNREVPFLRRQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 HMTARLTVADLVAFgryPYSKGRLTIED-KAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPL 163
Cdd:PRK10908 89 HLLMDRTVYDNVAI---PLIIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 351592836 164 NNLDMKHAMGMMKLMQRAcHELGKTVVLVLHDINFASWYSDYIIAMKNGRV 214
Cdd:PRK10908 166 GNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-227 |
6.59e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 73.71 E-value: 6.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHM---TA 88
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLfsaTL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 89 R--LTVADlvafgrypyskgrltieDKAHIDQSIAYLN---LDDL--RDRFLD--------ELSGGQRQRAFVAMVLCQD 153
Cdd:PRK11160 431 RdnLLLAA-----------------PNASDEALIEVLQqvgLEKLleDDKGLNawlgeggrQLSGGEQRRLGIARALLHD 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 154 TDYVLLDEPLNNLDMKHAMGMMKLMqrACHELGKTVVLVLHDINfASWYSDYIIAMKNGRVIRHGTKNDIITPE 227
Cdd:PRK11160 494 APLLLLDEPTEGLDAETERQILELL--AEHAQNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELLAQQ 564
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-197 |
8.15e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.28 E-value: 8.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQdnhmTARL- 90
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQ----TPTLf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 --TVADLVAFgryPYSKGRLTIEDKAHIDqSIAYLNLDD-LRDRFLDELSGGQRQRA-------FVAMVLcqdtdyvLLD 160
Cdd:PRK10247 94 gdTVYDNLIF---PWQIRNQQPDPAIFLD-DLERFALPDtILTKNIAELSGGEKQRIslirnlqFMPKVL-------LLD 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 351592836 161 EPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDIN 197
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-224 |
1.22e-14 |
|
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: 72.85 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 16 VVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARlTVADL 95
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 96 VAFGrypySKGRLTIEDkahIDQSIAYLNLDDLRDRF-------LDE----LSGGQRQRAFVAMVLCQDTDYVLLDEPLN 164
Cdd:TIGR01193 568 LLLG----AKENVSQDE---IWAACEIAEIKDDIENMplgyqteLSEegssISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 165 NLDM----KHAMGMMKLMQrachelgKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDII 224
Cdd:TIGR01193 641 NLDTitekKIVNNLLNLQD-------KTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELL 696
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-225 |
1.93e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSN-TPSDVLARRLSI 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKlDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQDNHMTARLTVADLVAFGRYPYSK--GRLTIE-DKAHIDQSIAYLNLD---DLrDRFLDELSGGQRQRAFVAMVLCQD 153
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKvcGVNIIDwREMRVRAAMMLLRVGlkvDL-DEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 154 TDYVLLDEPLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNG-----RVIRHGTKNDIIT 225
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDVSNDDIVR 239
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-206 |
2.54e-14 |
|
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: 70.47 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 28 GITSIIGPNGAGKSTMLSIVsrllgmdAGSVTVDGLDVSNTPS--DVL-ARRLSILRqdNHMTaRLTVADLVAFGRYPY- 103
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKIL-------AGKLKPNLGKFDDPPDwdEILdEFRGSELQ--NYFT-KLLEGDVKVIVKPQYv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 104 ------SKGR----LTIEDKAH-IDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAM 172
Cdd:cd03236 97 dlipkaVKGKvgelLKKKDERGkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|....
gi 351592836 173 GMMKLMQRACHElGKTVVLVLHDINFASWYSDYI 206
Cdd:cd03236 177 NAARLIRELAED-DNYVLVVEHDLAVLDYLSDYI 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-206 |
4.13e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 25 PARG-ITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvsnTPSDVLAR-RLSILRqdNHMTA----RLTVA----- 93
Cdd:PRK13409 96 PKEGkVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEP-----SWDEVLKRfRGTELQ--NYFKKlyngEIKVVhkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 94 -DLVAfgryPYSKGRL-----TIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLD 167
Cdd:PRK13409 169 vDLIP----KVFKGKVrellkKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 351592836 168 MKHAMGMMKLMQrachEL--GKTVVLVLHDINFASWYSDYI 206
Cdd:PRK13409 245 IRQRLNVARLIR----ELaeGKYVLVVEHDLAVLDYLADNV 281
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-224 |
6.05e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.95 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDG-----LDVSntpsdvlarr 76
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvsalLELG---------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 77 lSILRQDnhmtarLTVADLVafgrypYSKGRL---TIED-KAHIDQSIAYLNLDDlrdrFLDE----LSGGQRQR-AFvA 147
Cdd:COG1134 97 -AGFHPE------LTGRENI------YLNGRLlglSRKEiDEKFDEIVEFAELGD----FIDQpvktYSSGMRARlAF-A 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 148 MVLCQDTDYVLLDEPLNNLD---MKHAMG-MMKLMQRachelGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:COG1134 159 VATAVDPDILLVDEVLAVGDaafQKKCLArIRELRES-----GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
.
gi 351592836 224 I 224
Cdd:COG1134 234 I 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-225 |
7.46e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.35 E-value: 7.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETaVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLG-----MDAGSVTVDGLDVSNTpSDVLA--RRLSILRQ 82
Cdd:PRK14271 31 FAGKT-VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRSIFNY-RDVLEfrRRVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 83 DNHMTARLTVADLVAFGRYPYSKGRLTIEDKAHIDQSIAYLnLDDLRDRFLD---ELSGGQRQRAFVAMVLCQDTDYVLL 159
Cdd:PRK14271 109 RPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGL-WDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 160 DEPLNNLDMKHAMGMMKLMQRACHELgkTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT 225
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-217 |
8.29e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 8.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDV--SNTpSDVLARRLSILRQD 83
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfAST-TAALAAGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 84 NHMTARLTVADLVAFGRYPYSKGRLTIED-KAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEP 162
Cdd:PRK11288 88 LHLVPEMTVAENLYLGQLPHKGGIVNRRLlNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 163 LNNLDMKHAMGMMKLMQRACHElGKTVVLVLH--DINFAswYSDYIIAMKNGRVIRH 217
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAE-GRVILYVSHrmEEIFA--LCDAITVFKDGRYVAT 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-219 |
1.56e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.69 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 32 IIGPNGAGKSTMLSIVS--RLLGMD-AGSVTVDGLDVSntpSDVLARRLSILRQDN----HMTAR--LTVADLVAFGRYP 102
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAfrSPKGVKgSGSVLLNGMPID---AKEMRAISAYVQQDDlfipTLTVRehLMFQAHLRMPRRV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 103 YSKGRltiedKAHIDQSIAYLNLDDLRD------RFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMK 176
Cdd:TIGR00955 133 TKKEK-----RERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQ 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 351592836 177 LMQRACHElGKTVVLVLH----DI--NFaswysDYIIAMKNGRVIRHGT 219
Cdd:TIGR00955 208 VLKGLAQK-GKTIICTIHqpssELfeLF-----DKIILMAEGRVAYLGS 250
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-223 |
1.73e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.19 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 15 AVVDDVSIELPARGITSIIGPNGAGKStmLSiVSRLLGM-------DAGSVTVDGLDVSntPSDVLARRLSILRQDN--- 84
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKS--LT-CAAALGIlpagvrqTAGRVLLDGKPVA--PCALRGRKIATIMQNPrsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 ----HMTARLTVADLVAFGRYPyskgrltieDKAHIDQSIAYLNLDDlRDRFLD----ELSGGQRQRAFVAMVLCQDTDY 156
Cdd:PRK10418 92 fnplHTMHTHARETCLALGKPA---------DDATLTAALEAVGLEN-AARVLKlypfEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 157 VLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-219 |
2.30e-13 |
|
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: 67.05 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 16 VVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARLTVADL 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 96 VAFGRYPYSK--GRLTIEDKAhidqsiaylnlddlrdrflDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAmg 173
Cdd:cd03369 103 DPFDEYSDEEiyGALRVSEGG-------------------LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD-- 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 351592836 174 mmKLMQRACHEL--GKTVVLVLHDINFASWYsDYIIAMKNGRVIRHGT 219
Cdd:cd03369 162 --ALIQKTIREEftNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-162 |
3.03e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.00 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTpsdvlARRLSILRQDN 84
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA-----RHRRAVCPRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 HM----------TarLTVADLVAFgrypysKGRLTIEDKAHIDQSIAYL----NLDDLRDRFLDELSGGQRQRafvaMVL 150
Cdd:NF033858 80 YMpqglgknlypT--LSVFENLDF------FGRLFGQDAAERRRRIDELlratGLAPFADRPAGKLSGGMKQK----LGL 147
|
170
....*....|....*.
gi 351592836 151 C----QDTDYVLLDEP 162
Cdd:NF033858 148 CcaliHDPDLLILDEP 163
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-196 |
3.87e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.06 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 11 YGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvsntpsdvlARRLSILRQDNHM--TA 88
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVPQKLYLdtTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 89 RLTVADLVAFgrYPYSKgrltiedKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDM 168
Cdd:PRK09544 83 PLTVNRFLRL--RPGTK-------KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
170 180
....*....|....*....|....*...
gi 351592836 169 KHAMGMMKLMQRACHELGKTVVLVLHDI 196
Cdd:PRK09544 154 NGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
29-219 |
1.27e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 67.05 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 29 ITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARlTVADLVAFGRYPYSKGRL 108
Cdd:TIGR00958 509 VVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSG-SVRENIAYGLTDTPDEEI 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 109 TIEDK-AHIDQSIAylNLDDLRDRFLDE----LSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRAch 183
Cdd:TIGR00958 588 MAAAKaANAHDFIM--EFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRA-- 663
|
170 180 190
....*....|....*....|....*....|....*.
gi 351592836 184 elGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGT 219
Cdd:TIGR00958 664 --SRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGT 696
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-223 |
2.05e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKS-TMLSIVSRLL--GMDAGSVTVDGLDVSNTPSDVL----ARRLSILRQDN 84
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAanGRIGGSATFNGREILNLPEKELnklrAEQISMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 hMTArLTvadlvafgryPYSK-GRLTIE--------DKAH-IDQSIAYLN---LDDLRDR---FLDELSGGQRQRAFVAM 148
Cdd:PRK09473 107 -MTS-LN----------PYMRvGEQLMEvlmlhkgmSKAEaFEESVRMLDavkMPEARKRmkmYPHEFSGGMRQRVMIAM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 149 VLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-223 |
2.50e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.37 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYY--------GETAV--VDDVSIELpARGIT-SIIGPNGAGKSTMlsivSRLLGM----DAGSVTVDGLDVSNTPS 70
Cdd:PRK11308 10 DLKKHYpvkrglfkPERLVkaLDGVSFTL-ERGKTlAVVGESGCGKSTL----ARLLTMietpTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 71 DvlARRLsiLRQDNHMTARLTVADLvafgrYPYSKGRLTIEDKAHI----------DQSIAYLNLDDLR----DRFLDEL 136
Cdd:PRK11308 85 E--AQKL--LRQKIQIVFQNPYGSL-----NPRKKVGQILEEPLLIntslsaaerrEKALAMMAKVGLRpehyDRYPHMF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 137 SGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIR 216
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVE 235
|
....*..
gi 351592836 217 HGTKNDI 223
Cdd:PRK11308 236 KGTKEQI 242
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-243 |
4.53e-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: 65.23 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLL--GMDAGSVTVDGLD-VSNTPSDVLARRLSILRQ 82
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPlKASNIRDTERAGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 83 DNHMTARLTVADLVAFGRYPYSKGRLTIED----KAHidQSIAYLNLDDLRD-RFLDELSGGQRQRAFVAMVLCQDTDYV 157
Cdd:TIGR02633 86 ELTLVPELSVAENIFLGNEITLPGGRMAYNamylRAK--NLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 158 LLDEPLNNLDMKHAMGMMKLMqRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVI-----RHGTKNDIITPEALKDI 232
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDII-RDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVatkdmSTMSEDDIITMMVGREI 242
|
250
....*....|..
gi 351592836 233 YDMDIN-VHEIG 243
Cdd:TIGR02633 243 TSLYPHePHEIG 254
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-166 |
1.29e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVS-NTPSDVLARRLSILRQD 83
Cdd:PRK10762 8 KGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 84 NHMTARLTVADLVAFGRYPYSK-GRLTIED-KAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDE 161
Cdd:PRK10762 88 LNLIPQLTIAENIFLGREFVNRfGRIDWKKmYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
....*
gi 351592836 162 PLNNL 166
Cdd:PRK10762 168 PTDAL 172
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-197 |
1.34e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.18 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 11 YGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDvsntPSD---VLARRLSI-------L 80
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV----PFKrrkEFARRIGVvfgqrsqL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDnhmtarLTVADLVAFGRYPYSkgrltIED---KAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYV 157
Cdd:COG4586 108 WWD------LPAIDSFRLLKAIYR-----IPDaeyKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 351592836 158 LLDEPLNNLD--MKHAmgMMKLMQRACHELGKTVVLVLHDIN 197
Cdd:COG4586 177 FLDEPTIGLDvvSKEA--IREFLKEYNRERGTTILLTSHDMD 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-215 |
1.43e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.78 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 4 TSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMlsivSRLL-GM---DAGSVTVDGLDVSN-TPSDVLARRLS 78
Cdd:PRK10419 15 HGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTL----ARLLvGLespSQGNVSWRGEPLAKlNRAQRKAFRRD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 79 I--LRQD--NHMTARLTVADLVafgRYPYsKGRLTIEDKAHIDQSIAYLNLDDLRDRFLD----ELSGGQRQRAFVAMVL 150
Cdd:PRK10419 91 IqmVFQDsiSAVNPRKTVREII---REPL-RHLLSLDKAERLARASEMLRAVDLDDSVLDkrppQLSGGQLQRVCLARAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 151 CQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVI 215
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-218 |
1.49e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 3 ITSGI-KKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGmDAGSVTVDGLDVSN-TPSDVLA--RRLS 78
Cdd:PRK15134 287 IRKGIlKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNlNRRQLLPvrHRIQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 79 ILRQD--NHMTARLTVADLVAFGRYPYSKGRLTIEDKAHIDQSIAYLNLD-DLRDRFLDELSGGQRQRAFVAMVLCQDTD 155
Cdd:PRK15134 366 VVFQDpnSSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 156 YVLLDEPLNNLD---MKHAMGMMKLMQRAcHELgkTVVLVLHDINFASWYSDYIIAMKNGRVIRHG 218
Cdd:PRK15134 446 LIILDEPTSSLDktvQAQILALLKSLQQK-HQL--AYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-233 |
2.62e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.19 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQdnhmTARL-- 90
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ----TPFLfs 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 -TVADLVAFGRYPYSKGRltIEDKAHidqsIAYLNLDDLR-----DRFLDE----LSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:PRK10789 403 dTVANNIALGRPDATQQE--IEHVAR----LASVHDDILRlpqgyDTEVGErgvmLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 161 EPLNNLDMKHAMGMMKLMQRACHelGKTVVLVLHDINfASWYSDYIIAMKNGRVIRHGTKNDIIT-PEALKDIY 233
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQqSGWYRDMY 547
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-227 |
4.23e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 32 IIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQdnhmtARLTVADLVAFGRYPYSK----GR 107
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQ-----SPVLFSGTVRFNIDPFSEhndaDL 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 108 LTIEDKAHIDQSIAY--LNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKhamgMMKLMQRACHEL 185
Cdd:PLN03232 1342 WEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR----TDSLIQRTIREE 1417
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 351592836 186 GK--TVVLVLHDINfASWYSDYIIAMKNGRVIRHGTKNDIITPE 227
Cdd:PLN03232 1418 FKscTMLVIAHRLN-TIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-224 |
5.59e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.90 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 9 KYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTA 88
Cdd:PRK13657 343 SYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 89 RlTVADLVAFGRYPYSKGRLtiEDKAHIDQSIAYLNLDDLR-DRFLDE----LSGGQRQRAFVAMVLCQDTDYVLLDEPL 163
Cdd:PRK13657 423 R-SIEDNIRVGRPDATDEEM--RAAAERAQAHDFIERKPDGyDTVVGErgrqLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 164 NNLDmkhAMGMMKLmQRACHEL--GKTVVLVLH---DINFAswysDYIIAMKNGRVIRHGTKNDII 224
Cdd:PRK13657 500 SALD---VETEAKV-KAALDELmkGRTTFIIAHrlsTVRNA----DRILVFDNGRVVESGSFDELV 557
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-194 |
7.28e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.82 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 29 ITSIIGPNGAGKSTML-SIVSRLLGMD-AGSVTVDGldvsNTPSDVLARRLSILRQDN----HMTARLTVAdLVAFGRYP 102
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLnALAGRIQGNNfTGTILANN----RKPTKQILKRTGFVTQDDilypHLTVRETLV-FCSLLRLP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 103 YSkgrLTIEDKAHIDQS-IAYLNLDD-----LRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMK 176
Cdd:PLN03211 171 KS---LTKQEKILVAESvISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170
....*....|....*...
gi 351592836 177 LMQRACHElGKTVVLVLH 194
Cdd:PLN03211 248 TLGSLAQK-GKTIVTSMH 264
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-219 |
1.05e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.50 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKStmlSIVSRLLG-MDA--GSVTVDGlDVSNTPSDVLARRLSILR------- 81
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKS---SLLSALLAeMDKveGHVHMKG-SVAYVPQQAWIQNDSLREnilfgka 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 -QDNHMTARLTVADLVAFGRYPYSKGRLTIEDKAhidqsiayLNLddlrdrfldelSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:TIGR00957 725 lNEKYYQQVLEACALLPDLEILPSGDRTEIGEKG--------VNL-----------SGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 161 EPLNNLD-------MKHAMGMMKLMQrachelGKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGT 219
Cdd:TIGR00957 786 DPLSAVDahvgkhiFEHVIGPEGVLK------NKTRILVTHGISYLP-QVDVIIVMSGGKISEMGS 844
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
12-220 |
1.30e-10 |
|
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: 59.08 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIvsrLLG-----MDAGSVTVDGLDVSNTPSDVLARrLSILrqdnhm 86
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKT---IMGhpkyeVTEGEILFKGEDITDLPPEERAR-LGIF------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 87 tarltvadlVAFgRYPYSKGRLTIEDkahidqsiaYLnlddlrdRFLDE-LSGGQRQRAFVAMVLCQDTDYVLLDEPLNN 165
Cdd:cd03217 81 ---------LAF-QYPPEIPGVKNAD---------FL-------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 166 LDMKH----AMGMMKLmqracHELGKTVVLVLHDINFAswysDYIIA-----MKNGRVIRHGTK 220
Cdd:cd03217 135 LDIDAlrlvAEVINKL-----REEGKSVLIITHYQRLL----DYIKPdrvhvLYDGRIVKSGDK 189
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-215 |
1.44e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPS-DVLARRLSILRQD 83
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSkEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 84 NHMTARLTVADLVAFGRYPySKGRLTIEDKAHIDQSIAYLNLD---DLRDRfLDELSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYP-TKGMFVDQDKMYRDTKAIFDELDidiDPRAK-VATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 161 EPLNNLDMKHAMGMMKLMqRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVI 215
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTII-RKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-223 |
1.87e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.11 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 17 VDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTpSDVLARRLsilRQDNHM---------T 87
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM-KDDEWRAV---RSDIQMifqdplaslN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 88 ARLTVADLVA--FGRYPYSKGRLTIEDKAHIDQSIAYLnLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNN 165
Cdd:PRK15079 113 PRMTIGEIIAepLRTYHPKLSRQEVKDRVKAMMLKVGL-LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 166 LDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-167 |
7.46e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 11 YGETAVVD--DVSIELPARgiTSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGlDVsntpsdVLARrlsiLRQDNHMTA 88
Cdd:PRK11147 13 FSDAPLLDnaELHIEDNER--VCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DL------IVAR----LQQDPPRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 89 RLTVADLVAFG---------RYPYSKGRLTIE--DK-----AHIDQSIAYLNLDDLRDRF--------------LDELSG 138
Cdd:PRK11147 80 EGTVYDFVAEGieeqaeylkRYHDISHLVETDpsEKnlnelAKLQEQLDHHNLWQLENRInevlaqlgldpdaaLSSLSG 159
|
170 180
....*....|....*....|....*....
gi 351592836 139 GQRQRAFVAMVLCQDTDYVLLDEPLNNLD 167
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
10-219 |
8.73e-10 |
|
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: 58.29 E-value: 8.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTmlsiVSRLL----GMDAGSVTVDGLDVSNTPSDVLARRLSILRQD-- 83
Cdd:COG5265 367 YDPERPILKGVSFEVPAGKTVAIVGPSGAGKST----LARLLfrfyDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDtv 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 84 --NHmtarlTVADLVAFGRyPySKGRLTIED---KAHIDQSIAylNLDDLRD-----RFLdELSGGQRQRAFVAMVLCQD 153
Cdd:COG5265 443 lfND-----TIAYNIAYGR-P-DASEEEVEAaarAAQIHDFIE--SLPDGYDtrvgeRGL-KLSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 154 TDYVLLDEPLNNLDMKHAMGMMKLMQRACHelGKTVVLVLH------DinfaswySDYIIAMKNGRVIRHGT 219
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGT 575
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-213 |
2.10e-09 |
|
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: 55.90 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 16 VVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVD----GLDVSN-TPSDVLA-RRLSI------LRQD 83
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQaSPREILAlRRRTIgyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 84 NHMTARLTVAD-LVAFGRypyskGRLTIEDKAHidQSIAYLNLDdlrdrflDEL--------SGGQRQRAFVAMVLCQDT 154
Cdd:COG4778 106 PRVSALDVVAEpLLERGV-----DREEARARAR--ELLARLNLP-------ERLwdlppatfSGGEQQRVNIARGFIADP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 155 DYVLLDEPLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGR 213
Cdd:COG4778 172 PLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-219 |
2.46e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.55 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 29 ITSIIGPNGAGKSTMLSIvsrLLGMDAGSVTVDGLDVSNTP--SDVLARRLSILRQDNHMTARLTVADLV---AFGRYPY 103
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDV---LAGRKTGGYIEGDIRISGFPkkQETFARISGYCEQNDIHSPQVTVRESLiysAFLRLPK 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 104 SKGRltiEDKAH-IDQSIAYLNLDDLRDRF-----LDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKL 177
Cdd:PLN03140 985 EVSK---EEKMMfVDEVMELVELDNLKDAIvglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT 1061
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 351592836 178 MqRACHELGKTVVLVLH----DInFASWysDYIIAMK-NGRVIRHGT 219
Cdd:PLN03140 1062 V-RNTVDTGRTVVCTIHqpsiDI-FEAF--DELLLMKrGGQVIYSGP 1104
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-222 |
2.55e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 19 DVSIELPARGITSIIGPNGAGKSTMLSivsRLLGMdagsvtvdgLDVSNtpSDVLARRlSIL---RQDNHMTArlTVADL 95
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQ---SLLSQ---------FEISE--GRVWAER-SIAyvpQQAWIMNA--TVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 96 VAFgrypyskgrLTIEDKAHIDQSIAYLNLD-DLR------DRFLDE----LSGGQRQRAFVAMVLCQDTDYVLLDEPLN 164
Cdd:PTZ00243 741 ILF---------FDEEDAARLADAVRVSQLEaDLAqlggglETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 351592836 165 NLDmKHamgmmkLMQRACHEL------GKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKND 222
Cdd:PTZ00243 812 ALD-AH------VGERVVEECflgalaGKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSSAD 867
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-219 |
2.67e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.04 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 10 YYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTAR 89
Cdd:PRK10790 350 YRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 90 lTVADLVAFGRYPyskgrltieDKAHIDQSIAYLNLDDLRDRFLD-----------ELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:PRK10790 430 -TFLANVTLGRDI---------SEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351592836 159 LDEPLNNLDmkhaMGMMKLMQRACHELGK--TVVLVLHDINFASwYSDYIIAMKNGRVIRHGT 219
Cdd:PRK10790 500 LDEATANID----SGTEQAIQQALAAVREhtTLVVIAHRLSTIV-EADTILVLHRGQAVEQGT 557
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-201 |
3.51e-09 |
|
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: 56.48 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETAVVDDVSIE-LPARGItSIIGPNGAGKSTMLSIVSrllgmdagsvtvdGLDvsnTPSDVLAR-----RLSILR 81
Cdd:TIGR03719 12 KVVPPKKEILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMA-------------GVD---KDFNGEARpqpgiKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 QDNHMTARLTVADLVAFG---------RY---------PYSKGRLTIEDKAHIDQSIAYLNLDDLrDRFLD--------- 134
Cdd:TIGR03719 75 QEPQLDPTKTVRENVEEGvaeikdaldRFneisakyaePDADFDKLAAEQAELQEIIDAADAWDL-DSQLEiamdalrcp 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 135 -------ELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHamgmMKLMQRACHELGKTVVLVLHDI----NFASW 201
Cdd:TIGR03719 154 pwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTHDRyfldNVAGW 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-224 |
3.70e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.95 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 17 VDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQD--NHMTARLTVAD 94
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDpsTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 95 LVAFgryPYskgRL-----TIEDKAHIDQSIAYLNLddLRDR---FLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNL 166
Cdd:PRK15112 109 ILDF---PL---RLntdlePEQREKQIIETLRQVGL--LPDHasyYPHMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 351592836 167 DMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDII 224
Cdd:PRK15112 181 DMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-223 |
4.06e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELpARGIT-SIIGPNGAGKS-TMLSIVsRLLGMDAGSVTVDGLdvsntpsdVLARR----LSILRQDNH 85
Cdd:PRK10261 27 QKIAAVRNLSFSL-QRGETlAIVGESGSGKSvTALALM-RLLEQAGGLVQCDKM--------LLRRRsrqvIELSEQSAA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 86 MTARLTVADLVAFGRYPYSKGRLTIEDKAHIDQSI--------------AYLNLDDLR--------DRFLDELSGGQRQR 143
Cdd:PRK10261 97 QMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIrlhqgasreeamveAKRMLDQVRipeaqtilSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 144 AFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDI 223
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
28-219 |
4.08e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 54.92 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 28 GITSIIGPNGAGKSTMLsivsrllgmdagsvtvDGLDVSNTPSdvLARRLSILRQDNHM---TARLTVADLvAFgrYPYS 104
Cdd:cd03240 23 PLTLIVGQNGAGKTTII----------------EALKYALTGE--LPPNSKGGAHDPKLireGEVRAQVKL-AF--ENAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 105 KGRLTIEDKAHIDQSIAYLNLDDLRDRFLDE---LSGGQRQ------RAFVAMVLCQDTDYVLLDEPLNNLDMKH-AMGM 174
Cdd:cd03240 82 GKKYTITRSLAILENVIFCHQGESNWPLLDMrgrCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 351592836 175 MKLMQRACHELGKTVVLVLHDINFASwYSDYIIamkngRVIRHGT 219
Cdd:cd03240 162 AEIIEERKSQKNFQLIVITHDEELVD-AADHIY-----RVEKDGR 200
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
34-168 |
4.82e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 34 GPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSdvlARRLSILrqdNHMTArlTVADLVAFGRYPYSKGRLTIEDK 113
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR---SRFMAYL---GHLPG--LKADLSTLENLHFLCGLHGRRAK 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 114 AHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDM 168
Cdd:PRK13543 116 QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-219 |
4.87e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.25 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 16 VVDDVSIELPARGITSIIGPNGAGKS-TMLSIVsRLLG------------------MDAGSVTVDGLD------------ 64
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSIL-RLLPsppvvypsgdirfhgeslLHASEQTLRGVRgnkiamifqepm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 65 VSNTP----SDVLARRLSILRQDNHMTARLTVadlvafgrypyskgrLTIEDKAHIDQSIAYLNlddlrdRFLDELSGGQ 140
Cdd:PRK15134 103 VSLNPlhtlEKQLYEVLSLHRGMRREAARGEI---------------LNCLDRVGIRQAAKRLT------DYPHQLSGGE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 141 RQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGT 219
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-228 |
6.33e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 5 SGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSN-TPsdVLARRLSI--LR 81
Cdd:PRK15439 15 RSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTP--AKAHQLGIylVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 QDNHMTARLTVADLVAFG--RYPYSKGRLTiedkAHIDQSIAYLNLD------DLRDRFLDELSGGqrqrafvamvLCQD 153
Cdd:PRK15439 93 QEPLLFPNLSVKENILFGlpKRQASMQKMK----QLLAALGCQLDLDssagslEVADRQIVEILRG----------LMRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 154 TDYVLLDEPLNNLDMKHAMGMMKLMqRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHG-----TKNDII---T 225
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRI-RELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGktadlSTDDIIqaiT 237
|
...
gi 351592836 226 PEA 228
Cdd:PRK15439 238 PAA 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-194 |
7.43e-09 |
|
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: 53.31 E-value: 7.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 14 TAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLlgmdagsvtvdgldvsntpsdvlarrlsilrqdnhmtarltva 93
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL------------------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 94 dlvafgrYPYSKGRLTIEDKAH---IDQSiAYLNLDDLRDRFL----DELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNL 166
Cdd:cd03223 51 -------WPWGSGRIGMPEGEDllfLPQR-PYLPLGTLREQLIypwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180
....*....|....*....|....*...
gi 351592836 167 DmkhaMGMMKLMQRACHELGKTVVLVLH 194
Cdd:cd03223 123 D----EESEDRLYQLLKELGITVISVGH 146
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
16-219 |
8.07e-09 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 55.73 E-value: 8.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 16 VVDDVSIELPARGITSIIGPNGAGKSTMLSIvsrLLGMD---AGSVTVDGLDVSNTPSDVLARRLSILRQD-NHMTArlT 91
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRL---LLGFEtpeSGSVFYDGQDLAGLDVQAVRRQLGVVLQNgRLMSG--S 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 92 VADLVAFGrypyskGRLTIEDkAHIDQSIAYLNlDDLRD------RFLDE----LSGGQRQRAFVAMVLCQDTDYVLLDE 161
Cdd:TIGR03797 543 IFENIAGG------APLTLDE-AWEAARMAGLA-EDIRAmpmgmhTVISEgggtLSGGQRQRLLIARALVRKPRILLFDE 614
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 162 PLNNLDMKhamgmmklMQRACHE----LGKTVVLVLH---DINFAswysDYIIAMKNGRVIRHGT 219
Cdd:TIGR03797 615 ATSALDNR--------TQAIVSEslerLKVTRIVIAHrlsTIRNA----DRIYVLDAGRVVQQGT 667
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-200 |
1.62e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.63 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 25 PARGItSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSD----VLARRLSILRQDNHMTARLTVADLVafgR 100
Cdd:PRK10584 35 RGETI-ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEarakLRAKHVGFVFQSFMLIPTLNALENV---E 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 101 YP-YSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQ 179
Cdd:PRK10584 111 LPaLLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
|
170 180
....*....|....*....|.
gi 351592836 180 RACHELGKTVVLVLHDINFAS 200
Cdd:PRK10584 191 SLNREHGTTLILVTHDLQLAA 211
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-194 |
1.75e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.43 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 14 TAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVdgldvsntPSDvlaRRLSILRQDNHMTArLTVA 93
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PAG---ARVLFLPQRPYLPL-GTLR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 94 DLVAfgrYPYSKGRLTIEDKAHIDQSiayLNLDDLRDRfLDE-------LSGGQRQR-AFvAMVLCQDTDYVLLDEPLNN 165
Cdd:COG4178 444 EALL---YPATAEAFSDAELREALEA---VGLGHLAER-LDEeadwdqvLSLGEQQRlAF-ARLLLHKPDWLFLDEATSA 515
|
170 180
....*....|....*....|....*....
gi 351592836 166 LDMKHAMGMMKLMQRACHELgkTVVLVLH 194
Cdd:COG4178 516 LDEENEAALYQLLREELPGT--TVISVGH 542
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
18-199 |
1.89e-08 |
|
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: 52.36 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 18 DDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMdAGSVTVDGLDVSntpsdvlarrlsilrqdnhmtARLTVADLVA 97
Cdd:cd03227 12 VPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGG-AQSATRRRSGVK---------------------AGCIVAAVSA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 98 FGRYpyskgrltiedkahidqsiaylnlddlrdrFLDELSGGQRQRAFVAMVL----CQDTDYVLLDEPLNNLDMKHAMG 173
Cdd:cd03227 70 ELIF------------------------------TRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQA 119
|
170 180
....*....|....*....|....*..
gi 351592836 174 MM-KLMQRACHelGKTVVLVLHDINFA 199
Cdd:cd03227 120 LAeAILEHLVK--GAQVIVITHLPELA 144
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-224 |
1.98e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLS-IVSRLLGMDAGSVTVDGlDVSNTPsdvlarRLSILrqdnhmtARL 90
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-TVAYVP------QVSWI-------FNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 TVADLVAFGRyPYSKGRLtieDKAhIDQSIAYLNLDDLRDRFLDE-------LSGGQRQRAFVAMVLCQDTDYVLLDEPL 163
Cdd:PLN03130 694 TVRDNILFGS-PFDPERY---ERA-IDVTALQHDLDLLPGGDLTEigergvnISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351592836 164 NNLDMKHAMGMM-KLMQRachEL-GKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGTKNDII 224
Cdd:PLN03130 769 SALDAHVGRQVFdKCIKD---ELrGKTRVLVTNQLHFLS-QVDRIILVHEGMIKEEGTYEELS 827
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
11-194 |
2.43e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 11 YGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvSNTPSDVLA--RRLSILRQDNHMTA 88
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER---QSIKKDLCTyqKQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 89 RLTVADLVAFGRYpYSKGRLtiedkaHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDM 168
Cdd:PRK13540 88 YLTLRENCLYDIH-FSPGAV------GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*.
gi 351592836 169 KHAMGMMKLMQrACHELGKTVVLVLH 194
Cdd:PRK13540 161 LSLLTIITKIQ-EHRAKGGAVLLTSH 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-220 |
2.46e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPS---DVLARRLSILRQDNH--MT 87
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPYasLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 88 ARLTVADLVAfgrYPYSKGRLtIEDKAHIDQSIAYLNLDDLRD----RFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPL 163
Cdd:PRK10261 416 PRQTVGDSIM---EPLRVHGL-LPGKAAAARVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 164 NNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTK 220
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR 548
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-207 |
3.27e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.80 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 29 ITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVlarrlsilrqdnhmtarltvadlvafgrypyskgrl 108
Cdd:cd03222 27 VIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 109 tiedkahidqsiaylnlddlrdrfldELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKT 188
Cdd:cd03222 71 --------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKT 124
|
170
....*....|....*....
gi 351592836 189 VVLVLHDINFASWYSDYII 207
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIH 143
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
12-200 |
3.93e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.11 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvsntpsdvlaRRLSILRQDNHmtarlt 91
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG------------EPIRRQRDEYH------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 92 vADLVAFGRYPYSKGRLTIEDKAHIDQSIA-YLNLDDLRD--------RFLD----ELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:PRK13538 74 -QDLLYLGHQPGIKTELTALENLRFYQRLHgPGDDEALWEalaqvglaGFEDvpvrQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 351592836 159 LDEPLNNLDmKHAMGMMK-LMQRAChELGKTVVLVLH-DINFAS 200
Cdd:PRK13538 153 LDEPFTAID-KQGVARLEaLLAQHA-EQGGMVILTTHqDLPVAS 194
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-241 |
5.90e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLS-IVSRLLGMDAGSVTVDGlDVSNTPsdvlarRLSILrqdnhmtARLT 91
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-SVAYVP------QVSWI-------FNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 92 VADLVAFGRyPYSKGRLTiedKAhIDQSIAYLNLDDLRDRFLDEL-------SGGQRQRAFVAMVLCQDTDYVLLDEPLN 164
Cdd:PLN03232 695 VRENILFGS-DFESERYW---RA-IDVTALQHDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 165 NLDMKHAMGMMKlmqrAC--HEL-GKTVVLVLHDINFASwYSDYIIAMKNGRVIRHGT-----KNDIITPEALKDIYDMD 236
Cdd:PLN03232 770 ALDAHVAHQVFD----SCmkDELkGKTRVLVTNQLHFLP-LMDRIILVSEGMIKEEGTfaelsKSGSLFKKLMENAGKMD 844
|
....*
gi 351592836 237 INVHE 241
Cdd:PLN03232 845 ATQEV 849
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
13-219 |
7.18e-08 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 52.64 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHM---TAR 89
Cdd:TIGR03796 491 EPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLfegTVR 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 90 --LTVADLvafgrypyskgrlTIEDKAHI----DQSIaylnLDDLRDR------FLDE----LSGGQRQRAFVAMVLCQD 153
Cdd:TIGR03796 571 dnLTLWDP-------------TIPDADLVrackDAAI----HDVITSRpggydaELAEgganLSGGQRQRLEIARALVRN 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 351592836 154 TDYVLLDEPLNNLDMK-HAMGMMKLMQRAChelgkTVVLVLH------DinfaswySDYIIAMKNGRVIRHGT 219
Cdd:TIGR03796 634 PSILILDEATSALDPEtEKIIDDNLRRRGC-----TCIIVAHrlstirD-------CDEIIVLERGKVVQRGT 694
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
3-218 |
7.93e-08 |
|
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: 51.11 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 3 ITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTML-SIVSRLLGMDA--GSVTVDGLDVSNTPSdvLARRLSI 79
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLkALANRTEGNVSveGDIHYNGIPYKEFAE--KYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 L--RQDNHMtARLTVADLVAFGRypyskgrltiedkahidqsiaylnldDLR-DRFLDELSGGQRQRAFVAMVLCQDTDY 156
Cdd:cd03233 87 YvsEEDVHF-PTLTVRETLDFAL--------------------------RCKgNEFVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 157 VLLDEPLNNLDMKHAMGMMKLMQRACHELGKTvvlvlhdiNFASWYS---------DYIIAMKNGRVIRHG 218
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVLKTT--------TFVSLYQasdeiydlfDKVLVLYEGRQIYYG 202
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
12-220 |
1.19e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 51.22 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIvsrLLG-----MDAGSVTVDGLDVSNTPSDVLARR---LS----- 78
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKV---LMGhpkyeVTSGSILLDGEDILELSPDERARAgifLAfqypv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 79 -IlrqdnhmtARLTVADLVafgRYPYSKGRL----TIEDKAHIDQSIAYLNLD-DLRDRFLDE-LSGGQRQRAFVAMVLC 151
Cdd:COG0396 88 eI--------PGVSVSNFL---RTALNARRGeelsAREFLKLLKEKMKELGLDeDFLDRYVNEgFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 152 QDTDYVLLDEPLNNLD---MKH-AMGMMKLmqracHELGKTVVLVLHdinfaswYS--------DYIIAMKNGRVIRHGT 219
Cdd:COG0396 157 LEPKLAILDETDSGLDidaLRIvAEGVNKL-----RSPDRGILIITH-------YQrildyikpDFVHVLVDGRIVKSGG 224
|
.
gi 351592836 220 K 220
Cdd:COG0396 225 K 225
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
13-167 |
1.57e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.26 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 13 ETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVlarrLSILRQDNHMTARLTV 92
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY----CTYIGHNLGLKLEMTV 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 351592836 93 ADLVAFGRYPYSKGRLtiedkahIDQSIAYLNLDDLRDRFLDELSGG-QRQRAFVAMVLCQdTDYVLLDEPLNNLD 167
Cdd:PRK13541 88 FENLKFWSEIYNSAET-------LYAAIHYFKLHDLLDEKCYSLSSGmQKIVAIARLIACQ-SDLWLLDEVETNLS 155
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-194 |
3.35e-07 |
|
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: 50.90 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 16 VVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVdgldvsntPSDvlaRRLSILRQDNHMTARlTVADL 95
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK--------PAK---GKLFYVPQRPYMTLG-TLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 96 VAfgrYPYSKgrLTIEDKAHIDQS-IAYL---NLDDLRDR---------FLDELSGGQRQRAFVAMVLCQDTDYVLLDEP 162
Cdd:TIGR00954 535 II---YPDSS--EDMKRRGLSDKDlEQILdnvQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|....
gi 351592836 163 LN--NLDMKHAmgmmklMQRACHELGKTVVLVLH 194
Cdd:TIGR00954 610 TSavSVDVEGY------MYRLCREFGITLFSVSH 637
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-194 |
3.92e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 29 ITSIIGPNGAGKSTMLSIVSRLLGMdaGSVTVDGLDVSNTPSD-VLARRLSILRQDNHMTARLTVADLVAFGRYPYSKGR 107
Cdd:TIGR00956 791 LTALMGASGAGKTTLLNVLAERVTT--GVITGGDRLVNGRPLDsSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKS 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 108 LTIEDK-AHIDQSIAYLNLDDLRDRFLDE----LSGGQRQRAFVAMVLCQDTDYVL-LDEPLNNLDMKHAMGMMKLMqRA 181
Cdd:TIGR00956 869 VSKSEKmEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLM-RK 947
|
170
....*....|...
gi 351592836 182 CHELGKTVVLVLH 194
Cdd:TIGR00956 948 LADHGQAILCTIH 960
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-168 |
6.33e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDgldvsntPSDvlarRLSIL 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD-------PNE----RLGKL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 81 RQDNHMTARLTVADLVAFGRYP-----------YSKGRLTIEDKAHI-DQSIAYLNLD-------------------DLR 129
Cdd:PRK15064 70 RQDQFAFEEFTVLDTVIMGHTElwevkqerdriYALPEMSEEDGMKVaDLEVKFAEMDgytaearagelllgvgipeEQH 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 351592836 130 DRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDM 168
Cdd:PRK15064 150 YGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI 188
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-225 |
7.54e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.54 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLL--GMDAGSVTVDGLDV-SNTPSDVLARRLSILRQ 82
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphGTYEGEIIFEGEELqASNIRDTERAGIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 83 DNHMTARLTVADLVAFGRYPYSKGRLTiEDKAHI--DQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:PRK13549 90 ELALVKELSVLENIFLGNEITPGGIMD-YDAMYLraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 161 EPLNNLDMKHAMGMMKLMqRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVI-----RHGTKNDIIT 225
Cdd:PRK13549 169 EPTASLTESETAVLLDII-RDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIgtrpaAGMTEDDIIT 237
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-222 |
1.05e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 22 IELPARgiTSIIGPNGAGKSTMLSIVSRLLGMDAGSV--------------TVDGLDVSNTPSDVLARrlsilrqdnhmt 87
Cdd:PLN03073 532 IDLDSR--IAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDLSSNPLLYMMR------------ 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 88 arltvadlvAFGRYPYSKGRltiedkAHIDQSIAYLNLdDLRDRFldELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLD 167
Cdd:PLN03073 598 ---------CFPGVPEQKLR------AHLGSFGVTGNL-ALQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 168 MKHAMGMMK---LMQRAchelgktVVLVLHDINFASWYSDYIIAMKNGRVIR-HGTKND 222
Cdd:PLN03073 660 LDAVEALIQglvLFQGG-------VLMVSHDEHLISGSVDELWVVSEGKVTPfHGTFHD 711
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-235 |
1.22e-06 |
|
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: 49.17 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 16 VVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARLTVADL 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 96 VAFGRYPYSKGRLTIEdKAHIDQSIAYL--NLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKhAMG 173
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALE-LAHLKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE-TDN 1458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 174 MMKLMQRACHElGKTVVLVLHDINFASWYSDyIIAMKNGRVIRHGTKNDIITPEALkdIYDM 235
Cdd:TIGR00957 1459 LIQSTIRTQFE-DCTVLTIAHRLNTIMDYTR-VIVLDKGEVAEFGAPSNLLQQRGI--FYSM 1516
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-207 |
1.60e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDG---LDVSN--TPS-DVLA 74
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqLAWVNqeTPAlPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 75 RRLSIL--RQDNHMTARLTVADLVAFGR-YPYSKGRLTIEDKAHIDQSIAYLnLDDL------RDRFLDELSGGQRQRAF 145
Cdd:PRK10636 81 LEYVIDgdREYRQLEAQLHDANERNDGHaIATIHGKLDAIDAWTIRSRAASL-LHGLgfsneqLERPVSDFSGGWRMRLN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 146 VAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQrachELGKTVVLVLHDINFASWYSDYII 207
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLK----SYQGTLILISHDRDFLDPIVDKII 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-201 |
1.73e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETAVVDDVSIE-LPARGItSIIGPNGAGKSTMLSIVSrllgmdagsvtvdGLDvsnTPSDVLAR-----RLSILR 81
Cdd:PRK11819 14 KVVPPKKQILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMA-------------GVD---KEFEGEARpapgiKVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 82 QDNHMTARLTVADLVAFG---------RY---------PYSKGRLTIEDKAHIDQSIAYLNLDDLrDRFLD--------- 134
Cdd:PRK11819 77 QEPQLDPEKTVRENVEEGvaevkaaldRFneiyaayaePDADFDALAAEQGELQEIIDAADAWDL-DSQLEiamdalrcp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 135 -------ELSGGQRQRafVAmvLC----QDTDYVLLDEPLNNLDmkhAMGMMKLmQRACHELGKTVVLVLHDI----NFA 199
Cdd:PRK11819 156 pwdakvtKLSGGERRR--VA--LCrlllEKPDMLLLDEPTNHLD---AESVAWL-EQFLHDYPGTVVAVTHDRyfldNVA 227
|
..
gi 351592836 200 SW 201
Cdd:PRK11819 228 GW 229
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-227 |
1.78e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 32 IIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQdnhmtARLTVADLVAFGRYPYSKgrltiE 111
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQ-----APVLFSGTVRFNLDPFNE-----H 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 112 DKAHIDQSIAYLNLDDL--RDRF-LD--------ELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDmkhaMGMMKLMQR 180
Cdd:PLN03130 1340 NDADLWESLERAHLKDVirRNSLgLDaevseageNFSVGQRQLLSLARALLRRSKILVLDEATAAVD----VRTDALIQK 1415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 351592836 181 ACHELGK--TVVLVLHDINfASWYSDYIIAMKNGRVIRHGTKNDIITPE 227
Cdd:PLN03130 1416 TIREEFKscTMLIIAHRLN-TIIDCDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
12-218 |
1.84e-06 |
|
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: 47.64 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 12 GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIvsrLLGMDA-----GSVTVDGLDVSNTPSDVLARR-LSILRQDNH 85
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKT---IAGHPSyevtsGTILFKGQDLLELEPDERARAgLFLAFQYPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 86 MTARLTVADLV--AFGRYPYSKGRLTIEDKA---HIDQSIAYLNLD-DLRDRFLDE-LSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:TIGR01978 88 EIPGVSNLEFLrsALNARRSARGEEPLDLLDfekLLKEKLALLDMDeEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351592836 159 LDEPLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDIN-FASWYSDYIIAMKNGRVIRHG 218
Cdd:TIGR01978 168 LDEIDSGLDIDALKIVAEGINRLREP-DRSFLIITHYQRlLNYIKPDYVHVLLDGRIVKSG 227
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
32-227 |
2.24e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 47.60 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 32 IIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNhmtarLTVADLVAFGRYPYSKgrlTIE 111
Cdd:cd03288 52 ICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDP-----ILFSGSIRFNLDPECK---CTD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 112 DKAHIDQSIAYLN---------LDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRAC 182
Cdd:cd03288 124 DRLWEALEIAQLKnmvkslpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAF 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 351592836 183 HElgKTVVLVLHDINfASWYSDYIIAMKNGRVIRHGTKNDIITPE 227
Cdd:cd03288 204 AD--RTVVTIAHRVS-TILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-214 |
3.10e-06 |
|
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: 46.27 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 15 AVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVS-NTPSDVLARRLSILRQDNHMTA---RL 90
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrRSPRDAIRAGIAYVPEDRKREGlvlDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 91 TVADLVAFGRYpyskgrltiedkahidqsiaylnlddlrdrfldeLSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKH 170
Cdd:cd03215 94 SVAENIALSSL----------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 351592836 171 AMGMMKLMqRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRV 214
Cdd:cd03215 140 KAEIYRLI-RELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-229 |
3.19e-06 |
|
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: 47.51 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 17 VDDVSIELPARGITSIIGPNGAGKS-TMLSIVSRLLGMDAGSVTVDGLDVS-NTPSDVLARRLSILRQDNH--------- 85
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVDiRNPAQAIRAGIAMVPEDRKrhgivpilg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 86 MTARLTVADLVAFGrypyskGRLTIEDKAH---IDQSIAYLNLDDLR-DRFLDELSGGQRQRAFVAMVLCQDTDYVLLDE 161
Cdd:TIGR02633 356 VGKNITLSVLKSFC------FKMRIDAAAElqiIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 351592836 162 PLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDINFASWYSDYIIAMKNGRV----IRHGTKNDIITPEAL 229
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLkgdfVNHALTQEQVLAAAL 500
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-227 |
3.31e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 17 VDDVSIELPARGITSIIGPNGAGKSTMLSIvsrLLGMD---AGSVTVDGLDVS-NTPSDVLARRLSIL---RQDNHMTAR 89
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNC---LFGVDkraGGEIRLNGKDISpRSPLDAVKKGMAYItesRRDNGFFPN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 90 LTVADLVAF------GRYpysKGRLTIEDKaHIDQSIAYLNLDDLR------DRFLDELSGGQRQRAFVAMVLCQDTDYV 157
Cdd:PRK09700 356 FSIAQNMAIsrslkdGGY---KGAMGLFHE-VDEQRTAENQRELLAlkchsvNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 158 LLDEPLNNLDMKHAMGMMKLMqRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIITPE 227
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVM-RQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-225 |
3.80e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 16 VVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRL--------------------------------LGM---------- 53
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgdeeqnVGMknvnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 54 ------------DAGSVTVDGLDVSNTPSDVLARRLSILRQDNhMTARLTVADLVAFGRYPYSKGRLTIEDK-AHIDQSI 120
Cdd:PTZ00265 1263 eggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEP-MLFNMSIYENIKFGKEDATREDVKRACKfAAIDEFI 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 121 AYL--NLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDInf 198
Cdd:PTZ00265 1342 ESLpnKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-- 1419
|
250 260 270
....*....|....*....|....*....|...
gi 351592836 199 ASW-YSDYIIAMKN----GRVIR-HGTKNDIIT 225
Cdd:PTZ00265 1420 ASIkRSDKIVVFNNpdrtGSFVQaHGTHEELLS 1452
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
19-215 |
4.19e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.10 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 19 DVSIElpaRG-ITSIIGPNGAGKSTMLSIvsrLLGM---DAGSVTVDGLDVSntpsdvlARRLSILRQdnHMTARLTvaD 94
Cdd:COG4615 352 DLTIR---RGeLVFIVGGNGSGKSTLAKL---LTGLyrpESGEILLDGQPVT-------ADNREAYRQ--LFSAVFS--D 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 95 LVAFGRYPyskGRLTIEDKAHIDQSIAYLNLDDL----RDRFLD-ELSGGQRQR-AFVAMVLcQDTDYVLLDE------- 161
Cdd:COG4615 415 FHLFDRLL---GLDGEADPARARELLERLELDHKvsveDGRFSTtDLSQGQRKRlALLVALL-EDRPILVFDEwaadqdp 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 162 -----------PlnnlDMKhamgmmklmqrachELGKTVVLVLHDINFASwYSDYIIAMKNGRVI 215
Cdd:COG4615 491 efrrvfytellP----ELK--------------ARGKTVIAISHDDRYFD-LADRVLKMDYGKLV 536
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-214 |
5.12e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 37 GAGKSTMLSIVSRLLGMDAGSVTVDGLDVS-NTPSDvlARRLSIL-----RQDNHMTARLTVADLVAFG-RYPYSKGRLT 109
Cdd:PRK11288 289 GAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRD--AIRAGIMlcpedRKAEGIIPVHSVADNINISaRRHHLRAGCL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 110 IEDK---AHIDQSIAYLNLDDL-RDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDM--KHAmgmmklMQRACH 183
Cdd:PRK11288 367 INNRweaENADRFIRSLNIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVgaKHE------IYNVIY 440
|
170 180 190
....*....|....*....|....*....|....
gi 351592836 184 EL---GKTVVLVLHDINFASWYSDYIIAMKNGRV 214
Cdd:PRK11288 441 ELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-224 |
1.21e-05 |
|
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: 45.95 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 9 KYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIvsrLLGMD-----AGSV------------------------- 58
Cdd:TIGR03269 8 KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHV---LRGMDqyeptSGRIiyhvalcekcgyverpskvgepcpv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 59 --------TVDGLDVSNTPSDVLARRLSILRQDNH-MTARLTVADLVAfgrypYSKGRLTIEDKAHIDQSIAYLNLDDLR 129
Cdd:TIGR03269 85 cggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFaLYGDDTVLDNVL-----EALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 130 DRFLD---ELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYI 206
Cdd:TIGR03269 160 HRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*...
gi 351592836 207 IAMKNGRVIRHGTKNDII 224
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVV 257
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-222 |
1.24e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 6 GIKKYYGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVT-VDGLDVSNTPSDVLARrlsiLRQDn 84
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwSENANIGYYAQDHAYD----FEND- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 85 hmtarLTVADLVAFGRYPyskgrltiedkAHIDQSI-AYL-----NLDDLRdRFLDELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:PRK15064 399 -----LTLFDWMSQWRQE-----------GDDEQAVrGTLgrllfSQDDIK-KSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 159 LDEPLNNLDMKHamgmMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIR-HGTKND 222
Cdd:PRK15064 462 MDEPTNHMDMES----IESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEE 522
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
18-51 |
1.44e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 41.82 E-value: 1.44e-05
10 20 30
....*....|....*....|....*....|....
gi 351592836 18 DDVSIELPARGITSIIGPNGAGKSTMLSIVSRLL 51
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-196 |
1.66e-05 |
|
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: 45.77 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 8 KKYYGETA-VVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVlarrlsilRQDNHM 86
Cdd:TIGR01257 1945 KVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV--------HQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 87 TARLTVADLVAFGR---YPYSK--GRLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDE 161
Cdd:TIGR01257 2017 CPQFDAIDDLLTGRehlYLYARlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190
....*....|....*....|....*....|....*
gi 351592836 162 PLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDI 196
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSM 2130
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-198 |
1.70e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 32 IIGPNGAGKSTMLSIVSRLLGMDAGSVTVdgldvsntpsdvlARRLSILRQDNHmTARL----TVADLVAFGrypysKGR 107
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRIHC-------------GTKLEVAYFDQH-RAELdpekTVMDNLAEG-----KQE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 108 LTIEDKA-HIdqsiaylnLDDLRDrFL----------DELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKhamgMMK 176
Cdd:PRK11147 411 VMVNGRPrHV--------LGYLQD-FLfhpkramtpvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE----TLE 477
|
170 180
....*....|....*....|..
gi 351592836 177 LMQRACHELGKTVVLVLHDINF 198
Cdd:PRK11147 478 LLEELLDSYQGTVLLVSHDRQF 499
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-161 |
1.87e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGETavvddvSIELPaRGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSD---------V 72
Cdd:COG0419 5 LRLENFRSYRDTE------TIDFD-DGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEeasvelefeH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 73 LARRLSILRQDNHMTARLT---------VADLVAFGRYPYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDE-------- 135
Cdd:COG0419 78 GGKRYRIERRQGEFAEFLEakpserkeaLKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQlsgldpie 157
|
170 180
....*....|....*....|....*..
gi 351592836 136 -LSGGQRQRAFVAMVLCQDTDYVLLDE 161
Cdd:COG0419 158 tLSGGERLRLALADLLSLILDFGSLDE 184
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-229 |
1.87e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.39 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 16 VVDDVSIELpARG-ITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVS-NTPSDVLARRLSIL---RQDN----HM 86
Cdd:COG1129 267 VVRDVSFSV-RAGeILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRAGIAYVpedRKGEglvlDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 87 TAR--LTVADLVAFGRYPY-SKGRLtiedKAHIDQSIAYLNL--DDLRDRfLDELSGGQRQRAFVAMVLCQDTDYVLLDE 161
Cdd:COG1129 346 SIRenITLASLDRLSRGGLlDRRRE----RALAEEYIKRLRIktPSPEQP-VGNLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 351592836 162 PLNNLDM--KHAmgMMKLMQRACHElGKTVVLV-------LHdinfaswYSDYIIAMKNGRVIRHGTKNDiITPEAL 229
Cdd:COG1129 421 PTRGIDVgaKAE--IYRLIRELAAE-GKAVIVIsselpelLG-------LSDRILVMREGRIVGELDREE-ATEEAI 486
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-215 |
2.37e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.02 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 16 VVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSN-TPSDVLARRLSILRQDNH---MTARLT 91
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlSPRERRRLGVAYIPEDRLgrgLVPDMS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 92 VADLVAFGRY---PYSKGRLtiedkahIDQSIAYLNLDDLRDRF----------LDELSGGQRQRAFVAMVLCQDTDYVL 158
Cdd:COG3845 353 VAENLILGRYrrpPFSRGGF-------LDRKAIRAFAEELIEEFdvrtpgpdtpARSLSGGNQQKVILARELSRDPKLLI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 159 LDEPLNNLDMKHAMGMMKLMQRACHElGKTVVLVLHDIN--FAswYSDYIIAMKNGRVI 215
Cdd:COG3845 426 AAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDeiLA--LSDRIAVMYEGRIV 481
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
130-223 |
2.66e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.35 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 130 DRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELGKTVVLVLHDINFASWYSDYIIAM 209
Cdd:PRK11022 148 DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVM 227
|
90
....*....|....
gi 351592836 210 KNGRVIRHGTKNDI 223
Cdd:PRK11022 228 YAGQVVETGKAHDI 241
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-168 |
4.86e-05 |
|
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: 44.13 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 14 TAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvsntpsdvlarRLSILRQDNHMTARlTVA 93
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPG-TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 94 DLVAFGrYPYSKGRLTIEDKA-HIDQSIAYLNLDDlrDRFLDE----LSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDM 168
Cdd:TIGR01271 505 DNIIFG-LSYDEYRYTSVIKAcQLEEDIALFPEKD--KTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-223 |
6.10e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 32 IIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHmtarltvADLVA-----FGRYPYSKG 106
Cdd:PRK10938 34 FVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNN-------TDMLSpgeddTGRTTAEII 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 107 RLTIEDKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHElG 186
Cdd:PRK10938 107 QDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-G 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 351592836 187 KTVVLVL---HDI-NFAswysDYIIAMKNGRVIRHGTKNDI 223
Cdd:PRK10938 186 ITLVLVLnrfDEIpDFV----QFAGVLADCTLAETGEREEI 222
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
32-213 |
8.25e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.42 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 32 IIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGLDVSNTPSDVLARRLSILRQDNHMTARLTvadlvafgrypysKGRLTIE 111
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL-------------GPEGKPA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 112 DKAHIDQSIAYLNLDD---LRD-RFLD-ELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELG 186
Cdd:PRK10522 421 NPALVEKWLERLKMAHkleLEDgRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMG 500
|
170 180
....*....|....*....|....*..
gi 351592836 187 KTVVLVLHDINFASwYSDYIIAMKNGR 213
Cdd:PRK10522 501 KTIFAISHDDHYFI-HADRLLEMRNGQ 526
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-209 |
8.26e-05 |
|
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: 42.63 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 19 DVSIELPARGITSIIGPNGAGKSTM----------------LSIVSR--LLGMDAGSVT-VDGLDVSntpsdvlarrLSI 79
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAYARqfLGQMDKPDVDsIEGLSPA----------IAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQDNHMTARLTVA---DLVAFGRYPYSKGRLTIEDKAHIDQSIAYLNLDdlrdRFLDELSGGQRQRAFVAMVLCQDTDY 156
Cdd:cd03270 83 DQKTTSRNPRSTVGtvtEIYDYLRLLFARVGIRERLGFLVDVGLGYLTLS----RSAPTLSGGEAQRIRLATQIGSGLTG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 157 VL--LDEPLNNLDMKHAMGMMKLMQRaCHELGKTVVLVLHDINfASWYSDYIIAM 209
Cdd:cd03270 159 VLyvLDEPSIGLHPRDNDRLIETLKR-LRDLGNTVLVVEHDED-TIRAADHVIDI 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-195 |
1.46e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 11 YGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVtvdGLDVSNTPSDVLARRLSILRQD----NHM 86
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---GLAKGIKLGYFAQHQLEFLRADesplQHL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 87 tARLTVADLVAFGRyPYSKGRLTIEDKahidqsiaylnLDDLRDRFldelSGGQRQRAFVAMVLCQDTDYVLLDEPLNNL 166
Cdd:PRK10636 399 -ARLAPQELEQKLR-DYLGGFGFQGDK-----------VTEETRRF----SGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
170 180
....*....|....*....|....*....
gi 351592836 167 DMKhamgMMKLMQRACHELGKTVVLVLHD 195
Cdd:PRK10636 462 DLD----MRQALTEALIDFEGALVVVSHD 486
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
116-223 |
1.64e-04 |
|
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: 42.69 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 116 IDQSIAYLNLDdlrdRFLDELSGGQRQRAFVAM--------VLcqdtdYVlLDEPLNNLdmkHAMGMMKLMQ--RACHEL 185
Cdd:TIGR00630 473 IDVGLDYLSLS----RAAGTLSGGEAQRIRLATqigsgltgVL-----YV-LDEPSIGL---HQRDNRRLINtlKRLRDL 539
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 351592836 186 GKTVVLVLHD---INFAswysDYIIAM------KNGRVIRHGTKNDI 223
Cdd:TIGR00630 540 GNTLIVVEHDedtIRAA----DYVIDIgpgageHGGEVVASGTPEEI 582
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-52 |
2.61e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.52 E-value: 2.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 351592836 1 MIITS-GIKKYYGetavVDDVSIELP-ARGITSIIGPNGAGKSTMLSIVSRLLG 52
Cdd:COG3950 1 MRIKSlTIENFRG----FEDLEIDFDnPPRLTVLVGENGSGKTTLLEAIALALS 50
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
107-225 |
2.63e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.71 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 107 RLTIEDKAHIDQSIAYlnlddlrdrfldELSGGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELG 186
Cdd:PRK15093 142 RVGIKDHKDAMRSFPY------------ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNN 209
|
90 100 110
....*....|....*....|....*....|....*....
gi 351592836 187 KTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDIIT 225
Cdd:PRK15093 210 TTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
18-44 |
3.03e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 40.56 E-value: 3.03e-04
10 20
....*....|....*....|....*..
gi 351592836 18 DDVSIELPaRGITSIIGPNGAGKSTML 44
Cdd:pfam13476 10 RDQTIDFS-KGLTLITGPNGSGKTTIL 35
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
105-224 |
3.12e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 105 KGRLTIedkaHIDQSIAYLNLDdlrdRFLDELSGGQRQRAFVAMVLCQDTDYV--LLDEPLNNLdmkHAMGMMKLMQ--R 180
Cdd:PRK00635 454 KSRLSI----LIDLGLPYLTPE----RALATLSGGEQERTALAKHLGAELIGItyILDEPSIGL---HPQDTHKLINviK 522
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 351592836 181 ACHELGKTVVLVLHD---INFAswysDYII------AMKNGRVIRHGTKNDII 224
Cdd:PRK00635 523 KLRDQGNTVLLVEHDeqmISLA----DRIIdigpgaGIFGGEVLFNGSPREFL 571
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
9-57 |
3.54e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 3.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 351592836 9 KYYGETAVVDdvsielPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGS 57
Cdd:pfam02463 11 KSYAKTVILP------FSPGFTAIVGPNGSGKSNILDAILFVLGERSAK 53
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-167 |
3.61e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 11 YGETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVS-----------RLLGMDAGSvtvdgldvSNTPSDVlARRLSI 79
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndlTLFGRRRGS--------GETIWDI-KKHIGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQDNHMTARL--TVADLVAFGrYPYSKGRL-TIEDKAHI--DQSIAYLNLDD-LRDRFLDELSGGQRQRAFVAMVLCQD 153
Cdd:PRK10938 341 VSSSLHLDYRVstSVRNVILSG-FFDSIGIYqAVSDRQQKlaQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKH 419
|
170
....*....|....
gi 351592836 154 TDYVLLDEPLNNLD 167
Cdd:PRK10938 420 PTLLILDEPLQGLD 433
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-192 |
6.77e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 2 IITSGIKKYYGET-----AVVDDVSIELPARGITSIIGPNGAGKSTML-SIVSRL---LGMDAGSVTVDGLD----VSNT 68
Cdd:TIGR00956 57 ILTRGFRKLKKFRdtktfDILKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTdgfHIGVEGVITYDGITpeeiKKHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 69 PSDVLarrlSILRQDNHMtARLTVADLVAFG---RYPYSKGRLTIED--KAHI-DQSIAYLNLDDLRDR-----FLDELS 137
Cdd:TIGR00956 137 RGDVV----YNAETDVHF-PHLTVGETLDFAarcKTPQNRPDGVSREeyAKHIaDVYMATYGLSHTRNTkvgndFVRGVS 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 351592836 138 GGQRQRAFVAMVLCQDTDYVLLDEPLNNLDMKHAMGMMKLMQRACHELgKTVVLV 192
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANIL-DTTPLV 265
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
24-194 |
8.08e-04 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 39.88 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 24 LPARGITSIIGPNGAGKST-MLSIV------SRLLGMDAGSVTV---DGLDvsntPSDVLARRLSILRQDnhmtarltva 93
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFlALQLAaavaagGPWLGRRVPPGKVlylAAED----DRGELRRRLKALGAD---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 94 dlvafgrypYSKGRLTIEDKAHIDQSIAYLNLDDLRDRFLDELsggqRQRAFVAMVLcqDT--DYVLLDEPLNNlDMKHA 171
Cdd:COG3598 76 ---------LGLPFADLDGRLRLLSLAGDLDDTDDLEALERAI----EEEGPDLVVI--DPlaRVFGGDENDAE-EMRAF 139
|
170 180
....*....|....*....|...
gi 351592836 172 MGMmklMQRACHELGKTVVLVLH 194
Cdd:COG3598 140 LNP---LDRLAERTGAAVLLVHH 159
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-167 |
1.22e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.53 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 16 VVDDVSIELPARGITSIIGPNGAGKS-TMLSIVSRLLGMDAGSVTVDGLDVS-NTPSDVLARRLSILRQDNHMTARLTVA 93
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKiRNPQQAIAQGIAMVPEDRKRDGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 94 D------LVAFGRYpysKGRLTIEDKA---HIDQSIAYLNLD----DLRdrfLDELSGGQRQRAFVAMVLCQDTDYVLLD 160
Cdd:PRK13549 357 GvgknitLAALDRF---TGGSRIDDAAelkTILESIQRLKVKtaspELA---IARLSGGNQQKAVLAKCLLLNPKILILD 430
|
....*..
gi 351592836 161 EPLNNLD 167
Cdd:PRK13549 431 EPTRGID 437
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-52 |
1.83e-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: 38.83 E-value: 1.83e-03
10 20 30
....*....|....*....|....*....|....
gi 351592836 19 DVSIELPaRGITSIIGPNGAGKSTMLSIVSRLLG 52
Cdd:COG3593 16 DLSIELS-DDLTVLVGENNSGKSSILEALRLLLG 48
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
17-41 |
2.26e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.27 E-value: 2.26e-03
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-41 |
2.30e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 2.30e-03
10 20
....*....|....*....|....*
gi 351592836 17 VDDVSIELPaRGITSIIGPNGAGKS 41
Cdd:COG1196 15 ADPTTIPFE-PGITAIVGPNGSGKS 38
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-167 |
2.96e-03 |
|
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: 38.30 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 1 MIITSGIKKYY-GETAVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDaGSVTVDGLDVSNTPSDVLARRLSI 79
Cdd:cd03289 3 MTVKDLTAKYTeGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 80 LRQDNHMTARLTVADLVAFGRYPYSKGRLTIED---KAHIDQSIAYLNLDDLRDRFLdeLSGGQRQRAFVAMVLCQDTDY 156
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEvglKSVIEQFPGQLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAKI 159
|
170
....*....|.
gi 351592836 157 VLLDEPLNNLD 167
Cdd:cd03289 160 LLLDEPSAHLD 170
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
17-41 |
3.09e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 37.44 E-value: 3.09e-03
10 20
....*....|....*....|....*
gi 351592836 17 VDDVSIELPaRGITSIIGPNGAGKS 41
Cdd:cd03278 13 ADKTTIPFP-PGLTAIVGPNGSGKS 36
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
30-52 |
3.71e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 37.55 E-value: 3.71e-03
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-51 |
3.92e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.21 E-value: 3.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 351592836 1 MIITSGIKKYYGetaVVDDVSIELPaRGITSIIGPNGAGKSTMLSIVSRLL 51
Cdd:COG4717 1 MKIKELEIYGFG---KFRDRTIEFS-PGLNVIYGPNEAGKSTLLAFIRAML 47
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
7-224 |
4.39e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 37.49 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 7 IKKYYGET-AVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDAGSVTVDGldvsntpsdvlarRLSILRQDNH 85
Cdd:PRK13546 29 IPKHKNKTfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-------------EVSVIAISAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 86 MTARLTVADLVAFGRYPYSKGRLTIedKAHIDQSIAYLNLDDLRDRFLDELSGGQRQRAFVAMVLCQDTDYVLLDEPLNN 165
Cdd:PRK13546 96 LSGQLTGIENIEFKMLCMGFKRKEI--KAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 351592836 166 LDMKHAMGMMKLMQRAcHELGKTVVLVLHDINFASWYSDYIIAMKNGRVIRHGTKNDII 224
Cdd:PRK13546 174 GDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-63 |
5.61e-03 |
|
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: 37.97 E-value: 5.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 351592836 15 AVVDDVSIELPARGITSIIGPNGAGKSTMLSIVSRLLGMDaGSVTVDGL 63
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGV 1280
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
24-194 |
5.85e-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: 36.98 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 24 LPARGITSIIGPNGAGKSTMLSIVSR-------LLGMDAGSVTVDGLDVSNT-PSDVLARRLSILRQDNHMTARLTVADL 95
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLAAavatgkpWLGGPRVPEQGKVLYVSAEgPADELRRRLRAAGADLDLPARLLFLSL 109
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351592836 96 VAFGRYPY--SKGRLTIEDKAHIDQSIAYLNLDDLrdrfldelsggqrqrafvamvlcqdtdyVLLDePL-----NNLDM 168
Cdd:pfam13481 110 VESLPLFFldRGGPLLDADVDALEAALEEVEDPDL----------------------------VVID-PLaralgGDENS 160
|
170 180
....*....|....*....|....*..
gi 351592836 169 KHAMGMM-KLMQRACHELGKTVVLVLH 194
Cdd:pfam13481 161 NSDVGRLvKALDRLARRTGATVLLVHH 187
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