|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-254 |
5.12e-124 |
|
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: 361.67 E-value: 5.12e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAFPYSVKETVSLGRYAHQkGWFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRIL 160
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHL-GLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 161 LLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIKKVYKTQI 240
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEA 239
|
250
....*....|....
gi 730207193 241 KNHPHPEIAKPQLL 254
Cdd:COG1120 240 RVIEDPVTGRPLVL 253
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-255 |
2.79e-101 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 303.58 E-value: 2.79e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAFPYSVKETVSLGRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQ----- 155
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPHGSS-----AAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 156 --QPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEeLTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIK 233
Cdd:COG4559 156 dgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRG-GGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLE 234
|
250 260
....*....|....*....|..
gi 730207193 234 KVYKTQIKNHPHPEIAKPQLLL 255
Cdd:COG4559 235 RVYGADLRVLAHPEGGCPQVLP 256
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-255 |
3.13e-99 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 298.61 E-value: 3.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAFPYSVKETVSLGRYAHQkgwfnSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQ----- 155
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPHG-----LSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 156 -QPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIKK 234
Cdd:PRK13548 157 gPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRR 236
|
250 260
....*....|....*....|.
gi 730207193 235 VYKTQIKNHPHPEIAKPQLLL 255
Cdd:PRK13548 237 VYGADVLVQPHPETGAPLVLP 257
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-245 |
1.64e-82 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 255.01 E-value: 1.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPltqysPKQLARMMAVL 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGE--QAFPYSVKETVSLGRYAHqKGWFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPR 158
Cdd:COG1121 81 PQRAEvdWDFPITVRDVVLMGRYGR-RGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 159 ILLLDEPTNHLDLSFQKELLDLLKKWaAEEELTVVSIFHDLNLASLYCDRLLLMeNGEVLIVDTPAEVLKEERIKKVYKT 238
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRAYGG 237
|
....*..
gi 730207193 239 QIKNHPH 245
Cdd:COG1121 238 PVALLAH 244
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
2.64e-81 |
|
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: 249.66 E-value: 2.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 3 TVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 83 hgeqafpysvketvslgryahqkgwfnswhdedeqivqkVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLL 162
Cdd:cd03214 81 ---------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 163 DEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVL 218
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-256 |
4.24e-76 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 239.15 E-value: 4.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAFPYSVKETVSLGRyahqKGWFNSW---HDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQP 157
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGR----SPWLSLWgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 158 RILLLDEPTNHLDLSFQKELLDLLKKWAAEEElTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIKKVYK 237
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFD 236
|
250
....*....|....*....
gi 730207193 238 TQIKNHPHPEIAKPQLLLV 256
Cdd:PRK11231 237 VEAEIHPEPVSGTPMCVVR 255
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-218 |
7.71e-71 |
|
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: 223.95 E-value: 7.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 4 VKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSpkqlaRMMAVLPQH 83
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 84 GE--QAFPYSVKETVSLGRYAHqKGWFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILL 161
Cdd:cd03235 77 RSidRDFPISVRDVVLMGLYGH-KGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 162 LDEPTNHLDLSFQKELLDLLKKWAAeEELTVVSIFHDLNLASLYCDRLLLMeNGEVL 218
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-246 |
7.74e-70 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 222.65 E-value: 7.74e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAFPYSVKETVSLGRYAHQKGWFNSwhdEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRIL 160
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYSKGRLTA---EDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 161 LLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIKKVYKTQI 240
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDI 237
|
....*.
gi 730207193 241 KNHPHP 246
Cdd:COG4604 238 EVEEID 243
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
12-257 |
1.01e-67 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 217.37 E-value: 1.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 12 AGGE-VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQHGEQAFPY 90
Cdd:TIGR03873 11 AGGRlIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVEQDSDTAVPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 91 SVKETVSLGRYAHQKGWFNSwHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLD 170
Cdd:TIGR03873 91 TVRDVVALGRIPHRSLWAGD-SPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 171 LSFQKELLDLLKKWAAeEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIKKVYKTQIKNHPHPEIAK 250
Cdd:TIGR03873 170 VRAQLETLALVRELAA-TGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIRAVYGVDATVLTHPDTGR 248
|
....*..
gi 730207193 251 PQLLLVP 257
Cdd:TIGR03873 249 PIIAFSP 255
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-233 |
5.15e-66 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 217.79 E-value: 5.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAFPYSVKETVSLGRYAHqKGWFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRIL 160
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPH-RSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730207193 161 LLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIK 233
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRR-LVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR 233
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-232 |
1.58e-61 |
|
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: 200.25 E-value: 1.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:COG1122 1 IELENLSFSYPGGtPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGE-QAFPYSVKETVSLGryahqkgWFNSWHDEDE--QIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQP 157
Cdd:COG1122 81 FQNPDdQLFAPTVEEDVAFG-------PENLGLPREEirERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 158 RILLLDEPTNHLDLSFQKELLDLLKKWaAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERI 232
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-228 |
6.74e-60 |
|
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: 196.95 E-value: 6.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG----EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM 76
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MAVLPQHGEQAF-P-YSVKETVSLGRYAHQKgwfnswhDEDEQIVQKVMEQTGIT-RLQDKSIVELSGGEKQRVFLAQAL 153
Cdd:COG1124 81 VQMVFQDPYASLhPrHTVDRILAEPLRIHGL-------PDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 154 AQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLK 228
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-229 |
1.19e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 195.67 E-value: 1.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQySPKQLARMMAVLP 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QhgEQAFP--YSVKETVSL-GRYAHQKGwfnswhDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPR 158
Cdd:COG1131 80 Q--EPALYpdLTVRENLRFfARLYGLPR------KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730207193 159 ILLLDEPTNHLDLSFQKELLDLLKKWAAEEeltvVSIF---HDLNLASLYCDRLLLMENGEVLIVDTPAEVLKE 229
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEG----KTVLlstHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-243 |
4.30e-58 |
|
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: 191.99 E-value: 4.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARmMAVL 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQhgEQAFPY--SVKEtvSLGRYAHQKGwfnSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPR 158
Cdd:COG4555 80 PD--ERGLYDrlTVRE--NIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 159 ILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIfHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKE---ERIKKV 235
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSS-HIMQEVEALCDRVVILHKGKVVAQGSLDELREEigeENLEDA 231
|
....*...
gi 730207193 236 YKTQIKNH 243
Cdd:COG4555 232 FVALIGSE 239
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-236 |
1.55e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 185.26 E-value: 1.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM--- 76
Cdd:COG3638 2 MLELRNLSKRYPGGtPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MAVLPQHgeqaFP----YSVKETVSLGRYAHQ---KGWFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFL 149
Cdd:COG3638 82 IGMIFQQ----FNlvprLSVLTNVLAGRLGRTstwRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 150 AQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVlIVDTPAEVLKE 229
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV-VFDGPPAELTD 236
|
....*..
gi 730207193 230 ERIKKVY 236
Cdd:COG3638 237 AVLREIY 243
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-216 |
1.68e-55 |
|
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: 184.21 E-value: 1.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 4 VKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLP 81
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHGE-QAFPYSVKETVSLG-RYAHQKgwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:cd03225 82 QNPDdQFFGPTVEEEVAFGlENLGLP------EEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 160 LLLDEPTNHLDLSFQKELLDLLKKWaAEEELTVVSIFHDLNLASLYCDRLLLMENGE 216
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-236 |
5.30e-55 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 184.80 E-value: 5.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 5 KNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQHG 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 85 EQAFPYSVKETVSLGRYAHQKgWFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDE 164
Cdd:PRK10253 91 TTPGDITVQELVARGRYPHQP-LFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 730207193 165 PTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIKKVY 236
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-241 |
2.09e-54 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 183.49 E-value: 2.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFR--------EGSIDVEGRPLTQYSPKQ 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 73 LARMMAVLPQHGEQAFPYSVKETVSLGRYAHQKGWFNSWHdEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQA 152
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTH-RDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 153 LAQ---------QPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTP 223
Cdd:PRK13547 160 LAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
250
....*....|....*...
gi 730207193 224 AEVLKEERIKKVYKTQIK 241
Cdd:PRK13547 240 ADVLTPAHIARCYGFAVR 257
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-241 |
5.23e-52 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 176.18 E-value: 5.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFrEGSIDVEGRPLTQYSPKQLARMMAVLPQHGEQAFPYSVKETV 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 97 SLGRYAHQKgwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQ-------QPRILLLDEPTNHL 169
Cdd:COG4138 91 ALHQPAGAS------SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 730207193 170 DLSFQKELLDLLKKWAAEEELTVVSIfHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIKKVYKTQIK 241
Cdd:COG4138 165 DVAQQAALDRLLRELCQQGITVVMSS-HDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFR 235
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-236 |
6.27e-52 |
|
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: 175.95 E-value: 6.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM--- 76
Cdd:TIGR02315 1 MLEVENLSKVYPNGkQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MAVLPQHGEQAFPYSVKETVSLGRYAHQKGW---FNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQAL 153
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKPTWrslLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 154 AQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEvLKEERIK 233
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSE-LDDEVLR 239
|
...
gi 730207193 234 KVY 236
Cdd:TIGR02315 240 HIY 242
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-227 |
1.07e-51 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 182.80 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGE-----VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSP---KQ 72
Cdd:COG1123 260 LLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 73 LARMMAVLPQHGEQAF-P-YSVKETVSLGRYAHqkGWFNSwhDEDEQIVQKVMEQTGI-TRLQDKSIVELSGGEKQRVFL 149
Cdd:COG1123 340 LRRRVQMVFQDPYSSLnPrMTVGDIIAEPLRLH--GLLSR--AERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 150 AQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVL 227
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-251 |
3.10e-51 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 174.98 E-value: 3.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 3 TVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQ 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 83 HGEQAFPYSVKETVSLGRYAhqkgwfnsWHD-------EDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQ 155
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRYP--------WHGalgrfgaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 156 QPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIKKV 235
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQI 244
|
250
....*....|....*.
gi 730207193 236 YKTQIKNHPHPEIAKP 251
Cdd:PRK10575 245 YGIPMGILPHPAGAAP 260
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-211 |
4.03e-51 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 172.03 E-value: 4.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 10 GYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGrpltqyspkqlARMMAVLPQHGE--QA 87
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEvpDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 88 FPYSVKETVSLGRYAHQKGWfnSWHD-EDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPT 166
Cdd:NF040873 70 LPLTVRDLVAMGRWARRGLW--RRLTrDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 730207193 167 NHLDLSFQKELLDLLKKWAAeEELTVVSIFHDLNLASLYCDRLLL 211
Cdd:NF040873 148 TGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
|
|
| CbiZ |
COG1865 |
Adenosylcobinamide amidohydrolase [Coenzyme transport and metabolism]; |
281-476 |
1.18e-50 |
|
Adenosylcobinamide amidohydrolase [Coenzyme transport and metabolism];
Pssm-ID: 441470 Cd Length: 224 Bit Score: 171.98 E-value: 1.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 281 IVLQSPMNLRTMSSGITGAGIGWHSSFVHRVVPMEYDCSDHKAEMAEYLQENGFLPSETVGMMTAVPAETASYQLFEDGD 360
Cdd:COG1865 14 LVVRFPGPRRVLSTAVLNGGLREARAVFNHQVPEDYDRTDPEEYLAEVLARLGLPPGDTVGLLTAADMENAAIAEESFGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 361 LSIFIIVSAG-------------NTHRDRPRN--INTWLFINGKISEEAFIQSAMTAAEAKISVLNELEGSGAGSAGQSA 425
Cdd:COG1865 94 LSVTAVVTAGvsnavragadpasYYEPRPPPPgtINIIVLINAPLSDGALVNAVITATEAKTAALQELGIGSRYSGGLAT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 730207193 426 GISTDSICIAAIQQGESIAYAGTATPLGKLISEGIYTCTKEAILKYRSSKA 476
Cdd:COG1865 174 GTGTDAIAVAAPPDGEPLTYAGKHTKLGELIGRAVYEAVREALRRQNGLTP 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-231 |
1.59e-50 |
|
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: 179.71 E-value: 1.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFR---EGSIDVEGRPLTQYSPKQLAR 75
Cdd:COG1123 4 LLEVRDLSVRYPGGDvpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 76 MMAVLPQHGEQAF-PYSVKETVSLGRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALA 154
Cdd:COG1123 84 RIGMVFQDPMTQLnPVTVGDQIAEALENLGLS-----RAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 155 QQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEER 231
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-236 |
1.91e-50 |
|
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: 171.98 E-value: 1.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPK---QLARMM 77
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 AVLPQHGEQAFPYSVKETVSLGRYAHQ---KGWFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALA 154
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRstwRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 155 QQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVlIVDTPAEVLKEERIKK 234
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI-VFDGPPAELTDEVLDE 239
|
..
gi 730207193 235 VY 236
Cdd:cd03256 240 IY 241
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-236 |
7.47e-50 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 170.60 E-value: 7.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLT---GGYAggeVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM- 76
Cdd:COG0411 4 LLEVRGLTkrfGGLV---AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MAVLPQHGeQAFP-YSVKETVSLGRYAHQKGWFNS-------WHDEDEQIVQKVME---QTGITRLQDKSIVELSGGEKQ 145
Cdd:COG0411 81 IARTFQNP-RLFPeLTVLENVLVAAHARLGRGLLAallrlprARREEREARERAEElleRVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 146 RVFLAQALAQQPRILLLDEPT---NHLDLsfqKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDT 222
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAaglNPEET---EELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
250
....*....|....
gi 730207193 223 PAEVLKEERIKKVY 236
Cdd:COG0411 237 PAEVRADPRVIEAY 250
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-217 |
2.63e-49 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 166.42 E-value: 2.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQySPKQLARMMAVLP 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHgeqafpysvketVSLgrYAHQKGWFNswhdedeqivqkvmeqtgitrlqdksiVELSGGEKQRVFLAQALAQQPRILL 161
Cdd:cd03230 80 EE------------PSL--YENLTVREN---------------------------LKLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 162 LDEPTNHLDLSFQKELLDLLKKWAAeEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
4.09e-49 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 167.91 E-value: 4.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGE----VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM 76
Cdd:COG1136 4 LLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MA-----VLpqhgeQAF---PY-SVKETVSLG-RYAHQKgwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQR 146
Cdd:COG1136 84 RRrhigfVF-----QFFnllPElTALENVALPlLLAGVS------RKERRERARELLERVGLGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 147 VFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASlYCDRLLLMENGEV 217
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-217 |
7.66e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.53 E-value: 7.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLP 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHgeqafPYSVKETVslgrYAHQKGWFNSWHDE-DEQIVQKVMEQTGIT-RLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:COG4619 81 QE-----PALWGGTV----RDNLPFPFQLRERKfDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 160 LLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-231 |
8.77e-49 |
|
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: 167.23 E-value: 8.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 4 VKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM------- 76
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgigrtfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 -MAVLPQHgeqafpySVKETVSLGRYAHQKGWFNSWH--DEDEQIVQKVM---EQTGITRLQDKSIVELSGGEKQRVFLA 150
Cdd:cd03219 83 iPRLFPEL-------TVLENVMVAAQARTGSGLLLARarREEREARERAEellERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 151 QALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWaAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEE 230
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
.
gi 730207193 231 R 231
Cdd:cd03219 235 R 235
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-216 |
3.39e-48 |
|
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: 163.18 E-value: 3.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 3 TVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 83 hgeqafpysvketvslgryahqkgwfnswhdedeqivqkvmeqtgitrlqdksiveLSGGEKQRVFLAQALAQQPRILLL 162
Cdd:cd00267 81 --------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 730207193 163 DEPTNHLDLSFQKELLDLLKKWaAEEELTVVSIFHDLNLASLYCDRLLLMENGE 216
Cdd:cd00267 105 DEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-226 |
1.38e-46 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 164.89 E-value: 1.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlaRMMAVL 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGeqA-FPY-SVKETVSLG-RYAHQKGwfnswhDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQP 157
Cdd:COG3842 83 FQDY--AlFPHlTVAENVAFGlRMRGVPK------AEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 158 RILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEV 226
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-217 |
1.64e-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: 160.73 E-value: 1.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGG----EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM- 76
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 ---MAVLPQHgeqaF---PY-SVKETVSLG-RYAHQKGWfnswhdEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVF 148
Cdd:cd03255 81 rrhIGFVFQS----FnllPDlTALENVELPlLLAGVPKK------ERRERAEELLERVGLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 149 LAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASlYCDRLLLMENGEV 217
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-217 |
6.34e-46 |
|
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: 159.59 E-value: 6.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG----EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLA-- 74
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 75 -RMMAVLPQHGEQAFP--YSVKETVSLGRYAHQKGWfnswhDEDEQIVQKVMEQTGI---TRLQDKSIVELSGGEKQRVF 148
Cdd:cd03257 81 rKEIQMVFQDPMSSLNprMTIGEQIAEPLRIHGKLS-----KKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 149 LAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-230 |
2.82e-45 |
|
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: 168.09 E-value: 2.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHGEQaFPYSVKETVSLGRYahqkgwfnswHDEDEQIVQkVMEQTGI------------TRLQDKSIvELSGGEKQRV 147
Cdd:COG2274 554 VLQDVFL-FSGTIRENITLGDP----------DATDEEIIE-AARLAGLhdfiealpmgydTVVGEGGS-NLSGGQRQRL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 148 FLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAeeELTVVSIFHDLNLASLyCDRLLLMENGEVLIVDTPAEVL 227
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELL 697
|
...
gi 730207193 228 KEE 230
Cdd:COG2274 698 ARK 700
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-218 |
3.85e-45 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 156.91 E-value: 3.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlaRMMAVLP 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHGeqA-FPY-SVKETVSLGRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:cd03259 79 QDY--AlFPHlTVAENIAFGLKLRGVP-----KAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 160 LLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVL 218
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-236 |
7.51e-45 |
|
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: 156.68 E-value: 7.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM-MAV 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQhGEQAFPY-SVKETVSLGRYAHQKgwfnswHDEDEQIVQKVME----------QTGITrlqdksiveLSGGEKQRVF 148
Cdd:COG0410 83 VPE-GRRIFPSlTVEENLLLGAYARRD------RAEVRADLERVYElfprlkerrrQRAGT---------LSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 149 LAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLK 228
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRR-LNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
....*...
gi 730207193 229 EERIKKVY 236
Cdd:COG0410 226 DPEVREAY 233
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-227 |
1.71e-44 |
|
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: 155.78 E-value: 1.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 22 FEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPltqysPKQLARMMAVLPQHGEQA--FPYSVKETVSLG 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVPQRHEFAwdFPISVAHTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 100 RYAHQkGWFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLD 179
Cdd:TIGR03771 76 RTGHI-GWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 730207193 180 LLKKWAAEEeLTVVSIFHDLNLASLYCDRLLLMeNGEVLIVDTPAEVL 227
Cdd:TIGR03771 155 LFIELAGAG-TAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQ 200
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-228 |
2.97e-44 |
|
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: 155.52 E-value: 2.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM---M 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 AVLPQHGeqA-F-PYSVKETVSLGRYAHQKgwfnswHDEDE--QIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQAL 153
Cdd:COG1127 85 GMLFQGG--AlFdSLTVFENVAFPLREHTD------LSEAEirELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 154 AQQPRILLLDEPTNHLD--LSfqKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLK 228
Cdd:COG1127 157 ALDPEILLYDEPTAGLDpiTS--AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-217 |
3.01e-44 |
|
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: 154.34 E-value: 3.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 3 TVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLtqySPKQLARMMAVLP 81
Cdd:cd03226 1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QH-GEQAFPYSVKETVSLGryahqkgwfNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRIL 160
Cdd:cd03226 78 QDvDYQLFTDSVREELLLG---------LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 161 LLDEPTNHLDLSFQKELLDLLKKWAAEEElTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-216 |
1.66e-42 |
|
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: 148.87 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYS--PKQLARMMAV 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHGeQAFPY-SVKETVSLGryahqkgwfnswhdedeqivqkvmeqtgitrlqdksiveLSGGEKQRVFLAQALAQQPR 158
Cdd:cd03229 81 VFQDF-ALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 159 ILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGE 216
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-229 |
2.00e-42 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 149.89 E-value: 2.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM-MAVL 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQhGEQAFPY-SVKETVSLGRYAHQKgwfnswhDEDEQIVQKVMEQtgITRLQDKSIV---ELSGGEKQRVFLAQALAQQ 156
Cdd:cd03224 81 PE-GRRIFPElTVEENLLLGAYARRR-------AKRKARLERVYEL--FPRLKERRKQlagTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730207193 157 PRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKE 229
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRE-LRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-234 |
2.62e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 151.04 E-value: 2.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEG-RPLTQYSPKQLARMMA 78
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 VLPQHGEQAFPYS-VKETVSLG-------RyahqkgwfnswhDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLA 150
Cdd:TIGR04520 81 MVFQNPDNQFVGAtVEDDVAFGlenlgvpR------------EEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 151 QALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLAsLYCDRLLLMENGEVLIVDTPAEVLK-E 229
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSqV 227
|
....*
gi 730207193 230 ERIKK 234
Cdd:TIGR04520 228 ELLKE 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-230 |
3.41e-42 |
|
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: 157.61 E-value: 3.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:COG4988 337 IELEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHgeqafPY----SVKETVSLGRyahqkgwfnswHDEDEQIVQKVMEQTG----ITRLQDK--SIVE-----LSGGEKQ 145
Cdd:COG4988 417 PQN-----PYlfagTIRENLRLGR-----------PDASDEELEAALEAAGldefVAALPDGldTPLGeggrgLSGGQAQ 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 146 RVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAeeELTVVSIFHDLNLASLyCDRLLLMENGEVLIVDTPAE 225
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
....*
gi 730207193 226 VLKEE 230
Cdd:COG4988 558 LLAKN 562
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-232 |
4.79e-42 |
|
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: 148.77 E-value: 4.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGG----EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKqlarmM 77
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 AVLPQHGeQAFPY-SVKETVSLGRYAHQKGWfnswhDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQ 156
Cdd:cd03293 76 GYVFQQD-ALLPWlTVLDNVALGLELQGVPK-----AEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 157 PRILLLDEPTNHLD----LSFQKELLDLLKkwaaEEELTVVSIFHDLNLASLYCDRLLLMENgevlivdTPAEVLKEERI 232
Cdd:cd03293 150 PDVLLLDEPFSALDaltrEQLQEELLDIWR----ETGKTVLLVTHDIDEAVFLADRVVVLSA-------RPGRIVAEVEV 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-232 |
7.53e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 149.47 E-value: 7.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG----EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKqlarm 76
Cdd:COG1116 7 ALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MAVLPQhgeQA--FPY-SVKETVSLGryAHQKGWFnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQAL 153
Cdd:COG1116 82 RGVVFQ---EPalLPWlTVLDNVALG--LELRGVP---KAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 154 AQQPRILLLDEPTNHLD----LSFQKELLDLlkkWaAEEELTVVSIFHDLNLASLYCDRLLLMENGevlivdtPAEVLKE 229
Cdd:COG1116 154 ANDPEVLLMDEPFGALDaltrERLQDELLRL---W-QETGKTVLFVTHDVDEAVFLADRVVVLSAR-------PGRIVEE 222
|
...
gi 730207193 230 ERI 232
Cdd:COG1116 223 IDV 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-230 |
4.65e-41 |
|
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: 154.54 E-value: 4.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:COG4987 334 LELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHgeqafPY----SVKETVSLGRyahqkgwfnswhDE--DEQIVQkVMEQTGI------------TRLQDKSiVELSG 141
Cdd:COG4987 414 VPQR-----PHlfdtTLRENLRLAR------------PDatDEELWA-ALERVGLgdwlaalpdgldTWLGEGG-RRLSG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 142 GEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEelTVVSIFHDLNLASLyCDRLLLMENGEVLIVD 221
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVEQG 551
|
....*....
gi 730207193 222 TPAEVLKEE 230
Cdd:COG4987 552 THEELLAQN 560
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-245 |
5.43e-41 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 147.00 E-value: 5.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 20 ISFEVCEGELFGILGPNGSGKTTLLKMISGALNFrEGSIDVEGRPLTQYSPKQLARMMAVLPQHGEQAFPYSVKETVSLG 99
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 100 RYAHQKgwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQ-------QPRILLLDEPTNHLDLS 172
Cdd:PRK03695 94 QPDKTR------TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730207193 173 fQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIKKVYKTQIKNHPH 245
Cdd:PRK03695 168 -QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLDV 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
16-235 |
6.50e-41 |
|
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: 146.33 E-value: 6.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlaRMMAVLPQhGEQAFPY-SVKE 94
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQ-NYALFPHmTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 95 TVSLGrYAHQKgwfnswhDEDEQIVQKVMEQT---GITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDL 171
Cdd:cd03299 91 NIAYG-LKKRK-------VDKKEIERKVLEIAemlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730207193 172 SFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIKKV 235
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFV 226
|
|
| CbiZ |
pfam01955 |
Adenosylcobinamide amidohydrolase; This prokaryotic protein family includes CbiZ which ... |
289-464 |
1.07e-40 |
|
Adenosylcobinamide amidohydrolase; This prokaryotic protein family includes CbiZ which converts adenosylcobinamide (AdoCbi) to adenosylcobyric acid (AdoCby), an intermediate of the de novo coenzyme B12 biosynthetic route.
Pssm-ID: 426529 Cd Length: 193 Bit Score: 144.62 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 289 LRTMSSGITGAGIGWHSSFVHRVVPMEYDCSDHKAEMAEYLQENGFLPSETVGMMTAVPAETASYQLFEDGDLSIFIIVS 368
Cdd:pfam01955 5 RRVLSSAVLNGGLREARAVFNHQVPKGYDRDDPAEYLEEYLEELGLDPEDTVGLLTAADMENAAIAEESFEDLEVTAVAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 369 AG--N-------THRDRPRN---INTWLFINGKISEEAFIQSAMTAAEAKISVLNELEGSGAGSAGQSAGISTDSICIAA 436
Cdd:pfam01955 85 AGvsNavragdpASYYLPPPpgtINIIVVINAPLTDGALVNALITATEAKTAALQDLGIRSRYSGGLATGTGTDAIAVAS 164
|
170 180
....*....|....*....|....*....
gi 730207193 437 IQQGES-IAYAGTATPLGKLISEGIYTCT 464
Cdd:pfam01955 165 PPEGERrIPYAGKHTKLGELIGRAVYEAV 193
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-228 |
1.50e-40 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 145.34 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM---MA 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 VLPQHGEQAFPYSVKETVSLGRYAHqkgwFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPR 158
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREH----TRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 159 ILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLK 228
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-261 |
2.24e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 148.37 E-value: 2.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPL-TQYSPKQlaRMMAVL 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRE--RRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHgEQAFPY-SVKETVSLGryAHQKGWFNswhdedEQIVQKVMEQ---TGITRLQDKSIVELSGGEKQRVFLAQALAQQ 156
Cdd:COG1118 81 FQH-YALFPHmTVAENIAFG--LRVRPPSK------AEIRARVEELlelVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 157 PRILLLDEPTNHLD------LsfQKELLDLLkkwaaeEELTVVSIF--HDLNLASLYCDRLLLMENGEVLIVDTPAEVLK 228
Cdd:COG1118 152 PEVLLLDEPFGALDakvrkeL--RRWLRRLH------DELGGTTVFvtHDQEEALELADRVVVMNQGRIEQVGTPDEVYD 223
|
250 260 270
....*....|....*....|....*....|....
gi 730207193 229 EERIKKVYK-TQIKNHPHPEIAKPQLllvpEADG 261
Cdd:COG1118 224 RPATPFVARfLGCVNVLRGRVIGGQL----EADG 253
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-241 |
9.74e-40 |
|
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: 143.69 E-value: 9.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREG-SIDVEGRPLTQYSPKQLARMMAV 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHGEQAFPY--SVKETV------SLGRYAHqkgwfnsWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQ 151
Cdd:COG1119 83 VSPALQLRFPRdeTVLDVVlsgffdSIGLYRE-------PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 152 ALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLN--LASLycDRLLLMENGEVLIVDTPAEVLKE 229
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeiPPGI--THVLLLKDGRVVAAGPKEEVLTS 233
|
250
....*....|..
gi 730207193 230 ERIKKVYKTQIK 241
Cdd:COG1119 234 ENLSEAFGLPVE 245
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-247 |
2.46e-39 |
|
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: 142.44 E-value: 2.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE-VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMA-V 79
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHGeqAFPY-SVKETVSLgrYAHQKGWfnswhdEDEQIVQKVMEQTGITRLQDKSIV-----ELSGGEKQRVFLAQAL 153
Cdd:cd03295 81 IQQIG--LFPHmTVEENIAL--VPKLLKW------PKEKIRERADELLALVGLDPAEFAdryphELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 154 AQQPRILLLDEPTNHLD----LSFQKELLDLlkkwaaEEEL--TVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVL 227
Cdd:cd03295 151 AADPPLLLMDEPFGALDpitrDQLQEEFKRL------QQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
250 260
....*....|....*....|
gi 730207193 228 keerikkvyktqikNHPHPE 247
Cdd:cd03295 225 --------------RSPAND 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-217 |
2.88e-39 |
|
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: 141.95 E-value: 2.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG----EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQL--- 73
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 74 ARMMAVLPQH----------GEQAFPYSVketvslgryahqkgwfnsWHDEDEQIVQKVMEQTGITRLQDKS---IVELS 140
Cdd:cd03258 81 RRRIGMIFQHfnllssrtvfENVALPLEI------------------AGVPKAEIEERVLELLELVGLEDKAdayPAQLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 141 GGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-167 |
3.16e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 138.93 E-value: 3.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQHgEQAFP-YSVKET 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQD-PQLFPrLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 96 VSLGRYAhqKGWFNswhDEDEQIVQKVMEQTGIT----RLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTN 167
Cdd:pfam00005 80 LRLGLLL--KGLSK---REKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-234 |
4.47e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 141.67 E-value: 4.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQySPKQLARM---M 77
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKLrrkV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 AVLPQHGEqAFP-YSVKETVSLG-RYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQ 155
Cdd:COG1126 80 GMVFQQFN-LFPhLTVLENVTLApIKVKKMS-----KAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 156 QPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVL---KEERI 232
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRD-LAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFenpQHERT 232
|
..
gi 730207193 233 KK 234
Cdd:COG1126 233 RA 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-227 |
9.25e-39 |
|
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: 141.63 E-value: 9.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 20 ISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQL----ARMMAVLPQHGeQAFPY-SVKE 94
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSF-ALLPHrTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 95 TVSLG-RYAHQKgwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSF 173
Cdd:cd03294 122 NVAFGlEVQGVP------RAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 730207193 174 QKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVL 227
Cdd:cd03294 196 RREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-211 |
1.24e-38 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 139.15 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQySPKQLARMMAVL 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PqHGEQAFPY-SVKETVSLgrYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:COG4133 81 G-HADGLKPElTVRENLRF--WAALYG-----LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 730207193 160 LLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASlyCDRLLL 211
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAA--ARVLDL 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-229 |
1.41e-38 |
|
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: 140.06 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlaRMMAVLP 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHgEQAFPY-SVKETVSLGRYAHQKgwfnswhDEDEqIVQKVMEQTGITRLQD---KSIVELSGGEKQRVFLAQALAQQP 157
Cdd:cd03300 79 QN-YALFPHlTVFENIAFGLRLKKL-------PKAE-IKERVAEALDLVQLEGyanRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 730207193 158 RILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKE 229
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-288 |
4.90e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 140.37 E-value: 4.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLtQYSPKQLARMMA- 78
Cdd:PRK13636 5 ILKVEELNYNYSDGtHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLREs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 ---VLPQHGEQAFPYSVKETVSLGRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQ 155
Cdd:PRK13636 84 vgmVFQDPDNQLFSASVYQDVSFGAVNLKLP-----EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 156 QPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVL-KEERIKK 234
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFaEKEMLRK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 730207193 235 VyktqikNHPHPEIAKPQLLLvPEADGghdadFKIDARFLDVGQDRIVLQSPMN 288
Cdd:PRK13636 239 V------NLRLPRIGHLMEIL-KEKDG-----FVFDELDLTISQARKTLNSWKN 280
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-226 |
7.54e-38 |
|
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: 138.08 E-value: 7.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLK----MISGALNFR-EGSIDVEGRPL--TQYSPKQLA 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRllnrLNDLIPGAPdEGEVLLDGKDIydLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 75 RMMAVLPQHgEQAFPYSVKETVSLGRYAHQKgwfnSWHDEDEQIVQKVMEQTGIT-RLQDKSIV-ELSGGEKQRVFLAQA 152
Cdd:cd03260 81 RRVGMVFQK-PNPFPGSIYDNVAYGLRLHGI----KLKEELDERVEEALRKAALWdEVKDRLHAlGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 153 LAQQPRILLLDEPTNHLD-LSFQK--ELLDLLKKwaaeeELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEV 226
Cdd:cd03260 156 LANEPEVLLLDEPTSALDpISTAKieELIAELKK-----EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-216 |
7.88e-38 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 135.97 E-value: 7.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGG--EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHgeqafPYsvketvslgryahqkgwfnswhdedeqivqkvmeqtgitrLQDKSIVE--LSGGEKQRVFLAQALAQQP 157
Cdd:cd03228 81 VPQD-----PF----------------------------------------LFSGTIREniLSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 158 RILLLDEPTNHLDLSFQKELLDLLKKWAaeEELTVVSIFHDLNLASLyCDRLLLMENGE 216
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALA--KGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-228 |
2.19e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.22 E-value: 2.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHGEQAF-PYSVKETVSLGRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPR 158
Cdd:PRK13635 86 VFQNPDNQFvGATVQDDVAFGLENIGVP-----REEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 159 ILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLAsLYCDRLLLMENGEVLIVDTPAEVLK 228
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-226 |
4.19e-37 |
|
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: 136.31 E-value: 4.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlaRMMAVLP 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHgEQAFPY-SVKETVSLG-RYAHQKgwfnSWHDEDEqIVQKVMEQTGITRL---QDKSIVELSGGEKQRVFLAQALAQQ 156
Cdd:cd03296 81 QH-YALFRHmTVFDNVAFGlRVKPRS----ERPPEAE-IRAKVHELLKLVQLdwlADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730207193 157 PRILLLDEPTNHLDLSFQKElldlLKKWAAE--EELTVVSIF--HDLNLASLYCDRLLLMENGEVLIVDTPAEV 226
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKE----LRRWLRRlhDELHVTTVFvtHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-230 |
7.82e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 135.27 E-value: 7.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTggYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlaRMMAVL 80
Cdd:COG3840 1 MLRLDDLT--YRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGeQAFPY-SVKETVSLGRYAHQKgwFNSwhdEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:COG3840 77 FQEN-NLFPHlTVAQNIGLGLRPGLK--LTA---EQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 160 LLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEE 230
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-217 |
8.34e-37 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 134.58 E-value: 8.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPK--QLARMMAV 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHGEqAFPY-SVKETVSLG-RYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQP 157
Cdd:cd03262 81 VFQQFN-LFPHlTVLENITLApIKVKGMS-----KAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 158 RILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKD-LAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-217 |
2.35e-36 |
|
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: 133.87 E-value: 2.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHGeQAFPYSVKETVSLGRYAHqkgwfnswhdEDEQIVQkVMEQTGITRLQDKS-------IVE----LSGGEKQRVF 148
Cdd:cd03245 83 VPQDV-TLFYGTLRDNITLGAPLA----------DDERILR-AAELAGVTDFVNKHpngldlqIGErgrgLSGGQRQAVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 149 LAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEelTVVSIFHDLNLASLyCDRLLLMENGEV 217
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDL-VDRIIVMDSGRI 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
2.57e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 135.12 E-value: 2.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMA 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 VLPQHGEQAF-PYSVKETVSLG----RYAHQKGWfnswhdedeQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQAL 153
Cdd:PRK13632 87 IIFQNPDNQFiGATVEDDIAFGlenkKVPPKKMK---------DIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 154 AQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLyCDRLLLMENGEVLIVDTPAEVLKEERI 232
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-218 |
2.88e-36 |
|
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: 133.19 E-value: 2.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 20 ISFEvCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLtQYSPKQL-----ARMMAVLPQHGeQAFPY-SVK 93
Cdd:cd03297 17 IDFD-LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL-FDSRKKInlppqQRKIGLVFQQY-ALFPHlNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 94 ETVSLGRYAHQKGwfnswhdEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSF 173
Cdd:cd03297 94 ENLAFGLKRKRNR-------EDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 730207193 174 QKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVL 218
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-226 |
5.81e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 136.36 E-value: 5.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlaRMMAVL 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHgeqafpY------SVKETVSLG-RYAHQKGwfnswhDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQAL 153
Cdd:COG3839 81 FQS------YalyphmTVYENIAFPlKLRKVPK------AEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 154 AQQPRILLLDEPTNHLD----LSFQKELLDLLKkwaaeeELTVVSIF--HD----LNLAslycDRLLLMENGEVLIVDTP 223
Cdd:COG3839 149 VREPKVFLLDEPLSNLDaklrVEMRAEIKRLHR------RLGTTTIYvtHDqveaMTLA----DRIAVMNDGRIQQVGTP 218
|
...
gi 730207193 224 AEV 226
Cdd:COG3839 219 EEL 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-282 |
9.65e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 135.21 E-value: 9.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG----EVLKGISFEVCEGELFGILGPNGSGKTTLLKMIsgalNFRE----GSIDVEGRPLTQYSPKQ 72
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI----NLLErptsGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 73 LARM---MAVLPQH----------GEQAFPysvketvsLgRYAhqkGWfnswhdEDEQIVQKVME---QTGITRLQDKSI 136
Cdd:COG1135 77 LRAArrkIGMIFQHfnllssrtvaENVALP--------L-EIA---GV------PKAEIRKRVAElleLVGLSDKADAYP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 137 VELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGE 216
Cdd:COG1135 139 SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 217 VLIVDTPAEVLKeerikkvyktqiknHPHPEIAKpqlLLVPEADGGHDADFKIDARFLDVGQDRIV 282
Cdd:COG1135 219 IVEQGPVLDVFA--------------NPQSELTR---RFLPTVLNDELPEELLARLREAAGGGRLV 267
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-217 |
1.13e-35 |
|
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: 130.41 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQhgeqafpysvketvslgryahqkgwfnswhdEDEqivqkvmeqtgitrLQDKSIVE--LSGGEKQRVFLAQALAQQP 157
Cdd:cd03246 81 LPQ-------------------------------DDE--------------LFSGSIAEniLSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 158 RILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLyCDRLLLMENGEV 217
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAA-LKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-228 |
1.27e-35 |
|
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: 131.86 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLtQYSPKQLARMMAV 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHgEQAFPY-SVKETVSLgrYAHQKGWFnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPR 158
Cdd:cd03263 80 CPQF-DALFDElTVREHLRF--YARLKGLP---KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 159 ILLLDEPTNHLDLSFQKELLDLLKKwaAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEvLK 228
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILE--VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE-LK 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-218 |
4.15e-35 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 131.93 E-value: 4.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEV-LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLarmMAVL 80
Cdd:PRK15056 7 IVVNDVTVTWRNGHTaLRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGE--QAFPYSVKETVSLGRYAHQkGWFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPR 158
Cdd:PRK15056 84 PQSEEvdWSFPVLVEDVVMMGRYGHM-GWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 159 ILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIfHDLNLASLYCDrLLLMENGEVL 218
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVST-HNLGSVTEFCD-YTVMVKGTVL 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
5.26e-35 |
|
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: 129.62 E-value: 5.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGeLFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYsPKQLARMMAVLP 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHgeqaFPYSVKETVS-LGRYAhqkGWFNSWHDEDE-QIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:cd03264 79 QE----FGVYPNFTVReFLDYI---AWLKGIPSKEVkARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730207193 160 LLLDEPTNHLD----LSFQKELLDLlkkwaAEEELTVVSIfHDLNLASLYCDRLLLMENGEVL 218
Cdd:cd03264 152 LIVDEPTAGLDpeerIRFRNLLSEL-----GEDRIVILST-HIVEDVESLCNQVAVLNKGKLV 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-217 |
7.51e-35 |
|
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: 132.48 E-value: 7.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGE----VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFR---EGSIDVEGRPLTQYSPKQL 73
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 74 ARM----MAVLPQHgeqafPYS-------VKETVSLGRYAHQKGWfnswHDEDEQIVQKVMEQTGITRlqDKSIV----- 137
Cdd:COG0444 81 RKIrgreIQMIFQD-----PMTslnpvmtVGDQIAEPLRIHGGLS----KAEARERAIELLERVGLPD--PERRLdryph 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 138 ELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-245 |
1.66e-34 |
|
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: 129.12 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlarmMAVLPQHGeqAFPY-SVKET 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR----MVVFQNYS--LLPWlTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 96 VSLG--RYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSF 173
Cdd:TIGR01184 75 IALAvdRVLPDLS-----KSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 174 QKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMEN------GEVLIVDTPAEVLKEErikkvyktqIKNHPH 245
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNgpaaniGQILEVPFPRPRDRLE---------VVEDPS 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-225 |
1.82e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.63 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM--- 76
Cdd:COG2884 1 MIRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MAV-------LPQHgeqafpySVKETVSLG-RYAHQKgwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVF 148
Cdd:COG2884 81 IGVvfqdfrlLPDR-------TVYENVALPlRVTGKS------RKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 149 LAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAE 225
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEE-INRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-199 |
2.11e-34 |
|
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: 135.18 E-value: 2.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:TIGR02868 335 LELRDLSAGYPGApPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQ--HgeqAFPYSVKETVSLGRyahqkgwfnswHDEDEQIVQKVMEQTG----ITRLQD---KSIVE----LSGGEKQRV 147
Cdd:TIGR02868 415 AQdaH---LFDTTVRENLRLAR-----------PDATDEELWAALERVGladwLRALPDgldTVLGEggarLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 730207193 148 FLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLkkWAAEEELTVVSIFHDL 199
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
4.27e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 129.43 E-value: 4.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLtQYSPKQLARMMA- 78
Cdd:PRK13639 1 ILETRDLKYSYPDGtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 ---VLPQHGEQAFPYSVKETVSLGRYAhqkgwFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQ 155
Cdd:PRK13639 80 vgiVFQNPDDQLFAPTVEEDVAFGPLN-----LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 156 QPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERI 232
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYD-LNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-236 |
1.21e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 128.69 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTqysPKQLARM---- 76
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIgylp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 --------MAVlpqhGEQAfpysvketVSLGRYahqKGWfnSWHDEDEQIvQKVMEQTGITRLQDKSIVELSGGEKQRVF 148
Cdd:COG4152 78 eerglypkMKV----GEQL--------VYLARL---KGL--SKAEAKRRA-DEWLERLGLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 149 LAQALAQQPRILLLDEPTNHLD-----LsFQKELLDLlkkwaAEEELTVvsIF--HDLNLASLYCDRLLLMENGEVLIVD 221
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDpvnveL-LKDVIREL-----AAKGTTV--IFssHQMELVEELCDRIVIINKGRKVLSG 211
|
250
....*....|....*
gi 730207193 222 TPAEVLKEERIKKVY 236
Cdd:COG4152 212 SVDEIRRQFGRNTLR 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-226 |
4.12e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.77 E-value: 4.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGE---VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMM 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 AVLPQHGEQAF-PYSVKETVSLGryAHQKGWFnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQ 156
Cdd:PRK13650 84 GMVFQNPDNQFvGATVEDDVAFG--LENKGIP---HEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 157 PRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLyCDRLLLMENGEVLIVDTPAEV 226
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVAL-SDRVLVMKNGQVESTSTPREL 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-212 |
4.18e-33 |
|
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: 131.64 E-value: 4.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAG-GEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:TIGR02857 322 LEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHgEQAFPYSVKETVSLGRyahqkgwfnswHDEDEQIVQKVMEQTGITRLQ-----------DKSIVELSGGEKQRVFL 149
Cdd:TIGR02857 402 PQH-PFLFAGTIAENIRLAR-----------PDASDAEIREALERAGLDEFVaalpqgldtpiGEGGAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730207193 150 AQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAaeEELTVVSIFHDLNLASLyCDRLLLM 212
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
4.46e-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: 124.79 E-value: 4.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGY----AGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQySPKQLARM 76
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MAVLPQhGEQAFPY-SVKETVS-LGRYAHQKGwfnswhDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALA 154
Cdd:cd03266 80 LGFVSD-STGLYDRlTARENLEyFAGLYGLKG------DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730207193 155 QQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIfHDLNLASLYCDRLLLMENGEVL 218
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFST-HIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-228 |
6.06e-33 |
|
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: 124.40 E-value: 6.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQySPKQLARMMAVLP 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHgeqafpYSVKETVSlGR---YAHQKGWFNSWHDEDEQIVQkVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPR 158
Cdd:cd03265 80 QD------LSVDDELT-GWenlYIHARLYGVPGAERRERIDE-LLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 159 ILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEvLK 228
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE-LK 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-227 |
1.32e-32 |
|
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: 127.14 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 20 ISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLtQYSPKQL-----ARMMAVLPQHGeQAFP-YSVK 93
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL-QDSARGIflpphRRRIGYVFQEA-RLFPhLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 94 ETVslgRYAHQKGWFNSWHDEDEQIVqkvmEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSF 173
Cdd:COG4148 96 GNL---LYGRKRAPRAERRISFDEVV----ELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 174 QKELLDLLKKWAAEEELTVVSIFHDLN-LASLyCDRLLLMENGEVLIVDTPAEVL 227
Cdd:COG4148 169 KAEILPYLERLRDELDIPILYVSHSLDeVARL-ADHVVLLEQGRVVASGPLAEVL 222
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-229 |
3.43e-32 |
|
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: 129.48 E-value: 3.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:COG4618 331 LSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHGEqAFPYSVKETVSlgRYAhqkgwfnswhDEDEQIVQKVMEQTGI------------TRLQDKSIVeLSGGEKQRV 147
Cdd:COG4618 411 LPQDVE-LFDGTIAENIA--RFG----------DADPEKVVAAAKLAGVhemilrlpdgydTRIGEGGAR-LSGGQRQRI 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 148 FLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLyCDRLLLMENGEVLIVDTPAEVL 227
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA-LKARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVL 554
|
..
gi 730207193 228 KE 229
Cdd:COG4618 555 AR 556
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-217 |
3.76e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 128.64 E-value: 3.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVeGRPLTqyspkqlarmMAVL 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAFP-YSVKETVSLGRyahqkgwfnswHDEDEQIVQKVMEQTGITR-LQDKSIVELSGGEKQRVFLAQALAQQPR 158
Cdd:COG0488 384 DQHQEELDPdKTVLDELRDGA-----------PGGTEQEVRGYLGRFLFSGdDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 159 ILLLDEPTNHLDLSFQKELLDLLKKWAAeeelTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALEEALDDFPG----TVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-217 |
5.65e-32 |
|
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: 128.26 E-value: 5.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGaLNFREGSIDVEGRPLTQYSPKQL----ARMMAVlpqhgeqaF--PY 90
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRALrplrRRMQVV--------FqdPF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 91 S-------VKETVSLGRYAHQKGWfnSwHDEDEQIVQKVMEQTGITR-LQDKSIVELSGGEKQRVFLAQALAQQPRILLL 162
Cdd:COG4172 373 GslsprmtVGQIIAEGLRVHGPGL--S-AAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 163 DEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
6.22e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 123.32 E-value: 6.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMA 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 VLPQHGEQAFPYS-VKETVSLGRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQP 157
Cdd:PRK13648 87 IVFQNPDNQFVGSiVKYDVAFGLENHAVP-----YDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730207193 158 RILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLAsLYCDRLLLMENGEVLIVDTPAEVLKEE 230
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-235 |
6.29e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 123.37 E-value: 6.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGAL---NFREGSIDVEGRPLTQYSPKQLARM 76
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MAVLPQHGEQAF-PYSVKETVSLGRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQ 155
Cdd:PRK13640 86 VGIVFQNPDNQFvGATVGDDVAFGLENRAVP-----RPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 156 QPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLyCDRLLLMENGEVLIVDTPAEVL-KEERIKK 234
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFsKVEMLKE 239
|
.
gi 730207193 235 V 235
Cdd:PRK13640 240 I 240
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-218 |
6.40e-32 |
|
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: 122.06 E-value: 6.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 15 EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEG-RPLTQySPKQLARMMAVLPQHGEQAFPYSVK 93
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKR-RKKFLRRIGVVFGQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 94 ETVSLGRYAHQKgwfnswhDEDE--QIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDL 171
Cdd:cd03267 114 DSFYLLAAIYDL-------PPARfkKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 730207193 172 SFQKELLDLLKKWAAEEELTVVSIFHDL-NLASLyCDRLLLMENGEVL 218
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLLTSHYMkDIEAL-ARRVLVIDKGRLL 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-198 |
1.17e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 127.10 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 4 VKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRpltqyspkqlARMmAVLPQH 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG----------LRI-GYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 84 GEQAFPYSVKETVSLG---------------------------------RYAHQKGWfnswhdEDEQIVQKVMEQTGIT- 129
Cdd:COG0488 70 PPLDDDLTVLDTVLDGdaelraleaeleeleaklaepdedlerlaelqeEFEALGGW------EAEARAEEILSGLGFPe 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 130 RLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLsfqkELLDLLKKWAAEEELTVVSIFHD 198
Cdd:COG0488 144 EDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEFLKNYPGTVLVVSHD 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-239 |
1.46e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 127.59 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE-VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:COG1132 340 IEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQ-----HGeqafpySVKETVSLGRyahqkgwfnSWHDEDEqiVQKVMEQTG----ITRLQDK--SIV-----ELSGGEK 144
Cdd:COG1132 420 PQdtflfSG------TIRENIRYGR---------PDATDEE--VEEAAKAAQahefIEALPDGydTVVgergvNLSGGQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 145 QRVFLAQALAQQPRILLLDEPTNHLD----LSFQKELLDLLKkwaaeeELTVVSIFHdlNLASL-YCDRLLLMENGEVLI 219
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDteteALIQEALERLMK------GRTTIVIAH--RLSTIrNADRILVLDDGRIVE 554
|
250 260
....*....|....*....|.
gi 730207193 220 VDTPAEVLKEERI-KKVYKTQ 239
Cdd:COG1132 555 QGTHEELLARGGLyARLYRLQ 575
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-289 |
1.61e-31 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 124.07 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 20 ISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLtqyspkQLARMMAVLPQHG-------EQA--FP- 89
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL------FDSRKGIFLPPEKrrigyvfQEArlFPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 90 YSVKETVSLGRyahqkgWFnSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHL 169
Cdd:TIGR02142 90 LSVRGNLRYGM------KR-ARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 170 DLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVL---------KEERIKKVYKTQI 240
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWaspdlpwlaREDQGSLIEGVVA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 241 KNHPHPEIAKPQL----LLVPEADG--GHDADFKIDARFLDVGQDRIVLQSPMNL 289
Cdd:TIGR02142 243 EHDQHYGLTALRLggghLWVPENLGptGARLRLRVPARDVSLALQKPEATSIRNI 297
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-226 |
1.73e-31 |
|
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: 121.00 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGE----VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARm 76
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 maVLPQH-G--EQAFP----YSVKETVSL-----GryahqkgwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEK 144
Cdd:COG4181 87 --LRARHvGfvFQSFQllptLTALENVMLplelaG------------RRDARARARALLERVGLGHRLDHYPAQLSGGEQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 145 QRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLyCDRLLLMENGEvLIVDTPA 224
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGR-LVEDTAA 230
|
..
gi 730207193 225 EV 226
Cdd:COG4181 231 TA 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-219 |
1.97e-31 |
|
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: 120.01 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGrPLTQYSPKQLARMMAVLP 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-KSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHGeqAFPY-SVKETVSLGRYAHQKgwfnswhdeDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRIL 160
Cdd:cd03268 80 APG--FYPNlTARENLRLLARLLGI---------RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 161 LLDEPTNHLDLSFQKELLDLLKKWaAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLI 219
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-229 |
2.50e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 123.66 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQ--------- 72
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDrkvgfvfqh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 73 --LARMMAVLPQhgeQAFPYSVketvsLGRYAHQKGwfnswhdedEQIVQKVM---EQTGITRLQDKSIVELSGGEKQRV 147
Cdd:PRK10851 83 yaLFRHMTVFDN---IAFGLTV-----LPRRERPNA---------AAIKAKVTqllEMVQLAHLADRYPAQLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 148 FLAQALAQQPRILLLDEPTNHLDLSFQKElldlLKKWAAE--EELTVVSIF--HDLNLASLYCDRLLLMENGEVLIVDTP 223
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKE----LRRWLRQlhEELKFTSVFvtHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
....*.
gi 730207193 224 AEVLKE 229
Cdd:PRK10851 222 DQVWRE 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-234 |
3.11e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 120.63 E-value: 3.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMI-------SGALNFREGSIDVeGRPLTQysPKQL 73
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRVGDITIDT-ARSLSQ--QKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 74 ARMmavLPQH------GEQAFPY-SVKETVSLGRYAHQKgwfnSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQR 146
Cdd:PRK11264 80 IRQ---LRQHvgfvfqNFNLFPHrTVLENIIEGPVIVKG----EPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 147 VFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGeVLIVDTPAEV 226
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQ-LAQEKRTMVIVTHEMSFARDVADRAIFMDQG-RIVEQGPAKA 230
|
250
....*....|..
gi 730207193 227 L----KEERIKK 234
Cdd:PRK11264 231 LfadpQQPRTRQ 242
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-216 |
3.82e-31 |
|
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: 119.28 E-value: 3.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLA---RM 76
Cdd:TIGR02673 1 MIEFHNVSKAYPGGvAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPllrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MAVLPQHGEQAFPYSVKETVSLG-RYAHQKGwfnswhDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQ 155
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPlEVRGKKE------REIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 156 QPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGE 216
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKR-LNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-217 |
5.84e-31 |
|
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: 118.90 E-value: 5.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlaRMMAVLP 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHgEQAFP-YSVKETVSLG-RYAHQKgwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:cd03301 79 QN-YALYPhMTVYDNIAFGlKLRKVP------KDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 160 LLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-216 |
8.65e-31 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 116.01 E-value: 8.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIdvegrpltqyspkqlarmmavlp 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 qhgeqafpySVKETVSLGRYAHqkgwfnswhdedeqivqkvmeqtgitrlqdksiveLSGGEKQRVFLAQALAQQPRILL 161
Cdd:cd03221 58 ---------TWGSTVKIGYFEQ-----------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 162 LDEPTNHLDLSFQKELLDLLKKWAAeeelTVVSIFHDLNLASLYCDRLLLMENGE 216
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-218 |
9.68e-31 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 119.55 E-value: 9.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGR-----PLTQYSPKQLAR 75
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsgaelELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 76 MM----AVLPQHGEQAFPYSVKETVSLGRYAHQKGwfNSWHDEDEQIVQKVMEQTGI--TRLQDKSiVELSGGEKQRVFL 149
Cdd:TIGR02323 83 LMrtewGFVHQNPRDGLRMRVSAGANIGERLMAIG--ARHYGNIRATAQDWLEEVEIdpTRIDDLP-RAFSGGMQQRLQI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 150 AQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVL 218
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-235 |
1.23e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.15 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGG-----EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPK--QLA 74
Cdd:PRK13637 3 IKIENLTHIYMEGtpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 75 RMMAVLPQHGE-QAFPYSVKETVSLGRyahqkgwfNSWHDEDEQI---VQKVMEQTGITR--LQDKSIVELSGGEKQRVF 148
Cdd:PRK13637 83 KKVGLVFQYPEyQLFEETIEKDIAFGP--------INLGLSEEEIenrVKRAMNIVGLDYedYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 149 LAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLK 228
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
....*...
gi 730207193 229 E-ERIKKV 235
Cdd:PRK13637 235 EvETLESI 242
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-220 |
1.75e-30 |
|
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: 117.38 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLtQYSPKQLarmMAVLP 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNR---IGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 qhgEQAFPYSvKETV--SLGRYAHQKGWfnSWHDEDEQIvQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:cd03269 77 ---EERGLYP-KMKVidQLVYLAQLKGL--KKEEARRRI-DEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 160 LLLDEPTNHLD----LSFQKELLDLlkkwaAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIV 220
Cdd:cd03269 150 LILDEPFSGLDpvnvELLKDVIREL-----ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-236 |
1.87e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.21 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM-MAV 79
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHG--------EQAFpYSVKETVSLGRyahqkgwfnswhDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQ 151
Cdd:COG1137 83 LPQEAsifrkltvEDNI-LAVLELRKLSK------------KEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 152 ALAQQPRILLLDEPtnhldlsF-----------QKELLDLLKKWAA--------EEELTVvsifhdlnlaslyCDRLLLM 212
Cdd:COG1137 150 ALATNPKFILLDEP-------FagvdpiavadiQKIIRHLKERGIGvlitdhnvRETLGI-------------CDRAYII 209
|
250 260
....*....|....*....|....
gi 730207193 213 ENGEVLIVDTPAEVLKEERIKKVY 236
Cdd:COG1137 210 SEGKVLAEGTPEEILNNPLVRKVY 233
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-236 |
3.23e-30 |
|
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: 117.26 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM-MAVL 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAFPYSVKETVSLGRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRIL 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLS-----KKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 161 LLDEPTNHLD-LSFQ--KELLDLLKKW---------AAEEELTVvsifhdlnlaslyCDRLLLMENGEVLIVDTPAEVLK 228
Cdd:cd03218 156 LLDEPFAGVDpIAVQdiQKIIKILKDRgigvlitdhNVRETLSI-------------TDRAYIIYEGKVLAEGTPEEIAA 222
|
....*...
gi 730207193 229 EERIKKVY 236
Cdd:cd03218 223 NELVRKVY 230
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-236 |
3.27e-30 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 117.38 E-value: 3.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM-MAVL 80
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAFPYSVKETVsLGRYAHQKgwfNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRIL 160
Cdd:TIGR04406 82 PQEASIFRKLTVEENI-MAVLEIRK---DLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 161 LLDEPTNHLD-LSFQ--KELLDLLKkwaaEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIKKVY 236
Cdd:TIGR04406 158 LLDEPFAGVDpIAVGdiKKIIKHLK----ERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVY 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-217 |
5.94e-30 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 114.45 E-value: 5.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlARmmavlp 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-AR------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHGeqafpysvKETVslgryaHQkgwfnswhdedeqivqkvmeqtgitrlqdksiveLSGGEKQRVFLAQALAQQPRILL 161
Cdd:cd03216 74 RAG--------IAMV------YQ----------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 162 LDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRR-LRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-217 |
8.06e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 122.63 E-value: 8.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:PRK11160 339 LTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQ--HgeqAFPYSVKETVSLGryAHQKGwfnswhdeDEQIVQkVMEQTGITRL--QDKSI--------VELSGGEKQRV 147
Cdd:PRK11160 419 VSQrvH---LFSATLRDNLLLA--APNAS--------DEALIE-VLQQVGLEKLleDDKGLnawlgeggRQLSGGEQRRL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 148 FLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEelTVVSIFHDL-NLASLycDRLLLMENGEV 217
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLtGLEQF--DRICVMDNGQI 551
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-222 |
1.27e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 116.50 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG----EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlarm 76
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 mAVLPQHgEQAFPY-SVKETVSLG-RYAHQKgwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALA 154
Cdd:COG4525 79 -GVVFQK-DALLPWlNVLDNVAFGlRLRGVP------KAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 155 QQPRILLLDEPTNHLDlSFQKELLD--LLKKWaAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDT 222
Cdd:COG4525 151 ADPRFLLMDEPFGALD-ALTREQMQelLLDVW-QRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVER 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
1.65e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 116.83 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:PRK13652 3 LIETRDLCYSYSGSkEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQH-GEQAFPYSVKETVSLGRyahqkgwFNSWHDED--EQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQ 156
Cdd:PRK13652 83 VFQNpDDQIFSPTVEQDIAFGP-------INLGLDEEtvAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730207193 157 PRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEE 230
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-217 |
2.01e-29 |
|
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: 120.94 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG----EVLKGISFEVCEGELFGILGPNGSGKT----TLLKMISGALNFREGSIDVEGRPLTQYSPKQ 72
Cdd:COG4172 6 LLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 73 LAR-------------MMAVLPQH--GEQafpysVKETVSL-----GRYAHQKgwfnswhdedeqiVQKVMEQTGITrlQ 132
Cdd:COG4172 86 LRRirgnriamifqepMTSLNPLHtiGKQ-----IAEVLRLhrglsGAAARAR-------------ALELLERVGIP--D 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 133 DKSIV-----ELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCD 207
Cdd:COG4172 146 PERRLdayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFAD 225
|
250
....*....|
gi 730207193 208 RLLLMENGEV 217
Cdd:COG4172 226 RVAVMRQGEI 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-230 |
3.02e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 117.62 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTqySPKQLARM-MAVL 80
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARArIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAFPYSVKET-VSLGRYahqkgwFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:PRK13536 120 PQFDNLDLEFTVRENlLVFGRY------FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 160 LLLDEPTNHLDLSFQKELLDLLKKWAAEEElTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEE 230
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-217 |
3.94e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 120.20 E-value: 3.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTT----LLKMISGalnfrEGSIDVEGRPLTQYSPKQL---ARMMAVLPQHgeqaf 88
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQD----- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 89 PYS-------VKETVSLGRYAHQKGWFNSwhdEDEQIVQKVMEQTGI---TRLQDKSivELSGGEKQRVFLAQALAQQPR 158
Cdd:PRK15134 371 PNSslnprlnVLQIIEEGLRVHQPTLSAA---QREQQVIAVMEEVGLdpeTRHRYPA--EFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 159 ILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-215 |
4.30e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 114.80 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlarmmAVL 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHgEQAFPY-SVKETVSLGRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:PRK11248 76 FQN-EGLLPWrNVQDNVAFGLQLAGVE-----KMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 160 LLLDEPTNHLDlSFQKELLD--LLKKWaAEEELTVVSIFHDLNLASLYCDRLLLMENG 215
Cdd:PRK11248 150 LLLDEPFGALD-AFTREQMQtlLLKLW-QETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-217 |
1.54e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 113.48 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSI-----DVEGRPLTQYSPKQLAR 75
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrDGQLRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 76 MM----AVLPQHGEQAFPYSVKETVSLGRYAHQKGW--FNSWHDEDEQIVQKVmeQTGITRLQDKSiVELSGGEKQRVFL 149
Cdd:PRK11701 86 LLrtewGFVHQHPRDGLRMQVSAGGNIGERLMAVGArhYGDIRATAGDWLERV--EIDAARIDDLP-TTFSGGMQQRLQI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 150 AQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-217 |
2.60e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.90 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG----EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLA-- 74
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 75 -RMMAVLPQH----------GEQAFPYSVKetvslgryahqkGWfnswhdEDEQIVQKV---MEQTGITRLQDKSIVELS 140
Cdd:PRK11153 81 rRQIGMIFQHfnllssrtvfDNVALPLELA------------GT------PKAEIKARVtelLELVGLSDKADRYPAQLS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 141 GGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-218 |
3.24e-28 |
|
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: 110.72 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLT------GGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFR--EGSIDVEGRPLtqySPKQL 73
Cdd:cd03213 4 LSFRNLTvtvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPL---DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 74 ARMMAVLPQHgEQAFPY-SVKETVSLGryAHQKGwfnswhdedeqivqkvmeqtgitrlqdksiveLSGGEKQRVFLAQA 152
Cdd:cd03213 81 RKIIGYVPQD-DILHPTlTVRETLMFA--AKLRG--------------------------------LSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 153 LAQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNlASLY--CDRLLLMENGEVL 218
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRR-LADTGRTIICSIHQPS-SEIFelFDKLLLLSQGRVI 191
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-227 |
4.86e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 111.72 E-value: 4.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMI-------SGALnfREGSIDVEGRPLTQYSPKQL 73
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDL--IVDGLKVNDPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 74 ARMmaVLPQHgeQAFPY-SVKETVSLGRyAHQKGwfnSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQA 152
Cdd:PRK09493 79 AGM--VFQQF--YLFPHlTALENVMFGP-LRVRG---ASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 153 LAQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVL 227
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQD-LAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-229 |
7.88e-28 |
|
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: 110.78 E-value: 7.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGY-AGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMIsgalnFR-----EGSIDVEGRPLTQYSPKQLAR 75
Cdd:cd03253 1 IEFENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL-----FRfydvsSGSILIDGQDIREVTLDSLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 76 MMAVLPQHgEQAFPYSVKETVSLGRyahqkgwfnsWHDEDEQIV---QKVMEQTGITRLQDK--SIV-----ELSGGEKQ 145
Cdd:cd03253 76 AIGVVPQD-TVLFNDTIGYNIRYGR----------PDATDEEVIeaaKAAQIHDKIMRFPDGydTIVgerglKLSGGEKQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 146 RVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEelTVVSIFHdlNLASLY-CDRLLLMENGEVLIVDTPA 224
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAH--RLSTIVnADKIIVLKDGRIVERGTHE 220
|
....*
gi 730207193 225 EVLKE 229
Cdd:cd03253 221 ELLAK 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-218 |
1.03e-27 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 111.44 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG---------EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPK 71
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 72 QLARMMAVLpQHGEQAFPYSVKETVSLGRYAHQKGWFNSWHDEDEQI--VQKVMEQTGI-TRLQDKSIVELSGGEKQRVF 148
Cdd:TIGR02769 82 QRRAFRRDV-QLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKarIAELLDMVGLrSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 149 LAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVL 218
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-230 |
1.28e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 112.21 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKqlARM-MAVL 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH--ARQrVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAFPYSVKETVSL-GRYahqkgwFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVfGRY------FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 160 LLLDEPTNHLDLSFQKELLDLLKKWAAEEElTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEE 230
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-218 |
1.76e-27 |
|
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: 109.67 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFRE---GSIDVEGRPLtqySPKQLARMMAVLPQHGEQAFPYSV 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR---KPDQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 93 KETV------SLGRyaHQKGWFNSWHDEDEqivqkVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPT 166
Cdd:cd03234 99 RETLtytailRLPR--KSSDAIRKKRVEDV-----LLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 730207193 167 NHLDLSFQKELLDLLKKWAAEEELTVVSIfHD--LNLASLYcDRLLLMENGEVL 218
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTI-HQprSDLFRLF-DRILLLSSGEIV 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-217 |
1.83e-27 |
|
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: 109.12 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 24 VCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKqlARMMAVLPQHgEQAFPY-SVKETVSLGRYA 102
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQE-NNLFAHlTVEQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 103 HQKgwfnsWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLK 182
Cdd:cd03298 98 GLK-----LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 730207193 183 KWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-218 |
1.87e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.98 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:PRK13647 5 IEVEDLHFRYKDGtKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQH-GEQAFPYSVKETVSLGRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:PRK13647 85 FQDpDDQVFSSTVWDDVAFGPVNMGLD-----KDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 160 LLLDEPTNHLDLSFQKELLDLLKKWAAEEElTVVSIFHDLNLASLYCDRLLLMENGEVL 218
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-229 |
2.75e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 112.73 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlaRMMAVLP 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHgEQAFPY-SVKETVSLG-RYahQKgwfnswhDEDEQIVQKVMEQTGITRLQ---DKSIVELSGGEKQRVFLAQALAQQ 156
Cdd:PRK09452 93 QS-YALFPHmTVFENVAFGlRM--QK-------TPAAEITPRVMEALRMVQLEefaQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 157 PRILLLDEPTNHLDLSFQKELLDLLKkwAAEEELTVVSIF--HDLNLASLYCDRLLLMENGEVLIVDTPAEVLKE 229
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELK--ALQRKLGITFVFvtHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-228 |
3.00e-27 |
|
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: 109.24 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE-VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHgEQAFPYSVKETVSLGRyahqkgwfNSWHDEDEQIVQKvmeQTGITRLQDKS-------IVE----LSGGEKQRVFL 149
Cdd:cd03254 83 LQD-TFLFSGTIMENIRLGR--------PNATDEEVIEAAK---EAGAHDFIMKLpngydtvLGEnggnLSQGERQLLAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 150 AQALAQQPRILLLDEPTNHLD----LSFQKELLDLLKKwaaeeeLTVVSIFHDLNLAsLYCDRLLLMENGEVLIVDTPAE 225
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDteteKLIQEALEKLMKG------RTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDE 223
|
...
gi 730207193 226 VLK 228
Cdd:cd03254 224 LLA 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-217 |
3.86e-27 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 107.40 E-value: 3.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSpKQLARMMAV 79
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQhgeQAFPYSVKETVSLGRyahqkgwfnswhdedeqivqkvmeqtgitrlqdksivELSGGEKQRVFLAQALAQQPRI 159
Cdd:cd03247 80 LNQ---RPYLFDTTLRNNLGR-------------------------------------RFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 160 LLLDEPTNHLDLSFQKELLDLLKKWAaeEELTVVSIFHDLnLASLYCDRLLLMENGEV 217
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVL--KDKTLIWITHHL-TGIEHMDKILFLENGKI 174
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-236 |
3.94e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 110.30 E-value: 3.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLT-QYSPKQLARM---MAVLPQHGE-QAFPYS 91
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKLrkkVSLVFQFPEaQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 92 VKETVSLGRYAhqkgwFNSWHDEDEQIVQKVMEQTGI-TRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLD 170
Cdd:PRK13641 103 VLKDVEFGPKN-----FGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 171 LSFQKELLDLLKKWAAEEElTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKE-ERIKKVY 236
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDkEWLKKHY 243
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-217 |
6.86e-27 |
|
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: 107.49 E-value: 6.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEV-LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLA---RMM 77
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 AVLPQHGEQAFPYSVKETVSLGRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQP 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVP-----PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 158 RILLLDEPTNHLDLSFQKELLDLLKKWAAeEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-230 |
7.80e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.20 E-value: 7.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlAR-----MmavLPQHgeqaF--- 88
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD-AIalgigM---VHQH----Fmlv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 89 -PYSVKETVSLGRyAHQKGWFNSWHDEDEQIvQKVMEQTGitrLQ---DKSIVELSGGEKQRVFLAQALAQQPRILLLDE 164
Cdd:COG3845 93 pNLTVAENIVLGL-EPTKGGRLDRKAARARI-RELSERYG---LDvdpDAKVEDLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 165 PTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLN--LAslYCDRLLLMENGEVliVDT--PAEVLKEE 230
Cdd:COG3845 168 PTAVLTPQEADELFEILRR-LAAEGKSIIFITHKLRevMA--IADRVTVLRRGKV--VGTvdTAETSEEE 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-217 |
8.35e-27 |
|
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: 106.36 E-value: 8.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 3 TVKNLTGGYAggevLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM-MAVLP 81
Cdd:cd03215 6 EVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 Q--HGEQAFP-YSVKETVSLGRYahqkgwfnswhdedeqivqkvmeqtgitrlqdksiveLSGGEKQRVFLAQALAQQPR 158
Cdd:cd03215 82 EdrKREGLVLdLSVAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 159 ILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLN-LASLyCDRLLLMENGEV 217
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRE-LADAGKAVLLISSELDeLLGL-CDRILVMYEGRI 182
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-222 |
1.12e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 108.62 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 6 NLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLA------RMM-- 77
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafrrdiQMVfq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 ----AVLPQHgeqafpySVKETV--------SLgryahqkgwfnswhDEDEQI--VQKVMEQTGIT-RLQDKSIVELSGG 142
Cdd:PRK10419 97 dsisAVNPRK-------TVREIIreplrhllSL--------------DKAERLarASEMLRAVDLDdSVLDKRPPQLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 143 EKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEvlIVDT 222
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQ--IVET 233
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-236 |
3.25e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 106.50 E-value: 3.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYspkQLARMM--- 77
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTAKIMrea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 -AVLPQhGEQAFP-YSVKETVSLGryahqkGWFNSwHDEDEQIVQKVMEQtgITRLQDKSIVE---LSGGEKQRVFLAQA 152
Cdd:PRK11614 82 vAIVPE-GRRVFSrMTVEENLAMG------GFFAE-RDQFQERIKWVYEL--FPRLHERRIQRagtMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 153 LAQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERI 232
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQ-LREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
....
gi 730207193 233 KKVY 236
Cdd:PRK11614 231 RSAY 234
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-210 |
9.21e-26 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 104.23 E-value: 9.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 4 VKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM----MAV 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFrrekLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHGEQAFPYSVKETVSLGrYAHQKgwfNSWHDEDEQIVQkVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLG-LKYKK---LSKKEKREKKKE-ALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 730207193 160 LLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLyCDRLL 210
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLE-LNDEGKTIIIVTHDPEVAKQ-ADRVI 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-232 |
1.02e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.72 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 3 TVKNLTGGyaggEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQ-LARMMAVLP 81
Cdd:COG1129 258 EVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVP 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 Q--HGEQAFPY-SVKETVSLGRYA-HQKGWFNSWHDEDEqIVQKVMEQTGI-TRLQDKSIVELSGGEKQRVFLAQALAQQ 156
Cdd:COG1129 334 EdrKGEGLVLDlSIRENITLASLDrLSRGGLLDRRRERA-LAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 157 PRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLN-LASLyCDRLLLMENGEvlIVDT-PAEVLKEERI 232
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRE-LAAEGKAVIVISSELPeLLGL-SDRILVMREGR--IVGElDREEATEEAI 486
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-226 |
1.20e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.00 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLA-RMM-- 77
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPiNMMfq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 --AVLPQHG-EQAFPYSVKETvSLGRyahqkgwfnswhdedEQIVQKVMEQTGITRLQD---KSIVELSGGEKQRVFLAQ 151
Cdd:PRK11607 99 syALFPHMTvEQNIAFGLKQD-KLPK---------------AEIASRVNEMLGLVHMQEfakRKPHQLSGGQRQRVALAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 152 ALAQQPRILLLDEPTNHLDLSF----QKELLDLLKKWAAeeelTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEV 226
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILERVGV----TCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-229 |
2.12e-25 |
|
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: 109.12 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGE--VLK---GISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDV----EGRPLTQYSPK 71
Cdd:TIGR03269 279 IIKVRNVSKRYISVDrgVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 72 QLARM---MAVLpqHGEQA-FPYS-----VKETVSLgryahqkgwfnswHDEDEQIVQK---VMEQTGITRLQDKSIV-- 137
Cdd:TIGR03269 359 GRGRAkryIGIL--HQEYDlYPHRtvldnLTEAIGL-------------ELPDELARMKaviTLKMVGFDEEKAEEILdk 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 138 ---ELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMEN 214
Cdd:TIGR03269 424 ypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRD 503
|
250
....*....|....*
gi 730207193 215 GEVLIVDTPAEVLKE 229
Cdd:TIGR03269 504 GKIVKIGDPEEIVEE 518
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-272 |
3.10e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.55 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLT---------GGYAGG------------EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSID 59
Cdd:COG4586 1 IIEVENLSktyrvyekePGLKGAlkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 60 VEGrpltqYSP----KQLARMMAV-----------LPqhgeqafpysVKETVSLGR--YAHQKGWFNSWHDEdeqivqkV 122
Cdd:COG4586 81 VLG-----YVPfkrrKEFARRIGVvfgqrsqlwwdLP----------AIDSFRLLKaiYRIPDAEYKKRLDE-------L 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 123 MEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLN-L 201
Cdd:COG4586 139 VELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdI 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 730207193 202 ASLyCDRLLLMENGEvLIVDTPAEVLKEE-RIKKVYKTQIKNhPHPEIAKPQLLLVPEADGGHdADFKIDAR 272
Cdd:COG4586 219 EAL-CDRVIVIDHGR-IIYDGSLEELKERfGPYKTIVLELAE-PVPPLELPRGGEVIEREGNR-VRLEVDPR 286
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-235 |
3.78e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.40 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGE------VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQ----YSP 70
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDeenlWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 71 KQLARMMAVLPQHgeQAFPYSVKETVSLGRyahqkgwfNSWHDEDEQIVQKV---MEQTGITRLQDKSIVELSGGEKQRV 147
Cdd:PRK13633 84 RNKAGMVFQNPDN--QIVATIVEEDVAFGP--------ENLGIPPEEIRERVdesLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 148 FLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLAsLYCDRLLLMENGEVLIVDTPAEVL 227
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIF 232
|
....*....
gi 730207193 228 KE-ERIKKV 235
Cdd:PRK13633 233 KEvEMMKKI 241
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-232 |
4.02e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 103.99 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQysPKQLARMM---- 77
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE--AREDTRLMfqda 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 AVLPQHgeqafpySVKETVSLGryahQKGwfnSWHDEDEQivqkVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQP 157
Cdd:PRK11247 91 RLLPWK-------KVIDNVGLG----LKG---QWRDAALQ----ALAAVGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 158 RILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV---LIVDTP----------- 223
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldLTVDLPrprrrgsarla 232
|
250
....*....|..
gi 730207193 224 ---AEVLkeERI 232
Cdd:PRK11247 233 eleAEVL--QRV 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-232 |
4.36e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.80 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlARMM--A 78
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAAgiA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 VLPQhgEQA-FPY-SVKETVSLGRYAHQKGWFNswHDEDEQIVQKVMEQTGI-----TRLQDksiveLSGGEKQRVFLAQ 151
Cdd:COG1129 83 IIHQ--ELNlVPNlSVAENIFLGREPRRGGLID--WRAMRRRARELLARLGLdidpdTPVGD-----LSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 152 ALAQQPRILLLDEPTNHLDlsfQKE---LLDLLKKwAAEEELTVVSIFHDLN-LASLyCDRLLLMENGEvLIVDTPAEVL 227
Cdd:COG1129 154 ALSRDARVLILDEPTASLT---EREverLFRIIRR-LKAQGVAIIYISHRLDeVFEI-ADRVTVLRDGR-LVGTGPVAEL 227
|
....*
gi 730207193 228 KEERI 232
Cdd:COG1129 228 TEDEL 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-217 |
4.49e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 103.12 E-value: 4.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLkgISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlaRMMAVL 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMR--FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHgEQAFPY-SVKETVSLG-----RYAHQKgwfnswHDEDEQIVQKVmeqtGITRLQDKSIVELSGGEKQRVFLAQALA 154
Cdd:PRK10771 77 FQE-NNLFSHlTVAQNIGLGlnpglKLNAAQ------REKLHAIARQM----GIEDLLARLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730207193 155 QQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-227 |
7.11e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 103.63 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQHGEQAF-PYSVKET 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFvGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 96 VSLGryahqkgwFNSWHDEDEQIVQKVMEQTGITRLQD---KSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLS 172
Cdd:PRK13642 103 VAFG--------MENQGIPREEMIKRVDEALLAVNMLDfktREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 173 FQKELLDLLKKWAAEEELTVVSIFHDLNLASlYCDRLLLMENGEVLIVDTPAEVL 227
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAPSELF 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-217 |
8.50e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 102.81 E-value: 8.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKmisgALN--------FR-EGSIDVEGRPLtqYSPK- 71
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLR----CLNrmndlipgARvEGEILLDGEDI--YDPDv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 72 ---QLARMMAVLPQHGeQAFPYSVKETVSLG-RYAHQKgwfnSWHDEDEqIVQKVMEQTGI-----TRLqDKSIVELSGG 142
Cdd:COG1117 86 dvvELRRRVGMVFQKP-NPFPKSIYDNVAYGlRLHGIK----SKSELDE-IVEESLRKAALwdevkDRL-KKSALGLSGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 143 EKQRVFLAQALAQQPRILLLDEPTNHLD-LSFQK--ELLDLLKKwaaeeELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDpISTAKieELILELKK-----DYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-236 |
8.65e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 102.76 E-value: 8.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM---- 76
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgvvr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 ----------MAVL-----PQH---------GEQAFP-YSVKETVSLGRYAHqkgwfnsWhdedeqivqkvMEQTGITRL 131
Cdd:PRK11300 85 tfqhvrlfreMTVIenllvAQHqqlktglfsGLLKTPaFRRAESEALDRAAT-------W-----------LERVGLLEH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 132 QDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLL 211
Cdd:PRK11300 147 ANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYV 226
|
250 260
....*....|....*....|....*
gi 730207193 212 MENGEVLIVDTPAEVLKEERIKKVY 236
Cdd:PRK11300 227 VNQGTPLANGTPEEIRNNPDVIKAY 251
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-216 |
9.73e-25 |
|
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: 107.56 E-value: 9.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 23 EVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGR----PltQY-SPKQLARMMAVLPQHGEQAFPYSvketvs 97
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykP--QYiSPDYDGTVEEFLRSANTDDFGSS------ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 98 lgryahqkgWFNswhdedEQIVQKVmeqtGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKEL 177
Cdd:COG1245 434 ---------YYK------TEIIKPL----GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
|
170 180 190
....*....|....*....|....*....|....*....
gi 730207193 178 LDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMEnGE 216
Cdd:COG1245 495 AKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE-GE 532
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-241 |
1.82e-24 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 101.32 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 4 VKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQH 83
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKIGSLIESPPLY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 84 GEQAFPYSVK-ETVSLGRyahqkgwfnswhdeDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLL 162
Cdd:TIGR03740 83 ENLTARENLKvHTTLLGL--------------PDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLIL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 163 DEPTNHLDLSFQKELLDLLKKWaAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDtpaEVLKEERIKKVYKTQIK 241
Cdd:TIGR03740 149 DEPTNGLDPIGIQELRELIRSF-PEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG---KINKSENLEKLFVEVVK 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-239 |
2.29e-24 |
|
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: 101.08 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 15 EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQhgE-QAFPYSVK 93
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQ--EpVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 94 ETVSLGRyahqkgwfNSWHDEDEQIVQKVMEQTG-ITRLQDK-------SIVELSGGEKQRVFLAQALAQQPRILLLDEP 165
Cdd:cd03249 95 ENIRYGK--------PDATDEEVEEAAKKANIHDfIMSLPDGydtlvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 166 TNHLDLSFQKELLDLLKKwaAEEELTVVSIFHdlNLASL-YCDRLLLMENGEVLIVDTPAEVLKEE-RIKKVYKTQ 239
Cdd:cd03249 167 TSALDAESEKLVQEALDR--AMKGRTTIVIAH--RLSTIrNADLIAVLQNGQVVEQGTHDELMAQKgVYAKLVKAQ 238
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-238 |
2.42e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 102.01 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGAL---NFREGSIDVEGRplTQYSPKQLARMM 77
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGR--TVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 AVLPQHGEQAFP-------YSVKETVSLGRYAHQKGW---FNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRV 147
Cdd:PRK09984 82 RKSRANTGYIFQqfnlvnrLSVLENVLIGALGSTPFWrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 148 FLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIvDTPAEVL 227
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFY-DGSSQQF 240
|
250
....*....|.
gi 730207193 228 KEERIKKVYKT 238
Cdd:PRK09984 241 DNERFDHLYRS 251
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-226 |
2.43e-24 |
|
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: 105.65 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFR--EGSI----------------DVEGR 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 64 P-----------------LTQYSPKQLARMMAVLPQhgeQAFPYSVKETV--SLGRYAHQKGWfnswhdEDEQIVQKVME 124
Cdd:TIGR03269 81 PcpvcggtlepeevdfwnLSDKLRRRIRKRIAIMLQ---RTFALYGDDTVldNVLEALEEIGY------EGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 125 QTGITRLQDKSI---VELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNL 201
Cdd:TIGR03269 152 LIEMVQLSHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEV 231
|
250 260
....*....|....*....|....*
gi 730207193 202 ASLYCDRLLLMENGEVLIVDTPAEV 226
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-236 |
2.93e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.12 E-value: 2.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM-MAVL 80
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAFPYSVKEtvSLGRYAHQKGWFNSWHDEDEqiVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRIL 160
Cdd:PRK10895 84 PQEASIFRRLSVYD--NLMAVLQIRDDLSAEQREDR--ANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 161 LLDEPTNHLDlsfQKELLDLLK--KWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIKKVY 236
Cdd:PRK10895 160 LLDEPFAGVD---PISVIDIKRiiEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-229 |
3.16e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.02 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLT-QYSPKQLAR------MMAVLPQHgeQAFP 89
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPlrkkvgIVFQFPEH--QLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 90 YSVKETVSLGRYAhqkgwFNSWHDEDEQIVQKVMEQTGITR-LQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNH 168
Cdd:PRK13634 101 ETVEKDICFGPMN-----FGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 169 LDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKE 229
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-217 |
4.00e-24 |
|
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: 100.30 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPltqySPkQLARMMAVLPQhgeqafpYSVKET 95
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV----SS-LLGLGGGFNPE-------LTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 96 VSL-GR-YAHQKgwfnswhDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSF 173
Cdd:cd03220 105 IYLnGRlLGLSR-------KEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 730207193 174 QKELLDLLKKWAAEEElTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:cd03220 178 QEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-217 |
7.40e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 104.54 E-value: 7.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKG-ISFEVCEGELFGILGPNGSGKTTLLKMISGALNFReGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHgEQAFPYSVKETVSLGRyahqkgwfnswHDEDEQIVQKVMEQTGI------------TRLQDKSIvELSGGEKQRVF 148
Cdd:PRK11174 429 GQN-PQLPHGTLRDNVLLGN-----------PDASDEQLQQALENAWVseflpllpqgldTPIGDQAA-GLSVGQAQRLA 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 149 LAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKwaAEEELTVVSIFHDLN-LASlyCDRLLLMENGEV 217
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA--ASRRQTTLMVTHQLEdLAQ--WDQIWVMQDGQI 561
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-224 |
8.15e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.50 E-value: 8.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVL-KGISFEVCEGElfGIL--GPNGSGKTTLLKMISGALNFREGSIDvegRPltqyspkQLARMM 77
Cdd:COG4178 362 ALALEDLTLRTPDGRPLlEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIA---RP-------AGARVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 aVLPQHgeqafPY----SVKETVSlgrYAHQKGWFNswhdeDEQIVQkVMEQTGITRLQDKSIVE------LSGGEKQRV 147
Cdd:COG4178 430 -FLPQR-----PYlplgTLREALL---YPATAEAFS-----DAELRE-ALEAVGLGHLAERLDEEadwdqvLSLGEQQRL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 148 FLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKkwAAEEELTVVSIFHDLNLASLYCDRLLLMENG--EVLIVDTPA 224
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGHRSTLAAFHDRVLELTGDGswQLLPAEAPA 571
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-230 |
8.86e-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: 99.61 E-value: 8.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGY--AGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQhgeQAFPYS--VKETVSLGRyahqkgwfnswHDEDEQIVQKVMEQTG----ITRLQ---DKSI----VELSGGEKQR 146
Cdd:cd03251 81 VSQ---DVFLFNdtVAENIAYGR-----------PGATREEVEEAARAANahefIMELPegyDTVIgergVKLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 147 VFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEelTVVSIFHDLNLASlYCDRLLLMENGEVLIVDTPAEV 226
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIE-NADRIVVLEDGKIVERGTHEEL 223
|
....
gi 730207193 227 LKEE 230
Cdd:cd03251 224 LAQG 227
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-223 |
9.88e-24 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 99.11 E-value: 9.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLkmisGALnFR-----EGSIDVEGRPLTQYSPKQLA 74
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLL----LAL-FRlvelsSGSILIDGVDISKIGLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 75 RMMAVLPQHgEQAFPYSVKETV-SLGRYAhqkgwfnswhdeDEQIVQkVMEQTGItrlqdKSIVE--------------- 138
Cdd:cd03244 78 SRISIIPQD-PVLFSGTIRSNLdPFGEYS------------DEELWQ-ALERVGL-----KEFVEslpggldtvveegge 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 139 -LSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEelTVVSIFHDLNlASLYCDRLLLMENGEV 217
Cdd:cd03244 139 nLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDC--TVLTIAHRLD-TIIDSDRILVLDKGRV 215
|
....*.
gi 730207193 218 LIVDTP 223
Cdd:cd03244 216 VEFDSP 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-215 |
1.77e-23 |
|
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: 98.66 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYA----GG---EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGalNFR--EGSIDV--EGRP--LTQ 67
Cdd:COG4778 4 LLEVENLSKTFTlhlqGGkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG--NYLpdSGSILVrhDGGWvdLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 68 YSPKQLARMMA-----------VLPQhgeqafpYSVKETVSLGRYAHQKGwfnswHDEDEQIVQKVMEQTGI-TRLQDKS 135
Cdd:COG4778 82 ASPREILALRRrtigyvsqflrVIPR-------VSALDVVAEPLLERGVD-----REEARARARELLARLNLpERLWDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 136 IVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLkkwaaeEEL-----TVVSIFHDLNLASLYCDRLL 210
Cdd:COG4778 150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELI------EEAkargtAIIGIFHDEEVREAVADRVV 223
|
....*
gi 730207193 211 LMENG 215
Cdd:COG4778 224 DVTPF 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-213 |
1.88e-23 |
|
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: 99.02 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 26 EGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEgRPLTQYSPKQL---------ARMMAVLPQHGEQAFpysvketv 96
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYIkadyegtvrDLLSSITKDFYTHPY-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 97 slgryahqkgwFNSwhdedeqivqKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKE 176
Cdd:cd03237 95 -----------FKT----------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 730207193 177 LLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLME 213
Cdd:cd03237 154 ASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
1.88e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.16 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGG-----EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSID---VEGRPLTQYSP--- 70
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 71 ------------------KQLARMMAVLPQHGE-QAFPYSVKETVSLGRYAhqkgwFNSWHDEDEQIVQKVMEQTG--IT 129
Cdd:PRK13651 83 vleklviqktrfkkikkiKEIRRRVGVVFQFAEyQLFEQTIEKDIIFGPVS-----MGVSKEEAKKRAAKYIELVGldES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 130 RLQdKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRL 209
Cdd:PRK13651 158 YLQ-RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDN-LNKQGKTIILVTHDLDNVLEWTKRT 235
|
250 260
....*....|....*....|..
gi 730207193 210 LLMENGEVLIVDTPAEVLKEER 231
Cdd:PRK13651 236 IFFKDGKIIKDGDTYDILSDNK 257
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-216 |
1.88e-23 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 103.35 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 23 EVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGR----PltQY-SPKQLARMMAVLpqhgeqafpYSVKETVS 97
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykP--QYiKPDYDGTVEDLL---------RSITDDLG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 98 lgryahqkgwfNSWHDEDeqivqkVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKEL 177
Cdd:PRK13409 430 -----------SSYYKSE------IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 492
|
170 180 190
....*....|....*....|....*....|....*....
gi 730207193 178 LDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMEnGE 216
Cdd:PRK13409 493 AKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE-GE 530
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-221 |
2.45e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.00 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG-----EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLAR 75
Cdd:COG1101 1 MLELKNLSKTFNPGtvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 76 MMAVL---PQHGeQAFPYSVKETVSLgryAHQKGWFNSWH----DEDEQIVQKVMEQTGI---TRLQDKsiVE-LSGGEK 144
Cdd:COG1101 81 YIGRVfqdPMMG-TAPSMTIEENLAL---AYRRGKRRGLRrgltKKRRELFRELLATLGLgleNRLDTK--VGlLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 145 QRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVlIVD 221
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI-ILD 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-200 |
2.79e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.55 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGAL--NFR-EGSIDVEGRPLTQYSPKQlaRMM 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLspAFSaSGEVLLNGRRLTALPAEQ--RRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 AVLPQHgEQAFPY-SVKETVSLGRYAHQKGwfnswhDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQ 156
Cdd:COG4136 79 GILFQD-DLLFPHlSVGENLAFALPPTIGR------AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 730207193 157 PRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLN 200
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-229 |
3.03e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGY-AG----GEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSP----KQ 72
Cdd:PRK13649 3 INLQNVSYTYqAGtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 73 LARMMAVLPQHGE-QAFPYSVKETVSLGRYAhqkgwFNSWHDEDEQIVQKVMEQTGITR-LQDKSIVELSGGEKQRVFLA 150
Cdd:PRK13649 83 IRKKVGLVFQFPEsQLFEETVLKDVAFGPQN-----FGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 151 QALAQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKE 229
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKK-LHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-218 |
3.27e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.31 E-value: 3.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMIS--GALNFR---EGSIDVEGRPLtqYSPK---- 71
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNI--YSPRtdtv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 72 QLARMMAVLPQHgEQAFPYSVKETVSLGRYahqkgwFNSWHDED--EQIVQKVMEQTGI-----TRLQDkSIVELSGGEK 144
Cdd:PRK14239 83 DLRKEIGMVFQQ-PNPFPMSIYENVVYGLR------LKGIKDKQvlDEAVEKSLKGASIwdevkDRLHD-SALGLSGGQQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 145 QRVFLAQALAQQPRILLLDEPTNHLD-LSFQK--ELLDLLKKwaaeeELTVVSIFHDLNLASLYCDRLLLMENGEVL 218
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDpISAGKieETLLGLKD-----DYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-217 |
3.41e-23 |
|
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: 97.54 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQHgEQAFPYSVKET 95
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQE-PVLFARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 96 VSLGRYAHqkgwfnswhdEDEQIV---QKVMEQTGITRLQDKSIVE-------LSGGEKQRVFLAQALAQQPRILLLDEP 165
Cdd:cd03248 108 IAYGLQSC----------SFECVKeaaQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 730207193 166 TNHLDLSFQKELLDLLKKWaaEEELTVVSIFHDLNLASlYCDRLLLMENGEV 217
Cdd:cd03248 178 TSALDAESEQQVQQALYDW--PERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-229 |
3.66e-23 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 96.83 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFR--EGSIDVEGRPLTQYSPKQLARMmav 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERARL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 lpqhgeqafpysvketvslgryahqkGWFNSWhdedeqivQKVMEQTGITrLQD--KSIVE-LSGGEKQRVFLAQALAQQ 156
Cdd:cd03217 78 --------------------------GIFLAF--------QYPPEIPGVK-NADflRYVNEgFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 157 PRILLLDEPTNHLDLSFQKELLDLLKKWaAEEELTVVSIFHDLNLASLY-CDRLLLMENGEvlIVDT-PAEVLKE 229
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGR--IVKSgDKELALE 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-232 |
3.97e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.03 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 4 VKNLT-GGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM-MAVLP 81
Cdd:COG3845 260 VENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIP 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 Q--HGEQAFP-YSVKETVSLGRYAH---QKGWFNSWHDEDEQiVQKVMEQTGI-TRLQDKSIVELSGGEKQRVFLAQALA 154
Cdd:COG3845 340 EdrLGRGLVPdMSVAENLILGRYRRppfSRGGFLDRKAIRAF-AEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELS 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 155 QQPRILLLDEPTNHLDLS----FQKELLDLLKKWAAeeeltVVSIFHDLN-LASLyCDRLLLMENGEvlIVDT-PAEVLK 228
Cdd:COG3845 419 RDPKLLIAAQPTRGLDVGaiefIHQRLLELRDAGAA-----VLLISEDLDeILAL-SDRIAVMYEGR--IVGEvPAAEAT 490
|
....
gi 730207193 229 EERI 232
Cdd:COG3845 491 REEI 494
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-230 |
4.83e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.49 E-value: 4.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQHgEQAFPYSVKET 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQE-PVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 96 VSLGryahqkgwFNSWHDEDEQIVQKV---------MEQTGITRLQDKSiVELSGGEKQRVFLAQALAQQPRILLLDEPT 166
Cdd:TIGR00958 575 IAYG--------LTDTPDEEIMAAAKAanahdfimeFPNGYDTEVGEKG-SQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730207193 167 NHLDLSFQKelldLLKKWAAEEELTVVSIFHDLNLASlYCDRLLLMENGEVLIVDTPAEVLKEE 230
Cdd:TIGR00958 646 SALDAECEQ----LLQESRSRASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-241 |
5.10e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 98.12 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGR----------PLTQYSPK 71
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 72 QL----ARMMAVLpQHGEQAFPYSVKETVS------LGRyahqkgwfnSWHDEDEQIVqKVMEQTGIT-RLQDKSIVELS 140
Cdd:PRK10619 86 QLrllrTRLTMVF-QHFNLWSHMTVLENVMeapiqvLGL---------SKQEARERAV-KYLAKVGIDeRAQGKYPVHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 141 GGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIV 220
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
250 260
....*....|....*....|....
gi 730207193 221 DTPAEVL---KEERIKKVYKTQIK 241
Cdd:PRK10619 234 GAPEQLFgnpQSPRLQQFLKGSLK 257
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-234 |
6.05e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.40 E-value: 6.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 4 VKNLTGgYAGGEVlKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSP-KQLARMMAVLPQ 82
Cdd:PRK09700 268 VRNVTS-RDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 83 HGEQA--FP-YSVKETVSLGRYAHQKGWFNSW---HDEDEQivQKVMEQTGITRLQ----DKSIVELSGGEKQRVFLAQA 152
Cdd:PRK09700 346 SRRDNgfFPnFSIAQNMAISRSLKDGGYKGAMglfHEVDEQ--RTAENQRELLALKchsvNQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 153 LAQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERI 232
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQ-LADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEI 502
|
..
gi 730207193 233 KK 234
Cdd:PRK09700 503 MA 504
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-226 |
1.04e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 97.11 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLarmmavl 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 pqHGEQAFPYSVKETVSLgRYAHQKGwfnswhdedeqIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRIL 160
Cdd:PRK09544 77 --YLDTTLPLTVNRFLRL-RPGTKKE-----------DILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 161 LLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMeNGEVLIVDTPAEV 226
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVV 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-245 |
1.25e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.50 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 20 ISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSP----KQLARMMAVLPQHGE-QAFPYSVKE 94
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKPVRKKVGVVFQFPEsQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 95 TVSLGRYAhqkgwFNSWHDEDEQIVQKVMEQTGITR-LQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSF 173
Cdd:PRK13643 105 DVAFGPQN-----FGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 730207193 174 QKELLDLLKKWAAEEElTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIKKVYKTQIKNHPH 245
Cdd:PRK13643 180 RIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHELGVPKATH 250
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-236 |
1.28e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 96.72 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 4 VKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMM------ 77
Cdd:COG4674 13 VEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGigrkfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 --AVLPQHgeqafpySVKETVSLGrYAHQKGWFNSWH----DEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQ 151
Cdd:COG4674 93 kpTVFEEL-------TVFENLELA-LKGDRGVFASLFarltAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 152 ALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAaeEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEER 231
Cdd:COG4674 165 LLAQDPKLLLLDEPVAGMTDAETERTAELLKSLA--GKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQADPR 242
|
....*
gi 730207193 232 IKKVY 236
Cdd:COG4674 243 VIEVY 247
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
10-200 |
1.99e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.55 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 10 GYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQ----H 83
Cdd:PRK10247 14 GYLAGDakILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQtptlF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 84 GEQ-----AFPYSVKetvslgryaHQKgwfnswhdEDEQIVQKVMEQTGI-TRLQDKSIVELSGGEKQRVFLAQALAQQP 157
Cdd:PRK10247 94 GDTvydnlIFPWQIR---------NQQ--------PDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 730207193 158 RILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLN 200
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-229 |
2.13e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.92 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGR---PL-------TQYSPKQLARMMAVLpqHGe 85
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsaLLelgagfhPELTGRENIYLNGRL--LG- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 86 qafpYSVKETvslgryahqkgwfnswhdedEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEP 165
Cdd:COG1134 118 ----LSRKEI--------------------DEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 166 TNHLDLSFQKELLDLLKKWAAEEElTV--VSifHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKE 229
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELRESGR-TVifVS--HSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-227 |
3.10e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.57 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQHGEQAFPYSVKETV 96
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 97 sLGRYAHQKGWFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKE 176
Cdd:PRK10070 124 -LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 730207193 177 LLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVL 227
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-207 |
3.44e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.87 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISgALNFREGSIDVEGRPL--------TQYSPKQL 73
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGRVEffnqniyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 74 ARMMA-VLPQhgEQAFPYSVKETVSLGRYahqkgwFNSWHD--EDEQIVQKVMEQTG----ITRLQDKSIVELSGGEKQR 146
Cdd:PRK14258 87 RRQVSmVHPK--PNLFPMSVYDNVAYGVK------IVGWRPklEIDDIVESALKDADlwdeIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 147 VFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCD 207
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-212 |
6.46e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 96.34 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 19 GISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM---MAVLPQHgeqafPYS---- 91
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQD-----PYAslnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 92 ---VKETVSLGRYAHQKGWfnswHDEDEQIVQKVMEQTGITRLQ-DKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTN 167
Cdd:COG4608 111 rmtVGDIIAEPLRIHGLAS----KAERRERVAELLELVGLRPEHaDRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 730207193 168 HLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLM 212
Cdd:COG4608 187 ALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVM 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-216 |
1.16e-21 |
|
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: 92.53 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE-----VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRpltqyspkqlarm 76
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MAVLPQhgeQAF--PYSVKETVSLGryahqkgwfnswHDEDEQIVQKVME---------------QT-----GITrlqdk 134
Cdd:cd03250 68 IAYVSQ---EPWiqNGTIRENILFG------------KPFDEERYEKVIKacalepdleilpdgdLTeigekGIN----- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 135 siveLSGGEKQRVFLAQALAQQPRILLLDEP--------TNHLdlsFQKELLDLLKKWAaeeelTVVSIFHDLNLASlYC 206
Cdd:cd03250 128 ----LSGGQKQRISLARAVYSDADIYLLDDPlsavdahvGRHI---FENCILGLLLNNK-----TRILVTHQLQLLP-HA 194
|
250
....*....|
gi 730207193 207 DRLLLMENGE 216
Cdd:cd03250 195 DQIVVLDNGR 204
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-239 |
1.20e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.30 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLtQYSPK---QLARMM 77
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 AVLPQHGEQAFPYS-VKETVSLGryahqkgwFNSWHDEDEQIVQKVMEQTGIT---RLQDKSIVELSGGEKQRVFLAQAL 153
Cdd:PRK13638 80 ATVFQDPEQQIFYTdIDSDIAFS--------LRNLGVPEAEITRRVDEALTLVdaqHFRHQPIQCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 154 AQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSiFHDLNLASLYCDRLLLMENGEVLIVDTPAEVL-KEERI 232
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIS-SHDIDLIYEISDAVYVLRQGQILTHGAPGEVFaCTEAM 230
|
....*..
gi 730207193 233 KKVYKTQ 239
Cdd:PRK13638 231 EQAGLTQ 237
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-243 |
1.24e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.28 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGE-VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQ-LARMMA 78
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 VLPQHGEQAFpysvketvsLGRYAHQKGWFNSWH-----DEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQAL 153
Cdd:PRK13644 81 IVFQNPETQF---------VGRTVEEDLAFGPENlclppIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 154 AQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHdlNLASLY-CDRLLLMENGEVLIVDTPAEVLKEERI 232
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKK-LHEKGKTIVYITH--NLEELHdADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
250 260
....*....|....*....|
gi 730207193 233 KKVYKT---------QIKNH 243
Cdd:PRK13644 229 QTLGLTppslielaeNLKMH 248
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-234 |
1.69e-21 |
|
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: 94.15 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGY--AGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNfREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQhgeQAFPYSVKETVSLGRYAhqkgwfnSWHDEDeqiVQKVMEQTGItrlqdKSIVE----------------LSGGE 143
Cdd:cd03289 82 IPQ---KVFIFSGTFRKNLDPYG-------KWSDEE---IWKVAEEVGL-----KSVIEqfpgqldfvlvdggcvLSHGH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 144 KQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKwaAEEELTVVSIFHDLNlASLYCDRLLLMENGEVLIVDTP 223
Cdd:cd03289 144 KQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ--AFADCTVILSEHRIE-AMLECQRFLVIEENKVRQYDSI 220
|
250
....*....|.
gi 730207193 224 AEVLKEERIKK 234
Cdd:cd03289 221 QKLLNEKSHFK 231
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-202 |
2.27e-21 |
|
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: 91.79 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 4 VKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPkQLARMMAVLpqh 83
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 84 GEQAfpySVKETVSLGRYAHqkgWFNSWHDeDEQIVQkVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLD 163
Cdd:cd03231 79 GHAP---GIKTTLSVLENLR---FWHADHS-DEQVEE-ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 730207193 164 EPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLA 202
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-223 |
2.64e-21 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 91.70 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGG--EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHgEQAFPYSVKETVSLgryahqkgwFNSWHDEDEQIVQKVMEqtgitrlqdkSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:cd03369 87 IPQD-PTLFSGTIRSNLDP---------FDEYSDEEIYGALRVSE----------GGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 160 LLLDEPTNHLDLSFQKelldLLKKWAAEE--ELTVVSIFHDLNlASLYCDRLLLMENGEVLIVDTP 223
Cdd:cd03369 147 LVLDEATASIDYATDA----LIQKTIREEftNSTILTIAHRLR-TIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-187 |
7.79e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 95.07 E-value: 7.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 4 VKNLTGgyAGgevLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQ-LARMMAVLPQ 82
Cdd:PRK10762 260 VDNLSG--PG---VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 83 HGEQ---AFPYSVKETVSLGRYAH-QKGWFNSWHDEDEQIVQKVMEQTGI-TRLQDKSIVELSGGEKQRVFLAQALAQQP 157
Cdd:PRK10762 335 DRKRdglVLGMSVKENMSLTALRYfSRAGGSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRP 414
|
170 180 190
....*....|....*....|....*....|
gi 730207193 158 RILLLDEPTNHLDLSFQKELLDLLKKWAAE 187
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAE 444
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-230 |
1.50e-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: 90.62 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 13 GGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQHgEQAFPYSV 92
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQE-NVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 93 KETVSLGRYA---HQKGWFNSWHDEDEQIVQKvmeQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHL 169
Cdd:cd03252 93 RDNIALADPGmsmERVIEAAKLAGAHDFISEL---PEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 170 DLSFQKELLDLLKKWAAEEelTVVSIFHDLNlASLYCDRLLLMENGEVLIVDTPAEVLKEE 230
Cdd:cd03252 170 DYESEHAIMRNMHDICAGR--TVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-288 |
1.75e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 92.63 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 32 ILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPK--------------QLARMmavlpqhgeqaFP-YSVKETV 96
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclppekrrigyvfQDARL-----------FPhYKVRGNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 97 SLGRYAHQKGWFNswhdedeQIVQKVmeqtGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKE 176
Cdd:PRK11144 98 RYGMAKSMVAQFD-------KIVALL----GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 177 LLDLLKKWAAEEELTVVSIFHDLN----LAslycDRLLLMENGEVLIVDTPAEV---------LKEERIKKVYKTQI-KN 242
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDeilrLA----DRVVVLEQGKVKAFGPLEEVwassamrpwLPKEEQSSILKVTVlEH 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 730207193 243 HPHPEIAK----PQLLLVPEADGGHDADFKIDARFLDVGqdrIVLQSPMN 288
Cdd:PRK11144 243 HPHYAMTAlalgDQHLWVNKLDAPLGTALRIRIQASDVS---LVLQPPQQ 289
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-232 |
1.79e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.84 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVE----------GRPLTQYSP------KQLARMMAV 79
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSkkiknfKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHGE-QAFPYSVKETVSLGRYAhqkgwFNSWHDEDEQIVQKVMEQTGI-TRLQDKSIVELSGGEKQRVFLAQALAQQP 157
Cdd:PRK13631 121 VFQFPEyQLFKDTIEKDIMFGPVA-----LGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 158 RILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERI 232
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-215 |
2.68e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.49 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 6 NLTGGYAGG----EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSpkqlARMMAVLP 81
Cdd:PRK11629 10 NLCKRYQEGsvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLS----SAAKAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHgEQAFPYsvketvslgRYAHQKGWFNSW----------HDEDEQIVQKVMEQTGITRLQDKS---IVELSGGEKQRVF 148
Cdd:PRK11629 86 NQ-KLGFIY---------QFHHLLPDFTALenvamplligKKKPAEINSRALEMLAAVGLEHRAnhrPSELSGGERQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 149 LAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASlYCDRLLLMENG 215
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAK-RMSRQLEMRDG 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-217 |
4.19e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 89.07 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGE----VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM 76
Cdd:PRK10584 6 IVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MAVLPQHGEQAF----PYSVKETVSLGryAHQKGwfNSWHDEDEQIVQkVMEQTGITRLQDKSIVELSGGEKQRVFLAQA 152
Cdd:PRK10584 86 RAKHVGFVFQSFmlipTLNALENVELP--ALLRG--ESSRQSRNGAKA-LLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 153 LAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASlYCDRLLLMENGEV 217
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAA-RCDRRLRLVNGQL 224
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-229 |
5.77e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 90.74 E-value: 5.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALN---------FREGSIDvegrpLTQYSPKQ----LARMMAVLPQ 82
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhvtadrFRWNGID-----LLKLSPRErrkiIGREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 83 H-----------GEQafpysVKETVSLGRYahqKGWFNSWHDEDEQIVQKVMEQTGITrlQDKSIV-----ELSGGEKQR 146
Cdd:COG4170 97 EpsscldpsakiGDQ-----LIEAIPSWTF---KGKWWQRFKWRKKRAIELLHRVGIK--DHKDIMnsyphELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 147 VFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEV 226
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQI 246
|
...
gi 730207193 227 LKE 229
Cdd:COG4170 247 LKS 249
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-202 |
5.92e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 87.80 E-value: 5.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPkQLARMMAVLp 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 qhGEQAfpySVKETVSLGRYAHqkgWFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILL 161
Cdd:TIGR01189 79 --GHLP---GLKPELSALENLH---FWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 730207193 162 LDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLA 202
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-171 |
9.21e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.20 E-value: 9.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 4 VKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFR--EGSIDVEGRPLTQYSPKQLARMMAVLp 81
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEvtSGSILLDGEDILELSPDERARAGIFL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 qhgeqAFPYSVK-ETVSLG---RYAHqkgwfNSWHDED------EQIVQKVMEQTGItrlqDKSIVE------LSGGEKQ 145
Cdd:COG0396 82 -----AFQYPVEiPGVSVSnflRTAL-----NARRGEElsarefLKLLKEKMKELGL----DEDFLDryvnegFSGGEKK 147
|
170 180
....*....|....*....|....*.
gi 730207193 146 RVFLAQALAQQPRILLLDEPTNHLDL 171
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDI 173
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-198 |
9.29e-20 |
|
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: 91.92 E-value: 9.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 3 TVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGAlnfrEGSIDVEGRPltqyspkQLARMMAVLP 81
Cdd:TIGR03719 6 TMNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV----DKDFNGEARP-------QPGIKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHGEQAFPYSVKETVSLGrYAHQKGW---FNS----WHDEDEQIVQKVMEQTgitRLQDK-------------------- 134
Cdd:TIGR03719 75 QEPQLDPTKTVRENVEEG-VAEIKDAldrFNEisakYAEPDADFDKLAAEQA---ELQEIidaadawdldsqleiamdal 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 135 -------SIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDlsfqKELLDLLKKWAAEEELTVVSIFHD 198
Cdd:TIGR03719 151 rcppwdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-231 |
1.04e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 92.49 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 20 ISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTqysPKQLA-RM----MAvlpqhgeQAFP-Y--- 90
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIAtRRrvgyMS-------QAFSlYgel 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 91 SVKETVSLgryaHQKgWFnswHDEDEQI---VQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTN 167
Cdd:NF033858 355 TVRQNLEL----HAR-LF---HLPAAEIaarVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 168 HLDL----SFQKELLDLlkkwAAEEELTvvsIF---HDLNLAsLYCDRLLLMENGEVLIVDTPAEvLKEER 231
Cdd:NF033858 427 GVDPvardMFWRLLIEL----SREDGVT---IFistHFMNEA-ERCDRISLMHAGRVLASDTPAA-LVAAR 488
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-228 |
1.28e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.16 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 5 KNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlaRMMAVLPQhG 84
Cdd:PRK11432 10 KNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQ-S 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 85 EQAFPY-SVKETVSLGRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLD 163
Cdd:PRK11432 87 YALFPHmSLGENVGYGLKMLGVP-----KEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 164 EPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLK 228
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-232 |
1.33e-19 |
|
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: 91.42 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGAL--NFREGSIDVEGRPLTQYSPKQLARM-M 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTERAgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 AVLPQHGEQAFPYSVKETVSLGRYAHQKGWFNSWhDEDEQIVQKVMEQTGITRLQDKSIV-ELSGGEKQRVFLAQALAQQ 156
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAY-NAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 157 PRILLLDEPTNHLDLSFQKELLDLLKKWAAeEELTVVSIFHDLNLASLYCDRLLLMENGEvLIVDTPAEVLKEERI 232
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQ-HVATKDMSTMSEDDI 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-226 |
1.52e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 89.90 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlaRMMAV 79
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHgeqafpY------SVKETVS-------LGRyahqkgwfnswhdedEQIVQKVMEQTGITRLQ---DKSIVELSGGE 143
Cdd:PRK11650 81 VFQN------YalyphmSVRENMAyglkirgMPK---------------AEIEERVAEAARILELEpllDRKPRELSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 144 KQRVFLAQALAQQPRILLLDEPTNHLD--LSFQK--ELLDLlkkwaaEEELTVVSIF--HD----LNLAslycDRLLLME 213
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLDakLRVQMrlEIQRL------HRRLKTTSLYvtHDqveaMTLA----DRVVVMN 209
|
250
....*....|...
gi 730207193 214 NGEVLIVDTPAEV 226
Cdd:PRK11650 210 GGVAEQIGTPVEV 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-242 |
1.82e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM-MAV 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHGEQAFPYSVKETVSLGRYAHQKGWFNSWHD--EDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQP 157
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKVCGVNIIDwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 158 RILLLDEPTNHLDlsfQKE------LLDLLKKwaaeEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEER 231
Cdd:PRK09700 165 KVIIMDEPTSSLT---NKEvdylflIMNQLRK----EGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDI 237
|
250
....*....|.
gi 730207193 232 IKKVYKTQIKN 242
Cdd:PRK09700 238 VRLMVGRELQN 248
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-227 |
2.07e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.23 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 6 NLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLK----MISGALNFR-EGSIDVEGRPLTQYSPK-QLARMMAV 79
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRtlnrMNDKVSGYRySGDVLLGGRSIFNYRDVlEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHgEQAFPYSVKETVSLGRYAHQKgwfnSWHDEDEQIVQKVMEQTGI-----TRLQDkSIVELSGGEKQRVFLAQALA 154
Cdd:PRK14271 106 LFQR-PNPFPMSIMDNVLAGVRAHKL----VPRKEFRGVAQARLTEVGLwdavkDRLSD-SPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730207193 155 QQPRILLLDEPTNHLDLSFQKELLDLLKKWAaeEELTVVSIFHDLNLASLYCDRLLLMENGEvLIVDTPAEVL 227
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGR-LVEEGPTEQL 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-232 |
3.36e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.99 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNF--REGSIDVEGRPLTQYSPKQLARMMA 78
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGEELQASNIRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 VLpQHGEQAF-PY-SVKETVSLGRYAHQKGWFNswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQ 156
Cdd:PRK13549 85 AI-IHQELALvKElSVLENIFLGNEITPGGIMD--YDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 157 PRILLLDEPTNHLDLSFQKELLDLLKKWAAeEELTVVSIFHDLNLASLYCDRLLLMENGEVlIVDTPAEVLKEERI 232
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTICVIRDGRH-IGTRPAAGMTEDDI 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-227 |
3.46e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.02 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLtqYSPKQLARMMAV-------LPQHGEQAF 88
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVL--YFGKDIFQIDAIklrkevgMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 89 PY-SVKETVSLGRYAHQKgwfnSWHDEDEQIVQKVMEQTGI-----TRLQDKSiVELSGGEKQRVFLAQALAQQPRILLL 162
Cdd:PRK14246 103 PHlSIYDNIAYPLKSHGI----KEKREIKKIVEECLRKVGLwkevyDRLNSPA-SQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 163 DEPTNHLDLSFQKELLDLLKKwaAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVL 227
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITE--LKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-252 |
3.63e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.53 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGG-----EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSP----KQ 72
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 73 LARMMAVLPQHGE-QAFPYSVKETVSLGRYAhqkgwFNSWHDEDEQIVQKVMEQTGITR-LQDKSIVELSGGEKQRVFLA 150
Cdd:PRK13646 83 VRKRIGMVFQFPEsQLFEDTVEREIIFGPKN-----FKMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 151 QALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEE 230
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDK 237
|
250 260
....*....|....*....|..
gi 730207193 231 riKKVYKTQIKnhpHPEIAKPQ 252
Cdd:PRK13646 238 --KKLADWHIG---LPEIVQLQ 254
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-228 |
4.13e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 86.82 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFR-----EGSIDVEGRPLtqYSPK----Q 72
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNI--YSPDvdpiE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 73 LARMMAVLPQHgEQAFPY-SVKETVSLGryAHQKGWFNSwHDEDEQIVQKVMEQTGI-----TRLQDKSiVELSGGEKQR 146
Cdd:PRK14267 83 VRREVGMVFQY-PNPFPHlTIYDNVAIG--VKLNGLVKS-KKELDERVEWALKKAALwdevkDRLNDYP-SNLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 147 VFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLkkWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEV 226
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELL--FELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
..
gi 730207193 227 LK 228
Cdd:PRK14267 236 FE 237
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-231 |
7.07e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 87.49 E-value: 7.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 20 ISFEVCEGELFGILGPNGSGKTTLLKMISGALNF----REGSIDVEGRPLTQYSPKQLARM----MAVLPQHGEQAF-P- 89
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgrvMAEKLEFNGQDLQRISEKERRNLvgaeVAMIFQDPMTSLnPc 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 90 YSVKETVSLGRYAHQKGWfnswHDEDEQIVQKVMEQTGI----TRLqDKSIVELSGGEKQRVFLAQALAQQPRILLLDEP 165
Cdd:PRK11022 106 YTVGFQIMEAIKVHQGGN----KKTRRQRAIDLLNQVGIpdpaSRL-DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 166 TNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEER 231
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-229 |
8.14e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 89.97 E-value: 8.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGY--AGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNfREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQhgeQAFPYSVKETVSLGRYAHqkgwfnsWHDEDeqiVQKVMEQTGItrlqdKSIVE----------------LSGGE 143
Cdd:TIGR01271 1297 IPQ---KVFIFSGTFRKNLDPYEQ-------WSDEE---IWKVAEEVGL-----KSVIEqfpdkldfvlvdggyvLSNGH 1358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 144 KQRVFLAQALAQQPRILLLDEPTNHLD-LSFQKeLLDLLKKwaAEEELTVVSIFHDLNlASLYCDRLLLMENGEVLIVDT 222
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDpVTLQI-IRKTLKQ--SFSNCTVILSEHRVE-ALLECQQFLVIEGSSVKQYDS 1434
|
....*..
gi 730207193 223 PAEVLKE 229
Cdd:TIGR01271 1435 IQKLLNE 1441
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-171 |
1.05e-18 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 88.80 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIdvegrpltQYSPKqlARmMAVLP 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSEN--AN-IGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 QHGEQAFPysvkETVSLgryahqKGWFNSWHDE--DEQIVQKVMeqtgiTRL---QD---KSIVELSGGEKQRVFLAQAL 153
Cdd:PRK15064 389 QDHAYDFE----NDLTL------FDWMSQWRQEgdDEQAVRGTL-----GRLlfsQDdikKSVKVLSGGEKGRMLFGKLM 453
|
170
....*....|....*...
gi 730207193 154 AQQPRILLLDEPTNHLDL 171
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDM 471
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-218 |
1.39e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 85.06 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMI-------SGALNFREGSIDVEGRPltqySPKQlA 74
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIAGHQFDFSQKP----SEKA-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 75 RMM-----AVLPQHgeQAFPY-SVKETVS------LGRyahqkgwfnswhdEDEQIVQKVMEQTGITRLQDKSIV---EL 139
Cdd:COG4161 78 RLLrqkvgMVFQQY--NLWPHlTVMENLIeapckvLGL-------------SKEQAREKAMKLLARLRLTDKADRfplHL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 140 SGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVL 218
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRE-LSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-228 |
1.53e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.57 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 15 EVLKGISFEVCEGELFGILGPNGSGKTTLLKmisgALNFR-------EGSIDVEGRPLTQyspKQLARMMAVLPQHgEQA 87
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMN----ALAFRspkgvkgSGSVLLNGMPIDA---KEMRAISAYVQQD-DLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 88 FP-YSVKETvsLGRYAHQKGWFNSWHDEDEQIVQKVMEQTGI-----TRLQDKSIVE-LSGGEKQRVFLAQALAQQPRIL 160
Cdd:TIGR00955 111 IPtLTVREH--LMFQAHLRMPRRVTKKEKRERVDEVLQALGLrkcanTRIGVPGRVKgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 161 LLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIfHDLNlASLYC--DRLLLMENGEVLIVDTPAEVLK 228
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTI-HQPS-SELFElfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-217 |
1.63e-18 |
|
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: 88.34 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 15 EVLKGISFEVCEGELFGILGPNGSGKTTLLKmisgaLNFR-----EGSIDVEGRPLTQYSPKQLARMMAVLPQhgeqafp 89
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLAR-----LLFRfydvtSGRILIDGQDIRDVTQASLRAAIGIVPQ------- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 90 ysvkETV----SLG---RYAHqkgwfnsWHDEDEQIVQKV-MEQTG--ITRLQD--KSIV-----ELSGGEKQRVFLAQA 152
Cdd:COG5265 440 ----DTVlfndTIAyniAYGR-------PDASEEEVEAAArAAQIHdfIESLPDgyDTRVgerglKLSGGEKQRVAIART 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 153 LAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEelTVVSIFHDLnlaS--LYCDRLLLMENGEV 217
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRL---StiVDADEILVLEAGRI 570
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
15-227 |
2.08e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.84 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 15 EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLT--QYSPK-QLARMMAVLP-------QHG 84
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRsQRIRMIFQDPstslnprQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 85 EQAFPYSVKETVSLGRYAHQKgwfnswhdedeQIVQkVMEQTGItrLQDKSIV---ELSGGEKQRVFLAQALAQQPRILL 161
Cdd:PRK15112 107 SQILDFPLRLNTDLEPEQREK-----------QIIE-TLRQVGL--LPDHASYyphMLAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 162 LDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVL 227
Cdd:PRK15112 173 ADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-217 |
2.66e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 87.92 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDV-EGRPLTQYSPKQLARMMA- 78
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLEFLRAd 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 ---------VLPQHGEQAF-PYsvketvsLGRYAHQKgwfnswhdedeqivQKVMEQTGitrlqdksivELSGGEKQRVF 148
Cdd:PRK10636 392 esplqhlarLAPQELEQKLrDY-------LGGFGFQG--------------DKVTEETR----------RFSGGEKARLV 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 149 LAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWaaEEELTVVSifHDLNLASLYCDRLLLMENGEV 217
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVS--HDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-231 |
3.06e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.19 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFR-----EGSIDVEGRPLTQYSPKQLARM 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MAVLPQHGEQAFPYSVKETVSLG----RYAHQKGWFNS---WHDEDEQIVQKVMEqtgitRLqDKSIVELSGGEKQRVFL 149
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGlklnRLVKSKKELQErvrWALEKAQLWDEVKD-----RL-DAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 150 AQALAQQPRILLLDEPTNHLDLSFQKELLDL---LKKwaaeeELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEV 226
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLfleLKK-----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
....*
gi 730207193 227 LKEER 231
Cdd:PRK14247 233 FTNPR 237
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-214 |
4.61e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 81.43 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLT-GGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIdveGRPltqyspkQLARMMaVL 80
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMP-------EGEDLL-FL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHgeqafPY----SVKETVSlgrYAhqkgwfnsWHDEdeqivqkvmeqtgitrlqdksiveLSGGEKQRVFLAQALAQQ 156
Cdd:cd03223 70 PQR-----PYlplgTLREQLI---YP--------WDDV------------------------LSGGEQQRLAFARLLLHK 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 157 PRILLLDEPTNHLDLSFQKELLDLLKkwaaEEELTVVSIFHDLNLASLYcDRLLLMEN 214
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGHRPSLWKFH-DRVLDLDG 162
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-181 |
6.24e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.23 E-value: 6.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPltqyspkqlarmmAVL 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-------------IDD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAFpY-----------SVKETVSLgrYAHQKGwfnswhdEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFL 149
Cdd:PRK13539 69 PDVAEACH-YlghrnamkpalTVAENLEF--WAAFLG-------GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVAL 138
|
170 180 190
....*....|....*....|....*....|..
gi 730207193 150 AQALAQQPRILLLDEPTNHLDLSFQKELLDLL 181
Cdd:PRK13539 139 ARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-217 |
6.52e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.26 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGgyaggEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQ-LARMMAVL 80
Cdd:PRK15439 269 LTVEDLTG-----EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAFPY---SVKETVSlGRYAHQKGWfnsWHDE--DEQIVQKVMEQTGITRLQ-DKSIVELSGGEKQRVFLAQALA 154
Cdd:PRK15439 344 PEDRQSSGLYldaPLAWNVC-ALTHNRRGF---WIKParENAVLERYRRALNIKFNHaEQAARTLSGGNQQKVLIAKCLE 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730207193 155 QQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNDIYQLIRS-IAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-212 |
1.26e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.60 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 18 KGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQ---------------LA----RMMA 78
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwravrsdiqmifqdpLAslnpRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 --VLPQHGEQAFPYSVKETVslgryahqkgwfnswhdedEQIVQKVMEQTGI-TRLQDKSIVELSGGEKQRVFLAQALAQ 155
Cdd:PRK15079 118 geIIAEPLRTYHPKLSRQEV-------------------KDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 156 QPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLM 212
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-218 |
1.33e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.98 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMI-------SGALNFREGSIDVEGRPltqySPKQLA 74
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFDFSKTP----SDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 75 RM-----MaVLPQHgeQAFPY-SVKETVS------LGRyahqkgwfnswhdEDEQIVQKVMEQTGITRLQDKS---IVEL 139
Cdd:PRK11124 79 ELrrnvgM-VFQQY--NLWPHlTVQQNLIeapcrvLGL-------------SKDQALARAEKLLERLRLKPYAdrfPLHL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 140 SGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVL 218
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-169 |
1.39e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM-MAV 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHgEQAFP-YSVKETVSLGRYAHQkgwfnswhdEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPR 158
Cdd:PRK15439 91 VPQE-PLLFPnLSVKENILFGLPKRQ---------ASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170
....*....|.
gi 730207193 159 ILLLDEPTNHL 169
Cdd:PRK15439 161 ILILDEPTASL 171
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-217 |
2.15e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG----EVLKGISFEVCEGELFGILGPNGSGKT-TLLKMI----SGALNFREGSIDVEGRPLTQYSPK 71
Cdd:PRK15134 5 LLAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpSPPVVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 72 QLAR-------------MMAVLPQHGEQAFPYsvkETVSLGRYAHQKGwfnswhdEDEQIVQkVMEQTGI----TRLQDK 134
Cdd:PRK15134 85 TLRGvrgnkiamifqepMVSLNPLHTLEKQLY---EVLSLHRGMRREA-------ARGEILN-CLDRVGIrqaaKRLTDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 135 SiVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMEN 214
Cdd:PRK15134 154 P-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQN 232
|
...
gi 730207193 215 GEV 217
Cdd:PRK15134 233 GRC 235
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-219 |
2.27e-17 |
|
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: 81.54 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFR--EGSIDVEGRPLTQYSPKQLARM-MA 78
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEvtSGTILFKGQDLLELEPDERARAgLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 VLPQHGEQAFPYSVKETVSLGRYAHQKGWFNSWHDEDE--QIVQKVMEQTGITR-LQDKSIVE-LSGGEKQRVFLAQALA 154
Cdd:TIGR01978 81 LAFQYPEEIPGVSNLEFLRSALNARRSARGEEPLDLLDfeKLLKEKLALLDMDEeFLNRSVNEgFSGGEKKRNEILQMAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 155 QQPRILLLDEPTNHLDLSFQKELLDLLKKWaAEEELTVVSIFHDLN-LASLYCDRLLLMENGEVLI 219
Cdd:TIGR01978 161 LEPKLAILDEIDSGLDIDALKIVAEGINRL-REPDRSFLIITHYQRlLNYIKPDYVHVLLDGRIVK 225
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
10-218 |
2.46e-17 |
|
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: 84.79 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 10 GYaGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQHgeqafP 89
Cdd:TIGR01193 484 GY-GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQE-----P 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 90 Y----SVKETVSLGRYAhqkgwfNSWHDEDEQIVQKVMEQTGITRLQ---DKSIVE----LSGGEKQRVFLAQALAQQPR 158
Cdd:TIGR01193 558 YifsgSILENLLLGAKE------NVSQDEIWAACEIAEIKDDIENMPlgyQTELSEegssISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 159 ILLLDEPTNHLDLSFQKELLDLLKKWaaeEELTVVSIFHDLNLASLyCDRLLLMENGEVL 218
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNL---QDKTIIFVAHRLSVAKQ-SDKIIVLDHGKII 687
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-231 |
2.89e-17 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 81.83 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 13 GGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRplTQYSPkQLARMMavlpqhgeqafPYSV 92
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSS-QFSWIM-----------PGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 93 KETVSLG------RYahqkgwfnswhdedEQIVQKVMEQTGITRL--QDKSI-----VELSGGEKQRVFLAQALAQQPRI 159
Cdd:cd03291 115 KENIIFGvsydeyRY--------------KSVVKACQLEEDITKFpeKDNTVlgeggITLSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730207193 160 LLLDEPTNHLDLSFQKELLD--LLKKWAAEEELTVVSIFHDLNLAslycDRLLLMENGEVLIVDTPAEvLKEER 231
Cdd:cd03291 181 YLLDSPFGYLDVFTEKEIFEscVCKLMANKTRILVTSKMEHLKKA----DKILILHEGSSYFYGTFSE-LQSLR 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-223 |
3.61e-17 |
|
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: 85.07 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGY--AGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLtQYSPKQLARMMAV 79
Cdd:TIGR01257 929 VCVKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHGEQAFPYSVKETVSLgrYAHQKGwfNSWhDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:TIGR01257 1008 CPQHNILFHHLTVAEHILF--YAQLKG--RSW-EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730207193 160 LLLDEPTNHLDLSFQKELLDLLKKWAAEEelTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTP 223
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-198 |
3.63e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 84.22 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIdvegrpltqyspkqlarmmavlp 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI----------------------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 82 qhgeqafpySVKETVSLGrYAHQkgwFNSWHDEDEQIVQKVMEQTGITRL--------------------QDKSIVELSG 141
Cdd:TIGR03719 380 ---------EIGETVKLA-YVDQ---SRDALDPNKTVWEEISGGLDIIKLgkreipsrayvgrfnfkgsdQQKKVGQLSG 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 142 GEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAeeelTVVSIFHD 198
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAG----CAVVISHD 499
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-198 |
4.49e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 83.63 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 15 EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGAlnfrEGSIDVEGRPLTQYSpkqlarmMAVLPQHgeqafPY---- 90
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV----DKEFEGEARPAPGIK-------VGYLPQE-----PQldpe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 91 -SVKETVSLGrYAHQKGWFNSWHD------EDEQIVQKVMEQTGitRLQDK----------SIVE--------------- 138
Cdd:PRK11819 85 kTVRENVEEG-VAEVKAALDRFNEiyaayaEPDADFDALAAEQG--ELQEIidaadawdldSQLEiamdalrcppwdakv 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 730207193 139 --LSGGEKQRVFLAQALAQQPRILLLDEPTNHLDlsfqKELLDLLKKWAAEEELTVVSIFHD 198
Cdd:PRK11819 162 tkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-227 |
4.68e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 82.16 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGY--AGGEV--LKGISFEVCEGELFGILGPNGSGKTTLLKMISG---------ALNFREGSIDvegrpLTQ 67
Cdd:PRK15093 3 LLDIRNLTIEFktSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwrvtADRMRFDDID-----LLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 68 YSPKQLARM----MAVLPQHgeqafPYS-VKETVSLGRYAHQ-------KG-WFNSWHDEDEQIVQkVMEQTGITRLQD- 133
Cdd:PRK15093 78 LSPRERRKLvghnVSMIFQE-----PQScLDPSERVGRQLMQnipgwtyKGrWWQRFGWRKRRAIE-LLHRVGIKDHKDa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 134 -KSI-VELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLL 211
Cdd:PRK15093 152 mRSFpYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINV 231
|
250
....*....|....*.
gi 730207193 212 MENGEVLIVDTPAEVL 227
Cdd:PRK15093 232 LYCGQTVETAPSKELV 247
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-215 |
1.10e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.76 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGG-EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQ---LARM 76
Cdd:PRK10908 1 MIRFEHVSKAYLGGrQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MAVLPQHGEQAFPYSVKETVSLGRY-AHQKGwfnswhDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQ 155
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIiAGASG------DDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 156 QPRILLLDEPTNHLDLSFQKELLDLLKKWaAEEELTVVSIFHDLNLASLYCDRLLLMENG 215
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-227 |
1.15e-16 |
|
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: 82.46 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGY--AGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHgEQAFPYSVKETVSLGRYAhqkgwfnswhDEDEQIVQKVMEQTGITRLQDKSI-----------VELSGGEKQRVF 148
Cdd:TIGR02203 411 VSQD-VVLFNDTIANNIAYGRTE----------QADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 149 LAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKkwAAEEELTVVSIFHDLNLASlYCDRLLLMENGEVLIVDTPAEVL 227
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALE--RLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRIVERGTHNELL 555
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-199 |
1.30e-16 |
|
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: 79.33 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 26 EGELFGILGPNGSGKTTLLKMISGALNFREGSIDVE-----------GRPLTQYSPKQLARMM--AVLPQHGEQaFPYSV 92
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPpdwdeildefrGSELQNYFTKLLEGDVkvIVKPQYVDL-IPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 93 KETVS-LGRYAHQKGWFNswhdedeqivqKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDL 171
Cdd:cd03236 104 KGKVGeLLKKKDERGKLD-----------ELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*...
gi 730207193 172 SfQKELLDLLKKWAAEEELTVVSIFHDL 199
Cdd:cd03236 173 K-QRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-215 |
1.78e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.15 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNL--TGGYAGGEV--LKGISFEVCEGELFGILGPNGSGKTTLLKMISGAL--NFR-EGSIDVEGRPLTQYSPKQL 73
Cdd:PRK09473 12 LLDVKDLrvTFSTPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLaaNGRiGGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 74 ARM--------------------------MAVLPQH----GEQAFPYSVK--ETVSL-------GRYAHqkgwfnswhde 114
Cdd:PRK09473 92 NKLraeqismifqdpmtslnpymrvgeqlMEVLMLHkgmsKAEAFEESVRmlDAVKMpearkrmKMYPH----------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 115 deqivqkvmeqtgitrlqdksivELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVS 194
Cdd:PRK09473 161 -----------------------EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIM 217
|
250 260
....*....|....*....|.
gi 730207193 195 IFHDLNLASLYCDRLLLMENG 215
Cdd:PRK09473 218 ITHDLGVVAGICDKVLVMYAG 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-230 |
2.08e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 20 ISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARM-MAVLPQ--HGEQAFP-YSVKET 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgIMLCPEdrKAEGIIPvHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 96 VSLG-RYAHQK-GWF--NSWHDE--DEQIvqkvmEQTGI-TRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNH 168
Cdd:PRK11288 352 INISaRRHHLRaGCLinNRWEAEnaDRFI-----RSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 730207193 169 LDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVlivdtPAEVLKEE 230
Cdd:PRK11288 427 IDVGAKHEIYNVIYE-LAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI-----AGELAREQ 482
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-215 |
2.17e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 82.27 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRplTQYSPkQLARMMavlpqhgeqafPYSVKET 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSP-QTSWIM-----------PGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 96 VSLG------RYAhqkgwfnswhdedeQIVQKVMEQTGITRL--QDKSI-----VELSGGEKQRVFLAQALAQQPRILLL 162
Cdd:TIGR01271 507 IIFGlsydeyRYT--------------SVIKACQLEEDIALFpeKDKTVlgeggITLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 163 DEPTNHLDLSFQKELLD--LLKKWAAEEELTVVSIFHDLNLAslycDRLLLMENG 215
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFEscLCKLMSNKTRILVTSKLEHLKKA----DKILLLHEG 623
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-199 |
2.43e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.39 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 26 EGELFGILGPNGSGKTTLLKMISGAL--NF----REGSID--VE---GRPLTQYSpKQLA--RMMAVL-PQHGEQAfPYS 91
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELipNLgdyeEEPSWDevLKrfrGTELQNYF-KKLYngEIKVVHkPQYVDLI-PKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 92 VKETVS-LGRYAHQKGWFnswhdeDEqivqkVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLD 170
Cdd:PRK13409 176 FKGKVReLLKKVDERGKL------DE-----VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*....
gi 730207193 171 LSFQKELLDLLKKWAaeEELTVVSIFHDL 199
Cdd:PRK13409 245 IRQRLNVARLIRELA--EGKYVLVVEHDL 271
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-230 |
2.94e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 81.95 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQHgeqafPYSVKET 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQS-----PVLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 96 VSLGryahqkgwFNSWHDEDEQIVQKVMEQTGITRLQDKSIVEL-----------SGGEKQRVFLAQALAQQPRILLLDE 164
Cdd:PLN03232 1326 VRFN--------IDPFSEHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 165 PTNHLDLSFQKelldLLKKWAAEE--ELTVVSIFHDLNlASLYCDRLLLMENGEVLIVDTPAEVLKEE 230
Cdd:PLN03232 1398 ATASVDVRTDS----LIQRTIREEfkSCTMLVIAHRLN-TIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-199 |
4.66e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 80.60 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 26 EGELFGILGPNGSGKTTLLKMISGAL--NF----REGSIDvegRPLTQYSPKQLA---------RMMAVL-PQHGEQAfP 89
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkpNLgdydEEPSWD---EVLKRFRGTELQdyfkklangEIKVAHkPQYVDLI-P 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 90 YSVKETVS--LGRYahqkgwfnswhdeDEQ-IVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPT 166
Cdd:COG1245 174 KVFKGTVRelLEKV-------------DERgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|...
gi 730207193 167 NHLDLSFQKELLDLLKKwAAEEELTVVSIFHDL 199
Cdd:COG1245 241 SYLDIYQRLNVARLIRE-LAEEGKYVLVVEHDL 272
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-199 |
1.23e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 78.90 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 21 SFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQH--------GEQAFPYSV 92
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRnntdmlspGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 93 KETVSLgryahqkgwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLS 172
Cdd:PRK10938 103 AEIIQD-------------EVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190
....*....|....*....|....*....|
gi 730207193 173 FQKELLDLLKKWAAeEELTVVSI---FHDL 199
Cdd:PRK10938 170 SRQQLAELLASLHQ-SGITLVLVlnrFDEI 198
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-217 |
1.23e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 79.37 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQhGEQAFPYSVKET 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ-TPFLFSDTVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 96 VSLGRYahqkgwfNSWHDEDEQIVQKVMEQTGITRLQDKSIVE-------LSGGEKQRVFLAQALAQQPRILLLDEPTNH 168
Cdd:PRK10789 409 IALGRP-------DATQQEIEHVARLASVHDDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 730207193 169 LDLSFQKELLDLLKKWAaeEELTVVSIFHDLNlASLYCDRLLLMENGEV 217
Cdd:PRK10789 482 VDGRTEHQILHNLRQWG--EGRTVIISAHRLS-ALTEASEILVMQHGHI 527
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-216 |
1.31e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.51 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYA--GGEV--LKGISFEVCEGELFGILGPNGSGKT----TLLKMI--------SGALNFREGSIDVegRP 64
Cdd:PRK10261 12 VLAVENLNIAFMqeQQKIaaVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqagglvqCDKMLLRRRSRQV--IE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 65 LTQYSPKQLARM----MAVLPQHGEQAFP--YSVKETVSLGRYAHQkgwfNSWHDEDEQIVQKVMEQTGITrlQDKSIV- 137
Cdd:PRK10261 90 LSEQSAAQMRHVrgadMAMIFQEPMTSLNpvFTVGEQIAESIRLHQ----GASREEAMVEAKRMLDQVRIP--EAQTILs 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 138 ----ELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLME 213
Cdd:PRK10261 164 ryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMY 243
|
...
gi 730207193 214 NGE 216
Cdd:PRK10261 244 QGE 246
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
11-222 |
1.33e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.28 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 11 YAGGEVLKGISFEVCEGELFGILGPNGSGKT----TLLKMISGALNFREGSIDVEGRPltqYSPKQL-ARMMAVLPQHGE 85
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKP---VAPCALrGRKIATIMQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 86 QAF-PYS-----VKETV-SLGRYAhqkgwfnswhdeDEQIVQKVMEQTGIT---RLQDKSIVELSGGEKQRVFLAQALAQ 155
Cdd:PRK10418 90 SAFnPLHtmhthARETClALGKPA------------DDATLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 156 QPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEvlIVDT 222
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGR--IVEQ 222
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-217 |
1.50e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 79.52 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVL-KGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIdvegrpltQYSPKQlarMMAV 79
Cdd:PLN03073 508 IISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------FRSAKV---RMAV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQHGEQAFPYSVKETVSLGRyahqkgwfnSWHDEDEQIVQKVMEQTGIT-RLQDKSIVELSGGEKQRVFLAQALAQQPR 158
Cdd:PLN03073 577 FSQHHVDGLDLSSNPLLYMMR---------CFPGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPH 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 159 ILLLDEPTNHLDLSFQKELLDLLKKWAAeeelTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:PLN03073 648 ILLLDEPSNHLDLDAVEALIQGLVLFQG----GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-225 |
1.66e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.76 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMM---- 77
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMvfqs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 -AVLPQhgeqafpYSVKETVSLG-RYAHQKgwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQ 155
Cdd:PRK11000 84 yALYPH-------LSVAENMSFGlKLAGAK------KEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730207193 156 QPRILLLDEPTNHLD--LSFQK--ELLDLLKKWAAeeelTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAE 225
Cdd:PRK11000 151 EPSVFLLDEPLSNLDaaLRVQMriEISRLHKRLGR----TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-239 |
2.51e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.61 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE-VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHgeqafPYSVKET----VSLGRyahqkgwfnswhDEDEQIVQKVMEQT-----------GI-TRLQDKSiVELSGGEK 144
Cdd:PRK10790 421 QQD-----PVVLADTflanVTLGR------------DISEEQVWQALETVqlaelarslpdGLyTPLGEQG-NNLSVGQK 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 145 QRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKkwAAEEELTVVSIFHDLNlASLYCDRLLLMENGEVLIVDTPA 224
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALA--AVREHTTLVVIAHRLS-TIVEADTILVLHRGQAVEQGTHQ 559
|
250
....*....|....*.
gi 730207193 225 EVLKEE-RIKKVYKTQ 239
Cdd:PRK10790 560 QLLAAQgRYWQMYQLQ 575
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-169 |
2.82e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 6 NLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQ-LARMMAVLpqHG 84
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAII--YQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 85 E-QAFP-YSVKETVSLGRYAHQKGWFNSwhdedEQIVQKVMEQ---TGITRLQDKSIVELSGGEKQRVFLAQALAQQPRI 159
Cdd:PRK11288 87 ElHLVPeMTVAENLYLGQLPHKGGIVNR-----RLLNYEAREQlehLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170
....*....|
gi 730207193 160 LLLDEPTNHL 169
Cdd:PRK11288 162 IAFDEPTSSL 171
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-232 |
2.95e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 20 ISFEVCEGELFGILGPNGSGKTTLLKMISGALNFR-EGSIDVEGRPLTQYSPKQ-LARMMAVLP----QHGeqAFP-YSV 92
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNPQQaIAQGIAMVPedrkRDG--IVPvMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 93 KETV---SLGRYAHqkgwFNSWHDEDEQivqKVMEQTgITRLQDK------SIVELSGGEKQRVFLAQALAQQPRILLLD 163
Cdd:PRK13549 359 GKNItlaALDRFTG----GSRIDDAAEL---KTILES-IQRLKVKtaspelAIARLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 164 EPTNHLDLSFQKELLDLLKKWaAEEELTVVSIFHDLNLASLYCDRLLLMENGEvLIVDTPAEVLKEERI 232
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGK-LKGDLINHNLTQEQV 497
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-171 |
3.62e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 75.06 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISG--ALNFREGSIDVEGRPLTQYSPKQLARMMA 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 VLpqhgeqAFPYSVKET-VS------LGRYAHQKgwFNSWHDED-----EQIVQKV----MEQTGITRLQDKSiveLSGG 142
Cdd:CHL00131 87 FL------AFQYPIEIPgVSnadflrLAYNSKRK--FQGLPELDpleflEIINEKLklvgMDPSFLSRNVNEG---FSGG 155
|
170 180
....*....|....*....|....*....
gi 730207193 143 EKQRVFLAQALAQQPRILLLDEPTNHLDL 171
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDI 184
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-207 |
3.64e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.20 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 5 KNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLK-------MISGalnFR-EGSIDVEGRPL--TQYSPKQLA 74
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPG---FRvEGKVTFHGKNLyaPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 75 RMMAVLPQHgEQAFPYSVKETVSLG-RYAHQKGwfnswhDEDEqIVQKVMEQTGI-TRLQDK---SIVELSGGEKQRVFL 149
Cdd:PRK14243 91 RRIGMVFQK-PNPFPKSIYDNIAYGaRINGYKG------DMDE-LVERSLRQAALwDEVKDKlkqSGLSLSGGQQQRLCI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 150 AQALAQQPRILLLDEPTNHLD-LSFQK--ELLDLLKkwaaeEELTVVSIFHDLNLASLYCD 207
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDpISTLRieELMHELK-----EQYTIIIVTHNMQQAARVSD 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-220 |
9.52e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.84 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGAL--NFREGSIDVEGRPLTqyspKQLARMMAVLPQHgEQAFPY-SV 92
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgNNFTGTILANNRKPT----KQILKRTGFVTQD-DILYPHlTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 93 KET---VSLGRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVE-----LSGGEKQRVFLAQALAQQPRILLLDE 164
Cdd:PLN03211 158 RETlvfCSLLRLPKSLT-----KQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 165 PTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIV 220
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFF 288
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-217 |
1.16e-14 |
|
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: 76.02 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 20 ISFEVCEGELFGILGPNGSGKTTLLKMISGALNFR-EGSIDVEGRPLTQYSPKQLARM-MAVLPQ----HGeqAFP-YSV 92
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAgIAMVPEdrkrHG--IVPiLGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 93 KETVSLGryAHQKGWFNSWHDE--DEQIVQKVMEQTGI-TRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHL 169
Cdd:TIGR02633 357 GKNITLS--VLKSFCFKMRIDAaaELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 730207193 170 DLSFQKELLDLLKKWAAeEELTVVSIFHDLNLASLYCDRLLLMENGEV 217
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-170 |
1.35e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.93 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYaGGEVL-KGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVeGrpltqyspkqlarmmavl 80
Cdd:PRK11819 325 IEAENLSKSF-GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G------------------ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 pqhgeqafpysvkETVSLGrYAHQKgwfnswHD--EDEQIV-QKVMEQTGITRL--------------------QDKSIV 137
Cdd:PRK11819 385 -------------ETVKLA-YVDQS------RDalDPNKTVwEEISGGLDIIKVgnreipsrayvgrfnfkggdQQKKVG 444
|
170 180 190
....*....|....*....|....*....|...
gi 730207193 138 ELSGGEKQRVFLAQALAQQPRILLLDEPTNHLD 170
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-198 |
2.75e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 75.37 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 6 NLTGGY-AGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEG-----RpLTQYSPKQ----- 72
Cdd:PRK11147 5 SIHGAWlSFSDapLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivaR-LQQDPPRNvegtv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 73 ---LARMMAVLPQHGEQ--------AFPYSVKETVSLGRYAHQKGWFNSWHDEDEqiVQKVMEQTGITrlQDKSIVELSG 141
Cdd:PRK11147 84 ydfVAEGIEEQAEYLKRyhdishlvETDPSEKNLNELAKLQEQLDHHNLWQLENR--INEVLAQLGLD--PDAALSSLSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 142 GEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAeeelTVVSIFHD 198
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHD 212
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-203 |
5.67e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.60 E-value: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 19 GISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPkQLARMMAVLpqhGEQAfpySVKETVS- 97
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYL---GHQP---GIKTELTa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 98 ---LgRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQ 174
Cdd:PRK13538 92 lenL-RFYQRLH-----GPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180
....*....|....*....|....*....
gi 730207193 175 KELLDLLKKWAAEEELTVVSIFHDLNLAS 203
Cdd:PRK13538 166 ARLEALLAQHAEQGGMVILTTHQDLPVAS 194
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-171 |
9.56e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 70.98 E-value: 9.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFR--EGSIDVEGRPLTQYSPKQLArmma 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLELSPEDRA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 vlpqhGE---QAFPYSV-----------KETVSLGRYAHQKGWFNSWHDED---EQIVQKVMEQTGITRLQDksiVELSG 141
Cdd:PRK09580 77 -----GEgifMAFQYPVeipgvsnqfflQTALNAVRSYRGQEPLDRFDFQDlmeEKIALLKMPEDLLTRSVN---VGFSG 148
|
170 180 190
....*....|....*....|....*....|
gi 730207193 142 GEKQRVFLAQALAQQPRILLLDEPTNHLDL 171
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLDI 178
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-215 |
9.86e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 74.28 E-value: 9.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 27 GELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRP-LTQYSpkQLARMMAVLPQHGEQAFPYSVKETVSLgrYAHQK 105
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNIS--DVHQNMGYCPQFDAIDDLLTGREHLYL--YARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 106 GwfnSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKwA 185
Cdd:TIGR01257 2041 G---VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS-I 2116
|
170 180 190
....*....|....*....|....*....|
gi 730207193 186 AEEELTVVSIFHDLNLASLYCDRLLLMENG 215
Cdd:TIGR01257 2117 IREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-240 |
1.02e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.58 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQ-----YSPKQLARMMAVLPQHGE-QAFPY 90
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRKEIGLVFQFPEyQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 91 SVKETVSLGRYahqkgwfnSWHDEDEQIVQKVMEQTGITRLQD----KSIVELSGGEKQRVFLAQALAQQPRILLLDEPT 166
Cdd:PRK13645 107 TIEKDIAFGPV--------NLGENKQEAYKKVPELLKLVQLPEdyvkRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730207193 167 NHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKEERIkkVYKTQI 240
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL--LTKIEI 250
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-239 |
1.87e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 72.36 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEV--LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAV 79
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQH----------------GEQafpYSVKETVSLGRYAHQKGWFNSwhdedeqivqkvMEQtGITRLQDKSIVELSGGE 143
Cdd:PRK11176 422 VSQNvhlfndtianniayarTEQ---YSREQIEEAARMAYAMDFINK------------MDN-GLDTVIGENGVLLSGGQ 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 144 KQRVFLAQALAQQPRILLLDEPTNHLDLSFQKEL---LDLLKKwaaeeELTVVSIFHDLNLASlYCDRLLLMENGEVLIV 220
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIqaaLDELQK-----NRTSLVIAHRLSTIE-KADEILVVEDGEIVER 559
|
250 260
....*....|....*....|
gi 730207193 221 DTPAEVLKEERI-KKVYKTQ 239
Cdd:PRK11176 560 GTHAELLAQNGVyAQLHKMQ 579
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-221 |
3.42e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFR--EGSIDVEGRPLTQYSPkqlarmmaVLPQHGEQAFPYSVK 93
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTpvAGCVDVPDNQFGREAS--------LIDAIGRKGDFKDAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 94 ETVSLGRYAHQKGWFNSWHdedeqivqkvmeqtgitrlqdksivELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSF 173
Cdd:COG2401 117 ELLNAVGLSDAVLWLRRFK-------------------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 730207193 174 QKELLDLLKKWAAEEELTVVSIFHDLNLAS-LYCDRLLLMENGEVLIVD 221
Cdd:COG2401 172 AKRVARNLQKLARRAGITLVVATHHYDVIDdLQPDLLIFVGYGGVPEEK 220
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-198 |
3.86e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.52 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 4 VKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVeGRPLTqyspkqlarmMAVLPQH 83
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE----------VAYFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 84 GEQAFP-YSVKETVSLGRyahqkgwfnswhdedeqivQKVMeQTGITR-----LQD---------KSIVELSGGEKQRVF 148
Cdd:PRK11147 391 RAELDPeKTVMDNLAEGK-------------------QEVM-VNGRPRhvlgyLQDflfhpkramTPVKALSGGERNRLL 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 730207193 149 LAQALAQQPRILLLDEPTNHLDLsfqkELLDLLKKWAAEEELTVVSIFHD 198
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-216 |
3.96e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.54 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGY-AGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMA-- 78
Cdd:PRK10522 323 LELRNVTFAYqDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSav 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 ---------VLPQHGEQAfpysvketvslgryahqkgwfnswhdeDEQIVQKVMEQTGI---TRLQDKSI--VELSGGEK 144
Cdd:PRK10522 403 ftdfhlfdqLLGPEGKPA---------------------------NPALVEKWLERLKMahkLELEDGRIsnLKLSKGQK 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 145 QRVFLAQALAQQPRILLLDE------PtnHLDLSFQKELLDLLKkwaaEEELTVVSIFHDlNLASLYCDRLLLMENGE 216
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEwaadqdP--HFRREFYQVLLPLLQ----EMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-217 |
5.41e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.15 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAG-GEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVL 80
Cdd:PRK13657 335 VEFDDVSFSYDNsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQhgeQA--FPYSVKETVSLGRYahqkgwfNSWHDEDEQIVQKVMEQTGITRLQDK--SIV-----ELSGGEKQRVFLAQ 151
Cdd:PRK13657 415 FQ---DAglFNRSIEDNIRVGRP-------DATDEEMRAAAERAQAHDFIERKPDGydTVVgergrQLSGGERQRLAIAR 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 730207193 152 ALAQQPRILLLDEPTNHLDLSFQ---KELLDLLKKwaaeeELTVVSIFHDLNLASlYCDRLLLMENGEV 217
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEakvKAALDELMK-----GRTTFIIAHRLSTVR-NADRILVFDNGRV 547
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-230 |
6.26e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.53 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGgyAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQlarmmAVl 80
Cdd:PRK10982 250 ILEVRNLTS--LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE-----AI- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 pQHGeqaFPYSVKETVSLGRYAHQKGWFNSW------------------HDEDEQIVQKVMEQTgiTRLQDKSIVELSGG 142
Cdd:PRK10982 322 -NHG---FALVTEERRSTGIYAYLDIGFNSLisnirnyknkvglldnsrMKSDTQWVIDSMRVK--TPGHRTQIGSLSGG 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 143 EKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEElTVVSIFHDLNLASLYCDRLLLMENGEVL-IVD 221
Cdd:PRK10982 396 NQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLVAgIVD 474
|
....*....
gi 730207193 222 TpAEVLKEE 230
Cdd:PRK10982 475 T-KTTTQNE 482
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-245 |
6.64e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 70.69 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRpltqyspkqlARMMAVLPQHGEQafpYSVKETV 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----------AALIAISSGLNGQ---LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 97 SLgryahqKGWFNSWHDED-EQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQK 175
Cdd:PRK13545 107 EL------KGLMMGLTKEKiKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 176 ELLDLLKKWaAEEELTVVSIFHDLNLASLYCDRLLLMENGEVL-------IVDTPAEVLKE------ERIKKVYKTQIKN 242
Cdd:PRK13545 181 KCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKeygdikeVVDHYDEFLKKynqmsvEERKDFREEQISQ 259
|
...
gi 730207193 243 HPH 245
Cdd:PRK13545 260 FQH 262
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-227 |
1.11e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.54 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSP-KQLARMMAVL 80
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHrRAVCPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQH-GEQAFP-YSVKETVSL-GR-YAHQKGwfnswhdEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQ 156
Cdd:NF033858 82 PQGlGKNLYPtLSVFENLDFfGRlFGQDAA-------ERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 157 PRILLLDEPTNHLD-LSFQK--ELLDLLKkwAAEEELTVVsifhdlnLASLY------CDRLLLMENGEVLIVDTPAEVL 227
Cdd:NF033858 155 PDLLILDEPTTGVDpLSRRQfwELIDRIR--AERPGMSVL-------VATAYmeeaerFDWLVAMDAGRVLATGTPAELL 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-232 |
1.98e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.97 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQHgEQAFPYSVKET 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQD-PVLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 96 VS-LGRYAHQKGWfnsWHDEDEQIvqkvmeQTGITRLQDKSIVE-------LSGGEKQRVFLAQALAQQPRILLLDEPTN 167
Cdd:TIGR00957 1380 LDpFSQYSDEEVW---WALELAHL------KTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 168 HLDLsfqkELLDLLKKWAAE--EELTVVSIFHDLNLASLYCdRLLLMENGEVLIVDTPAEVLKEERI 232
Cdd:TIGR00957 1451 AVDL----ETDNLIQSTIRTqfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQRGI 1512
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-212 |
2.03e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.07 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSP---KQLARMMAVLPQHgeqafPYSV- 92
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQN-----PYGSl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 93 --KETV------------SLGRyahqkgwfnswhDEDEQIVQKVMEQTGI-TRLQDKSIVELSGGEKQRVFLAQALAQQP 157
Cdd:PRK11308 106 npRKKVgqileepllintSLSA------------AERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 730207193 158 RILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLM 212
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-179 |
3.39e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.20 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE--VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRpltqyspkqlarmMAV 79
Cdd:TIGR00957 637 ITVHNATFTWARDLppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAY 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 LPQhgeQAFPY--SVKETVSLGryahqkgwfnswHDEDEQIVQKVMEQTGI------------TRLQDKSiVELSGGEKQ 145
Cdd:TIGR00957 704 VPQ---QAWIQndSLRENILFG------------KALNEKYYQQVLEACALlpdleilpsgdrTEIGEKG-VNLSGGQKQ 767
|
170 180 190
....*....|....*....|....*....|....
gi 730207193 146 RVFLAQALAQQPRILLLDEPTNHLDLSFQKELLD 179
Cdd:TIGR00957 768 RVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-215 |
8.37e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 64.19 E-value: 8.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 15 EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALN--FREGSIDVEGRPLtqysPKQLARMMAVLPQHgeqafpysv 92
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPL----DKNFQRSTGYVEQQ--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 93 ketvslgrYAHqkgwfnswhdEDEQIVQKVMEQTGITRlqdksivELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLS 172
Cdd:cd03232 88 --------DVH----------SPNLTVREALRFSALLR-------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 730207193 173 FQKELLDLLKKwAAEEELTVV--------SIFHdlnlaslYCDRLLLMENG 215
Cdd:cd03232 143 AAYNIVRFLKK-LADSGQAILctihqpsaSIFE-------KFDRLLLLKRG 185
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
23-213 |
1.32e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 62.97 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 23 EVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRpltqyspkqlarMMAVLPQHgeqafpysvketvslgrya 102
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------TPVYKPQY------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 103 hqkgwfnswhdedeqivqkvmeqtgitrlqdksiVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLK 182
Cdd:cd03222 70 ----------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170 180 190
....*....|....*....|....*....|.
gi 730207193 183 KWAAEEELTVVSIFHDLNLASLYCDRLLLME 213
Cdd:cd03222 116 RLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-231 |
1.36e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.07 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQHgeqafPYSVKET 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQA-----PVLFSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 96 VslgRYAHQKgwFNSWHDED--EQIVQKVMEQTgITRLQ---DKSIVE----LSGGEKQRVFLAQALAQQPRILLLDEPT 166
Cdd:PLN03130 1329 V---RFNLDP--FNEHNDADlwESLERAHLKDV-IRRNSlglDAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 167 NHLDLSFQKelldLLKKWAAEE--ELTVVSIFHDLNlASLYCDRLLLMENGEVLIVDTPAEVLKEER 231
Cdd:PLN03130 1403 AAVDVRTDA----LIQKTIREEfkSCTMLIIAHRLN-TIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-171 |
1.56e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQyspKQLARMMAVLPQHGeqafpySVKET 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHLP------GLKAD 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 96 VSLGRYAHqkgWFNSWHD-EDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDL 171
Cdd:PRK13543 97 LSTLENLH---FLCGLHGrRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-217 |
1.90e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 63.05 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 15 EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGAlnfREGSIDVEGrpltqyspkqlarmmavlpqhgEQAFP-YSVK 93
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEG----------------------DIHYNgIPYK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 94 ETVSlgrYAHQKGWFNSwhDEDEQIVQKVMEQTGITRLQ---DKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLD 170
Cdd:cd03233 76 EFAE---KYPGEIIYVS--EEDVHFPTLTVRETLDFALRckgNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 171 LSFQKELLDLLKKWAAEEELTvvsifhdlNLASLY---------CDRLLLMENGEV 217
Cdd:cd03233 151 SSTALEILKCIRTMADVLKTT--------TFVSLYqasdeiydlFDKVLVLYEGRQ 198
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-232 |
2.30e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.58 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNF--REGSIDVEGRPLTQYSPKQLARMMAVLPqHGEQAF-PY-SV 92
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEVCRFKDIRDSEALGIVII-HQELALiPYlSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 93 KETVSLGRYAHQKGWFNsWHdEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLS 172
Cdd:NF040905 96 AENIFLGNERAKRGVID-WN-ETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 173 FQKELLDLLKKWAAeEELTVVSIFHDLNLASLYCDRLLLMENGE-VLIVDTPAEVLKEERI 232
Cdd:NF040905 174 DSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRtIETLDCRADEVTEDRI 233
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-229 |
2.53e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.90 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 5 KNLTGGYAGGE----VLKGISFEVCEGELFGILGPNGSGKTTLLKmISGALNF-REGSIDVEGRPLTQYSPKQLARMmav 79
Cdd:PRK10535 8 KDIRRSYPSGEeqveVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAGQDVATLDADALAQL--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 80 lpqhgeqafpysvketvslgRYAHQKGWFNSWH----------------------DEDEQIVQKVMEQTGITRLQDKSIV 137
Cdd:PRK10535 84 --------------------RREHFGFIFQRYHllshltaaqnvevpavyaglerKQRLLRAQELLQRLGLEDRVEYQPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 138 ELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASlYCDRLLLMENGEV 217
Cdd:PRK10535 144 QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQ-LRDRGHTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
250
....*....|..
gi 730207193 218 lIVDTPAEVLKE 229
Cdd:PRK10535 222 -VRNPPAQEKVN 232
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-200 |
4.94e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREG--SIDVEGRpltqyspkqlarmMA 78
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGnvSLDPNER-------------LG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 79 VLPQhgEQ-AFP-YSVKETVSLGryaHQKGW----------FNSWHDEDEQIvqKVME---------------------- 124
Cdd:PRK15064 68 KLRQ--DQfAFEeFTVLDTVIMG---HTELWevkqerdriyALPEMSEEDGM--KVADlevkfaemdgytaearagelll 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 125 QTGI-TRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKkwaaEEELTVVSIFHD---LN 200
Cdd:PRK15064 141 GVGIpEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLN----ERNSTMIIISHDrhfLN 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-165 |
1.18e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.09 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 20 ISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQL--AR-MMAVLPQHGEQAFPYSVKETV 96
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytVRkRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 730207193 97 SLGRYAHQkgwfnswHDEDEQIVQKVM---EQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLDEP 165
Cdd:PRK11831 106 AYPLREHT-------QLPAPLLHSTVMmklEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-232 |
1.86e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.82 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 5 KNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQ-LARMMAVLPQH 83
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 84 GEQAFPYSVKETVSLGRYAhQKGWFNSwHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRILLLD 163
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYP-TKGMFVD-QDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 164 EPTNHLDlsfQKELLDLLK--KWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEvLIVDTPAEVLKEERI 232
Cdd:PRK10982 160 EPTSSLT---EKEVNHLFTiiRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ-WIATQPLAGLTMDKI 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-232 |
2.33e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 4 VKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPK--QLA------R 75
Cdd:PRK10762 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssQEAgigiihQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 76 MMAVLPQhgeqafpYSVKETVSLGR-YAHQKGWFNsW---HDEDEQIVQKVmeqtGITRLQDKSIVELSGGEKQRVFLAQ 151
Cdd:PRK10762 87 ELNLIPQ-------LTIAENIFLGReFVNRFGRID-WkkmYAEADKLLARL----NLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 152 ALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAeEELTVVSIFHDLNLASLYCDRLLLMENGEvLIVDTPAEVLKEER 231
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALTDTETESLFRVIRELKS-QGRGIVYISHRLKEIFEICDDVTVFRDGQ-FIAEREVADLTEDS 232
|
.
gi 730207193 232 I 232
Cdd:PRK10762 233 L 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-226 |
2.71e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.87 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLARMMAVLPQ-----HGE----- 85
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQdpvlfDGTvrqnv 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 86 ----QAFPYSV---KETVSL-GRYAhqkgwfnswhDEDEQIVQKVMEQTGitrlqdksivELSGGEKQRVFLAQALAQQP 157
Cdd:PTZ00243 1405 dpflEASSAEVwaaLELVGLrERVA----------SESEGIDSRVLEGGS----------NYSVGQRQLMCMARALLKKG 1464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 158 R-ILLLDEPTNHLDLSFQKELLDLLKkwAAEEELTVVSIFHDLNLASLYcDRLLLMENGEVLIVDTPAEV 226
Cdd:PTZ00243 1465 SgFILMDEATANIDPALDRQIQATVM--SAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-225 |
1.04e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.20 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 15 EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGR---------------------PL-------- 65
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrskigvvsqdPLlfsnsikn 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 66 -TQYSPKQLARMMAVLPQHGEQAFPYSVKETVSLGRYAHQKGWFNSWHD-----------------EDEQIV---QKVME 124
Cdd:PTZ00265 479 nIKYSLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNttdsneliemrknyqtiKDSEVVdvsKKVLI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 125 QTGITRLQDK-------SIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFH 197
Cdd:PTZ00265 559 HDFVSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
250 260 270
....*....|....*....|....*....|.
gi 730207193 198 DLNLASlYCDRLLLM---ENGEVLIVDTPAE 225
Cdd:PTZ00265 639 RLSTIR-YANTIFVLsnrERGSTVDVDIIGE 668
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-263 |
2.14e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.87 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 20 ISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTQYSPKQLA---RMMAVLPQHG------EQAFPY 90
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalrRDIQFIFQDPyasldpRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 91 SVKETVSLGRYAHQkgwfnswhDEDEQIVQKVMEQTGITRLQD-KSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHL 169
Cdd:PRK10261 423 SIMEPLRVHGLLPG--------KAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 170 DLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLkeerikkvyktqiKNHPHPEIA 249
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF-------------ENPQHPYTR 561
|
250
....*....|....
gi 730207193 250 KpQLLLVPEADGGH 263
Cdd:PRK10261 562 K-LMAAVPVADPSR 574
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
5-215 |
2.23e-09 |
|
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: 57.34 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 5 KNLTGGY----AGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIdvegrpltQYSPKQLARMMAVL 80
Cdd:cd03290 1 VQVTNGYfswgSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV--------HWSNKNESEPSFEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQafpYSVKetvslgrYAHQKGWF-NSWHDED--------EQIVQKVMEQTGI------------TRLQDKSIvEL 139
Cdd:cd03290 73 TRSRNR---YSVA-------YAAQKPWLlNATVEENitfgspfnKQRYKAVTDACSLqpdidllpfgdqTEIGERGI-NL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 140 SGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDL-LKKWAAEEELTVVSIFHDLNLASlYCDRLLLMENG 215
Cdd:cd03290 142 SGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-170 |
1.48e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 1 MITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGrpltQYSPKQLARMMAVL 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER----QSIKKDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 PQHGEQAfpySVKETVSLGRYAHQKGWFNSWHDEDEQIVQKVmeqtGITRLQDKSIVELSGGEKQRVFLAQALAQQPRIL 160
Cdd:PRK13540 77 CFVGHRS---GINPYLTLRENCLYDIHFSPGAVGITELCRLF----SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLW 149
|
170
....*....|
gi 730207193 161 LLDEPTNHLD 170
Cdd:PRK13540 150 LLDEPLVALD 159
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-214 |
3.68e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 27 GELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRpltqyspKQLARMMAVLPQHGEQAFPYSV---KETVSLGRYAH 103
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN-------WQLAWVNQETPALPQPALEYVIdgdREYRQLEAQLH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 104 QKGWFN------SWHDEDEQI--------VQKVMEQTGITRLQ-DKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNH 168
Cdd:PRK10636 100 DANERNdghaiaTIHGKLDAIdawtirsrAASLLHGLGFSNEQlERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 730207193 169 LDLsfqkELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMEN 214
Cdd:PRK10636 180 LDL----DAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-194 |
6.89e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMIsgALNFREG------------------------- 56
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYM--AMHAIDGipkncqilhveqevvgddttalqcv 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 57 -SIDVEGRPLTQySPKQLARMMAVLPQHGEQAFPYSVKETVSLGRYAHQKgwFNSWHDEDEQIVQKVMEQTGITRL---- 131
Cdd:PLN03073 256 lNTDIERTQLLE-EEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQR--LEEIYKRLELIDAYTAEARAASILagls 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730207193 132 -----QDKSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAaeEELTVVS 194
Cdd:PLN03073 333 ftpemQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVS 398
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-217 |
7.59e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 54.80 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGE-----VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGRPLTqysPKQLARM 76
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 77 MavlpQHgeqafpYSVketVslgryahqkgwFNSWH----------DEDEQIVQKVMEQTGI---TRLQDK--SIVELSG 141
Cdd:COG4615 405 R----QL------FSA---V-----------FSDFHlfdrllgldgEADPARARELLERLELdhkVSVEDGrfSTTDLSQ 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 142 GEKQRVFLAQALAQQPRILLLDEptnhldlsfqkelldllkkWAAE----------EEL---------TVVSIFHD---L 199
Cdd:COG4615 461 GQRKRLALLVALLEDRPILVFDE-------------------WAADqdpefrrvfyTELlpelkargkTVIAISHDdryF 521
|
250
....*....|....*...
gi 730207193 200 NLAslycDRLLLMENGEV 217
Cdd:COG4615 522 DLA----DRVLKMDYGKL 535
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-211 |
8.22e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.61 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 27 GELFGILGPNGSGKTTLLKMISGALNFREGSIdvegrpltqyspkqlarmmavlpqhgeqafpysvkETVSLGRYAHQKG 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-----------------------------------IYIDGEDILEEVL 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 107 WFNSWHDEDEqivqkvmeqtgitrlqdkSIVELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDL-----L 181
Cdd:smart00382 47 DQLLLIIVGG------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180 190
....*....|....*....|....*....|....*.
gi 730207193 182 KKWAAEEELTVV------SIFHDLNLASLYCDRLLL 211
Cdd:smart00382 109 LLLKSEKNLTVIlttndeKDLGPALLRRRFDRRIVL 144
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-197 |
2.22e-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: 53.21 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 14 GEVL-KGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREG--SIDVEGRpltqyspkqlarmMAVLPQHgeqafPY 90
Cdd:TIGR00954 464 GDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGrlTKPAKGK-------------LFYVPQR-----PY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 91 svketVSLGRYAHQKGWFNS--------WHDED-EQIVQKVM------EQTGITRLQDKSIVeLSGGEKQRVFLAQALAQ 155
Cdd:TIGR00954 526 -----MTLGTLRDQIIYPDSsedmkrrgLSDKDlEQILDNVQlthileREGGWSAVQDWMDV-LSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 730207193 156 QPRILLLDEPTNHLDLSFQKELLDLLKKWAaeeeLTVVSIFH 197
Cdd:TIGR00954 600 KPQFAILDECTSAVSVDVEGYMYRLCREFG----ITLFSVSH 637
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-214 |
2.60e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 56 GSIDVEGRPLTQYSPKQLARMMAVLPQHgEQAFPYSVKETVSLGRyahqkgwfnswHDEDEQIVQKVMEQTGITRL---- 131
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQE-PMLFNMSIYENIKFGK-----------EDATREDVKRACKFAAIDEFiesl 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 132 ---QDKSI----VELSGGEKQRVFLAQALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHdlNLASL 204
Cdd:PTZ00265 1345 pnkYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH--RIASI 1422
|
170
....*....|.
gi 730207193 205 -YCDRLLLMEN 214
Cdd:PTZ00265 1423 kRSDKIVVFNN 1433
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-199 |
3.11e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 50.78 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLtGGYAGGEVlkgISFEvceGELFGILGPNGSGKTTLLKMISGALnfrEGSIDVEGRPLTQYSPKQLARMMAVL- 80
Cdd:COG0419 5 LRLENF-RSYRDTET---IDFD---DGLNLIVGPNGAGKSTILEAIRYAL---YGKARSRSKLRSDLINVGSEEASVELe 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 81 ------------PQhGEQAF-----PYSVKETVS----LGRYAHQKGWFNSWHDEDEQIVQKVMEQTGIT--RLQD---- 133
Cdd:COG0419 75 fehggkryrierRQ-GEFAEfleakPSERKEALKrllgLEIYEELKERLKELEEALESALEELAELQKLKqeILAQlsgl 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 730207193 134 KSIVELSGGEKQRVFLAQALAqqpriLLLDepTNHLDLSFQKELLDLLkkwaaeEELTVVSifHDL 199
Cdd:COG0419 154 DPIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDAL------EELAIIT--HVI 204
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-223 |
4.61e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 15 EVLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALN--FREGSIDVEGRPLTQyspKQLARMMAVLPQHGEQAFPYSV 92
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKKQ---ETFARISGYCEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 93 KETV---SLGRYAHQKGwfnswHDEDEQIVQKVMEQTGITRLQDK-----SIVELSGGEKQRVFLAQALAQQPRILLLDE 164
Cdd:PLN03140 971 RESLiysAFLRLPKEVS-----KEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 165 PTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYC-DRLLLMENGEVLIVDTP 223
Cdd:PLN03140 1046 PTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSIDIFEAfDELLLMKRGGQVIYSGP 1104
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
32-184 |
5.56e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 51.15 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 32 ILGPNGSGKTTLLKMISGALNFREGSIDVE------------------------GRPLTQYSPKQLARMMAVLPQHgEQA 87
Cdd:COG3950 30 LVGENGSGKTTLLEAIALALSGLLSRLDDVkfrkllirngefgdsaklilyygtSRLLLDGPLKKLERLKEEYFSR-LDG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 88 FPYSVKETVSLGRYahqKGWFNSWHDEDEQIVQKVMEQT-------------GITRLQ-----------DK-----SIVE 138
Cdd:COG3950 109 YDSLLDEDSNLREF---LEWLREYLEDLENKLSDELDEKleavrealnkllpDFKDIRidrdpgrlvilDKngeelPLNQ 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 139 LSGGEKQRVFLAQALAQQ--------------PRILLLDEPTNHLDLSFQKELLDLLKKW 184
Cdd:COG3950 186 LSDGERSLLALVGDLARRlaelnpalenplegEGIVLIDEIDLHLHPKWQRRILPDLRKI 245
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-215 |
9.58e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGALN---FREGSIDVEGRPLTqyspKQLARMMAVLPQ---HGEQAfp 89
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLD----SSFQRSIGYVQQqdlHLPTS-- 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 90 ySVKETVSLGRYAHQKgwfNSWHD-EDEQIVQKVMEQTGITRLQDkSIVELSGG-----EKQRVFLAQALAQQPRILL-L 162
Cdd:TIGR00956 852 -TVRESLRFSAYLRQP---KSVSKsEKMEYVEEVIKLLEMESYAD-AVVGVPGEglnveQRKRLTIGVELVAKPKLLLfL 926
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 730207193 163 DEPTNHLDLSFQKELLDLLKKWAAEEELTVVSIFHDLNLASLYCDRLLLMENG 215
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKG 979
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-170 |
1.32e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTTLLKMISG-----------ALNFREGSidveGRPLTQ--- 67
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGS----GETIWDikk 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 68 ---YSPKQLarmmavlpqHGEQAFPYSVKeTVSLGRYAHQKGWFNSWHDEDEQIVQKVMEQTGI-TRLQDKSIVELSGGE 143
Cdd:PRK10938 337 higYVSSSL---------HLDYRVSTSVR-NVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIdKRTADAPFHSLSWGQ 406
|
170 180
....*....|....*....|....*..
gi 730207193 144 KQRVFLAQALAQQPRILLLDEPTNHLD 170
Cdd:PRK10938 407 QRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-212 |
3.90e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.32 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISgalnfregsidvegrpltqysPKQLARMMAVLPQhgeqAFPYSvkETV 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL---------------------YASGKARLISFLP----KFSRN--KLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 97 SLGRYahqkgwfnswhdedeqivqKVMEQTGITRLQ-DKSIVELSGGEKQRVFLAQALAQQPR--ILLLDEPTNHLDLSF 173
Cdd:cd03238 64 FIDQL-------------------QFLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 730207193 174 QKELLDLLKKwAAEEELTVVSIFHDLNLASlYCDRLLLM 212
Cdd:cd03238 125 INQLLEVIKG-LIDLGNTVILIEHNLDVLS-SADWIIDF 161
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-228 |
4.57e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.58 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 2 ITVKNLTGGYAGGEVLKGISFEVCEGELFGILGPNGSGKTtllkmiSGALNFREGSIDVEGRPLTQYS----PKQLARMM 77
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**------RGALPAHV*GPDAGRRPWRF*TwcanRRALRRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 78 AV-LPQHGEQAFPYSVKETVSL-GRYahqkgwFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQ 155
Cdd:NF000106 88 G*hRPVR*GRRESFSGRENLYMiGR*------LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 730207193 156 QPRILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLYCDRLLLMENGEVlIVDTPAEVLK 228
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRS-MVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV-IADGKVDELK 232
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
125-183 |
5.96e-06 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 44.53 E-value: 5.96e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 730207193 125 QTGITRLQDKSIVELSGGEKQRVF---LAQALAQQ----------PRILLLDEPTNHLDLSFQKELLDLLKK 183
Cdd:pfam13558 19 EDGSEVETYRRSGGLSGGEKQLLAylpLAAALAAQygsaegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
138-201 |
6.35e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 6.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 730207193 138 ELSGGEKQRVFLAQALAQQPR---ILLLDEPTNHLDLSFQKELLDLLKKWAAEEElTVVSIFHDLNL 201
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDV 234
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
3-154 |
7.51e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.80 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 3 TVKNLtGGYAGGEVlkgISFE-VCEGELFGILGPNGSGKTTLLKMISGALnFREGsidvegrpltqySPKQLARMMAVLP 81
Cdd:cd03279 7 ELKNF-GPFREEQV---IDFTgLDNNGLFLICGPTGAGKSTILDAITYAL-YGKT------------PRYGRQENLRSVF 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730207193 82 QHGEQAFPYSVKETVSLGRY-AHQKGWFNswHDEDEQIVqkVMEQTGITRLQDKSIVELSGGEKQRVFLAQALA 154
Cdd:cd03279 70 APGEDTAEVSFTFQLGGKKYrVERSRGLD--YDQFTRIV--LLPQGEFDRFLARPVSTLSGGETFLASLSLALA 139
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-241 |
8.13e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFREGSIDVEGR------------PLT------------QYSPKQ 72
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvsviaisaglsgQLTgieniefkmlcmGFKRKE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 73 LARMMavlPQhgeqafpysVKETVSLGRYAHQKgwfnswhdedeqiVQKvmeqtgitrlqdksiveLSGGEKQRVFLAQA 152
Cdd:PRK13546 120 IKAMT---PK---------IIEFSELGEFIYQP-------------VKK-----------------YSSGMRAKLGFSIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 153 LAQQPRILLLDEPTNHLDLSFQKELLDLLKKWaAEEELTVVSIFHDLNLASLYCDRLLLMENGEVLIVDTPAEVLKE-ER 231
Cdd:PRK13546 158 ITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKyEA 236
|
250
....*....|
gi 730207193 232 IKKVYKTQIK 241
Cdd:PRK13546 237 FLNDFKKKSK 246
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-217 |
1.21e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 17 LKGISFEVCEGELFGILGPNGSGKTTLLKMISGALNFRE-GSIDVEGRpltqyspkqlarmMAVLPQHgEQAFPYSVKET 95
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT-------------VAYVPQV-SWIFNATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 96 VSLG------RYAHQKGWFNSWHDEDeqivqkVMEQTGITRLQDKSiVELSGGEKQRVFLAQALAQQPRILLLDEPTNHL 169
Cdd:PLN03130 699 ILFGspfdpeRYERAIDVTALQHDLD------LLPGGDLTEIGERG-VNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 730207193 170 DLSFQKELLDLLKKwaaeEEL---TVVSIFHDLNLASlYCDRLLLMENGEV 217
Cdd:PLN03130 772 DAHVGRQVFDKCIK----DELrgkTRVLVTNQLHFLS-QVDRIILVHEGMI 817
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
30-79 |
2.47e-04 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 42.97 E-value: 2.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 730207193 30 FGILGPNGSGKTTLLKMI---SGALNfREGSIDvEGRPLTQYSPKQLARMMAV 79
Cdd:cd04170 2 IALVGHSGSGKTTLAEALlyaTGAID-RLGRVE-DGNTVSDYDPEEKKRKMSI 52
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
139-199 |
4.77e-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: 4.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730207193 139 LSGGEKQRVFLAQALAQQ---PRILLLDEPTNHLDLSFQKELLDLLKKWAAEEElTVVSIFHDL 199
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNL 892
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
135-201 |
1.38e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.84 E-value: 1.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 135 SIVELSGGEKQ--RVFLAQALAQQP-RILLLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNL 201
Cdd:pfam13304 233 PAFELSDGTKRllALLAALLSALPKgGLLLIDEPESGLHPKLLRRLLELLKE-LSRNGAQLILTTHSPLL 301
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-230 |
1.60e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 16 VLKGISFEVCEGELFGILGPNGSGKTTLLKMISGAL--NFREGSIDVEGRPLTQYSPKQlarmmAVlpQHGeqaFPY--- 90
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVSD-----AI--DAG---LAYvte 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 91 -----------SVKETVS---LGRYAHqkgwfNSWHDEDEQIvqKVMEQTGiTRLQDKS------IVELSGGEKQRVFLA 150
Cdd:NF040905 345 drkgyglnlidDIKRNITlanLGKVSR-----RGVIDENEEI--KVAEEYR-KKMNIKTpsvfqkVGNLSGGNQQKVVLS 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 151 QALAQQPRILLLDEPTNHLDLSFQKELLDLLKKWAAEEElTVVSIFHDL-NLASLyCDRLLLMENGEvlIVdtpAEVLKE 229
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGK-GVIVISSELpELLGM-CDRIYVMNEGR--IT---GELPRE 489
|
.
gi 730207193 230 E 230
Cdd:NF040905 490 E 490
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-205 |
1.98e-03 |
|
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: 38.88 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 26 EGELFGILGPNGSGKTTLLKMISGALnfregsidvegrpltqyspkqLARMMAVLPQHGEQAFPYSVkeTVSLGRYahqk 105
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIGLAL---------------------GGAQSATRRRSGVKAGCIVA--AVSAELI---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 106 gwfnswhdedeqivqkvmeqtgITRLQdksiveLSGGEKQRVFLAQALA---QQPRIL-LLDEPTNHLDLSFQKELLDLL 181
Cdd:cd03227 73 ----------------------FTRLQ------LSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAI 124
|
170 180
....*....|....*....|....
gi 730207193 182 KKWAAeEELTVVSIFHDLNLASLY 205
Cdd:cd03227 125 LEHLV-KGAQVIVITHLPELAELA 147
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
139-199 |
2.70e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 2.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 730207193 139 LSGGEKQRVFLAQALA--QQPRIL-LLDEPTNhlDLSFQ--KELLDLLKKwaaeeeL-----TVVSIFHDL 199
Cdd:COG0178 827 LSGGEAQRVKLASELSkrSTGKTLyILDEPTT--GLHFHdiRKLLEVLHR------LvdkgnTVVVIEHNL 889
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-228 |
3.62e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 133 DKSIVELSGGEKQRVFLAQAL-AQQPRIL-LLDEPTNHLDLSFQKELLDLLKKwAAEEELTVVSIFHDLNLASLyCDRLL 210
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLgAELIGITyILDEPSIGLHPQDTHKLINVIKK-LRDQGNTVLLVEHDEQMISL-ADRII 548
|
90 100
....*....|....*....|....
gi 730207193 211 LME------NGEVLIVDTPAEVLK 228
Cdd:PRK00635 549 DIGpgagifGGEVLFNGSPREFLA 572
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
29-191 |
4.67e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.25 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 29 LFGILGPNGSGKTTLLKMISGAL------NFREGSIDVEGRPLTQYSPKQLARMMAVLPQHGEQAFPYSVKETVSLGRYA 102
Cdd:pfam13476 20 LTLITGPNGSGKTTILDAIKLALygktsrLKRKSGGGFVKGDIRIGLEGKGKAYVEITFENNDGRYTYAIERSRELSKKK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730207193 103 HQKGWFNSWHDEDEQIVQKVMEQTGITRLQDKSIVELSGGEKQRVFLAQALAQQPRIL--LLDEptnhlDLSFQKELLDL 180
Cdd:pfam13476 100 GKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKEKKERLEELekALEE-----KEDEKKLLEKL 174
|
170
....*....|.
gi 730207193 181 LKKWAAEEELT 191
Cdd:pfam13476 175 LQLKEKKKELE 185
|
|
| ATPS |
cd00517 |
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ... |
206-245 |
5.02e-03 |
|
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, catalyzes the transfer of an adenylyl group from ATP to sulfate, forming adenosine 5'-phosphosulfate (APS). This reaction is generally accompanied by a further reaction, catalyzed by APS kinase, in which APS is phosphorylated to yield 3'-phospho-APS (PAPS). In some organisms the APS kinase is a separate protein, while in others it is incorporated with ATP sulfurylase in a bifunctional enzyme that catalyzes both reactions. In bifunctional proteins, the domain that performs the kinase activity can be attached at the N-terminal end of the sulfurylase unit or at the C-terminal end, depending on the organism. While the reaction is ubiquitous among organisms, the physiological role of the reaction varies. In some organisms it is used to generate APS from sulfate and ATP, while in others it proceeds in the opposite direction to generate ATP from APS and pyrophosphate. ATP sulfurylase can be a monomer, a homodimer, or a homo-oligomer, depending on the organism. ATPS belongs to a large superfamily of nucleotidyltransferases that includes pantothenate synthetase (PanC), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. The enzymes of this family are structurally similar and share a dinucleotide-binding domain.
Pssm-ID: 173895 [Multi-domain] Cd Length: 353 Bit Score: 39.15 E-value: 5.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 730207193 206 CDRLLLMENGEVL-IVDTPA--EVLKEERIKKVYKTQIKNHPH 245
Cdd:cd00517 68 GERVALRYPGQPLaILTVEEiyEPDKEEEAARVFGTTDPHHPG 110
|
|
| |
