|
Name |
Accession |
Description |
Interval |
E-value |
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-241 |
4.36e-77 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 241.85 E-value: 4.36e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQgqEF--C 80
Cdd:COG1129 14 FGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAIIHQ--ELnlV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLFLGKEINQIGIRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:COG1129 92 PNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 161 SVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAGVTTEHEYEEIAEN 240
Cdd:COG1129 172 TEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVGRELEDLFPKRAAA 251
|
.
gi 1626716271 241 P 241
Cdd:COG1129 252 P 252
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
2.13e-63 |
|
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: 196.11 E-value: 2.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQgqefcd 81
Cdd:cd03216 9 RFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMVYQ------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 nldvasnlflgkeinqigirdddsmnsrarsvlktlssairvgspiasLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:cd03216 83 ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1626716271 162 VMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGV 210
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-221 |
3.26e-61 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 201.02 E-value: 3.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQgqEFC-- 80
Cdd:COG3845 15 FGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGMVHQ--HFMlv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLFLGKEINQIGIRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:COG3845 93 PNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 161 SVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEI 221
Cdd:COG3845 173 TPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEEL 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-206 |
2.46e-50 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 164.56 E-value: 2.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMgIASVFQ---GQEFC 80
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVFQnpdDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNL--DVASNLflgkeiNQIGIRDDDsMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTA 158
Cdd:cd03225 91 PTVeeEVAFGL------ENLGLPEEE-IEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 159 ALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGH 206
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-227 |
4.16e-50 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 172.04 E-value: 4.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGF--GHIYLNGEQVTIPSIREADRMGIASVFQGQEF 79
Cdd:PRK13549 14 TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTERAGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 CDNLDVASNLFLGKEINQIGIRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAA 159
Cdd:PRK13549 94 VKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 160 LSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAG 227
Cdd:PRK13549 174 LTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVG 241
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1-207 |
1.89e-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: 162.99 E-value: 1.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 1 MKFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQG-QEF 79
Cdd:cd03219 8 KRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTFQIpRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 -----CDNLDVASNLFLGKEINQIGIRDDDS-MNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILL 153
Cdd:cd03219 88 peltvLENVMVAAQARTGSGLLLARARREEReARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 154 DEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03219 168 DEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-227 |
1.39e-48 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 167.78 E-value: 1.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQGQEFCDNLDV 85
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGKEINQIGIRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQS 165
Cdd:PRK11288 97 AENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 166 AEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTV-ETSYEEIIAEIAG 227
Cdd:PRK11288 177 EQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMaQVDRDQLVQAMVG 239
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-207 |
1.64e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 160.61 E-value: 1.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIasVFQGQEFCD 81
Cdd:COG1131 9 RYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGY--VPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLFLGKEINQIGIRDDDSmnsRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:COG1131 87 DLTVRENLRFFARLYGLPRKEARE---RIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1626716271 162 VMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG1131 164 PEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-207 |
7.00e-46 |
|
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: 153.64 E-value: 7.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAdRMGIASVFQ---GQEFCDN 82
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL-RRKVGLVFQnpdDQLFAPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 L--DVAsnlfLGKEinQIGIRDDDsMNSRARSVLKtlssaiRVG------SPIASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:COG1122 93 VeeDVA----FGPE--NLGLPREE-IRERVEEALE------LVGlehladRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 155 EPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-207 |
1.97e-45 |
|
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: 153.09 E-value: 1.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 1 MKFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIasVFQGQEFC 80
Cdd:COG4555 9 KKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV--LPDERGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLFLGKEINQIgirDDDSMNSRARSVLKTLS-SAIRVGSpIASLSVGQRQTVAIARTLLNDPQLILLDEPTAA 159
Cdd:COG4555 87 DRLTVRENIRYFAELYGL---FDEELKKRIEELIELLGlEEFLDRR-VGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 160 LSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-212 |
2.07e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 152.12 E-value: 2.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIRE-----ADRMGIasVFQGQEFC 80
Cdd:COG1136 21 VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERElarlrRRHIGF--VFQFFNLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLFLGKEINQIGIRDDdsmNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:COG1136 99 PELTALENVALPLLLAGVSRKER---RERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 161 SVMQSAEVLAYIKRL-RSEGRSVVMVCHDlPDVFAVSDRIVVIRQGHVTGVHR 212
Cdd:COG1136 176 DSKTGEEVLELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1-207 |
2.16e-45 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 150.63 E-value: 2.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 1 MKFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQvtIPSIREADRMGIASVFQGQEFC 80
Cdd:cd03230 8 KRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD--IKKEPEEVKRRIGYLPEEPSLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLflgkeinqigirdddsmnsrarsvlktlssairvgspiaSLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:cd03230 86 ENLTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1626716271 161 SVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-242 |
2.24e-44 |
|
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: 150.57 E-value: 2.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 1 MKFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQ-GQEF 79
Cdd:COG0411 12 KRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIARTFQnPRLF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 C-----DNLDVA------SNLFLGKEINQIGIRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDP 148
Cdd:COG0411 92 PeltvlENVLVAaharlgRGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 149 QLILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGhvtgvhrtvetsyeEIIAEiaG 227
Cdd:COG0411 172 KLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFG--------------RVIAE--G 235
|
250
....*....|....*
gi 1626716271 228 vttehEYEEIAENPK 242
Cdd:COG0411 236 -----TPAEVRADPR 245
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-207 |
5.13e-44 |
|
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: 148.41 E-value: 5.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIRE-----ADRMGIasVFQGQEFC 80
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafrRRHIGF--VFQSFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLFLGKEINQIGIRDDdsmNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:cd03255 95 PDLTALENVELPLLLAGVPKKER---RERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 161 SVMQSAEVLAYIKRL-RSEGRSVVMVCHDlPDVFAVSDRIVVIRQGHV 207
Cdd:cd03255 172 DSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-207 |
6.44e-44 |
|
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: 148.35 E-value: 6.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT-IPSIREAdRMGIASVFQGQEFCDN 82
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITgLPPHERA-RAGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVASNLFLGKEINQIGIRDDDsmnsRAR-----SVLKTlssaiRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:cd03224 90 LTVEENLLLGAYARRRAKRKAR----LERvyelfPRLKE-----RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-206 |
2.65e-43 |
|
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: 145.41 E-value: 2.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPS-IREADRMGIASVFQGQEFCD 81
Cdd:cd03229 10 YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdELPPLRRRIGMVFQDFALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLFLGkeinqigirdddsmnsrarsvlktlssairvgspiasLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:cd03229 90 HLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1626716271 162 VMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGH 206
Cdd:cd03229 133 PITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-207 |
4.85e-43 |
|
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: 145.74 E-value: 4.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIReadRMGIASVFQGQEFCDN 82
Cdd:cd03259 10 YGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVASNLFLGKEINQIgirDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:cd03259 87 LTVAENIAFGLKLRGV---PKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1626716271 163 MQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03259 164 KLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
9-241 |
4.28e-42 |
|
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: 144.42 E-value: 4.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIRE-ADRMGIasVFQGQEFCDNLDVAS 87
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElARRIAY--VPQEPPAPFGLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NLFLG-----KEINQIGIRDDDsmnsRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:COG1120 95 LVALGryphlGLFGRPSAEDRE----AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 163 MQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV--TGVHRTVETsyEEIIAEIAGVTTEHEYEEIAE 239
Cdd:COG1120 171 AHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIvaQGPPEEVLT--PELLEEVYGVEARVIEDPVTG 248
|
..
gi 1626716271 240 NP 241
Cdd:COG1120 249 RP 250
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-208 |
5.43e-42 |
|
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: 142.19 E-value: 5.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMgIASVFQgqeFCDNLDVA 86
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVPQ---ALELLGLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 87 SnlFLGKEINQigirdddsmnsrarsvlktlssairvgspiasLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSA 166
Cdd:cd03214 89 H--LADRPFNE--------------------------------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1626716271 167 EVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVT 208
Cdd:cd03214 135 ELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-209 |
1.33e-41 |
|
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: 141.90 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT--------IPSIREADRMGIASVFqgqE 78
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEkerkrigyVPQRRSIDRDFPISVR---D 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 79 FcdnldVASNLFLGKEINQIGIRDDDSmnsRARSVLKtlssaiRVG------SPIASLSVGQRQTVAIARTLLNDPQLIL 152
Cdd:cd03235 90 V-----VLMGLYGHKGLFRRLSKADKA---KVDEALE------RVGlseladRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 153 LDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVI-RQGHVTG 209
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLnRTVVASG 213
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-216 |
2.16e-41 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 148.40 E-value: 2.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGF--GHIYLNGEQVTIPSIREADRMGIASVFQGQEFC 80
Cdd:NF040905 11 FPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALGIVIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLFLGKEINQIGIRDDDSMNSRARSVLKtlssaiRVG------SPIASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:NF040905 91 PYLSIAENIFLGNERAKRGVIDWNETNRRARELLA------KVGldespdTLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 155 EPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGhvtgvhRTVET 216
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDG------RTIET 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-207 |
3.91e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 141.77 E-value: 3.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT--------IPSIREADRMGIASVFqgqEF 79
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRrarrrigyVPQRAEVDWDFPITVR---DV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 cdnldVASNLFLGKEINQIGIRDDdsmNSRARSVLKtlssaiRVG------SPIASLSVGQRQTVAIARTLLNDPQLILL 153
Cdd:COG1121 98 -----VLMGRYGRRGLFRRPSRAD---REAVDEALE------RVGledladRPIGELSGGQQQRVLLARALAQDPDLLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 154 DEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG1121 164 DEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-207 |
7.98e-41 |
|
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: 147.36 E-value: 7.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIRE----ADRMGIasVFQgqefcd 81
Cdd:COG1123 278 VRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelRRRVQM--VFQ------ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 nlDVASNLF----LGKEI----NQIGIRDDDSMNSRARSVLKT--LSSAIRvGSPIASLSVGQRQTVAIARTLLNDPQLI 151
Cdd:COG1123 350 --DPYSSLNprmtVGDIIaeplRLHGLLSRAERRERVAELLERvgLPPDLA-DRYPHELSGGQRQRVAIARALALEPKLL 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 152 LLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG1123 427 ILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-206 |
1.56e-40 |
|
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: 137.38 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAdRMGIASVFQgqefcd 81
Cdd:cd00267 8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL-RRRIGYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 nldvasnlflgkeinqigirdddsmnsrarsvlktlssairvgspiasLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1626716271 162 VMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGH 206
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-227 |
1.85e-40 |
|
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: 146.12 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGF--GHIYLNGEQVTIPSIREADRMGIASVFQGQEF 79
Cdd:TIGR02633 10 TFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 CDNLDVASNLFLGKEINQIGIR-DDDSMNSRARSVLKTLS-SAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:TIGR02633 90 VPELSVAENIFLGNEITLPGGRmAYNAMYLRAKNLLRELQlDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAG 227
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-207 |
2.47e-40 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 139.18 E-value: 2.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMG--IASVFQgqef 79
Cdd:cd03257 14 GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRkeIQMVFQ---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 cdnlDVASNL----FLGKEINQI----GIRDDDSMNSRARSVLktlssAIRVGSPIA-------SLSVGQRQTVAIARTL 144
Cdd:cd03257 90 ----DPMSSLnprmTIGEQIAEPlrihGKLSKKEARKEAVLLL-----LVGVGLPEEvlnryphELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 145 LNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-208 |
2.77e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 136.34 E-value: 2.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT------IPSIREadRMGIasVFQGQEF 79
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkrreIPYLRR--RIGV--VFQDFRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 CDNLDVASNLFLGKEInqIGiRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAA 159
Cdd:COG2884 91 LPDRTVYENVALPLRV--TG-KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1626716271 160 LSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVT 208
Cdd:COG2884 168 LDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-208 |
5.07e-39 |
|
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: 136.47 E-value: 5.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRmGIASVFQgqefcdnlDV 85
Cdd:COG1124 18 VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR-RVQMVFQ--------DP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNL--------FLGKEINQIGIRDDDSmnsRARSVLKT--LSSAIRVGSPiASLSVGQRQTVAIARTLLNDPQLILLDE 155
Cdd:COG1124 89 YASLhprhtvdrILAEPLRIHGLPDREE---RIAELLEQvgLPPSFLDRYP-HQLSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 156 PTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHVT 208
Cdd:COG1124 165 PTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-207 |
5.63e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 136.34 E-value: 5.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRM--GIASVFQgqEFC--D 81
Cdd:COG3638 16 TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrRIGMIFQ--QFNlvP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLFLGKeINQIGI--------RDDDSMnsRARSVLKtlssaiRVG------SPIASLSVGQRQTVAIARTLLND 147
Cdd:COG3638 94 RLSVLTNVLAGR-LGRTSTwrsllglfPPEDRE--RALEALE------RVGladkayQRADQLSGGQQQRVAIARALVQE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 148 PQLILLDEPTAALSVMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG3638 165 PKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-240 |
7.39e-39 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 141.85 E-value: 7.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQGQEFCD 81
Cdd:PRK09700 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQELSVID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLFLG----KEINQIGIRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:PRK09700 94 ELTVLENLYIGrhltKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAGVTTEHEYEEI 237
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGRELQNRFNAM 253
|
...
gi 1626716271 238 AEN 240
Cdd:PRK09700 254 KEN 256
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
9-158 |
9.30e-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: 132.77 E-value: 9.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTiPSIREADRMGIASVFQGQEFCDNLDVASN 88
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 89 LFLGKEinqIGIRDDDSMNSRARSVLKTLS----SAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTA 158
Cdd:pfam00005 80 LRLGLL---LKGLSKREKDARAEEALEKLGlgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-207 |
1.07e-38 |
|
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: 135.32 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQvtIPSIREAD------RMGIasVFQGQEFCDN 82
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGED--ISGLSEAElyrlrrRMGM--LFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVASNLFLGkeINQIGIRDDDSMNSRARSVLKtlssaiRVGSP------IASLSVGQRQTVAIARTLLNDPQLILLDEP 156
Cdd:cd03261 92 LTVFENVAFP--LREHTRLSEEEIREIVLEKLE------AVGLRgaedlyPAELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 157 TAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03261 164 TAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-208 |
1.10e-38 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 135.11 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQGQEFCDNLDV 85
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGkeinQIGIRDDDSMNSRARSV------LKTlssaiRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAA 159
Cdd:COG0410 96 EENLLLG----AYARRDRAEVRADLERVyelfprLKE-----RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1626716271 160 LSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVT 208
Cdd:COG0410 167 LAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-207 |
1.53e-38 |
|
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: 141.19 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPG---FGHIYLNGEQVTIPSIREADRMgIASVFQgqEFC 80
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR-IGMVFQ--DPM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLFLGKEINQIGIRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:COG1123 94 TQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTAL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 161 SVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG1123 174 DVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-241 |
1.61e-38 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 140.91 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQGQEFCDN 82
Cdd:PRK10762 14 FPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVASNLFLGKEI-NQIGIRDDDSMNSRARSVLKTL----SSAIRVGSpiasLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:PRK10762 94 LTIAENIFLGREFvNRFGRIDWKKMYAEADKLLARLnlrfSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAGVTTEHEYEEI 237
Cdd:PRK10762 170 DALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRKLEDQYPRL 249
|
....
gi 1626716271 238 AENP 241
Cdd:PRK10762 250 DKAP 253
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-212 |
3.12e-38 |
|
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: 133.75 E-value: 3.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIReadrmgIASVFQGqefcDNL 83
Cdd:cd03293 15 GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------RGYVFQQ----DAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 ----DVASNLFLGKEINqiGIRDDDSMnSRARSVLKT--LSSAIRvgSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:cd03293 85 lpwlTVLDNVALGLELQ--GVPKAEAR-ERAEELLELvgLSGFEN--AYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1626716271 158 AALSvMQSAEVL--AYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVI--RQGHVTGVHR 212
Cdd:cd03293 160 SALD-ALTREQLqeELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVE 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
6-201 |
8.11e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 133.68 E-value: 8.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSireaDRMGIasVFQGqefcDNL-- 83
Cdd:COG1116 24 VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG----PDRGV--VFQE----PALlp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 --DVASNLFLGKEINQIGIRDDDSmnsRARSVLKtlssaiRVG------SPIASLSVGQRQTVAIARTLLNDPQLILLDE 155
Cdd:COG1116 94 wlTVLDNVALGLELRGVPKAERRE---RARELLE------LVGlagfedAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 156 PTAAL-----SVMQsAEVLAYikrLRSEGRSVVMVCHDLPDVFAVSDRIVV 201
Cdd:COG1116 165 PFGALdaltrERLQ-DELLRL---WQETGKTVLFVTHDVDEAVFLADRVVV 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
13-207 |
1.27e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 132.19 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 13 NLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipSIREADRmGIASVFQgqefcDN-----LDVAS 87
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT--ALPPAER-PVSMLFQ-----ENnlfphLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NLFLgkeinqiGIRDDDSMNSRARSVLKTLssAIRVG-------SPiASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:COG3840 91 NIGL-------GLRPGLKLTAEQRAQVEQA--LERVGlaglldrLP-GQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 161 SVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG3840 161 DPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRI 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-224 |
1.49e-37 |
|
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: 139.12 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqVTIPSIREADRMG-IASV------FQGqef 79
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING--VDLSDLDPASWRRqIAWVpqnpylFAG--- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 cdnlDVASNLFLGK------EINQIgIRDddsmnSRARSVLKTLSSAI--RVGSPIASLSVGQRQTVAIARTLLNDPQLI 151
Cdd:COG4988 426 ----TIRENLRLGRpdasdeELEAA-LEA-----AGLDEFVAALPDGLdtPLGEGGRGLSGGQAQRLALARALLRDAPLL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 152 LLDEPTAALSVMQSAEVLAYIKRLrSEGRSVVMVCHDLPDVfAVSDRIVVIRQGHVTGvhrtvETSYEEIIAE 224
Cdd:COG4988 496 LLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALL-AQADRILVLDDGRIVE-----QGTHEELLAK 561
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-236 |
3.13e-37 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 137.49 E-value: 3.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQGQEFCDN 82
Cdd:PRK15439 21 YSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVASNLFLGKEINQigirdDDSmnSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:PRK15439 101 LSVKENILFGLPKRQ-----ASM--QKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 163 MQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAGVTTEHEYEE 236
Cdd:PRK15439 174 AETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAITPAAREKSLSA 247
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-232 |
3.16e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 137.07 E-value: 3.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASV---FQGQEFCDNL 83
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAYVpedRKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 DVASNLFLG--KEINQIGIRDDDSMNSRARSVLKTLSsaIRVGS---PIASLSVGQRQTVAIARTLLNDPQLILLDEPTA 158
Cdd:COG1129 346 SIRENITLAslDRLSRGGLLDRRRERALAEEYIKRLR--IKTPSpeqPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 159 ALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAGVTTEH 232
Cdd:COG1129 424 GIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATEEAIMAAATGGAAAA 497
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-207 |
7.13e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.55 E-value: 7.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT---IPSIReadRMgIASVFQgqE---FCDN 82
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSampPPEWR---RQ-VAYVPQ--EpalWGGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 ldVASNLFLGKEINQIGIRDDdsmnsRARSVLKTLS-SAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:COG4619 90 --VRDNLPFPFQLRERKFDRE-----RALELLERLGlPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1626716271 162 VMQSAEVLAYIKRLR-SEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG4619 163 PENTRRVEELLREYLaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-207 |
9.91e-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: 129.57 E-value: 9.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAD-RMGIASVFQGQEFC 80
Cdd:cd03262 9 SFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElRQKVGMVFQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLFLGkeinQIGIR--DDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTA 158
Cdd:cd03262 89 PHLTVLENITLA----PIKVKgmSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1626716271 159 ALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03262 165 ALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-207 |
1.14e-36 |
|
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: 130.10 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAD----RMGIasVFQGQE 78
Cdd:COG1127 15 FGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrRIGM--LFQGGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 79 FCDNLDVASNL-FLGKEINQIgirDDDSMNSRARSVLKtlssaiRVG-------SPiASLSVGQRQTVAIARTLLNDPQL 150
Cdd:COG1127 93 LFDSLTVFENVaFPLREHTDL---SEAEIRELVLEKLE------LVGlpgaadkMP-SELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 151 ILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-207 |
1.62e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 129.73 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPS--IREAdRMGIASVFQgqEFC 80
Cdd:COG1126 11 FGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKkdINKL-RRKVGMVFQ--QFN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 --DNLDVASNLFLGkeinQIGIR--DDDSMNSRARSVLKtlssaiRVG-------SPiASLSVGQRQTVAIARTLLNDPQ 149
Cdd:COG1126 88 lfPHLTVLENVTLA----PIKVKkmSKAEAEERAMELLE------RVGladkadaYP-AQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 150 LILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPdvFA--VSDRIVVIRQGHV 207
Cdd:COG1126 157 VMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMG--FAreVADRVVFMDGGRI 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-207 |
2.02e-36 |
|
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: 128.53 E-value: 2.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipSIREADRmGIASVFQGQEFCD 81
Cdd:cd03301 9 RFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDR-DIAMVFQNYALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLFLGKEINqigIRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:cd03301 86 HMTVYDNIAFGLKLR---KVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1626716271 162 VMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03301 163 AKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-207 |
3.18e-36 |
|
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: 128.84 E-value: 3.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT---IPSIREAdRMGIASVFQGQEFC 80
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkGKALRQL-RRQIGMIFQQFNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLFLGKEINQIGIRDDDSMNS-----RARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDE 155
Cdd:cd03256 91 ERLSVLENVLSGRLGRRSTWRSLFGLFPkeekqRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 156 PTAALSVMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03256 171 PVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-206 |
1.44e-35 |
|
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: 125.19 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNG---EQVTIPSIREAdrmgIASVFQGqefcdn 82
Cdd:cd03228 15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlRDLDLESLRKN----IAYVPQD------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 ldvaSNLFlgkeinqigirdddsmnsrARSVLKTLssairvgspiasLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:cd03228 85 ----PFLF-------------------SGTIRENI------------LSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1626716271 163 MQSAEVLAYIKRLRsEGRSVVMVCHDLPDVfAVSDRIVVIRQGH 206
Cdd:cd03228 130 ETEALILEALRALA-KGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-207 |
5.94e-35 |
|
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: 125.43 E-value: 5.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT-IPsireADRMGIASVFQGQEFC 80
Cdd:cd03300 9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITnLP----PHKRPVNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLFLGKEINQIGIRDDDSMNSRARSVLKTLSSAIRVgspIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:cd03300 85 PHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRK---PSQLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 161 SVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03300 162 DLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
9-207 |
1.46e-34 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 124.81 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFG-HIYLNGEQ---VTIPSIREadRMGIASVFQGQEFCDN-- 82
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggEDVWELRK--RIGLVSPALQLRFPRDet 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 -LD-VASNLFlgkeiNQIGIRD--DDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTA 158
Cdd:COG1119 97 vLDvVLSGFF-----DSIGLYRepTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1626716271 159 ALSVMQSAEVLAYIKRLRSEG-RSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG1119 172 GLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-207 |
1.56e-34 |
|
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: 131.49 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNG---EQVTIPSIREAdrmgIASVFQGQE-FCDN 82
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlRQIDPASLRRQ----IGVVLQDVFlFSGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 ldVASNLFLGKEinqiGIRDDDsmnsrARSVLKT--LSSAIR---------VGSPIASLSVGQRQTVAIARTLLNDPQLI 151
Cdd:COG2274 565 --IRENITLGDP----DATDEE-----IIEAARLagLHDFIEalpmgydtvVGEGGSNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 152 LLDEPTAALSVMQSAEVLAYIKRLRsEGRSVVMVCHDLpDVFAVSDRIVVIRQGHV 207
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL-STIRLADRIIVLDKGRI 687
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-207 |
1.58e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 127.52 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT-IPsireADRMGIASVFQgqefc 80
Cdd:COG3842 14 RYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTgLP----PEKRNVGMVFQ----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 D-----NLDVASNL-FlgkeinqiGIR----DDDSMNSRARSVLKtlssaiRVG------SPIASLSVGQRQTVAIARTL 144
Cdd:COG3842 85 DyalfpHLTVAENVaF--------GLRmrgvPKAEIRARVAELLE------LVGlegladRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 145 LNDPQLILLDEPTAALSV-----MQsAEVLAYIKRLrseGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG3842 151 APEPRVLLLDEPLSALDAklreeMR-EELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-208 |
2.27e-34 |
|
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: 123.98 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEqvtIP---SIREADRMGIasVF-QGQ 77
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL---VPwkrRKKFLRRIGV--VFgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 78 EFCDNLDVASNLFLGKEINQIgirDDDsmnsRARSVLKTLSSAIRVG----SPIASLSVGQRQTVAIARTLLNDPQLILL 153
Cdd:cd03267 105 QLWWDLPVIDSFYLLAAIYDL---PPA----RFKKRLDELSELLDLEelldTPVRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 154 DEPTAALSVMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVT 208
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-202 |
2.65e-34 |
|
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: 123.44 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGF--LQPGF---GHIYLNGEQVTIPSI-READRMGIASVFQg 76
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndLIPGApdeGEVLLDGKDIYDLDVdVLELRRRVGMVFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 77 QEFCDNLDVASNLFLGKEINqiGIRDDDSMNSRARSVLKT--LSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:cd03260 89 KPNPFPGSIYDNVAYGLRLH--GIKLKEELDERVEEALRKaaLWDEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 155 EPTAALSVMQSAEVLAYIKRLRSEgRSVVMVCHDLPDVFAVSDRIVVI 202
Cdd:cd03260 167 EPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFL 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
12-208 |
6.00e-34 |
|
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: 125.98 E-value: 6.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 12 VNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGE-------QVTIPsireADRMGIASVFQGQEFCDNLD 84
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsarGIFLP----PHRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 85 VASNLflgkeinQIGIRDDDSMNSRARsvlktLSSAIRV-------GSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:COG4148 94 VRGNL-------LYGRKRAPRAERRIS-----FDEVVELlgighllDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSEGR-SVVMVCHDLPDVFAVSDRIVVIRQGHVT 208
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDiPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-207 |
8.91e-34 |
|
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: 122.45 E-value: 8.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREadrMGIASVFQGQEFCD 81
Cdd:cd03296 11 RFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---RNVGFVFQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLFLGKEINQIGIR-DDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:cd03296 88 HMTVFDNVAFGLRVKPRSERpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 161 SVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03296 168 DAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
9-227 |
3.53e-32 |
|
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: 118.21 E-value: 3.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT-IPSIREadrmGIASVFQGQEFCDNLDVAS 87
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITnLPPEKR----DISYVPQNYALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NLFLGKEINQIGIRDDDsmnSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAE 167
Cdd:cd03299 91 NIAYGLKKRKVDKKEIE---RKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 168 VLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQG---HVTGVHRTVETSYEEIIAEIAG 227
Cdd:cd03299 168 LREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGkliQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-205 |
7.79e-32 |
|
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: 116.55 E-value: 7.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPsIREADRMGiaSVFQGQEFCD 81
Cdd:cd03268 9 TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRRIG--ALIEAPGFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLFLGKeiNQIGIRDddsmnSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:cd03268 86 NLTARENLRLLA--RLLGIRK-----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1626716271 162 VMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQG 205
Cdd:cd03268 159 PDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-202 |
8.09e-32 |
|
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: 122.78 E-value: 8.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqVTIPSIREAD-RMGIASVFQgQEFCDNLDV 85
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG--VPLADADADSwRDQIAWVPQ-HPFLFAGTI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGKeinqigiRD-DDSMNSRA--RSVLKTLSSAI------RVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEP 156
Cdd:TIGR02857 413 AENIRLAR-------PDaSDAEIREAleRAGLDEFVAALpqgldtPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1626716271 157 TAALSVMQSAEVLAYIKRLrSEGRSVVMVCHDLPDVfAVSDRIVVI 202
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-207 |
9.34e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.79 E-value: 9.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipSIREADRmGIASVFQGQEFCD 81
Cdd:COG3839 12 SYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT--DLPPKDR-NIAMVFQSYALYP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLFLGKEINQIgirDDDSMNSRARSVLKTLSsairvgspI--------ASLSVGQRQTVAIARTLLNDPQLILL 153
Cdd:COG3839 89 HMTVYENIAFPLKLRKV---PKAEIDRRVREAAELLG--------LedlldrkpKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 154 DEPTAALSVMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
9-204 |
1.41e-31 |
|
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: 116.04 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIAS----VFQGQEFCDNLD 84
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGhadgLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 85 VASNLFlgkeinqiGIRDDDSmnsRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQ 164
Cdd:COG4133 98 FWAALY--------GLRADRE---AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1626716271 165 SAEVLAYIKRLRSEGRSVVMVCHDlpDVFAVSDRIVVIRQ 204
Cdd:COG4133 167 VALLAELIAAHLARGGAVLLTTHQ--PLELAAARVLDLGD 204
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-207 |
1.56e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 119.10 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIpSIREADRmGIASVFQgqefcD 81
Cdd:COG1118 11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-NLPPRER-RVGFVFQ-----H 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 -----NLDVASNLflgkeinQIGIRDDDSMNSRARSVLKTLSSAIRVGS-----PiASLSVGQRQTVAIARTLLNDPQLI 151
Cdd:COG1118 84 yalfpHMTVAENI-------AFGLRVRPPSKAEIRARVEELLELVQLEGladryP-SQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 152 LLDEPTAALSvmqsaevlAYIKR-LRSE--------GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG1118 156 LLDEPFGALD--------AKVRKeLRRWlrrlhdelGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-205 |
1.61e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.01 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 1 MKFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT-IPSIREAdRMGIASVFQGQEF 79
Cdd:PRK11300 13 MRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEgLPGHQIA-RMGVVRTFQHVRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 CDNLDVASNL-----------FLGKEINQIGIRdddsmnsraRSVLKTLSSAI----RVG------SPIASLSVGQRQTV 138
Cdd:PRK11300 92 FREMTVIENLlvaqhqqlktgLFSGLLKTPAFR---------RAESEALDRAAtwleRVGllehanRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 139 AIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQG 205
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-231 |
1.74e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 121.67 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASV---FQGQEFCDN 82
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAYIpedRLGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVASNLFLG----KEINQIGIRDDDSMNSRARSVLKTLSsaIRVGS---PIASLSVGQRQTVAIARTLLNDPQLILLDE 155
Cdd:COG3845 351 MSVAENLILGryrrPPFSRGGFLDRKAIRAFAEELIEEFD--VRTPGpdtPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 156 PTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAGVTTE 231
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATREEIGLLMAGVKEE 504
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-208 |
2.73e-31 |
|
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: 121.41 E-value: 2.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqVTIPSIREAD---RMGIAS----VFQGqefc 80
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG--VDLRDLDEDDlrrRIAVVPqrphLFDT---- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 dnlDVASNLFLGKEinqiGIRDDDsmnsrARSVLKT--LSSAI---------RVGSPIASLSVGQRQTVAIARTLLNDPQ 149
Cdd:COG4987 424 ---TLRENLRLARP----DATDEE-----LWAALERvgLGDWLaalpdgldtWLGEGGRRLSGGERRRLALARALLRDAP 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1626716271 150 LILLDEPTAALSVMQSAEVLAYIKRLrSEGRSVVMVCHDLPDVFAVsDRIVVIRQGHVT 208
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERM-DRILVLEDGRIV 548
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-207 |
3.05e-31 |
|
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: 114.07 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASV---FQGQEFCDNLD 84
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 85 VASNLFLGkeinqigirdddsmnsrarsvlktlssairvgspiASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQ 164
Cdd:cd03215 95 VAENIALS-----------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1626716271 165 SAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03215 140 KAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-207 |
4.55e-31 |
|
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: 114.70 E-value: 4.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 1 MKFGFVEALKSVNLSIQ---RQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNG-------EQVTIPSireaDRMGI 70
Cdd:cd03297 2 LCVDIEKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPP----QQRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 71 ASVFQGQEFCDNLDVASNLFLG-KEINQIGIRDddsmnsRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQ 149
Cdd:cd03297 78 GLVFQQYALFPHLNVRENLAFGlKRKRNREDRI------SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1626716271 150 LILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-207 |
4.89e-31 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 114.77 E-value: 4.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIasVFQGQEFCDNL 83
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGF--VSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 DVASNL-FLGKEINQIGirddDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:cd03266 94 TARENLeYFAGLYGLKG----DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1626716271 163 MQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03266 170 MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
13-213 |
5.60e-31 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 114.57 E-value: 5.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 13 NLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT--IPSIREadrmgIASVFQGQEFCDNLDVASNLF 90
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTglAPYQRP-----VSMLFQENNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 91 LGkeinqigIRDDDSMNSRARSVLKTLSSAIRVGSPIA----SLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSA 166
Cdd:TIGR01277 93 LG-------LHPGLKLNAEQQEKVVDAAQQVGIADYLDrlpeQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 167 EVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRT 213
Cdd:TIGR01277 166 EMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-208 |
8.40e-31 |
|
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: 113.89 E-value: 8.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQvtIPSIREADRMGIasVFQgqefcdnlDVA 86
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP--IKAKERRKSIGY--VMQ--------DVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 87 SNLF---LGKEInQIGIRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVM 163
Cdd:cd03226 82 YQLFtdsVREEL-LLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1626716271 164 QSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVT 208
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
8-207 |
1.18e-30 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 120.36 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqVTIPSIREAD-RMGIASVFQgqefcdnlDVA 86
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG--VDIRQIDPADlRRNIGYVPQ--------DPR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 87 snLFLGKeinqigIRDDDSMNSRA---RSVLKTLSSA--------------IRVGSPIASLSVGQRQTVAIARTLLNDPQ 149
Cdd:TIGR03375 550 --LFYGT------LRDNIALGAPYaddEEILRAAELAgvtefvrrhpdgldMQIGERGRSLSGGQRQAVALARALLRDPP 621
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 150 LILLDEPTAALSVMQSAEVLAYIKRLrSEGRSVVMVCHDLPdVFAVSDRIVVIRQGHV 207
Cdd:TIGR03375 622 ILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTS-LLDLVDRIIVMDNGRI 677
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-205 |
1.19e-30 |
|
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: 113.84 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqVTIPSIREAD-RMGIASVfqGQEfcdnld 84
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG--TDIRQLDPADlRRNIGYV--PQD------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 85 vaSNLFLGKeinqigIRD---------DDSMNSRA--RSVLKTLSS------AIRVGSPIASLSVGQRQTVAIARTLLND 147
Cdd:cd03245 87 --VTLFYGT------LRDnitlgaplaDDERILRAaeLAGVTDFVNkhpnglDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 148 PQLILLDEPTAALSvMQSAEVLayIKRLRS--EGRSVVMVCHDLPdVFAVSDRIVVIRQG 205
Cdd:cd03245 159 PPILLLDEPTSAMD-MNSEERL--KERLRQllGDKTLIIITHRPS-LLDLVDRIIVMDSG 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-207 |
2.31e-30 |
|
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: 113.44 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIRE--ADRMGIASVFQGQEFCD 81
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKARRRIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLFLGKEINQIgirDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:cd03258 96 SRTVFENVALPLEIAGV---PKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1626716271 162 VMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03258 173 PETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-227 |
5.84e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 113.26 E-value: 5.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT-IPSIREADRmgIASVFQ----GQefCDN 82
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTkLPEYKRAKY--IGRVFQdpmmGT--APS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVASNLFL----GKEINqIGIRDDDSMNSRARSVLKTLSSAI--RVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEP 156
Cdd:COG1101 97 MTIEENLALayrrGKRRG-LRRGLTKKRRELFRELLATLGLGLenRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 157 TAALSVMQSAEVLAYIKRLRSEGR-SVVMVCHDLPDVFAVSDRIVVIRQGhvtgvhrtvetsyeEIIAEIAG 227
Cdd:COG1101 176 TAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHEG--------------RIILDVSG 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
14-207 |
6.49e-30 |
|
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: 111.82 E-value: 6.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 14 LSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipSIREADRmGIASVFQGQEFCDNLDVASNLFLGK 93
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADR-PVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 94 EIN-QIGIRDDDSMNSRARSV-----LKTLSSAirvgspiasLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAE 167
Cdd:cd03298 96 SPGlKLTAEDRQAIEVALARVglaglEKRLPGE---------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1626716271 168 VLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03298 167 MLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-242 |
7.61e-30 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 116.75 E-value: 7.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQGQEFCDN 82
Cdd:PRK10982 8 FPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVASNLFLGKEINQIGIRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:PRK10982 88 RSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 163 MQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAGVTTEHEYEEIAENPK 242
Cdd:PRK10982 168 KEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVGRSLTQRFPDKENKPG 247
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-208 |
1.21e-29 |
|
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: 111.13 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQeVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTI--PSIREA-----DRMGIASVFQGQEFC 80
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKqpQKLRRRigylpQEFGVYPNFTVREFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVAsnlflgKEINQIGIRdddsmnSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:cd03264 94 DYIAWL------KGIPSKEVK------ARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 161 SVMQSAEVLAYIKRLrSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVT 208
Cdd:cd03264 162 DPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3-208 |
1.37e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 114.94 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMgIASVFQGQEFCDN 82
Cdd:PRK09536 13 FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVASNLFLGKEINQIGIRDDDSMNSRA-RSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:PRK09536 92 FDVRQVVEMGRTPHRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1626716271 162 VMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVT 208
Cdd:PRK09536 172 INHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
9-202 |
1.40e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 110.65 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGF---GHIYLNGEQVT-IPSirEADRMGIasVFQGQEFCDNLD 84
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTaLPA--EQRRIGI--LFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 85 VASNLflgkeinQIGIRDDDSMNSRARSVLKTLSSAIRVG---SPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:COG4136 93 VGENL-------AFALPPTIGRAQRRARVEQALEEAGLAGfadRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1626716271 162 VMQSAEVLAYI-KRLRSEGRSVVMVCHDLPDVFAVSdRIVVI 202
Cdd:COG4136 166 AALRAQFREFVfEQIRQRGIPALLVTHDEEDAPAAG-RVLDL 206
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-208 |
1.66e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.42 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMgIASVFQgqefcdNLDvas 87
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ-VGMVFQ------NPD--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NLFLGKEinqigIRDD------------DSMNSRARSVLKtlssaiRVG-------SPiASLSVGQRQTVAIARTLLNDP 148
Cdd:PRK13635 92 NQFVGAT-----VQDDvafglenigvprEEMVERVDQALR------QVGmedflnrEP-HRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 149 QLILLDEPTAALSVMQSAEVLAYIKRLRSEGR-SVVMVCHDLPDVfAVSDRIVVIRQGHVT 208
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEA-AQADRVIVMNKGEIL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-201 |
1.78e-29 |
|
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: 113.22 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGF---GHIYLNGEQVTIPSIREADRM---GIASVFQ-- 75
Cdd:COG0444 16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKIrgrEIQMIFQdp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 76 ----------GQEFCDNLDVAsnlflgkeinqiGIRDDDSMNSRARSVLKtlssaiRVGSPIAS---------LSVGQRQ 136
Cdd:COG0444 96 mtslnpvmtvGDQIAEPLRIH------------GGLSKAEARERAIELLE------RVGLPDPErrldrypheLSGGMRQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 137 TVAIARTLLNDPQLILLDEPTAALSV-MQsAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVV 201
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVtIQ-AQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAV 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
9-205 |
2.69e-29 |
|
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: 110.63 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSireADRMgiaSVFQGQEFCDNLDVASN 88
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG---PDRM---VVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LFLGKEinqiGIRDDDSMNSRARSVLKTLSsaiRVG------SPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:TIGR01184 75 IALAVD----RVLPDLSKSERRAIVEEHIA---LVGlteaadKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1626716271 163 MQSAEVLAYIKRLRSEGR-SVVMVCHDLPDVFAVSDRIVVIRQG 205
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-208 |
3.23e-29 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 110.31 E-value: 3.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT-IPSIREAdRMGIASVFQGQEFCDNLDV 85
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITkLPPHERA-RAGIAYVPQGREIFPRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGkeinqigirdddsMNSRARS-------------VLKTLSSaiRVGspiASLSVGQRQTVAIARTLLNDPQLIL 152
Cdd:TIGR03410 93 EENLLTG-------------LAALPRRsrkipdeiyelfpVLKEMLG--RRG---GDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1626716271 153 LDEPTAAL--SVMQsaEVLAYIKRLRSEGR-SVVMVCHDLPDVFAVSDRIVVIRQGHVT 208
Cdd:TIGR03410 155 LDEPTEGIqpSIIK--DIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVV 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-208 |
3.71e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.11 E-value: 3.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSireADRmgiASVFQGQEFCDNLDV 85
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG---ADR---GVVFQKDALLPWLNV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGKEINQIGIRDddsMNSRARSVLKtlssaiRVG------SPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAA 159
Cdd:COG4525 94 LDNVAFGLRLRGVPKAE---RRARAEELLA------LVGladfarRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 160 LSVMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVI--RQGHVT 208
Cdd:COG4525 165 LDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIV 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-209 |
3.78e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 115.65 E-value: 3.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNG---EQVTIPSIREAdrmgIASVFQgqefcD-- 81
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdiRDLTLESLRRQ----IGVVPQ-----Dtf 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 --NLDVASNLFLGKEinqiGIRDDDSMN----SRARSVLKTLSSAI--RVGSPIASLSVGQRQTVAIARTLLNDPQLILL 153
Cdd:COG1132 425 lfSGTIRENIRYGRP----DATDEEVEEaakaAQAHEFIEALPDGYdtVVGERGVNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 154 DEPTAALSVMQSAEVLAYIKRLRsEGRSVVMVCHDLPDVfAVSDRIVVIRQGHVTG 209
Cdd:COG1132 501 DEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTI-RNADRILVLDDGRIVE 554
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-207 |
4.42e-29 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 109.80 E-value: 4.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT------IPSIREadRMGIasVFQGQEF 79
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgraIPYLRR--KIGV--VFQDFRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 CDNLDVASNLFLGKEINQIGIRDddsMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAA 159
Cdd:cd03292 90 LPDRNVYENVAFALEVTGVPPRE---IRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 160 LSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
24-220 |
4.49e-29 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 112.20 E-value: 4.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 24 IVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIpsiREADRMGIASVFQGQEFCDNLDVASNLFLGKEINQIgirDD 103
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN---VPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKV---PR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 104 DSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL-----SVMQSaEVLAYIKRLrse 178
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALdkklrDQMQL-ELKTIQEQL--- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1626716271 179 GRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHrTVETSYEE 220
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIG-TPEEIYEE 191
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-207 |
4.69e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 113.12 E-value: 4.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT-IPsireADRMGIASVFQGQEFCD 81
Cdd:PRK09452 24 FDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThVP----AENRHVNTVFQSYALFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLFLGKEINQIGirdDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:PRK09452 100 HMTVFENVAFGLRMQKTP---AAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 162 V-----MQSAevlayIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK09452 177 YklrkqMQNE-----LKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-207 |
6.54e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 110.87 E-value: 6.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIpSIRE--ADRMGIASVFQGQE----FC 80
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY-SKRGllALRQQVATVFQDPEqqifYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 D-NLDVASNLF-LGKEINQIGIRDDDSMnsrarsvlkTLSSAIRV-GSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:PRK13638 94 DiDSDIAFSLRnLGVPEAEITRRVDEAL---------TLVDAQHFrHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-215 |
7.59e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 110.15 E-value: 7.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIyLNGeQVTIPSIREADRMgiasVFQGqefcd 81
Cdd:PRK11247 21 RYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG-TAPLAEAREDTRL----MFQD----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 nldvASNLFLGKEINQIGIRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:PRK11247 90 ----ARLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 162 VMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVtGVHRTVE 215
Cdd:PRK11247 166 ALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI-GLDLTVD 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-207 |
9.00e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 114.82 E-value: 9.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVtipSIREAD------RMGIASVFQGQEF 79
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV---ATLDADalaqlrREHFGFIFQRYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 CDNLDVASN-----LFLGKEINQigirdddsMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:PRK10535 98 LSHLTAAQNvevpaVYAGLERKQ--------RLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 155 EPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDlPDVFAVSDRIVVIRQGHV 207
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-207 |
1.17e-28 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 108.78 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGI------ASVFQ 75
Cdd:cd03218 9 RYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIgylpqeASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 76 GqefcdnLDVASNLFLGKEINQIgirDDDSMNSRARSVLKTLS-SAIRvGSPIASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:cd03218 89 K------LTVEENILAVLEIRGL---SKKEREEKLEELLEEFHiTHLR-KSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 155 EPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
7-207 |
2.54e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.37 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAD-RMGIASVFQGQE---FCDN 82
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDiRKKVGLVFQYPEyqlFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 L--DVA---SNLFLGKEinQIGIRDDDSMNsrarsVLKTLSSAIRVGSPIaSLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:PRK13637 101 IekDIAfgpINLGLSEE--EIENRVKRAMN-----IVGLDYEDYKDKSPF-ELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
13-207 |
6.12e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 106.98 E-value: 6.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 13 NLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGE--QVTIPSIREadrmgIASVFQGQEFCDNLDVASNLF 90
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRP-----VSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 91 LGkeINQiGIRdddsMNSRARSVLKTLSSAIRVGSPI----ASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSA 166
Cdd:PRK10771 94 LG--LNP-GLK----LNAAQREKLHAIARQMGIEDLLarlpGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1626716271 167 EVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK10771 167 EMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-207 |
8.00e-28 |
|
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: 104.99 E-value: 8.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqVTIPSIREAD-RMGIASVFQgqefcdnlDVas 87
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG--ADISQWDPNElGDHVGYLPQ--------DD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NLFLGkeinqigirdddsmnsrarsvlkTLSSAIrvgspiasLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAE 167
Cdd:cd03246 86 ELFSG-----------------------SIAENI--------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1626716271 168 VLAYIKRLRSEGRSVVMVCHDlPDVFAVSDRIVVIRQGHV 207
Cdd:cd03246 135 LNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
2-210 |
1.93e-27 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 108.79 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPS---IREADRMGIASVFQGQE 78
Cdd:TIGR01186 2 KTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSpveLREVRRKKIGMVFQQFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 79 FCDNLDVASNLFLGKEINQIgirDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTA 158
Cdd:TIGR01186 82 LFPHMTILQNTSLGPELLGW---PEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 159 ALSVMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGV 210
Cdd:TIGR01186 159 ALDPLIRDSMQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQV 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-212 |
2.06e-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: 105.77 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNG---EQVTIPSIREadrmGIASVFQgQEFCDNLD 84
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDISRKSLRS----MIGVVLQ-DTFLFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 85 VASNLFLGKEINqigiRDDDSMNS----RARSVLKTLSSAIR--VGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTA 158
Cdd:cd03254 93 IMENIRLGRPNA----TDEEVIEAakeaGAHDFIMKLPNGYDtvLGENGGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 159 ALSVMQSAEVLAYIKRLRsEGRSVVMVCHDLPDVfAVSDRIVVIRQGHV--TGVHR 212
Cdd:cd03254 169 NIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTI-KNADKILVLDDGKIieEGTHD 222
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
6-188 |
2.07e-27 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 104.43 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQV--TIPSIREAdRMGIASVFQGQEfcDNL 83
Cdd:TIGR01166 5 PEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdySRKGLLER-RQRVGLVFQDPD--DQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 ---DVASNLFLGKEinQIGIRDDDsMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:TIGR01166 82 faaDVDQDVAFGPL--NLGLSEAE-VERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180
....*....|....*....|....*...
gi 1626716271 161 SVMQSAEVLAYIKRLRSEGRSVVMVCHD 188
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-205 |
2.44e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 105.06 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 1 MKFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIpsireADRMGIASVFQGQEFC 80
Cdd:cd03269 8 KRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-----AARNRIGYLPEERGLY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLFLGKEINQIGIRDddsMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:cd03269 83 PKMKVIDQLVYLAQLKGLKKEE---ARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1626716271 161 SVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQG 205
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-207 |
2.61e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.97 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGE---------------------QVTIP-SIREAD 66
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRplaawspwelarrravlpqhsSLAFPfTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 67 RMGIASVFQGQEfcdnldvasnlflgkeinqigiRDDDsmnsRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLL- 145
Cdd:COG4559 97 ALGRAPHGSSAA----------------------QDRQ----IVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAq 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 146 ------NDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-207 |
5.21e-27 |
|
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: 105.42 E-value: 5.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPS---IREADRMGIASVFQGQE 78
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 79 FCDNLDVASNLFLGKEINQIG--IRDddsmnSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEP 156
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPraERE-----ERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 157 TAALSV-----MQSaEVLayikRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03294 188 FSALDPlirreMQD-ELL----RLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-207 |
5.36e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 106.71 E-value: 5.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEqvtIPSIREAD-RMGIASVFqGQE---FCD 81
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY---VPFKRRKEfARRIGVVF-GQRsqlWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 nLDVASNLFLGKEINQIGirdddsmNSRARSVLKTLSSAIRVGS----PIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:COG4586 111 -LPAIDSFRLLKAIYRIP-------DAEYKKRLDELVELLDLGElldtPVRQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 158 AALSVMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-208 |
3.24e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.86 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAD-RMGIASVFQGQEFC 80
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiRQEAGMVFQQFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLFLGKeINQIGIRDDDSmNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:PRK09493 90 PHLTALENVMFGP-LRVRGASKEEA-EKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1626716271 161 SVMQSAEVLAYIKRLRSEGRSVVMVCHDLPdvFA--VSDRIVVIRQGHVT 208
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEEGMTMVIVTHEIG--FAekVASRLIFIDKGRIA 215
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
8-202 |
3.84e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.16 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPgfghiylngeqvTIPSIREADRMGIASVFQGQEFCDNLdvas 87
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP------------TSGTVRRAGGARVAYVPQRSEVPDSL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 nlflgkeinQIGIRDDDSMNS-RARSVLKTLSSAIRV---------------GSPIASLSVGQRQTVAIARTLLNDPQLI 151
Cdd:NF040873 71 ---------PLTVRDLVAMGRwARRGLWRRLTRDDRAavddalervgladlaGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 152 LLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVfAVSDRIVVI 202
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-210 |
5.01e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 104.78 E-value: 5.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAdRMGIasVFQGQEFCDN 82
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR-KVGF--VFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVASNLFLGkeINQIGIRDDDSMNSRARSVLKTLSS------AIRVgsPiASLSVGQRQTVAIARTLLNDPQLILLDEP 156
Cdd:PRK10851 89 MTVFDNIAFG--LTVLPRRERPNAAAIKAKVTQLLEMvqlahlADRY--P-AQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 157 TAALSVMQSAEVLAYIKRLRSEGR-SVVMVCHDLPDVFAVSDRIVVIRQGHVTGV 210
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQA 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-205 |
5.46e-26 |
|
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: 101.43 E-value: 5.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipSIREADRMGIASVFQGQEFCD 81
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR--TDRKAARQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLFLGKEINqiGIRDDDsMNSRARSVLKTLSSAIRVGSPIASLSVGQRQ--TVAIArtLLNDPQLILLDEPTAA 159
Cdd:cd03263 89 ELTVREHLRFYARLK--GLPKSE-IKEEVELLLRVLGLTDKANKRARTLSGGMKRklSLAIA--LIGGPSVLLLDEPTSG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1626716271 160 LSVMQSAEVLAYIKRLRSeGRSVVMVCHDLPDVFAVSDRIVVIRQG 205
Cdd:cd03263 164 LDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-215 |
6.73e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.34 E-value: 6.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipSIREADRmGIASVFQGQEFCDN 82
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAER-GVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVASNLFLGKEINQIGIRDddsMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEP----TA 158
Cdd:PRK11000 90 LSVAENMSFGLKLAGAKKEE---INQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPlsnlDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 159 ALSVMQSAEVLAYIKRLrseGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVE 215
Cdd:PRK11000 167 ALRVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
7-207 |
7.08e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.00 E-value: 7.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT-----IPSIREAdrmgIASVFQGQefcD 81
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkgLMKLRES----VGMVFQDP---D 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLFLGKEINQIGIR-DDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:PRK13636 93 NQLFSASVYQDVSFGAVNLKlPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 161 SVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
12-209 |
1.51e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 105.01 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 12 VNLSIQRQEVIAIVGDNGAGKSTLIKVIAGfLQPGF--GHIYLNGEQVTIPSIREADRMGIASVFQGQE---FCDNLDVA 86
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKrdgIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 87 SNLFLG--KEINQIGIRDDDSMNSRARSVLKTLSsaIRVGSP---IASLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:PRK13549 360 KNITLAalDRFTGGSRIDDAAELKTILESIQRLK--VKTASPelaIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 162 VMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTG 209
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKG 485
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-216 |
1.70e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.14 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 1 MKFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKV----IAGFLQPGF-GHIYLNGEQVTIPSIREADRMgIASVFQ 75
Cdd:PRK14247 11 VSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlIELYPEARVsGEVYLDGQDIFKMDVIELRRR-VQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 76 GQEFCDNLDVASNLFLGKEINQIgIRDDDSMNSRARSVLKT--LSSAI--RVGSPIASLSVGQRQTVAIARTLLNDPQLI 151
Cdd:PRK14247 90 IPNPIPNLSIFENVALGLKLNRL-VKSKKELQERVRWALEKaqLWDEVkdRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 152 LLDEPTAALSVMQSAEVLAYIKRLRSEgRSVVMVCHDLPDVFAVSDRIVVIRQGHV--TGVHRTVET 216
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIveWGPTREVFT 234
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
21-228 |
2.45e-25 |
|
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: 100.66 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 21 VIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMgIASVFQGQEFCDNLDVASNLFLGKeINQIGI 100
Cdd:TIGR03873 29 LTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARR-VALVEQDSDTAVPLTVRDVVALGR-IPHRSL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 101 -----RDDDSMNSRARSVLKTLSSAIRvgsPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRL 175
Cdd:TIGR03873 107 wagdsPHDAAVVDRALARTELSHLADR---DMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVREL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 176 RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAGV 228
Cdd:TIGR03873 184 AATGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIRAVYGV 236
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
9-207 |
2.46e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.62 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIRE-ADRMGIasvfqgqefcdnLDVAS 87
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARRRAV------------LPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NL---FLGKEINQIGIRDDDSMNSRARSVlktLSSAIRV-------GSPIASLSVGQRQTVAIARTLL------NDPQLI 151
Cdd:PRK13548 86 SLsfpFTVEEVVAMGRAPHGLSRAEDDAL---VAAALAQvdlahlaGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 152 LLDEPTAALSVMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
8-223 |
2.57e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.64 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLnGEQVTIPSIREAD----RMGIASVFQGQEfcdnl 83
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKlkplRKKVGIVFQFPE----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 dvaSNLF---LGKEI----NQIGIRDDDSMnSRARSVLKT--LSSAIRVGSPIAsLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:PRK13634 96 ---HQLFeetVEKDIcfgpMNFGVSEEDAK-QKAREMIELvgLPEELLARSPFE-LSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 155 EPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV--TGVHRTVETSYEEIIA 223
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVflQGTPREIFADPDELEA 242
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-201 |
2.85e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.54 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSireADRmgiASVFQGQEFCDNLDVAS 87
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG---AER---GVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NLFLGKEINQIGirdDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVM---Q 164
Cdd:PRK11248 90 NVAFGLQLAGVE---KMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFtreQ 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 1626716271 165 SAEVLayIKRLRSEGRSVVMVCHDLPD-VFAVSDRIVV 201
Cdd:PRK11248 167 MQTLL--LKLWQETGKQVLLITHDIEEaVFMATELVLL 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-207 |
3.85e-25 |
|
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: 99.37 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipsiREAD--RMGIASVFQGQEF 79
Cdd:cd03265 9 KYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPRevRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 CDNLDVASNLFLGKEINQIGirdDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAA 159
Cdd:cd03265 85 DDELTGWENLYIHARLYGVP---GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1626716271 160 LSVMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03265 162 LDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
7-207 |
4.40e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 100.62 E-value: 4.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT-------IPSIREadRMGIasVFQ---G 76
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkyIRPVRK--RIGM--VFQfpeS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 77 QEFCDNLDvASNLFLGKEINQigirDDDSMNSRARSVLKTL--SSAIRVGSPIaSLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:PRK13646 97 QLFEDTVE-REIIFGPKNFKM----NLDEVKNYAHRLLMDLgfSRDVMSQSPF-QMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 155 EPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-209 |
8.14e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.88 E-value: 8.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAdRMGIASVFQG---QEFC 80
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV-RKFVGLVFQNpddQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNL--DVA---SNLFLgkeinqigirDDDSMNSRARSVLKTLS-SAIRVGSPiASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:PRK13652 94 PTVeqDIAfgpINLGL----------DEETVAHRVSSALHMLGlEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 155 EPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHVTG 209
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-207 |
9.87e-25 |
|
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: 98.91 E-value: 9.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEqvtipSIREAD----RMGIASVFQGQEFCDNL 83
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE-----DIREQDpvelRRKIGYVIQQIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 DVASNLFLGKEINQIG---IRDddsmnsRARSVLKTlssairVGSPIAS--------LSVGQRQTVAIARTLLNDPQLIL 152
Cdd:cd03295 91 TVEENIALVPKLLKWPkekIRE------RADELLAL------VGLDPAEfadrypheLSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 153 LDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-207 |
1.01e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.42 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAdRMGIASVFQG---QEFCDNL 83
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV-RSKVGLVFQDpddQVFSSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 --DVA---SNLFLGKeinqigirddDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTA 158
Cdd:PRK13647 98 wdDVAfgpVNMGLDK----------DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1626716271 159 ALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK13647 168 YLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
8-226 |
1.04e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 99.29 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAdRMGIASVFQgqefcdNLDvas 87
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI-RKKIGIIFQ------NPD--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NLFLGkeinqIGIRDDDSM---NSR-ARSVLKT--LSSAIRVG-------SPiASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:PRK13632 94 NQFIG-----ATVEDDIAFgleNKKvPPKKMKDiiDDLAKKVGmedyldkEP-QNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 155 EPTAALSVMQSAEVLAYIKRLRSEG-RSVVMVCHDLPDVFaVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIA 226
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILEKA 239
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-223 |
1.24e-24 |
|
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: 102.21 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 12 VNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGF-GHIYLNGEQVTIPSIREADRMGIASVFQGQE---FCDNLDVAS 87
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFeGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NLFLG--KEINQIGIRDDDSMNSRARSVLKTLSsaIRVGSP---IASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:TIGR02633 359 NITLSvlKSFCFKMRIDAAAELQIIGSAIQRLK--VKTASPflpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 163 MQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIA 223
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVLA 497
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-207 |
1.27e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.54 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipSIREAD----RMGIASVFQGqefcD 81
Cdd:COG1135 18 VTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLT--ALSERElraaRRKIGMIFQH----F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NL----DVASNLFLGKEINQIgirDDDSMNSRARSVLKtlssaiRVG-------SPiASLSVGQRQTVAIARTLLNDPQL 150
Cdd:COG1135 92 NLlssrTVAENVALPLEIAGV---PKAEIRKRVAELLE------LVGlsdkadaYP-SQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 151 ILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-224 |
1.57e-24 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 98.07 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGF---VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGE---QVTIPSIREAdrmgIASVFQ 75
Cdd:cd03253 7 TFAYdpgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirEVTLDSLRRA----IGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 76 gqefcD----NLDVASNLFLGK---------EINQIGIRDDDSMNSRArsvlktlSSAIRVGSPIASLSVGQRQTVAIAR 142
Cdd:cd03253 83 -----DtvlfNDTIGYNIRYGRpdatdeeviEAAKAAQIHDKIMRFPD-------GYDTIVGERGLKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 143 TLLNDPQLILLDEPTAALSVMQSAEVLAYIKRLrSEGRSVVMVCHDLPDVfAVSDRIVVIRQGHVtgvhrtVET-SYEEI 221
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTI-VNADKIIVLKDGRI------VERgTHEEL 222
|
...
gi 1626716271 222 IAE 224
Cdd:cd03253 223 LAK 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-222 |
2.06e-24 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 101.73 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQGQE---FCDNLD 84
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 85 VASNLFLG---KEINQIGIRDDDSMNSRARSVLktlsSAIRVGSP-----IASLSVGQRQTVAIARTLLNDPQLILLDEP 156
Cdd:PRK10982 343 IGFNSLISnirNYKNKVGLLDNSRMKSDTQWVI----DSMRVKTPghrtqIGSLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 157 TAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEII 222
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEIL 484
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-209 |
2.13e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.53 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 12 VNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIA---------SVFQGQEFCDN 82
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMlcpedrkaeGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVAS---NLFLGKEINqiGIRDDDSMNSRARSV-LKTLSSAirvgSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTA 158
Cdd:PRK11288 352 INISArrhHLRAGCLIN--NRWEAENADRFIRSLnIKTPSRE----QLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 159 ALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTG 209
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAG 476
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-251 |
3.07e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.91 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT-IPSIREADRMgiasVFQGQEFCDNLDVA 86
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLShVPPYQRPINM----MFQSYALFPHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 87 SNLFLGKEINQIGirdDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV---- 162
Cdd:PRK11607 110 QNIAFGLKQDKLP---KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrd 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 163 -MQsAEVLAYIKRLrseGRSVVMVCHDLPDVFAVSDRIVVIRQGhvtgvhRTVETSYEEIIAEIAgvTTEHEYEEIAENP 241
Cdd:PRK11607 187 rMQ-LEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRG------KFVQIGEPEEIYEHP--TTRYSAEFIGSVN 254
|
250
....*....|
gi 1626716271 242 KFDSMVRQRK 251
Cdd:PRK11607 255 VFEGVLKERQ 264
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-207 |
4.35e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 97.35 E-value: 4.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIpsIREAD--------------R 67
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINL--VRDKDgqlkvadknqlrllR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 68 MGIASVFQGQEFCDNLDVASNLfLGKEINQIGIRDDDSMNSRARSVLKT-LSSAIRVGSPIaSLSVGQRQTVAIARTLLN 146
Cdd:PRK10619 92 TRLTMVFQHFNLWSHMTVLENV-MEAPIQVLGLSKQEARERAVKYLAKVgIDERAQGKYPV-HLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 147 DPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-239 |
5.19e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 98.26 E-value: 5.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTiPSIReaDRMGiasvfqgqefcd 81
Cdd:COG4152 10 RFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-PEDR--RRIG------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 nldvasnlFLGKE---------INQI-------GIRDDDSMnSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLL 145
Cdd:COG4152 75 --------YLPEErglypkmkvGEQLvylarlkGLSKAEAK-RRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 146 NDPQLILLDEPTAALSVMqSAEVLA-YIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV-----------TGVHRT 213
Cdd:COG4152 146 HDPELLILDEPFSGLDPV-NVELLKdVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKvlsgsvdeirrQFGRNT 224
|
250 260
....*....|....*....|....*....
gi 1626716271 214 VETSYE---EIIAEIAGVTTEHEYEEIAE 239
Cdd:COG4152 225 LRLEADgdaGWLRALPGVTVVEEDGDGAE 253
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
9-207 |
6.10e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.49 E-value: 6.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAdRMGIASVFQgqefcdNLDvasN 88
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI-RHKIGMVFQ------NPD---N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LFLGKEI---------NQiGIrDDDSMNSRARSVLKTLS-SAIRVGSPiASLSVGQRQTVAIARTLLNDPQLILLDEPTA 158
Cdd:PRK13650 93 QFVGATVeddvafgleNK-GI-PHEEMKERVNEALELVGmQDFKEREP-ARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1626716271 159 ALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVfAVSDRIVVIRQGHV 207
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2-207 |
7.49e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 96.74 E-value: 7.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIY-----------LNGEQVTIPSIREAdrmgI 70
Cdd:PRK11264 12 KFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarsLSQQKGLIRQLRQH----V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 71 ASVFQGQEFCDNLDVASNLFLGKEINQIGIRDDDSmnSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQL 150
Cdd:PRK11264 88 GFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEAT--ARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 151 ILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-249 |
7.60e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.25 E-value: 7.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT-IPSIREAdRMGI------ASVFQGqefcd 81
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIThLPMHKRA-RLGIgylpqeASIFRK----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 nLDVASNLFLgkeINQIGIRDDDSMNSRARSVLKTLS-SAIRvGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAA- 159
Cdd:COG1137 93 -LTVEDNILA---VLELRKLSKKEREERLEELLEEFGiTHLR-KSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGv 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 160 --LSVmqsAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGhvtgvhrtvetsyeEIIAEiaGVTteheyEEI 237
Cdd:COG1137 168 dpIAV---ADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEG--------------KVLAE--GTP-----EEI 223
|
250
....*....|..
gi 1626716271 238 AENPKfdsmVRQ 249
Cdd:COG1137 224 LNNPL----VRK 231
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
9-208 |
1.13e-23 |
|
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: 99.82 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqvtipsireadrmgiASVFQ--GQEFCDNL--- 83
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG----------------ADLSQwdREELGRHIgyl 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 --DVAsnLFLG--KE-INQIGIRDDDSMNSRARS------VLK------TlssaiRVGSPIASLSVGQRQTVAIARTLLN 146
Cdd:COG4618 412 pqDVE--LFDGtiAEnIARFGDADPEKVVAAAKLagvhemILRlpdgydT-----RIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 147 DPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDlPDVFAVSDRIVVIRQGHVT 208
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHR-PSLLAAVDKLLVLRDGRVQ 545
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-212 |
1.35e-23 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 95.68 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGE---QVTIPSIReaDRMGIASvfqgQE---F 79
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirDLNLRWLR--SQIGLVS----QEpvlF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 cdNLDVASNLFLGKEinqigiRDDDSMNSRArSVLKTLSSAI---------RVGSPIASLSVGQRQTVAIARTLLNDPQL 150
Cdd:cd03249 90 --DGTIAENIRYGKP------DATDEEVEEA-AKKANIHDFImslpdgydtLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 151 ILLDEPTAALSVMQSAEVLAYIKRLRsEGRSVVMVCHDLPDVFAvSDRIVVIRQGHV--TGVHR 212
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVveQGTHD 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-222 |
1.59e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.09 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 10 KSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQGQE---FCDNLDVA 86
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 87 SNLFLGKEINQIGI---------RDDDSMNSRARSVLKTLSSAIRvgSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:PRK09700 360 QNMAISRSLKDGGYkgamglfheVDEQRTAENQRELLALKCHSVN--QNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEII 222
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEI 502
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-208 |
2.07e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.98 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLnGEQVTIpsireadrmgiaSVF-QGQEfcdNLDVAS 87
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKI------------GYFdQHQE---ELDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NLFlgKEINQIGirdDDSMNSRARSVLKT-LSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSvMQSA 166
Cdd:COG0488 395 TVL--DELRDGA---PGGTEQEVRGYLGRfLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD-IETL 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1626716271 167 EVL-----AYikrlrsEGrSVVMVCHD--LPDvfAVSDRIVVIRQGHVT 208
Cdd:COG0488 469 EALeealdDF------PG-TVLLVSHDryFLD--RVATRILEFEDGGVR 508
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
12-208 |
3.31e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.87 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 12 VNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNG-------EQVTIPsireADRMGIASVFQGQEFCDNLD 84
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLP----PEKRRIGYVFQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 85 VASNLflgkeinQIGIRDddSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQ 164
Cdd:PRK11144 93 VRGNL-------RYGMAK--SMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1626716271 165 SAEVLAYIKRLRSEGR-SVVMVCHDLPDVFAVSDRIVVIRQGHVT 208
Cdd:PRK11144 164 KRELLPYLERLAREINiPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-189 |
3.74e-23 |
|
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: 98.20 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipSIREADRMGIASVFQGQEFCDNLDVA 86
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS--SLDQDEVRRRVSVCAQDAHLFDTTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 87 SNLFLGKEinqiGIRDDDSMNSRARSVLKTLSSAI------RVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:TIGR02868 427 ENLRLARP----DATDEELWAALERVGLADWLRALpdgldtVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*....
gi 1626716271 161 SVMQSAEVLAYIkRLRSEGRSVVMVCHDL 189
Cdd:TIGR02868 503 DAETADELLEDL-LAALSGRTVVLITHHL 530
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-235 |
3.78e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 98.15 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQ---GQEFCDNLDV 85
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEdrkRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLG--KEINQIGIRDDDSMNSRARSVLKTLSSaIRVGS---PIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:PRK10762 348 KENMSLTalRYFSRAGGSLKHADEQQAVSDFIRLFN-IKTPSmeqAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 161 SVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAGVTTEHEYE 235
Cdd:PRK10762 427 DVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQEKLMAAAVGKLNRVNQE 501
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
9-243 |
3.82e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.08 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMgIASVFQGQEFCDNLDVASN 88
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LALLPQHHLTPEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LFLGKE--INQIG--IRDDDSMNSRARSVLKTLSSAIRvgsPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQ 164
Cdd:PRK11231 97 VAYGRSpwLSLWGrlSAEDNARVNQAMEQTRINHLADR---RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1626716271 165 SAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAGVTTEHEYEEIAENPKF 243
Cdd:PRK11231 174 QVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAEIHPEPVSGTPMC 252
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
9-207 |
4.00e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 93.38 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPG--FGHIYLNGEQVTIPSIREAdrmgIASVFQGQEFCDNLDVA 86
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFRKI----IGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 87 SNLFLgkeinqigirdddsmnsrarsvlktlSSAIRvgspiaSLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSA 166
Cdd:cd03213 101 ETLMF--------------------------AAKLR------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1626716271 167 EVLAYIKRLRSEGRSVVMVCHDLP-DVFAVSDRIVVIRQGHV 207
Cdd:cd03213 149 QVMSLLRRLADTGRTIICSIHQPSsEIFELFDKLLLLSQGRV 190
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-208 |
4.29e-23 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 92.76 E-value: 4.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVtipSIREADRMGIASVFQGQEFcdnldvas 87
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV---SDLEKALSSLISVLNQRPY-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 nLFLGKEINQIGIRdddsmnsrarsvlktlssairvgspiasLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAE 167
Cdd:cd03247 86 -LFDTTLRNNLGRR----------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1626716271 168 VLAYIKRLrSEGRSVVMVCHDLPDVFAVsDRIVVIRQGHVT 208
Cdd:cd03247 137 LLSLIFEV-LKDKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-224 |
5.05e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.99 E-value: 5.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLqPGFGHIYLNGEQvtipsIREAD----RMGIASVfqGQE---FCD 81
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIE-----LRELDpeswRKHLSWV--GQNpqlPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLdvASNLFLGKeinqIGIRDDDSMNSRARSVLKTLSSAIRVG--SPI----ASLSVGQRQTVAIARTLLNDPQLILLDE 155
Cdd:PRK11174 438 TL--RDNVLLGN----PDASDEQLQQALENAWVSEFLPLLPQGldTPIgdqaAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 156 PTAALSvMQSAE-VLAYIKRLrSEGRSVVMVCHDLPDVFAVsDRIVVIRQGhvtgvhRTVET-SYEEIIAE 224
Cdd:PRK11174 512 PTASLD-AHSEQlVMQALNAA-SRRQTTLMVTHQLEDLAQW-DQIWVMQDG------QIVQQgDYAELSQA 573
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
14-202 |
6.67e-23 |
|
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: 93.38 E-value: 6.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 14 LSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQvtipsiREADRMGIASVFQGQEFCDN--LDVASNLFL 91
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS------PGKGWRHIGYVPQRHEFAWDfpISVAHTVMS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 92 GKEiNQIG-IRDDDSMNSRA-RSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSvMQSAEVL 169
Cdd:TIGR03771 75 GRT-GHIGwLRRPCVADFAAvRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLD-MPTQELL 152
|
170 180 190
....*....|....*....|....*....|....
gi 1626716271 170 AYI-KRLRSEGRSVVMVCHDLPDVFAVSDRIVVI 202
Cdd:TIGR03771 153 TELfIELAGAGTAILMTTHDLAQAMATCDRVVLL 186
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-207 |
8.13e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.67 E-value: 8.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQGQE--FCDNlDV 85
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPEtqFVGR-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGKE---INQIGIRdddsmNSRARSVLKTLSSAIRVGSPiASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:PRK13644 96 EEDLAFGPEnlcLPPIEIR-----KRVDRALAEIGLEKYRHRSP-KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1626716271 163 MQSAEVLAYIKRLRSEGRSVVMVCHDLPDVfAVSDRIVVIRQGHV 207
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKI 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-212 |
8.29e-23 |
|
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: 93.45 E-value: 8.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQV---TIPSIREadRMGIASvfqgQE-FCDNL 83
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdyTLASLRR--QIGLVS----QDvFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 DVASNLFLGKEinqiGIRDDDSM----NSRARSVLKTLSSAI--RVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:cd03251 91 TVAENIAYGRP----GATREEVEeaarAANAHEFIMELPEGYdtVIGERGVKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 158 AALSVMQSAEVLAYIKRLrSEGRSVVMVCHDLPDVfAVSDRIVVIRQGHV--TGVHR 212
Cdd:cd03251 167 SALDTESERLVQAALERL-MKNRTTFVIAHRLSTI-ENADRIVVLEDGKIveRGTHE 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-207 |
9.34e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 9.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQV---TIPSIREAD--RMGIASVFQGQ 77
Cdd:COG4161 12 YGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRllRQKVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 78 EFCDNLDVASNLfLGKEINQIGIRDDDSMnSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:COG4161 92 NLWPHLTVMENL-IEAPCKVLGLSKEQAR-EKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG4161 170 AALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-215 |
1.02e-22 |
|
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: 93.27 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipSIRE-------ADRMGIasVFQG 76
Cdd:COG4181 23 GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF--ALDEdararlrARHVGF--VFQS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 77 QEFCDNLDVASNLFLGKEINqiGIRDDDsmnSRARSVLKtlssaiRVG-------SPiASLSVGQRQTVAIARTLLNDPQ 149
Cdd:COG4181 99 FQLLPTLTALENVMLPLELA--GRRDAR---ARARALLE------RVGlghrldhYP-AQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 150 LILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVfAVSDRIVVIRQGHVTGVHRTVE 215
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAATA 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-208 |
1.22e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.67 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHI---------YLNGEQVTIP--SIREADRMGIASVFQGQ 77
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVsipkglrigYLPQEPPLDDdlTVLDTVLDGDAELRALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 78 EfcdNLDVASNLF---------LGKEINQIGIRDDDSMNSRARSVLKTLS-SAIRVGSPIASLSVGQRQTVAIARTLLND 147
Cdd:COG0488 94 A---ELEELEAKLaepdedlerLAELQEEFEALGGWEAEARAEEILSGLGfPEEDLDRPVSELSGGWRRRVALARALLSE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 148 PQLILLDEPTAALSVmQSAEVLA-YIKRLRSegrSVVMVCHD---LpDvfAVSDRIVVIRQGHVT 208
Cdd:COG0488 171 PDLLLLDEPTNHLDL-ESIEWLEeFLKNYPG---TVLVVSHDryfL-D--RVATRILELDRGKLT 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-207 |
1.52e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.16 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQ------VTIPSIREAdRMGIASVFQG 76
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsktPSDKAIREL-RRNVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 77 QEFCDNLDVASNLfLGKEINQIGIrDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEP 156
Cdd:PRK11124 91 YNLWPHLTVQQNL-IEAPCRVLGL-SKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 157 TAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-207 |
1.61e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.60 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTI--PSIREAdRMGIASVFQG---QEFCD 81
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdkKSLLEV-RKTVGIVFQNpddQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NL--DVA---SNLFLGKEinqigirdddSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEP 156
Cdd:PRK13639 95 TVeeDVAfgpLNLGLSKE----------EVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 157 TAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-207 |
2.56e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 92.25 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQGQEFCDN 82
Cdd:PRK11614 15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVASNLFLGKeinqiGIRDDDSMNSRARSVLKTLSSAI-RVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:PRK11614 95 MTVEENLAMGG-----FFAERDQFQERIKWVYELFPRLHeRRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1626716271 162 VMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK11614 170 PIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-189 |
4.88e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.42 E-value: 4.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQV-TIPSIREAD----RMGIASVFQG--QEF 79
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsKLSSAAKAElrnqKLGFIYQFHHllPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 CDNLDVASNLFLGKeinqigiRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAA 159
Cdd:PRK11629 103 TALENVAMPLLIGK-------KKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190
....*....|....*....|....*....|.
gi 1626716271 160 LSVMQSAEVLAYIKRL-RSEGRSVVMVCHDL 189
Cdd:PRK11629 176 LDARNADSIFQLLGELnRLQGTAFLVVTHDL 206
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-207 |
5.49e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 93.33 E-value: 5.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIRE--ADRMGIASVFQGqeFcdNL 83
Cdd:PRK11153 18 IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARRQIGMIFQH--F--NL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 ----DVASNLFLGKEINqiGIRDDDSmnsRARsVLKTLSsaiRVG-------SPiASLSVGQRQTVAIARTLLNDPQLIL 152
Cdd:PRK11153 94 lssrTVFDNVALPLELA--GTPKAEI---KAR-VTELLE---LVGlsdkadrYP-AQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 153 LDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-207 |
5.56e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.30 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqvTIPSIreadrMGIASVFQGQefcdnLDV 85
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVSAL-----LELGAGFHPE-----LTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGKEINqiGIRDDDsMNSRARSV-------------LKTLSSAIRVgspiaslsvgqRQTVAIARTLlnDPQLIL 152
Cdd:COG1134 106 RENIYLNGRLL--GLSRKE-IDEKFDEIvefaelgdfidqpVKTYSSGMRA-----------RLAFAVATAV--DPDILL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 153 LDEptaALSVMQSA---EVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG1134 170 VDE---VLAVGDAAfqkKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-201 |
6.21e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 92.87 E-value: 6.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRM--GIASVFQgqefcd 81
Cdd:COG4608 29 GVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrRMQMVFQ------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 nlDVASNLFLGKEINQI--------GIRDDDSMNSRARSVLKtlssaiRVGSPIASL-------SVGQRQTVAIARTLLN 146
Cdd:COG4608 103 --DPYASLNPRMTVGDIiaeplrihGLASKAERRERVAELLE------LVGLRPEHAdryphefSGGQRQRIGIARALAL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 147 DPQLILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVV 201
Cdd:COG4608 175 NPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAV 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-212 |
6.21e-22 |
|
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: 94.78 E-value: 6.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqVTIPSIREAD-RMGIASVFQgQEFCDNLD 84
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG--HDLADYTLASlRRQVALVSQ-DVVLFNDT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 85 VASNLFLGK--EINQIGIRDDDSMnSRARSVLKTLSSAIR--VGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:TIGR02203 422 IANNIAYGRteQADRAEIERALAA-AYAQDFVDKLPLGLDtpIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 161 SVMQSAEVLAYIKRLRsEGRSVVMVCHDLPDVfAVSDRIVVIRQGHVT--GVHR 212
Cdd:TIGR02203 501 DNESERLVQAALERLM-QGRTTLVIAHRLSTI-EKADRIVVMDDGRIVerGTHN 552
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-207 |
9.50e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.14 E-value: 9.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHI-YLN--GEQVTIPSIREADRMGIASV---FQG 76
Cdd:PRK11701 16 YGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMrdGQLRDLYALSEAERRRLLRTewgFVH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 77 QEFCDNL--DVASNLFLGKEINQIGIRDDDSMNSRARSVLKTLS-SAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILL 153
Cdd:PRK11701 96 QHPRDGLrmQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEiDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 154 DEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK11701 176 DEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
8-207 |
1.05e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 91.35 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAdRMGIASVFQGQE--FCDNLdV 85
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL-RKHIGIVFQNPDnqFVGSI-V 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGKEINQIgirDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQS 165
Cdd:PRK13648 102 KYDVAFGLENHAV---PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1626716271 166 AEVLAYIKRLRSEGR-SVVMVCHDLPDVfAVSDRIVVIRQGHV 207
Cdd:PRK13648 179 QNLLDLVRKVKSEHNiTIISITHDLSEA-MEADHVIVMNKGTV 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-224 |
1.10e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 90.62 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSiREADRMGIASVFQgqefcdnldva 86
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD-PAWLRRQVGVVLQ----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 87 SNLFLGKEinqigIRDDDSMNSRARSVLKTLSSA--------IR---------VGSPIASLSVGQRQTVAIARTLLNDPQ 149
Cdd:cd03252 84 ENVLFNRS-----IRDNIALADPGMSMERVIEAAklagahdfISelpegydtiVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 150 LILLDEPTAALSVMQSAEVLAYIKRLrSEGRSVVMVCHDLPDVfAVSDRIVVIRQGhvtgvhRTVET-SYEEIIAE 224
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLSTV-KNADRIIVMEKG------RIVEQgSHDELLAE 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-207 |
1.21e-21 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 93.98 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGfLQPGFGHIYLNGEQVTipSIREAD------RMGIasVFQ-- 75
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLD--GLSRRAlrplrrRMQV--VFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 76 ----------GQ---EfcdnldvasnlflGKEINQIGIrDDDSMNSRARSVLKtlssaiRVGSPIASL-------SVGQR 135
Cdd:COG4172 372 fgslsprmtvGQiiaE-------------GLRVHGPGL-SAAERRARVAEALE------EVGLDPAARhryphefSGGQR 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 136 QTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-212 |
2.08e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.55 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAD--RMGIASVFQGQEFCDNLD 84
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 85 VASNLFLGKEINqiGIRDDDsMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQ 164
Cdd:PRK10908 96 VYDNVAIPLIIA--GASGDD-IRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 165 SAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHR 212
Cdd:PRK10908 173 SEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVG 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
7-242 |
2.17e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 90.10 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGF--LQPGF---GHIYLNGEQVTIPSIREAD-RMGIASVFQgqefc 80
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDIYDPDVDVVElRRRVGMVFQ----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 dnldvASNLF---------LGKEINqiGIRDDDSMNSRARSVLKtlSSAI------RVGSPIASLSVGQRQTVAIARTLL 145
Cdd:COG1117 100 -----KPNPFpksiydnvaYGLRLH--GIKSKSELDEIVEESLR--KAALwdevkdRLKKSALGLSGGQQQRLCIARALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 146 NDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEgRSVVMVCHDLPDVFAVSDRIVVIRQGHVtgvhrtVEtsyeeiiaei 225
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL------VE---------- 233
|
250
....*....|....*..
gi 1626716271 226 AGVTteheyEEIAENPK 242
Cdd:COG1117 234 FGPT-----EQIFTNPK 245
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-204 |
2.32e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 90.17 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGhiylngeqvtipSIREADRMGIASVFQGQEFCDN 82
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG------------VIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVASNLFLgkeINQIGIRDDDSMnsrarSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:PRK09544 82 LPLTVNRFL---RLRPGTKKEDIL-----PALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1626716271 163 MQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQ 204
Cdd:PRK09544 154 NGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-207 |
2.84e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.57 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQGQEFCDNLDVASN 88
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRRLSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LFLGKEInqigiRDD---DSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQS 165
Cdd:PRK10895 99 LMAVLQI-----RDDlsaEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1626716271 166 AEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK10895 174 IDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-225 |
3.00e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 92.56 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLN-GEQ---VTIPSIREADR----MGIA---- 71
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvdMTKPGPDGRGRakryIGILhqey 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 72 SVFQGQEFCDNLDVASNLFLGKE---------INQIGIRDDdsmnsRARSVLKTLSSairvgspiaSLSVGQRQTVAIAR 142
Cdd:TIGR03269 375 DLYPHRTVLDNLTEAIGLELPDElarmkavitLKMVGFDEE-----KAEEILDKYPD---------ELSEGERHRVALAQ 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 143 TLLNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTvetsyEEI 221
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP-----EEI 515
|
....
gi 1626716271 222 IAEI 225
Cdd:TIGR03269 516 VEEL 519
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
9-228 |
3.64e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.51 E-value: 3.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLqPGFGHIYLNGEQVTIPSIREADRMGiASVFQGQEFCDNLDVASN 88
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHR-AYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LFLGkeinqigiRDDDSMNSRARSVLKTLSSAIRV----GSPIASLSVGQRQTVAIARTLLN-------DPQLILLDEPT 157
Cdd:COG4138 90 LALH--------QPAGASSEAVEQLLAQLAEALGLedklSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV--TGVHRTVETsyEEIIAEIAGV 228
Cdd:COG4138 162 NSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLvaSGETAEVMT--PENLSEVFGV 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-207 |
4.49e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.93 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADrmgIASVFQGQEFCD 81
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD---ICMVFQSYALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLFLGKEINQIGirdDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:PRK11432 92 HMSLGENVGYGLKMLGVP---KEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1626716271 162 VMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK11432 169 ANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-216 |
5.14e-21 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 92.05 E-value: 5.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKStlikVIA----GFLQPGF----GHIYLNGEQV------TIPSIREADrmg 69
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKS----VTAlsilRLLPDPAahpsGSILFDGQDLlglserELRRIRGNR--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 70 IASVFQgqefcdnlD--VASN-LF-LGKEINQI-----GIRDDDSmnsRARsVLKTLSsaiRVG-----SPIAS----LS 131
Cdd:COG4172 94 IAMIFQ--------EpmTSLNpLHtIGKQIAEVlrlhrGLSGAAA---RAR-ALELLE---RVGipdpeRRLDAyphqLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 132 VGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHVtgv 210
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEI--- 235
|
....*.
gi 1626716271 211 hrtVET 216
Cdd:COG4172 236 ---VEQ 238
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-207 |
6.37e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.02 E-value: 6.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSiREAD---RMGIASVFQgqefc 80
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAD-PEAQkllRQKIQIVFQ----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 dnlDVASNLFLGKEINQI-----GIRDDDSMNSRARSVLKTLSsaiRVGspiasL------------SVGQRQTVAIART 143
Cdd:PRK11308 100 ---NPYGSLNPRKKVGQIleeplLINTSLSAAERREKALAMMA---KVG-----LrpehydryphmfSGGQRQRIAIARA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 144 LLNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
9-187 |
1.42e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.85 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREadrmgiASVFQG-QEFC-DNLDVA 86
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE------ACHYLGhRNAMkPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 87 SNLFLGKEINqigirdddsmNSRARSVLKTLSsaiRVG-SPIA-----SLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:PRK13539 92 ENLEFWAAFL----------GGEELDIAAALE---AVGlAPLAhlpfgYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*..
gi 1626716271 161 SVMQSAEVLAYIKRLRSEGRSVVMVCH 187
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1-207 |
1.52e-20 |
|
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: 87.33 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 1 MKFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPG---FGHIYLNGEQVTIPSIREAdrmgIASVFQGQ 77
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKC----VAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 78 EFCDNLDVA-----SNLFLGKEINQIGIRDddsmnSRARSVLKTLSSAIRVGSP-IASLSVGQRQTVAIARTLLNDPQLI 151
Cdd:cd03234 91 ILLPGLTVRetltyTAILRLPRKSSDAIRK-----KRVEDVLLRDLALTRIGGNlVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 152 LLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHD-LPDVFAVSDRIVVIRQGHV 207
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-207 |
1.84e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 87.76 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQ----PGfGHIYLNGEQVT-----IPSIREAdRMGIASVFQGQ 77
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAG-SHIELLGRTVQregrlARDIRKS-RANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 78 EFCDNLDVASNLFLGKEINQIGIRDDDSMNSRARSvLKTLSSAIRVG------SPIASLSVGQRQTVAIARTLLNDPQLI 151
Cdd:PRK09984 96 NLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQK-QRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 152 LLDEPTAALSVMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-223 |
2.11e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.41 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQ---VTIPSIREAdrmgIASVFQgQEFCDNLD 84
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDirtVTRASLRRN----IAVVFQ-DAGLFNRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 85 VASNLFLGKEinqiGIRDDDSMNSRARS------VLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTA 158
Cdd:PRK13657 425 IEDNIRVGRP----DATDEEMRAAAERAqahdfiERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 159 ALSVMQSAEVLAYIKRLRsEGRSVVMVCHDLPDVfAVSDRIVVIRQGHVtgvhrtVET-SYEEIIA 223
Cdd:PRK13657 501 ALDVETEAKVKAALDELM-KGRTTFIIAHRLSTV-RNADRILVFDNGRV------VESgSFDELVA 558
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-198 |
2.26e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 87.52 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVI--AGFLQPGF---GHIYLNGEQVTIPSIREAD-RMGIASVFQgQEFC 80
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVtitGSIVYNGHNIYSPRTDTVDlRKEIGMVFQ-QPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLFLGKEINqiGIRDDDSMNSRARSVLKtlSSAI------RVGSPIASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:PRK14239 98 FPMSIYENVVYGLRLK--GIKDKQVLDEAVEKSLK--GASIwdevkdRLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1626716271 155 EPTAALSVMQSAEVLAYIKRLRSEgRSVVMVCHDLPDVFAVSDR 198
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDR 216
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
2-207 |
3.09e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.06 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQV-TIPSIREADRMGIasvfqgqefc 80
Cdd:COG4604 10 RYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSRELAKRLAI---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 dnldvasnlfLGKEiNQIGIR---------------------DDDSMNSRArsvLKTLS-SAIRvGSPIASLSVGQRQTV 138
Cdd:COG4604 80 ----------LRQE-NHINSRltvrelvafgrfpyskgrltaEDREIIDEA---IAYLDlEDLA-DRYLDELSGGQRQRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 139 AIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPdvFAV--SDRIVVIRQGHV 207
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDIN--FAScyADHIVAMKDGRV 214
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-228 |
3.34e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 87.35 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 1 MKFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIRE-ADRMGIASvfQGQEF 79
Cdd:PRK10253 15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvARRIGLLA--QNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 CDNLDVASNLFLGKEINQ-IGIR----DDDSMNSRARSVLKTLSSairvGSPIASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:PRK10253 93 PGDITVQELVARGRYPHQpLFTRwrkeDEEAVTKAMQATGITHLA----DQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 155 EPTAALSVMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAGV 228
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGL 243
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-206 |
5.32e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.96 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 12 VNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVtiPSIREADRMGIASVFQgqefCDNLD----VAS 87
Cdd:PRK13536 60 LSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV--PARARLARARIGVVPQ----FDNLDleftVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NLFLGKEINQIGIRDDDSMNSrarSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSvmQSAE 167
Cdd:PRK13536 134 NLLVFGRYFGMSTREIEAVIP---SLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD--PHAR 208
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1626716271 168 VLAYiKRLRS---EGRSVVMVCHDLPDVFAVSDRIVVIRQGH 206
Cdd:PRK13536 209 HLIW-ERLRSllaRGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
8-207 |
5.94e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 86.68 E-value: 5.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNG----EQVTIPSIREADRMgiasVFQGQefcDNL 83
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsDEENLWDIRNKAGM----VFQNP---DNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 DVAS----NLFLGKEinQIGIrDDDSMNSRARSVLKtlssaiRVG------SPIASLSVGQRQTVAIARTLLNDPQLILL 153
Cdd:PRK13633 98 IVATiveeDVAFGPE--NLGI-PPEEIRERVDESLK------KVGmyeyrrHAPHLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 154 DEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVfAVSDRIVVIRQGHV 207
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-210 |
1.02e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.78 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 2 KFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNG---EQVTIPSIREADRMGIASVFQGQE 78
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 79 FCDNLDVASNLFLGKEINQIGI--RDDDSMNSRARSVLKTLSSairvGSPiASLSVGQRQTVAIARTLLNDPQLILLDEP 156
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAeeRREKALDALRQVGLENYAH----SYP-DELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 157 TAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGV 210
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV 246
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
9-207 |
1.07e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.04 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREA---DRMGIASVFQGQEfcdnldv 85
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkkLRKKVSLVFQFPE------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 aSNLFLGKEINQI--GIRD----DDSMNSRARSVLKT--LSSAIRVGSPIaSLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:PRK13641 96 -AQLFENTVLKDVefGPKNfgfsEDEAKEKALKWLKKvgLSEDLISKSPF-ELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
9-207 |
1.47e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.80 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGF---GHIYLNGEQVTIPSIREADrmgiASVFQGQEFCDNLDV 85
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDAKEMRAIS----AYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLflgkeINQIGIRDDDSMNSRAR-----SVLKTLS----SAIRVGSP--IASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:TIGR00955 117 REHL-----MFQAHLRMPRRVTKKEKrervdEVLQALGlrkcANTRIGVPgrVKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 155 EPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDlP--DVFAVSDRIVVIRQGHV 207
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQ-PssELFELFDKIILMAEGRV 245
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
9-228 |
2.74e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.21 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLqPGFGHIYLNGEQVTIPSIREADRMGiASVFQGQEFCDNLDVASN 88
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHR-AYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LFLGkeinqigiRDDDSMNSRARSVLKTLSSAIRV----GSPIASLSVGQRQTVAIARTLL-----NDP--QLILLDEPT 157
Cdd:PRK03695 90 LTLH--------QPDKTRTEAVASALNEVAEALGLddklGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAGV 228
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGV 232
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-225 |
6.33e-19 |
|
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: 82.19 E-value: 6.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFlqPGF----GHIYLNGEQVTIPSIREADRMGIASVFQGQEfcdn 82
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYevteGEILFKGEDITDLPPEERARLGIFLAFQYPP---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 ldvasnlflgkEINqiGIRDDDSMnsraRSVLKTLSSairvgspiaslsvGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:cd03217 88 -----------EIP--GVKNADFL----RYVNEGFSG-------------GEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 163 MQSAEVLAYIKRLRSEGRSVVMVCH--DLPDvFAVSDRIVVIRQGHVtgvhrtVETSYEEIIAEI 225
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHyqRLLD-YIKPDRVHVLYDGRI------VKSGDKELALEI 195
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-205 |
6.45e-19 |
|
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: 82.87 E-value: 6.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLN--GEQV--------TIPSIREaDRMGIASVFq 75
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVdlaqasprEILALRR-RTIGYVSQF- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 76 gqefcdnLD----------VASNLFlgkeinQIGIRDDDSMNsRARSVLKTLSSAIRV-GSPIASLSVGQRQTVAIARTL 144
Cdd:COG4778 102 -------LRviprvsaldvVAEPLL------ERGVDREEARA-RARELLARLNLPERLwDLPPATFSGGEQQRVNIARGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 145 LNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQG 205
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-207 |
6.71e-19 |
|
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: 82.46 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQV-TIPSIREADRMGI----ASVFQGQefcd 81
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIsTIPLEDLRSSLTIipqdPTLFSGT---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 nldVASNLflgkeiNQIGIRDDDSmnsrarsvlktLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:cd03369 98 ---IRSNL------DPFDEYSDEE-----------IYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1626716271 162 VMQSAEVLAYIKRLRSeGRSVVMVCHDLPDVfAVSDRIVVIRQGHV 207
Cdd:cd03369 158 YATDALIQKTIREEFT-NSTILTIAHRLRTI-IDYDKILVMDAGEV 201
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-207 |
7.65e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.93 E-value: 7.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEqvtipSIREAD----RMGIASVfqGQEfcd 81
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV-----PLVQYDhhylHRQVALV--GQE--- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 nldvaSNLFLGKEINQI--GIRDDDSMNSRARSVLKTLSSAI---------RVGSPIASLSVGQRQTVAIARTLLNDPQL 150
Cdd:TIGR00958 564 -----PVLFSGSVRENIayGLTDTPDEEIMAAAKAANAHDFImefpngydtEVGEKGSQLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 151 ILLDEPTAALsvmqSAEVLAYIKRLRS-EGRSVVMVCHDLPDVfAVSDRIVVIRQGHV 207
Cdd:TIGR00958 639 LILDEATSAL----DAECEQLLQESRSrASRTVLLIAHRLSTV-ERADQILVLKKGSV 691
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-207 |
8.02e-19 |
|
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: 82.54 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqVTIPSIREAD---RMGI----ASVFQGqefc 80
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG--VDISKIGLHDlrsRISIipqdPVLFSG---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 dnlDVASNL-FLGK----EINQIgiRDDDSMNSRARSVLKTLSSAIRVGSpiASLSVGQRQTVAIARTLLNDPQLILLDE 155
Cdd:cd03244 93 ---TIRSNLdPFGEysdeELWQA--LERVGLKEFVESLPGGLDTVVEEGG--ENLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 156 PTAALSvMQSAEVLAyiKRLRSE--GRSVVMVCHDLPDVFAvSDRIVVIRQGHV 207
Cdd:cd03244 166 ATASVD-PETDALIQ--KTIREAfkDCTVLTIAHRLDTIID-SDRILVLDKGRV 215
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
9-207 |
1.18e-18 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 85.09 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEqvtipSIREADR--MG--IASVFQGQEfcdnld 84
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGA-----DLKQWDRetFGkhIGYLPQDVE------ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 85 vasnLFLGKEINQIGiRDDDSMNSRARSVLKTLSSA----IR--------VGSPIASLSVGQRQTVAIARTLLNDPQLIL 152
Cdd:TIGR01842 403 ----LFPGTVAENIA-RFGENADPEKIIEAAKLAGVheliLRlpdgydtvIGPGGATLSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 153 LDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDlPDVFAVSDRIVVIRQGHV 207
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKARGITVVVITHR-PSLLGCVDKILVLQDGRI 531
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
8-207 |
1.19e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.24 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLnGEQVTIPSIREAD----RMGIASVFQ---GQEFC 80
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEikpvRKKVGVVFQfpeSQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNldVASNLFLGKEinQIGIRDDDSMNSRARSV-LKTLSSAIRVGSPIaSLSVGQRQTVAIARTLLNDPQLILLDEPTAA 159
Cdd:PRK13643 100 ET--VLKDVAFGPQ--NFGIPKEKAEKIAAEKLeMVGLADEFWEKSPF-ELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 160 LSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-207 |
1.45e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 84.12 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipSIREADRmGIASVFQGQEFCDNL 83
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN--ELEPADR-DIAMVFQNYALYPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 DVASNLFLGKEINQIGirdDDSMNSRARSVLKTLSsairVGS-----PiASLSVGQRQTVAIARTLLNDPQLILLDEP-- 156
Cdd:PRK11650 92 SVRENMAYGLKIRGMP---KAEIEERVAEAARILE----LEPlldrkP-RELSGGQRQRVAMGRAIVREPAVFLFDEPls 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 157 --TAALSVMQSAEvlayIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK11650 164 nlDAKLRVQMRLE----IQRLhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
13-203 |
1.55e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.39 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 13 NLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEqvtipSIREadrmgiasvfQGQEFCDNLdvasnLFLG 92
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGE-----PIRR----------QRDEYHQDL-----LYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 93 keiNQIGIRDDDS------MNSRARSVLKT--LSSAI-RVG------SPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:PRK13538 81 ---HQPGIKTELTalenlrFYQRLHGPGDDeaLWEALaQVGlagfedVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSEGRSVVMVCHDlpDVFAVSDRIVVIR 203
Cdd:PRK13538 158 TAIDKQGVARLEALLAQHAEQGGMVILTTHQ--DLPVASDKVRKLR 201
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-208 |
2.96e-18 |
|
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: 81.04 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeQVTIPsireadrMGIASVFQGqefcdNLDV 85
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSL-------LGLGGGFNP-----ELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGKEINqiGIRDDDsMNSRARSV-------------LKTLSSAIRVgspiaslsvgqRQTVAIARTLlnDPQLIL 152
Cdd:cd03220 102 RENIYLNGRLL--GLSRKE-IDEKIDEIiefselgdfidlpVKTYSSGMKA-----------RLAFAIATAL--EPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 153 LDEPTAA--LSVMQSAevLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVT 208
Cdd:cd03220 166 IDEVLAVgdAAFQEKC--QRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
9-216 |
3.11e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.66 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTI--PSIREADRMGIASVFQgqefcdnlDVA 86
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnRAQRKAFRRDIQMVFQ--------DSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 87 SNLFLGKEINQIgIR---------DDDSMNSRARSVLKTLSSAIRVGSPI-ASLSVGQRQTVAIARTLLNDPQLILLDEP 156
Cdd:PRK10419 100 SAVNPRKTVREI-IReplrhllslDKAERLARASEMLRAVDLDDSVLDKRpPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 157 TAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGhvtgvhRTVET 216
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNG------QIVET 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
15-209 |
5.19e-18 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 83.30 E-value: 5.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 15 SIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYlngEQVTI---PSIREADRMGIASVFQGQEFCDNLDvaSNLFL 91
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDLKIsykPQYISPDYDGTVEEFLRSANTDDFG--SSYYK 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 92 GKEINQIGIrdDDSMNSrarsvlktlssairvgsPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAY 171
Cdd:COG1245 437 TEIIKPLGL--EKLLDK-----------------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1626716271 172 IKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVI-----RQGHVTG 209
Cdd:COG1245 498 IRRFaENRGKTAMVVDHDIYLIDYISDRLMVFegepgVHGHASG 541
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
9-225 |
5.55e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.92 E-value: 5.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAG--FLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQgqefcD----- 81
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTE-----Drkgyg 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 -NL--DVASNLFLG--KEINQIGIRDD-----------DSMNSRARSVLKTlssairVGSpiasLSVGQRQTVAIARTLL 145
Cdd:NF040905 351 lNLidDIKRNITLAnlGKVSRRGVIDEneeikvaeeyrKKMNIKTPSVFQK------VGN----LSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 146 NDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEI 225
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREEASQERIMRLI 500
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-207 |
7.33e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.29 E-value: 7.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHI---YLNGEQVTIPSIREAD------------------ 66
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEKVleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 67 --RMGIASVFQGQEFcdnldvasNLF---LGKEI----NQIGIRDDDSMnSRARSVLKTlssairVGSPIA-------SL 130
Cdd:PRK13651 102 eiRRRVGVVFQFAEY--------QLFeqtIEKDIifgpVSMGVSKEEAK-KRAAKYIEL------VGLDESylqrspfEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 131 SVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-207 |
7.72e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 7.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKST----LIKVIAGFlqpgfGHIYLNGEQVTIPSIRE--ADRMGIASVFQGQ 77
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFDGQPLHNLNRRQllPVRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 78 EFCDN--LDVASNLFLGKEINQIGIrdddSMNSRARSVLKT-----LSSAIRVGSPiASLSVGQRQTVAIARTLLNDPQL 150
Cdd:PRK15134 372 NSSLNprLNVLQIIEEGLRVHQPTL----SAAQREQQVIAVmeevgLDPETRHRYP-AEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 151 ILLDEPTAALSVMQSAEVLAYIKRLRSEGR-SVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
15-201 |
7.82e-18 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 80.14 E-value: 7.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 15 SIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIylngeqvtipsirEADRMGIAsvFQGQEFCDNLDVASNLFLGKE 94
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-------------EIELDTVS--YKPQYIKADYEGTVRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 95 INQIGIrdDDSMNSrarSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKR 174
Cdd:cd03237 86 TKDFYT--HPYFKT---EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180
....*....|....*....|....*...
gi 1626716271 175 LRSEGRSVVMVC-HDLPDVFAVSDRIVV 201
Cdd:cd03237 161 FAENNEKTAFVVeHDIIMIDYLADRLIV 188
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-207 |
1.10e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.52 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAdRMGIASVFQG--QEFCdNL 83
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL-RRKIGMVFQNpdNQFV-GA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 DVASNLFLGKEiNQiGIRDDDSMNSRARSVLKTLSSAIRVGSPiASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVM 163
Cdd:PRK13642 98 TVEDDVAFGME-NQ-GIPREEMIKRVDEALLAVNMLDFKTREP-ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1626716271 164 QSAEVLAYIKRLRSEGR-SVVMVCHDLpDVFAVSDRIVVIRQGHV 207
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQlTVLSITHDL-DEAASSDRILVMKAGEI 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-207 |
2.11e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.45 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMgIASVFQgqefcdnlDV 85
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQR-IRMIFQ--------DP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGKEINQI---GIRDDDSMNSRARSvlKTLSSAIR-VG--------SPIAsLSVGQRQTVAIARTLLNDPQLILL 153
Cdd:PRK15112 97 STSLNPRQRISQIldfPLRLNTDLEPEQRE--KQIIETLRqVGllpdhasyYPHM-LAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 154 DEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
12-212 |
3.22e-17 |
|
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: 81.00 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 12 VNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTiPSIREADRMGIASVFqgqefcdnldvaSNLFL 91
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT-ADNREAYRQLFSAVF------------SDFHL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 92 GKEINQIGIRDDDsmnSRARSVLKTLSSAIRVG------SPIAsLSVGQRQTVAIARTLLNDPQLILLDEPTAAlsvmQS 165
Cdd:COG4615 418 FDRLLGLDGEADP---ARARELLERLELDHKVSvedgrfSTTD-LSQGQRKRLALLVALLEDRPILVFDEWAAD----QD 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 166 AEVLAY-----IKRLRSEGRSVVMVCHDlpD-VFAVSDRIVVIRQGHVTGVHR 212
Cdd:COG4615 490 PEFRRVfytelLPELKARGKTVIAISHD--DrYFDLADRVLKMDYGKLVELTG 540
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-205 |
4.24e-17 |
|
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: 77.51 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqvtipsireadrmGIASVFQgQEFCDNLDVAS 87
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQ-EPWIQNGTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NLFLGKEINQigirdddsmnSRARSVLK--TLSSAIR---------VGSPIASLSVGQRQTVAIARTLLNDPQLILLDEP 156
Cdd:cd03250 85 NILFGKPFDE----------ERYEKVIKacALEPDLEilpdgdlteIGEKGINLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 157 TAAL------SVMQSAevlayIKRLRSEGRSVVMVCHDLpDVFAVSDRIVVIRQG 205
Cdd:cd03250 155 LSAVdahvgrHIFENC-----ILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
8-225 |
5.15e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 78.69 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQP---GFGHIYLNGEQVTIPSIREA-DRMGIasVFQGQefcDN- 82
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIrEKVGI--VFQNP---DNq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 ---LDVASNLFLGKEINQIgirDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAA 159
Cdd:PRK13640 97 fvgATVGDDVAFGLENRAV---PRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 160 LSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLpDVFAVSDRIVVIRQGHVTGVHRTVET-SYEEIIAEI 225
Cdd:PRK13640 174 LDPAGKEQILKLIRKLKKKnNLTVISITHDI-DEANMADQVLVLDDGKLLAQGSPVEIfSKVEMLKEI 240
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-212 |
7.51e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 79.76 E-value: 7.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSiREADRMGIASVFQgqefcDNLDVASN 88
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQ-----DPVVLADT 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LF----LGKEINQIGIRDDDSMNSRArSVLKTLSSAI--RVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSv 162
Cdd:PRK10790 431 FLanvtLGRDISEEQVWQALETVQLA-ELARSLPDGLytPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANID- 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 163 mqSAEVLAYIKRLRS--EGRSVVMVCHDLPDVFAvSDRIVVIRQGHVT--GVHR 212
Cdd:PRK10790 509 --SGTEQAIQQALAAvrEHTTLVVIAHRLSTIVE-ADTILVLHRGQAVeqGTHQ 559
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-205 |
7.71e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.69 E-value: 7.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 12 VNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFqgqefcDNLD----VAS 87
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQF------DNLDpdftVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NL-----FLGKEINQIgirdddsmNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:PRK13537 100 NLlvfgrYFGLSAAAA--------RALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1626716271 163 MQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQG 205
Cdd:PRK13537 172 QARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
9-207 |
1.03e-16 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 76.74 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMgIASVfqGQE---FCDNldV 85
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-VSLV--GQEpvlFARS--L 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGKEINQIGIRDDDSMNSRARSVLKTLSSAI--RVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVm 163
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYdtEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA- 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1626716271 164 QSAEVLAYIKRLRSEGRSVVMVCHDLPDVfAVSDRIVVIRQGHV 207
Cdd:cd03248 184 ESEQQVQQALYDWPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-213 |
1.05e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.19 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPG-----FGHIYLNGEQVTIPSIREAD-RMGIASVFQG 76
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIEvRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 77 QEFCDNLDVASNLFLGKEINQIgIRDDDSMNSRARSVLK--TLSSAI--RVGSPIASLSVGQRQTVAIARTLLNDPQLIL 152
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGL-VKSKKELDERVEWALKkaALWDEVkdRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 153 LDEPTAALSVMQSAEVLAYIKRLRSEgRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRT 213
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPT 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-207 |
1.45e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.97 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYL----NGEQVTIPS---------IREADRMG--I 70
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHElitnpyskkIKNFKELRrrV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 71 ASVFQGQEFcdnldvasNLF---LGKEIN----QIGIRDDDSMNSRARSVLKT-LSSAIRVGSPIaSLSVGQRQTVAIAR 142
Cdd:PRK13631 119 SMVFQFPEY--------QLFkdtIEKDIMfgpvALGVKKSEAKKLAKFYLNKMgLDDSYLERSPF-GLSGGQKRRVAIAG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 143 TLLNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
9-228 |
2.03e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.75 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMgIASVFQGQEFCDNLDVASN 88
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LFLGK-----EINQIGIRDDDSMNSRARSV-LKTLSSAIrvgspIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:PRK10575 106 VAIGRypwhgALGRFGAADREKVEEAISLVgLKPLAHRL-----VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 163 MQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAGV 228
Cdd:PRK10575 181 AHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGI 247
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-213 |
2.98e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.94 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqVTIPSIREAD-RMGIASVFQGQE-FCDNLdv 85
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG--QPIADYSEAAlRQAISVVSQRVHlFSATL-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGKE----------INQIGIR----DDDSMNS------RArsvlktlssairvgspiasLSVGQRQTVAIARTLL 145
Cdd:PRK11160 431 RDNLLLAAPnasdealievLQQVGLEklleDDKGLNAwlgeggRQ-------------------LSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 146 NDPQLILLDEPTAALSVMQSAEVLAYIKRLrSEGRSVVMVCHDLpdvFAVS--DRIVVIRQGHV--TGVHRT 213
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRL---TGLEqfDRICVMDNGQIieQGTHQE 559
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
8-206 |
3.89e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.67 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIRE--ADRMGIASVFQgqefcDNLdv 85
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwrAVRSDIQMIFQ-----DPL-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 AS---NLFLGkEINQIGIR------DDDSMNSRARSVLKtlssaiRVG--------SPiASLSVGQRQTVAIARTLLNDP 148
Cdd:PRK15079 109 ASlnpRMTIG-EIIAEPLRtyhpklSRQEVKDRVKAMML------KVGllpnlinrYP-HEFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1626716271 149 QLILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGH 206
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
16-201 |
5.01e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.54 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 16 IQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNgeqVTI---PSIREADRMGIASVFQGQEfcdNLDVASNLFLG 92
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKIsykPQYIKPDYDGTVEDLLRSI---TDDLGSSYYKS 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 93 KEINQIGIrdDDSMNSRarsvLKTLSSairvgspiaslsvGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYI 172
Cdd:PRK13409 436 EIIKPLQL--ERLLDKN----VKDLSG-------------GELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496
|
170 180 190
....*....|....*....|....*....|
gi 1626716271 173 KRL-RSEGRSVVMVCHDLPDVFAVSDRIVV 201
Cdd:PRK13409 497 RRIaEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
9-199 |
6.90e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.07 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQV--TIPSI-READRMGIASVFQGQefcdnLDV 85
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdfQRDSIaRGLLYLGHAPGIKTT-----LSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGKEINQigirDDDSMNSRARSVLKTLSSAirvgsPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQS 165
Cdd:cd03231 91 LENLRFWHADHS----DEQVEEALARVGLNGFEDR-----PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1626716271 166 AEVLAYIKRLRSEGRSVVMVCH-DLPDVFAVSDRI 199
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHqDLGLSEAGAREL 196
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
10-213 |
7.09e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 77.21 E-value: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 10 KSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNgeqvtiPSIREAdrmgiasVFQgQEFCDNLDVASNL 89
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRS------AKVRMA-------VFS-QHHVDGLDLSSNP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 90 FLGKEINQIGIRDddsmnSRARSVLKTLSSAIRVG-SPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVmqsAEV 168
Cdd:PLN03073 592 LLYMMRCFPGVPE-----QKLRAHLGSFGVTGNLAlQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL---DAV 663
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1626716271 169 LAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRT 213
Cdd:PLN03073 664 EALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGT 708
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
8-208 |
8.47e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.17 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT-------IPSIREadRMGIasVFQ---GQ 77
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkdIKQIRK--KVGL--VFQfpeSQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 78 EFCDNL--DVA---SNLFLGKEinqigirdDDSMNSRARSVLKTLSSAIRVGSPIaSLSVGQRQTVAIARTLLNDPQLIL 152
Cdd:PRK13649 98 LFEETVlkDVAfgpQNFGVSQE--------EAEALAREKLALVGISESLFEKNPF-ELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 153 LDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVT 208
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
9-212 |
8.50e-16 |
|
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: 76.78 E-value: 8.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGE---QVTIPSIREAdrmgIASVFQgqefcD---- 81
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdirDVTQASLRAA----IGIVPQ-----Dtvlf 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLFLGKEinqiGIRDDDsMNSRARsvLKTLSSAI---------RVGSPIASLSVGQRQTVAIARTLLNDPQLIL 152
Cdd:COG5265 445 NDTIAYNIAYGRP----DASEEE-VEAAAR--AAQIHDFIeslpdgydtRVGERGLKLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 153 LDEPTAALSVMQSAEVLAYIKRLrSEGRSVVMVCHDLPDVfAVSDRIVVIRQGHV--TGVHR 212
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREV-ARGRTTLVIAHRLSTI-VDADEILVLEAGRIveRGTHA 577
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-206 |
8.96e-16 |
|
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: 72.10 E-value: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIylngeqvtipsireadrmgiasvfqgqefcdnldvasn 88
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-------------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 lflgkeinqigirdddsmnsrarsvlkTLSSAIRVGSpIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVmQSAEV 168
Cdd:cd03221 58 ---------------------------TWGSTVKIGY-FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL-ESIEA 108
|
170 180 190
....*....|....*....|....*....|....*...
gi 1626716271 169 LayIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGH 206
Cdd:cd03221 109 L--EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-225 |
1.27e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQV--TIPSIREADRM--GIASVFQGQE---F 79
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEVKRLrkEIGLVFQFPEyqlF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 CDNL--DVA-SNLFLGKeinqigirDDDSMNSRARSVLK--TLSSAIRVGSPIaSLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:PRK13645 105 QETIekDIAfGPVNLGE--------NKQEAYKKVPELLKlvQLPEDYVKRSPF-ELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 155 EPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTVET-SYEEIIAEI 225
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIfSNQELLTKI 248
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
8-203 |
1.32e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.53 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqvtIPSIREADRMGIASVFQGQEFCDNLDVas 87
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG----QPTRQALQKNLVAYVPQSEEVDWSFPV-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 nlfLGKEINQIGIRDDDSMNSRARSVLKTLSSAI--RVG------SPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAA 159
Cdd:PRK15056 96 ---LVEDVVMMGRYGHMGWLRRAKKRDRQIVTAAlaRVDmvefrhRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1626716271 160 LSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIR 203
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-188 |
1.91e-15 |
|
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: 75.74 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAG---------FLQPGFGHIYLNGEQVTIPS--IREADRMGIASVFQ 75
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkdfngeaRPQPGIKVGYLPQEPQLDPTktVRENVEEGVAEIKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 76 GQefcDNLDVASNLF---------LGKE----INQIGIRDDDSMNSRarsvLKTLSSAIRV---GSPIASLSVGQRQTVA 139
Cdd:TIGR03719 99 AL---DRFNEISAKYaepdadfdkLAAEqaelQEIIDAADAWDLDSQ----LEIAMDALRCppwDADVTKLSGGERRRVA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1626716271 140 IARTLLNDPQLILLDEPTAALsvmqSAEVLAYIKR-LRSEGRSVVMVCHD 188
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHL----DAESVAWLERhLQEYPGTVVAVTHD 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-209 |
2.34e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIASVFQGQEfcdnldvA 86
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQ-------S 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 87 SNLFLGKEI---------NQIGIRDDdsmNSRARSVLKTLSSAIRV-----GSPIASLSVGQRQTVAIARTLLNDPQLIL 152
Cdd:PRK15439 350 SGLYLDAPLawnvcalthNRRGFWIK---PARENAVLERYRRALNIkfnhaEQAARTLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 153 LDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTG 209
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISG 483
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-194 |
3.88e-15 |
|
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: 72.01 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 20 EVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQvtIPSIREADRMGIASVFQGQEFCDNLDVASNLFLGKEINQIG 99
Cdd:TIGR01189 27 EALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP--LAEQRDEPHENILYLGHLPGLKPELSALENLHFWAAIHGGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 100 IRDDDsmNSRARSVLKTLSSAirvgsPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVmQSAEVLAYIKRLRSE- 178
Cdd:TIGR01189 105 QRTIE--DALAAVGLTGFEDL-----PAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK-AGVALLAGLLRAHLAr 176
|
170
....*....|....*..
gi 1626716271 179 GRSVVMVCH-DLPDVFA 194
Cdd:TIGR01189 177 GGIVLLTTHqDLGLVEA 193
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-213 |
5.48e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 74.28 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQV---TIPSIREAdrmgIASVFQGQE-FCD-- 81
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdyTLASLRNQ----VALVSQNVHlFNDti 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 --NLDVASNLFLGKEINQIGIRDDDSMN--SRARSVLKTLssairVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:PRK11176 434 anNIAYARTEQYSREQIEEAARMAYAMDfiNKMDNGLDTV-----IGENGVLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSEgRSVVMVCHDLPDVfAVSDRIVVIRQGHVT--GVHRT 213
Cdd:PRK11176 509 SALDTESERAIQAALDELQKN-RTSLVIAHRLSTI-EKADEILVVEDGEIVerGTHAE 564
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-202 |
5.74e-15 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 72.40 E-value: 5.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 20 EVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIpsIREadrmgiasvFQGQEFCD-----------------N 82
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEI--LDE---------FRGSELQNyftkllegdvkvivkpqY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LDVASNLFLGKEINQIGIRDDdsmNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:cd03236 96 VDLIPKAVKGKVGELLKKKDE---RGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1626716271 163 MQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVI 202
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-207 |
8.31e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.00 E-value: 8.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQV-------TIPSIREADRMGIasVFQGQEFCD 81
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifQIDAIKLRKEVGM--VFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLflGKEINQIGIRDDDSMNSRARSVLKTL----SSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:PRK14246 104 HLSIYDNI--AYPLKSHGIKEKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1626716271 158 AALSVMQSAEVLAYIKRLRSEgRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-215 |
1.26e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.45 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPgfghiylNGeqvtipsireadRMGIASVFQGQEFCDNL 83
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAA-------NG------------RIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 DVASNLFLGKEINQIGIRDDDSMNSRAR------SVL---KTLSSA------IR----VGSPIA---------SLSVGQR 135
Cdd:PRK09473 88 EKELNKLRAEQISMIFQDPMTSLNPYMRvgeqlmEVLmlhKGMSKAeafeesVRmldaVKMPEArkrmkmyphEFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 136 QTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGhvtgvhRTV 214
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAG------RTM 241
|
.
gi 1626716271 215 E 215
Cdd:PRK09473 242 E 242
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
9-188 |
1.28e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.90 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSiREADRMGIASVFQGQE-FCDNldVAS 87
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK-PEIYRQQVSYCAQTPTlFGDT--VYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NLFLGKEINQIGIRDDDSMNSRARSVL--KTLSsairvgSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQS 165
Cdd:PRK10247 100 NLIFPWQIRNQQPDPAIFLDDLERFALpdTILT------KNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180
....*....|....*....|....
gi 1626716271 166 AEVLAYIKRL-RSEGRSVVMVCHD 188
Cdd:PRK10247 174 HNVNEIIHRYvREQNIAVLWVTHD 197
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-207 |
1.84e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.33 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 12 VNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQvtIPSIRE----ADRMGIASVFQGQEFCDNLDVAS 87
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEN--IPAMSRsrlyTVRKRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NL-FLGKEINQIgirddDSMNSRARSVLKTLSSAIRVGSPI--ASLSVGQRQTVAIARTLLNDPQLILLDEPTaalsVMQ 164
Cdd:PRK11831 104 NVaYPLREHTQL-----PAPLLHSTVMMKLEAVGLRGAAKLmpSELSGGMARRAALARAIALEPDLIMFDEPF----VGQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 165 SAEVLAYIKRLRSE-----GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK11831 175 DPITMGVLVKLISElnsalGVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-258 |
2.38e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.53 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 1 MKFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGF--LQPGFGHIYLN------GEQVTIPS----------- 61
Cdd:TIGR03269 8 KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekCGYVERPSkvgepcpvcgg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 62 ---------------IREADRMGIASVFQgQEFC--DNLDVASNLFlgKEINQIGIRDDDSMNsRARSVLKTLSSAIRVG 124
Cdd:TIGR03269 88 tlepeevdfwnlsdkLRRRIRKRIAIMLQ-RTFAlyGDDTVLDNVL--EALEEIGYEGKEAVG-RAVDLIEMVQLSHRIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 125 SPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVmQSAEVL--AYIKRLRSEGRSVVMVCHdLPDVFA-VSDRIVV 201
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDP-QTAKLVhnALEEAVKASGISMVLTSH-WPEVIEdLSDKAIW 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1626716271 202 IRQGHVT--GVHRTVETSYEEIIAEIagvttEHEYEEIAENPkfdsMVRQRKLIDRTIS 258
Cdd:TIGR03269 242 LENGEIKeeGTPDEVVAVFMEGVSEV-----EKECEVEVGEP----IIKVRNVSKRYIS 291
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-207 |
3.47e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 72.35 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQvtIPSIREADRMGIASVFQGQEFCDNLDVAS 87
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD--IETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NLFLgkeINQIGIRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAE 167
Cdd:TIGR01257 1023 HILF---YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1626716271 168 VLAYIKRLRSeGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:TIGR01257 1100 IWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-205 |
3.61e-14 |
|
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: 69.67 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREAD---RMGIASVFQgQEFCDNLDV 85
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnRYSVAYAAQ-KPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGKEINQigirdddsmnSRARSVLKTLS-----------SAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:cd03290 96 EENITFGSPFNK----------QRYKAVTDACSlqpdidllpfgDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 155 EPTAALSVMQSAEVL--AYIKRLRSEGRSVVMVCHDLpDVFAVSDRIVVIRQG 205
Cdd:cd03290 166 DPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
20-202 |
3.61e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 72.12 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 20 EVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIylNGEqvtiPSIREadrmgIASVFQGQEFCDNL---------------- 83
Cdd:COG1245 100 KVTGILGPNGIGKSTALKILSGELKPNLGDY--DEE----PSWDE-----VLKRFRGTELQDYFkklangeikvahkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 -DVASNLFLGKeINQIGIRDDDSMnsRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:COG1245 169 vDLIPKVFKGT-VRELLEKVDERG--KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1626716271 163 MQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVI 202
Cdd:COG1245 246 YQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-244 |
3.63e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.09 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFgHI-----YLNGEQVTIPSIREADR-MG--IASVFQ 75
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNW-HVtadrfRWNGIDLLKLSPRERRKiIGreIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 76 GQEFCdnLDVASNlfLGKEINQ----------------------------IGIRD-DDSMNSRARsvlktlssairvgsp 126
Cdd:COG4170 97 EPSSC--LDPSAK--IGDQLIEaipswtfkgkwwqrfkwrkkraiellhrVGIKDhKDIMNSYPH--------------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 127 iaSLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQG 205
Cdd:COG4170 158 --ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1626716271 206 hvtgvhRTVET-SYEEIIAeiagvTTEHEYEE--IAENPKFD 244
Cdd:COG4170 236 ------QTVESgPTEQILK-----SPHHPYTKalLRSMPDFR 266
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-205 |
5.12e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipSIREADRM-----GIASVFQGQEFCDNL 83
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLH--QMDEEARAklrakHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 DVASNLFLGKEINqiGIRDDDSmNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVM 163
Cdd:PRK10584 104 NALENVELPALLR--GESSRQS-RNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1626716271 164 QSAEVLAYIKRL-RSEGRSVVMVCHDlPDVFAVSDRIVVIRQG 205
Cdd:PRK10584 181 TGDKIADLLFSLnREHGTTLILVTHD-LQLAARCDRRLRLVNG 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-197 |
5.41e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 69.81 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGF--LQPGF---GHIYLNGEQVTIPSIREAD-RMGIASVFQG-QEFC 80
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTFHGKNLYAPDVDPVEvRRRIGMVFQKpNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNldVASNLFLGKEINqiGIRDD-DSMNSRA--RSVL------KTLSSAIrvgspiaSLSVGQRQTVAIARTLLNDPQLI 151
Cdd:PRK14243 105 KS--IYDNIAYGARIN--GYKGDmDELVERSlrQAALwdevkdKLKQSGL-------SLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1626716271 152 LLDEPTAALSVMQSAEVLAYIKRLRsEGRSVVMVCHDLPDVFAVSD 197
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSD 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
9-207 |
1.68e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGF--------GHIYLNGEQVT-IPSIREADRMgiASVFQGQEF 79
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAaIDAPRLARLR--AVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 CDNLDVASNLFLG-----KEINQIGIRDDDSmnsrARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTL---------L 145
Cdd:PRK13547 95 AFAFSAREIVLLGryphaRRAGALTHRDGEI----AWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 146 NDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGR-SVVMVCHDlPDVFAV-SDRIVVIRQGHV 207
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHD-PNLAARhADRIAMLADGAI 233
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
9-190 |
1.83e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.28 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVtipsirEADRmgiaSVFQgQEFCdnldvasn 88
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI------KKDL----CTYQ-KQLC-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 lFLGkeiNQIGIRDDDSMNSRARSVLKTLSSAIRVGS-------------PIASLSVGQRQTVAIARTLLNDPQLILLDE 155
Cdd:PRK13540 78 -FVG---HRSGINPYLTLRENCLYDIHFSPGAVGITElcrlfslehlidyPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 1626716271 156 PTAALSVMQSAEVLAYIKRLRSEGRSVVMVCH-DLP 190
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLLTSHqDLP 189
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-208 |
2.24e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.62 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFveALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSiREADRMGIASVFQgqefcdnl 83
Cdd:PRK10522 336 GF--SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ-PEDYRKLFSAVFT-------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 DVasNLF---LGKEinqigirDDDSMNSRARSVLKTLSSAIRV---GSPIA--SLSVGQRQTVAIARTLLNDPQLILLDE 155
Cdd:PRK10522 405 DF--HLFdqlLGPE-------GKPANPALVEKWLERLKMAHKLeleDGRISnlKLSKGQKKRLALLLALAEERDILLLDE 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 156 PTAALSVMQSAE---VLayIKRLRSEGRSVVMVCHDlpD-VFAVSDRIVVIRQGHVT 208
Cdd:PRK10522 476 WAADQDPHFRREfyqVL--LPLLQEMGKTIFAISHD--DhYFIHADRLLEMRNGQLS 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
21-202 |
2.58e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 21 VIAIVGDNGAGKSTLIKVIAGFLQPGFGHIylnGEQVTIPSIREAdrmgiasvFQGQEFCDNL----------------- 83
Cdd:PRK13409 101 VTGILGPNGIGKTTAVKILSGELIPNLGDY---EEEPSWDEVLKR--------FRGTELQNYFkklyngeikvvhkpqyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 DVASNLFLG------KEINQIGIRDDdsmnsrarsVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:PRK13409 170 DLIPKVFKGkvrellKKVDERGKLDE---------VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1626716271 158 AALSVMQSAEVLAYIKRLrSEGRSVVMVCHDLPDVFAVSDRIVVI 202
Cdd:PRK13409 241 SYLDIRQRLNVARLIREL-AEGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-208 |
2.90e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAG--FLQPGfghiYLNGEQVTIPSIREAD--RMGIASVF---- 74
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevLLDDG----RIIYEQDLIVARLQQDppRNVEGTVYdfva 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 75 QG-QEFCDNL--------DVAS-----NLF-LGKEINQIGIRDDDSMNSRARSVLKTLSsaIRVGSPIASLSVGQRQTVA 139
Cdd:PRK11147 89 EGiEEQAEYLkryhdishLVETdpsekNLNeLAKLQEQLDHHNLWQLENRINEVLAQLG--LDPDAALSSLSGGWLRKAA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1626716271 140 IARTLLNDPQLILLDEPTAALSVmQSAEVLAyiKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVT 208
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDI-ETIEWLE--GFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-205 |
3.17e-13 |
|
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: 66.50 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 23 AIVGDNGAGKSTLIKVIAGFLQPGF--GHIYLNGEQVTIPSIREADrmgiasvfqgqeFCDNLDVASNlflgkeinqigi 100
Cdd:cd03232 37 ALMGESGAGKTTLLDVLAGRKTAGVitGEILINGRPLDKNFQRSTG------------YVEQQDVHSP------------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 101 rdddsmNSRARSVLKtLSSAIRvgspiaSLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGR 180
Cdd:cd03232 93 ------NLTVREALR-FSALLR------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQ 159
|
170 180
....*....|....*....|....*..
gi 1626716271 181 SVVMVCHDlP--DVFAVSDRIVVIRQG 205
Cdd:cd03232 160 AILCTIHQ-PsaSIFEKFDRLLLLKRG 185
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-217 |
4.04e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.96 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 12 VNLSIQRQEVIAIVGDNGAGKS-TLIKVIAGFLQPGF----GHIYLNGEQV------TIPSIReADRmgIASVFQgqEFC 80
Cdd:PRK15134 28 VSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLlhaseqTLRGVR-GNK--IAMIFQ--EPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DNLDVASNLflGKEINQI-----GIRDDdsmnsRARSvlKTLSSAIRVGSPIAS---------LSVGQRQTVAIARTLLN 146
Cdd:PRK15134 103 VSLNPLHTL--EKQLYEVlslhrGMRRE-----AARG--EILNCLDRVGIRQAAkrltdyphqLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 147 DPQLILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGhvtgvhRTVETS 217
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNG------RCVEQN 239
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-221 |
5.58e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKST-------LIKVIAGFLQPGFGHIYLNGEQVT---------IPSIREADr 67
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRQVIelseqsaaqMRHVRGAD- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 68 mgIASVFQGQEFCDN--LDVASNLFLGKEINQiGIRDDDSMnSRARSVLKTL----SSAIRVGSPiASLSVGQRQTVAIA 141
Cdd:PRK10261 106 --MAMIFQEPMTSLNpvFTVGEQIAESIRLHQ-GASREEAM-VEAKRMLDQVripeAQTILSRYP-HQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 142 RTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGhvtgvhRTVET-SYE 219
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQG------EAVETgSVE 254
|
..
gi 1626716271 220 EI 221
Cdd:PRK10261 255 QI 256
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
16-202 |
9.64e-13 |
|
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: 64.90 E-value: 9.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 16 IQRQEVIAIVGDNGAGKSTLIKVIAGFLQPgfghiylNGEQVTIPSIReadrmgiasvfqgqefcdnldvasnlflgkei 95
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIP-------NGDNDEWDGIT-------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 96 nqigirdddsmnsrarsvlktlssaIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRL 175
Cdd:cd03222 63 -------------------------PVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*...
gi 1626716271 176 RSEG-RSVVMVCHDLPDVFAVSDRIVVI 202
Cdd:cd03222 118 SEEGkKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-188 |
1.43e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGhiylngeqvtipSIREADRMGIASVFQGQEfcdNLD---- 84
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG------------RIHCGTKLEVAYFDQHRA---ELDpekt 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 85 VASNLFLGKEinqigirdDDSMNSRARSVLKTLS----SAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:PRK11147 400 VMDNLAEGKQ--------EVMVNGRPRHVLGYLQdflfHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
170 180
....*....|....*....|....*....
gi 1626716271 161 SVmqsaEVLAYIKRLRSEGR-SVVMVCHD 188
Cdd:PRK11147 472 DV----ETLELLEELLDSYQgTVLLVSHD 496
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-162 |
1.70e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.88 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 12 VNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLnGEQVTipsireadrmgIASVFQGQefcDNLDVASNLFL 91
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-----------LAYVDQSR---DALDPNKTVWE 405
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 92 ----GKEINQIGIRDddsMNSRA---RSVLKTLSSAIRVGspiaSLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:TIGR03719 406 eisgGLDIIKLGKRE---IPSRAyvgRFNFKGSDQQKKVG----QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-205 |
3.61e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 20 EVIAIVGDNGAGKSTLIKVIAGFLQP-GF-GHIYLNGEQVTIPSIReadRMGIasVFQGQEFCDNLDVASNLFLGKEINQ 97
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGnNFtGTILANNRKPTKQILK---RTGF--VTQDDILYPHLTVRETLVFCSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 98 IGIRDDDSMNSRARSVLKTL-----SSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYI 172
Cdd:PLN03211 170 PKSLTKQEKILVAESVISELgltkcENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170 180 190
....*....|....*....|....*....|....
gi 1626716271 173 KRLRSEGRSVVMVCHDLPD-VFAVSDRIVVIRQG 205
Cdd:PLN03211 250 GSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEG 283
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-188 |
4.77e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAG---------FLQPGFGHIYLNGEQVTIPS--IREADRMGIASVFQGQ 77
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkefegeaRPAPGIKVGYLPQEPQLDPEktVRENVEEGVAEVKAAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 78 efcDNLDVASNLF----------------LGKEINQIGIRDDDSMNSRArsvlktlSSAIRV---GSPIASLSVGQRQTV 138
Cdd:PRK11819 103 ---DRFNEIYAAYaepdadfdalaaeqgeLQEIIDAADAWDLDSQLEIA-------MDALRCppwDAKVTKLSGGERRRV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 139 AIARTLLNDPQLILLDEPTAALsvmqSAEVLAYIKR-LRSEGRSVVMVCHD 188
Cdd:PRK11819 173 ALCRLLLEKPDMLLLDEPTNHL----DAESVAWLEQfLHDYPGTVVAVTHD 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-228 |
5.01e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMG---------------- 69
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGdeeqnvgmknvnefsl 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 70 --------IASVFQ--------GQEFCD--------------------NLDVASNLFLGKEInqiGIRDDDSMNSRARSV 113
Cdd:PTZ00265 1261 tkeggsgeDSTVFKnsgkilldGVDICDynlkdlrnlfsivsqepmlfNMSIYENIKFGKED---ATREDVKRACKFAAI 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 114 LKTLSSA-----IRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEG-RSVVMVCH 187
Cdd:PTZ00265 1338 DEFIESLpnkydTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAH 1417
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1626716271 188 DLPDVfAVSDRIVVIRQGHVTGVHRTVETSYEEIIAEIAGV 228
Cdd:PTZ00265 1418 RIASI-KRSDKIVVFNNPDRTGSFVQAHGTHEELLSVQDGV 1457
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
7-237 |
1.27e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGflQPGF----GHIYLNGEQVTIPSIREADRMGIASVFQ------G 76
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAYkileGDILFKGESILDLEPEERAHLGIFLAFQypieipG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 77 QEFCDNLDVASN---LFLGK-EINQIgirdddsmnsrarSVLKTLSSAIRVGSPIAS---------LSVGQRQTVAIART 143
Cdd:CHL00131 99 VSNADFLRLAYNskrKFQGLpELDPL-------------EFLEIINEKLKLVGMDPSflsrnvnegFSGGEKKRNEILQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 144 LLNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCH--DLPDvFAVSDRIVVIRQGhvtgvhRTVETSYeei 221
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHyqRLLD-YIKPDYVHVMQNG------KIIKTGD--- 235
|
250
....*....|....*.
gi 1626716271 222 iAEIAGVTTEHEYEEI 237
Cdd:CHL00131 236 -AELAKELEKKGYDWL 250
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-245 |
1.75e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.28 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPG---------FGHIYLngEQVTIPSIREADRMGIASVF 74
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtadrmrFDDIDL--LRLSPRERRKLVGHNVSMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 75 QGQEFCdnLDVASNLflGKEINQiGI-------RDDDSMNSRARSVLKTLSsaiRVG---------SPIASLSVGQRQTV 138
Cdd:PRK15093 96 QEPQSC--LDPSERV--GRQLMQ-NIpgwtykgRWWQRFGWRKRRAIELLH---RVGikdhkdamrSFPYELTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 139 AIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGhvtgvhRTVETS 217
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCG------QTVETA 241
|
250 260 270
....*....|....*....|....*....|.
gi 1626716271 218 Y-EEIIaeiagVTTEHEYEE--IAENPKFDS 245
Cdd:PRK15093 242 PsKELV-----TTPHHPYTQalIRAIPDFGS 267
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-197 |
2.29e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 62.36 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIaGFLQPGFGHIYLNGE-----------QVTIPSIREADRMgiasVFQGQ 77
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRveffnqniyerRVNLNRLRRQVSM----VHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 78 EFCDnLDVASNLFLGKEInqIGIRDDDSMNSRARSVLKTLSSAIRVGSPI----ASLSVGQRQTVAIARTLLNDPQLILL 153
Cdd:PRK14258 98 NLFP-MSVYDNVAYGVKI--VGWRPKLEIDDIVESALKDADLWDEIKHKIhksaLDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1626716271 154 DEPTAALSVMQSAEVLAYIK--RLRSEgRSVVMVCHDLPDVFAVSD 197
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQslRLRSE-LTMVIVSHNLHQVSRLSD 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-160 |
2.58e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.79 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 20 EVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipsirEADRMG-IASVFQGQEFCDNLDVASNLFLgkeINQI 98
Cdd:PRK13543 38 EALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-----RGDRSRfMAYLGHLPGLKADLSTLENLHF---LCGL 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 99 GIRDDDSMNSRArsvLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:PRK13543 110 HGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-162 |
1.21e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 24 IVGDNGAGKSTLIKVIAGFLQPGFGHIYLnGEQVTipsireadrmgIASVFQGQefcDNLDVASNLFL----GKEINQIG 99
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK-----------LAYVDQSR---DALDPNKTVWEeisgGLDIIKVG 419
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 100 IRDddsMNSRArsvlktlssaiRVGS----------PIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:PRK11819 420 NRE---IPSRA-----------YVGRfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-207 |
1.37e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.49 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 1 MKFGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKV-------IAGFLQPGfgHIYLNGEQVTIPSIREADRMGIASV 73
Cdd:PRK14271 29 LGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRYSG--DVLLGGRSIFNYRDVLEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 74 FQ-GQEFcdNLDVASNLFLGKEINQIGIRDDDSMNSRARSVLKTLSSAI--RVGSPIASLSVGQRQTVAIARTLLNDPQL 150
Cdd:PRK14271 107 FQrPNPF--PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVkdRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 151 ILLDEPTAALSVMQSAEVLAYIKRLrSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
8-213 |
1.79e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.88 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqVTIPSIR-EADRMGIASVFQGQ-EFCDNldV 85
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD--IPLTKLQlDSWRSRLAVVSQTPfLFSDT--V 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGK-EINQIGIRDDDSMNSRARSVLKTLSS-AIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVM 163
Cdd:PRK10789 406 ANNIALGRpDATQQEIEHVARLASVHDDILRLPQGyDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGR 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 164 QSAEVLAYIKRLRsEGRSVVMVCHDLpDVFAVSDRIVVIRQGHVT--GVHRT 213
Cdd:PRK10789 486 TEHQILHNLRQWG-EGRTVIISAHRL-SALTEASEILVMQHGHIAqrGNHDQ 535
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-198 |
1.81e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.20 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGE------------------------------ 55
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrskigvvsqdpllfsnsik 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 56 ---QVTIPSIREADRMGIASVFQGQEFCDNLD-------------------VASNLFLGKEINQIGIRDDDSMNSRARSV 113
Cdd:PTZ00265 478 nniKYSLYSLKDLEALSNYYNEDGNDSQENKNkrnscrakcagdlndmsntTDSNELIEMRKNYQTIKDSEVVDVSKKVL 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 114 LKTLSSAIR------VGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRLR-SEGRSVVMVC 186
Cdd:PTZ00265 558 IHDFVSALPdkyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIA 637
|
250
....*....|....*...
gi 1626716271 187 HDLP------DVFAVSDR 198
Cdd:PTZ00265 638 HRLStiryanTIFVLSNR 655
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
9-205 |
2.45e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.59 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHI---------------YLNG----EQVTIPS-------- 61
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIarpagarvlflpqrpYLPLgtlrEALLYPAtaeafsda 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 62 -IREA-DRMGIasvfqgQEFCDNLDVASNLflgkeiNQIgirdddsmnsrarsvlktlssairvgspiasLSVGQRQTVA 139
Cdd:COG4178 459 eLREAlEAVGL------GHLAERLDEEADW------DQV-------------------------------LSLGEQQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 140 IARTLLNDPQLILLDEPTAALSVmqSAEVLAYiKRLRSE--GRSVVMVCHDlPDVFAVSDRIVVIRQG 205
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDE--ENEAALY-QLLREElpGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-205 |
2.64e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.80 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipsireadrMGIASVFQGQEFCDNLDVAS 87
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---------TNISDVHQNMGYCPQFDAID 2024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 NLFLGKEINQIGIR----DDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVM 163
Cdd:TIGR01257 2025 DLLTGREHLYLYARlrgvPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1626716271 164 QSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQG 205
Cdd:TIGR01257 2105 ARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-192 |
2.69e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSireaDRMGIASVFQGQEFCDNLDVasn 88
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGR----EASLIDAIGRKGDFKDAVEL--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 lflgkeINQIGirdddsmnsrarsvlktLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVmQSAEV 168
Cdd:COG2401 119 ------LNAVG-----------------LSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR-QTAKR 174
|
170 180
....*....|....*....|....*.
gi 1626716271 169 LAYI--KRLRSEGRSVVMVCHDlPDV 192
Cdd:COG2401 175 VARNlqKLARRAGITLVVATHH-YDV 199
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
9-205 |
2.71e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.63 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGF--GHIYLNG---EQVTIPSIreadrmgiasvfqgQEFCDNL 83
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYieGDIRISGfpkKQETFARI--------------SGYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 DVASN-------------LFLGKEINQigirdDDSMNSRARSV----LKTLSSAIrVGSP-IASLSVGQRQTVAIARTLL 145
Cdd:PLN03140 962 DIHSPqvtvresliysafLRLPKEVSK-----EEKMMFVDEVMelveLDNLKDAI-VGLPgVTGLSTEQRKRLTIAVELV 1035
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 146 NDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDlP--DVFAVSDRIVVIRQG 205
Cdd:PLN03140 1036 ANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ-PsiDIFEAFDELLLMKRG 1096
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-207 |
4.17e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.96 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqVTIPSIREAD-RMGIASV------FQGQeFCD 81
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--LNIAKIGLHDlRFKITIIpqdpvlFSGS-LRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 82 NLDVASNLflgkeinqigiRDDDSMNSRARSVLKTLSSAIRVGSPIA------SLSVGQRQTVAIARTLLNDPQLILLDE 155
Cdd:TIGR00957 1379 NLDPFSQY-----------SDEEVWWALELAHLKTFVSALPDKLDHEcaeggeNLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 156 PTAALSVMQSAEVLAYIkRLRSEGRSVVMVCHDLPDVFAVSdRIVVIRQGHV 207
Cdd:TIGR00957 1448 ATAAVDLETDNLIQSTI-RTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-223 |
4.65e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.96 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSireadrmgiasvfqgQEFCDNLDVASN 88
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQ---------------QAWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LFLGKEINQigirdddsmnSRARSV---------LKTLSSAIR--VGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:TIGR00957 719 ILFGKALNE----------KYYQQVleacallpdLEILPSGDRteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 158 AALSVMQSAEVLAYIKRLRS--EGRSVVMVCHD---LPDVfavsDRIVVIRQGHVTGVhrtveTSYEEIIA 223
Cdd:TIGR00957 789 SAVDAHVGKHIFEHVIGPEGvlKNKTRILVTHGisyLPQV----DVIIVMSGGKISEM-----GSYQELLQ 850
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
9-187 |
6.85e-10 |
|
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: 56.78 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYlngeqvtIPsireadrmgiasvfqgqeFCDNLdvasn 88
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-------MP------------------EGEDL----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LFLGKeinqigirdddsmnsRARSVLKTLSSAI-----RVgspiasLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVM 163
Cdd:cd03223 67 LFLPQ---------------RPYLPLGTLREQLiypwdDV------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180
....*....|....*....|....
gi 1626716271 164 QSAEVLAyikRLRSEGRSVVMVCH 187
Cdd:cd03223 126 SEDRLYQ---LLKELGITVISVGH 146
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
9-207 |
7.46e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 7.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGeqVTIPSIREAD---RMGI---ASV-FQGQ-EFc 80
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--CDISKFGLMDlrkVLGIipqAPVlFSGTvRF- 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 dNLDVASnlflgkEINqigirDDDSMNSRARSVLKtlsSAIR---------VGSPIASLSVGQRQTVAIARTLLNDPQLI 151
Cdd:PLN03130 1332 -NLDPFN------EHN-----DADLWESLERAHLK---DVIRrnslgldaeVSEAGENFSVGQRQLLSLARALLRRSKIL 1396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1626716271 152 LLDEPTAALSVMQSAEVLayiKRLRSEGRSVVM--VCHDLPDVFAvSDRIVVIRQGHV 207
Cdd:PLN03130 1397 VLDEATAAVDVRTDALIQ---KTIREEFKSCTMliIAHRLNTIID-CDRILVLDAGRV 1450
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
9-207 |
1.05e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPG-FGHIYLNGEQVTIP--------SIREADRMGiaSVFQGQEF 79
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPqvswifnaTVRENILFG--SDFESERY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 CDNLDVAS-----NLFLGKEINQIGIRDddsmnsrarsvlktlssairvgspiASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:PLN03232 711 WRAIDVTAlqhdlDLLPGRDLTEIGERG-------------------------VNISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 155 EPTAALSVMQSAEVLAYIKRLRSEGRSVVMVC---HDLPDVfavsDRIVVIRQGHV 207
Cdd:PLN03232 766 DPLSALDAHVAHQVFDSCMKDELKGKTRVLVTnqlHFLPLM----DRIILVSEGMI 817
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
9-272 |
2.13e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQP-GFGHIYLNGEQVTIP--------SIReaDRMGIASVFQGQEF 79
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTVAYVPqvswifnaTVR--DNILFGSPFDPERY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 80 CDNLDVAS-----NLFLGKEINQIGIRDddsmnsrarsvlktlssairvgspiASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:PLN03130 711 ERAIDVTAlqhdlDLLPGGDLTEIGERG-------------------------VNISGGQKQRVSMARAVYSNSDVYIFD 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 155 EPTAALSVMQSAEVlaYIKRLRSE--GRSVVMVC---HDLPDVfavsDRIVVIRQGHVTGvhrtvETSYEEIIA------ 223
Cdd:PLN03130 766 DPLSALDAHVGRQV--FDKCIKDElrGKTRVLVTnqlHFLSQV----DRIILVHEGMIKE-----EGTYEELSNngplfq 834
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 224 ---EIAGvttehEYEEIAENPKfdsmvrqRKLIDRTISAAVSHGTGHDSPLD 272
Cdd:PLN03130 835 klmENAG-----KMEEYVEENG-------EEEDDQTSSKPVANGNANNLKKD 874
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
18-206 |
2.61e-09 |
|
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: 54.69 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 18 RQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGH-IYLNGEqvtipsireadrmgiasvfqgqefcdnldvasnlflgkein 96
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 97 qigirdddsmnsRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYI---- 172
Cdd:smart00382 40 ------------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1626716271 173 --KRLRSEGRSVVMVCHDLPD-----VFAVSDRIVVIRQGH 206
Cdd:smart00382 108 llLLKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLIL 148
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
6-211 |
2.72e-09 |
|
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: 55.02 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIagflqpgfghIYLNGEQVTIPSIREADRMGIASVfqgqefcDNLDV 85
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG----------LYASGKARLISFLPKFSRNKLIFI-------DQLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 86 ASNLFLGkeinqigirdddsmnsrarsvlktlssAIRVGSPIASLSVGQRQTVAIARTLLNDPQ--LILLDEPTAALSVM 163
Cdd:cd03238 71 LIDVGLG---------------------------YLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 164 QSAEVLAYIKRLRSEGRSVVMVCHDlPDVFAVSDRIVVIrqGHVTGVH 211
Cdd:cd03238 124 DINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWIIDF--GPGSGKS 168
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-206 |
8.60e-09 |
|
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: 56.07 E-value: 8.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSireadrmgIASVFQGQefcdnldVASN 88
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQ--------TSWIMPGT-------IKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LFLGKEINQIgirdddsmnsRARSVLKT--LSSAIRV---------GSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:TIGR01271 507 IIFGLSYDEY----------RYTSVIKAcqLEEDIALfpekdktvlGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1626716271 158 AALSVMQSAEVL--AYIKRLRSEGRsvVMVCHDLpDVFAVSDRIVVIRQGH 206
Cdd:TIGR01271 577 THLDVVTEKEIFesCLCKLMSNKTR--ILVTSKL-EHLKKADKILLLHEGV 624
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-207 |
1.30e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.75 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 4 GFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT---IPSIREADRMGIAS--VFQGQ- 77
Cdd:PLN03232 1247 GLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfgLTDLRRVLSIIPQSpvLFSGTv 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 78 EFcdNLDVAS---NLFLGKEINQIGIRDDDSMNSRArsvlktLSSAIRVGSpiASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:PLN03232 1327 RF--NIDPFSehnDADLWEALERAHIKDVIDRNPFG------LDAEVSEGG--ENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 155 EPTAALSVMQSAEVLayiKRLRSEGRSVVM--VCHDLPDVFAVsDRIVVIRQGHV 207
Cdd:PLN03232 1397 EATASVDVRTDSLIQ---RTIREEFKSCTMlvIAHRLNTIIDC-DKILVLSSGQV 1447
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-191 |
1.43e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 24 IVGDNGAGKSTLIKVIAGFLQPGFG-HIYLNGEQ----VTIPSIREadRMGIASVFQGQEFCDNLDVaSNLFLGKEINQI 98
Cdd:PRK10938 291 IVGPNGAGKSTLLSLITGDHPQGYSnDLTLFGRRrgsgETIWDIKK--HIGYVSSSLHLDYRVSTSV-RNVILSGFFDSI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 99 GIRD--DDSMNSRARSVLKTLSSAIRVG-SPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRL 175
Cdd:PRK10938 368 GIYQavSDRQQKLAQQWLDILGIDKRTAdAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVL 447
|
170 180
....*....|....*....|
gi 1626716271 176 RSEGRS-VVMVCH---DLPD 191
Cdd:PRK10938 448 ISEGETqLLFVSHhaeDAPA 467
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-205 |
2.59e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 20 EVIAIVGDNGAGKSTLIKVIAgflqpgfghiylngEQVTIPSIREADRM----GIASVFQGQE-FCDNLDVASNLFLGKE 94
Cdd:TIGR00956 790 TLTALMGASGAGKTTLLNVLA--------------ERVTTGVITGGDRLvngrPLDSSFQRSIgYVQQQDLHLPTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 95 I----------NQIGIRDDDSMNSRARSVL--KTLSSAIrVGSPIASLSVGQRQTVAIARTLLNDPQLIL-LDEPTAALS 161
Cdd:TIGR00956 856 SlrfsaylrqpKSVSKSEKMEYVEEVIKLLemESYADAV-VGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1626716271 162 VMQSAEVLAYIKRLRSEGRSVVMVCHDlP--DVFAVSDRIVVIRQG 205
Cdd:TIGR00956 935 SQTAWSICKLMRKLADHGQAILCTIHQ-PsaILFEEFDRLLLLQKG 979
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
8-207 |
3.41e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.59 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQ-PG---FGHIYLNGEQVTIPSIREADRM---GIASVFQGQEFC 80
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGrvmAEKLEFNGQDLQRISEKERRNLvgaEVAMIFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 81 DN--LDVASNLFLGKEINQIGIRDddsmNSRARSVlkTLSSAIRVGSPIASLSV-------GQRQTVAIARTLLNDPQLI 151
Cdd:PRK11022 102 LNpcYTVGFQIMEAIKVHQGGNKK----TRRQRAI--DLLNQVGIPDPASRLDVyphqlsgGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 152 LLDEPTAALSVMQSAEVLAYIKRL-RSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-223 |
3.71e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGhiylngeqvtipSIREADRMGIASVFQGQEFcdnlDVASN 88
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG------------TVKWSENANIGYYAQDHAY----DFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LFLGKEINQ-IGIRDDDSMnsrARSVL-KTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSvMQSA 166
Cdd:PRK15064 399 LTLFDWMSQwRQEGDDEQA---VRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD-MESI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1626716271 167 EVL-----AYikrlrsEGrSVVMVCHDLPDVFAVSDRIVVIRQGHVTGVHRTvetsYEEIIA 223
Cdd:PRK15064 475 ESLnmaleKY------EG-TLIFVSHDREFVSSLATRIIEITPDGVVDFSGT----YEEYLR 525
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-207 |
6.78e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.32 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 6 VEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQV-TIPSIR-EADRMGIASVFQgqEFCDNL 83
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGKlQALRRDIQFIFQ--DPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 DvaSNLFLGKEINQI----GIRDDDSMNSRARSVLKtlssaiRVG-SPIAS------LSVGQRQTVAIARTLLNDPQLIL 152
Cdd:PRK10261 415 D--PRQTVGDSIMEPlrvhGLLPGKAAAARVAWLLE------RVGlLPEHAwrypheFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 153 LDEPTAALSVMQSAEVLAYIKRLRSE-GRSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
9-168 |
1.27e-07 |
|
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: 51.78 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGhiylngeqvtipSIREADRMGIASVFQgqeFCDNLDVASN 88
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG------------KIKHSGRISFSSQFS---WIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LFLGKEINQIgirdddsmnsRARSVLKT--LSSAIR---------VGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:cd03291 118 IIFGVSYDEY----------RYKSVVKAcqLEEDITkfpekdntvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170
....*....|.
gi 1626716271 158 AALSVMQSAEV 168
Cdd:cd03291 188 GYLDVFTEKEI 198
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-200 |
1.79e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.94 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 121 IRVGSPIASLSVGQRQTVAIARTLL---NDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLpDVFAVSD 197
Cdd:TIGR00630 821 IRLGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL-DVIKTAD 899
|
...
gi 1626716271 198 RIV 200
Cdd:TIGR00630 900 YII 902
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-191 |
1.96e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 13 NLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPgfghiyLNGEQVTipSIREADRMGIASVFQ--GQEFCDN----LDVA 86
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPL------LSGERQS--QFSHITRLSFEQLQKlvSDEWQRNntdmLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 87 SNLFlGKEINQIgIRDDDSMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL---SVM 163
Cdd:PRK10938 95 EDDT-GRTTAEI-IQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLdvaSRQ 172
|
170 180 190
....*....|....*....|....*....|.
gi 1626716271 164 QSAEVLAyikRLRSEGRSVVMVC---HDLPD 191
Cdd:PRK10938 173 QLAELLA---SLHQSGITLVLVLnrfDEIPD 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1-157 |
2.58e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 1 MKFG-FVeALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMGIAS------- 72
Cdd:NF033858 274 MRFGdFT-AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSqafslyg 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 73 ---VFQgqefcdNLDVASNLF-LGKEinQIGIRDDDSMnsrAR----SVLKTLSsairvgspiASLSVGQRQTVAIARTL 144
Cdd:NF033858 353 eltVRQ------NLELHARLFhLPAA--EIAARVAEML---ERfdlaDVADALP---------DSLPLGIRQRLSLAVAV 412
|
170
....*....|...
gi 1626716271 145 LNDPQLILLDEPT 157
Cdd:NF033858 413 IHKPELLILDEPT 425
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
9-200 |
3.56e-07 |
|
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: 49.92 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIagfLQPGFGHiYLNGEQVT------------IPSIREADRMGI------ 70
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDT---LYPALAR-RLHLKKEQpgnhdrieglehIDKVIVIDQSPIgrtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 71 -----ASVFQG--QEFCD-------NLDVASNLFLGKEINQI-GIRDDDSMN-----SRARSVLKTLSSA----IRVGSP 126
Cdd:cd03271 87 npatyTGVFDEirELFCEvckgkryNRETLEVRYKGKSIADVlDMTVEEALEffeniPKIARKLQTLCDVglgyIKLGQP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1626716271 127 IASLSVGQRQTVAIARTLLN---DPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLpDVFAVSDRIV 200
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL-DVIKCADWII 242
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
9-211 |
5.31e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.18 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLikviagflqpGFGHIYLNGEQVTIPSIREADRMgiasvFQGQEFCDNLDVASN 88
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL----------AFDTIYAEGQRRYVESLSAYARQ-----FLGQMDKPDVDSIEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LFLGKEINQIGIrdddSMNSR-----------------ARSVLKT-LSSAIRVGSP-------IASLSVGQRQTVAIART 143
Cdd:cd03270 76 LSPAIAIDQKTT----SRNPRstvgtvteiydylrllfARVGIRErLGFLVDVGLGyltlsrsAPTLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 144 LLNDPQLIL--LDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDlPDVFAVSDRIVVIRQGhvTGVH 211
Cdd:cd03270 152 IGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHVIDIGPG--AGVH 218
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
8-231 |
5.78e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.27 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIpsireadrmGIASVFQGQ-EFCDNLDVa 86
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALI---------AISSGLNGQlTGIENIEL- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 87 SNLFLG---KEINQIgirdddsmnsrARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEptaALSVM 163
Cdd:PRK13545 109 KGLMMGltkEKIKEI-----------IPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE---ALSVG 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1626716271 164 Q---SAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVT--GVHRTVETSYEEIIAEIAGVTTE 231
Cdd:PRK13545 175 DqtfTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKeyGDIKEVVDHYDEFLKKYNQMSVE 247
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
8-224 |
7.55e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.04 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 8 ALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIpsireADRMGIASVFQGQEfcdNLDVAS 87
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVI-----AISAGLSGQLTGIE---NIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 nLFLG---KEINQIgirdddsmnsrARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEptaALSVMQ 164
Cdd:PRK13546 111 -LCMGfkrKEIKAM-----------TPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 165 ---SAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVT--GVHRTVETSYEEIIAE 224
Cdd:PRK13546 176 qtfAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKdyGELDDVLPKYEAFLND 240
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-266 |
1.44e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.58 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAG--KSTLIKVIAGflqPGFGH---------IYLNGEQVTIPSIREAdRMGIA 71
Cdd:NF000106 23 FGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRrpwrf*twcANRRALRRTIG*HRPV-R*GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 72 SVFQGQEfcdnldvasNLFLGKEINQIGIRDddsMNSRARSVLKTLSSAIRVGSPIASLSVGQRQTVAIARTLLNDPQLI 151
Cdd:NF000106 99 ESFSGRE---------NLYMIGR*LDLSRKD---ARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 152 LLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQGHVTGvhrtvETSYEEIIAEIAGVTTE 231
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA-----DGKVDELKTKVGGRTLQ 241
|
250 260 270
....*....|....*....|....*....|....*
gi 1626716271 232 HEYEEIAENPKFDSMVRQRKLiDRTISAAVSHGTG 266
Cdd:NF000106 242 IRPAHAAELDRMVGAIAQAGL-DGIAGATADHEDG 275
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-207 |
1.51e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLngeqvtipsireADRMGIASVFQGQ-EFcdnldvas 87
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------------AKGIKLGYFAQHQlEF-------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 88 nlflgkeinqigIRDDDS-MNSRARSVLKTLSSAIR------------VGSPIASLSVGQRQTVAIARTLLNDPQLILLD 154
Cdd:PRK10636 388 ------------LRADESpLQHLARLAPQELEQKLRdylggfgfqgdkVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1626716271 155 EPTAALSV-MQSAEVLAYIKrlrSEGrSVVMVCHDLPDVFAVSDRIVVIRQGHV 207
Cdd:PRK10636 456 EPTNHLDLdMRQALTEALID---FEG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
24-161 |
2.20e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 24 IVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTipsireadrmGIASVFQGQefcdnldVASNLFLGKEINqigIRDD 103
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN----------NIAKPYCTY-------IGHNLGLKLEMT---VFEN 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1626716271 104 DSMNSRARSVLKTLSSAIR-------VGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALS 161
Cdd:PRK13541 91 LKFWSEIYNSAETLYAAIHyfklhdlLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-204 |
2.71e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 22 IAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNG-------EQVTiPSIreaDRMGIASVFQG----QEFCDNLDVASNLF 90
Cdd:PRK10636 30 VGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvNQET-PAL---PQPALEYVIDGdreyRQLEAQLHDANERN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 91 LGKEINQIGIRDDD----SMNSRARSVLKTLS-SAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVmqs 165
Cdd:PRK10636 106 DGHAIATIHGKLDAidawTIRSRAASLLHGLGfSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL--- 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 1626716271 166 AEVLAYIKRLRSEGRSVVMVCHDLPDVFAVSDRIVVIRQ 204
Cdd:PRK10636 183 DAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-208 |
3.24e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 46.87 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGF---GHIYLNGEQVTIpsireadrmgIASVFQGQE-FCDNLD 84
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKE----------FAEKYPGEIiYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 85 VasnlflgkEINQIGIRDddsmnsrarsvlkTLSSAIRV-GSPIAS-LSVGQRQTVAIARTLLNDPQLILLDEPTAALSV 162
Cdd:cd03233 93 V--------HFPTLTVRE-------------TLDFALRCkGNEFVRgISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 163 MQSAEVLAYIKRLRSEGRSVVMVC--HDLPDVFAVSDRIVVIRQGHVT 208
Cdd:cd03233 152 STALEILKCIRTMADVLKTTTFVSlyQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
9-207 |
3.94e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVTIPSIREADRMgIASVFQGQEFCD-----NL 83
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ-FSMIPQDPVLFDgtvrqNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 84 DV---ASNLFLGKEINQIGIRDddsmnsRARSVLKTLSSAIRVGSpiASLSVGQRQTVAIARTLLN-DPQLILLDEPTA- 158
Cdd:PTZ00243 1405 DPfleASSAEVWAALELVGLRE------RVASESEGIDSRVLEGG--SNYSVGQRQLMCMARALLKkGSGFILMDEATAn 1476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1626716271 159 ---ALSVMQSAEVL----AYikrlrsegrSVVMVCHDLPDVfAVSDRIVVIRQGHV 207
Cdd:PTZ00243 1477 idpALDRQIQATVMsafsAY---------TVITIAHRLHTV-AQYDKIIVMDHGAV 1522
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-209 |
1.92e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 123 VGSPIASLSVGQRQTVAIARTLL---NDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDlPDVFAVSDRI 199
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHD-PALLKQADYL 1771
|
90
....*....|
gi 1626716271 200 vvIRQGHVTG 209
Cdd:PRK00635 1772 --IEMGPGSG 1779
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
117-205 |
2.87e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 117 LSSAIRVGSP-------IASLSVGQRQTVAIARTLLNDPQLI--LLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCH 187
Cdd:PRK00635 457 LSILIDLGLPyltperaLATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH 536
|
90
....*....|....*...
gi 1626716271 188 DlPDVFAVSDRIVVIRQG 205
Cdd:PRK00635 537 D-EQMISLADRIIDIGPG 553
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
11-156 |
6.06e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 43.45 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 11 SVNLSIQRQeVIAIVGDNGAGKSTLIKVIAGFLQP--------GFGHIYLNGEQ----------------VTIPSIREAD 66
Cdd:COG3950 18 EIDFDNPPR-LTVLVGENGSGKTTLLEAIALALSGllsrlddvKFRKLLIRNGEfgdsaklilyygtsrlLLDGPLKKLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 67 RMGIASVFQGQEFCDNLDVASNL-----FLGKEINQIGIRDDDSMNSRARSVLKTLSSA------IRVGS---------- 125
Cdd:COG3950 97 RLKEEYFSRLDGYDSLLDEDSNLrefleWLREYLEDLENKLSDELDEKLEAVREALNKLlpdfkdIRIDRdpgrlvildk 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1626716271 126 -----PIASLSVGQRQTVA----IARTL----------LNDPQLILLDEP 156
Cdd:COG3950 177 ngeelPLNQLSDGERSLLAlvgdLARRLaelnpalenpLEGEGIVLIDEI 226
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
24-187 |
7.25e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 42.83 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 24 IVGDNGAGKSTLIKVIA---GFLQPGfGHIYLN----------GEQVTIpsIREADRMGIASVFQGQEFcdnLDVASNlf 90
Cdd:COG3910 42 FVGENGSGKSTLLEAIAvaaGFNPEG-GSKNFRfstresesalGEYLRL--SRGLPKPRDGFFLRAESF---FNVATY-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 91 lgkeINQIGIRDDDSMNSRArsvlktlssairvGSPIASLSVGQrQTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLA 170
Cdd:COG3910 114 ----LDELAAEGPGILDSYG-------------GRSLHEQSHGE-SFLALFENRFRGNGLYLLDEPEAALSPSRQLALLA 175
|
170
....*....|....*..
gi 1626716271 171 YIKRLRSEGRSVVMVCH 187
Cdd:COG3910 176 LIHDLVREGSQFIIATH 192
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
7-187 |
8.18e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.86 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 7 EALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGF--LQPGFGHIYLNGEQVTIPSIREADRMGIASVFQ--------- 75
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQypveipgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 76 ----------------GQEFCDNLDVASnlFLGKEINQIGIRDDdsmnsrarsvlkTLSSAIRVGspiasLSVGQRQTVA 139
Cdd:PRK09580 95 nqfflqtalnavrsyrGQEPLDRFDFQD--LMEEKIALLKMPED------------LLTRSVNVG-----FSGGEKKRND 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 140 IARTLLNDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCH 187
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
9-207 |
1.20e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYlngeqvtipsireADRmGIASVFQgQEFCDNLDVASN 88
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------------AER-SIAYVPQ-QAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 89 LFLGKEINQIGIRDDDSMnSRARSVLKTLSSAI--RVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAALSVMQSA 166
Cdd:PTZ00243 741 ILFFDEEDAARLADAVRV-SQLEADLAQLGGGLetEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1626716271 167 EVLAYIKRLRSEGRSVVMVCHDLpDVFAVSDRIVVIRQGHV 207
Cdd:PTZ00243 820 RVVEECFLGALAGKTRVLATHQV-HVVPRADYVVALGDGRV 859
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
9-226 |
1.21e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.68 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQrQEVIAIVGDNGAGKSTLIKVIAGFLQPGFG-----HIYLNGEQVTIPSIR-EADrmgIASVF-------- 74
Cdd:COG3593 14 IKDLSIELS-DDLTVLVGENNSGKSSILEALRLLLGPSSSrkfdeEDFYLGDDPDLPEIEiELT---FGSLLsrllrlll 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 75 ---QGQEFCDNLDVASNLF------LGKEINQIGIRDDDSMNSRARSVLKTLSSAIRV---------GSPIASLSVGQRQ 136
Cdd:COG3593 90 keeDKEELEEALEELNEELkealkaLNELLSEYLKELLDGLDLELELSLDELEDLLKSlslriedgkELPLDRLGSGFQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 137 TVAIA--RTLL-----NDPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDlPDVFAVS--DRIVVIRQGHV 207
Cdd:COG3593 170 LILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHS-PHLLSEVplENIRRLRRDSG 248
|
250
....*....|....*....
gi 1626716271 208 TGVHRTVETSYEEIIAEIA 226
Cdd:COG3593 249 GTTSTKLIDLDDEDLRKLL 267
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
23-206 |
1.57e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.82 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 23 AIVGDNGAGKSTLIKVIAGFLqpgFGHIYLNGEQVTIPS--IREADRMGIASVfqgqEFCDNLDV------ASNLFLgke 94
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYAL---TGELPPNSKGGAHDPklIREGEVRAQVKL----AFENANGKkytitrSLAILE--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 95 iNQIGIRDDDSmNSRARSVLKTLSSAIRVgspIASLSVgqrqTVAIARTLLNDPQLILLDEPTAALSVMQSAEVLAYI-- 172
Cdd:cd03240 96 -NVIFCHQGES-NWPLLDMRGRCSGGEKV---LASLII----RLALAETFGSNCGILALDEPTTNLDEENIEESLAEIie 166
|
170 180 190
....*....|....*....|....*....|....*
gi 1626716271 173 KRLRSEGRSVVMVCHDlPDVFAVSDRIV-VIRQGH 206
Cdd:cd03240 167 ERKSQKNFQLIVITHD-EELVDAADHIYrVEKDGR 200
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-200 |
2.26e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 123 VGSPIASLSVGQRQTVAIARTLLN---DPQLILLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDLpDVFAVSDRI 199
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYV 881
|
.
gi 1626716271 200 V 200
Cdd:PRK00635 882 L 882
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
102-160 |
9.34e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 9.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 102 DDDSMNSRARSVLKTLS-SAIRVGSPIASLSVGQRQTVAIARTLLNDPQLILLDEPTAAL 160
Cdd:PLN03073 316 DAYTAEARAASILAGLSfTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHL 375
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-229 |
1.86e-03 |
|
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: 39.61 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 126 PIASLSVGQRQTVAIARTLlnDPQLI----LLDEPTAALSVMQSAEVLAYIKRLRSEGRSVVMVCHDlPDVFAVSDRIVV 201
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQI--GSGLTgvlyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAADYVID 561
|
90 100 110
....*....|....*....|....*....|.
gi 1626716271 202 IRQGhvTGVH--RTV-ETSYEEIIAEIAGVT 229
Cdd:TIGR00630 562 IGPG--AGEHggEVVaSGTPEEILANPDSLT 590
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
9-205 |
2.56e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 38.35 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 9 LKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGFLQPGFGHIYLNGEQVT-IPSIREADRMGI----ASVFQGQ-EFcdN 82
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISkLPLHTLRSRLSIilqdPILFSGSiRF--N 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 83 LD-----VASNLFLGKEINQigirdddsMNSRARSVLKTLSSAIRVGSpiASLSVGQRQTVAIARTLLNDPQLILLDEPT 157
Cdd:cd03288 115 LDpeckcTDDRLWEALEIAQ--------LKNMVKSLPGGLDAVVTEGG--ENFSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1626716271 158 AALSvMQSAEVLAYIKRLRSEGRSVVMVCHDLPDVFAvSDRIVVIRQG 205
Cdd:cd03288 185 ASID-MATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRG 230
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
130-203 |
4.00e-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: 36.95 E-value: 4.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1626716271 130 LSVGQRQTVAIARTL----LNDPQLILLDEPTAALSvMQSAEVLAY-IKRLRSEGRSVVMVCHDlPDVFAVSDRIVVIR 203
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLD-PRDGQALAEaILEHLVKGAQVIVITHL-PELAELADKLIHIK 154
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-157 |
7.13e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 37.80 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 3 FGFVEALKSVNLSIQRQEVIAIVGDNGAGKSTLIKVIAGF--LQPgfGHIYLNGEQVTIPSIREADRMGIA--------- 71
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGArkIQQ--GRVEVLGGDMADARHRRAVCPRIAympqglgkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1626716271 72 -----SVFqgqefcDNLDVASNLF-LGKEinqigirdddsmnSRARSVLKTLSS------AIRvgsPIASLSVGQRQTVA 139
Cdd:NF033858 89 lyptlSVF------ENLDFFGRLFgQDAA-------------ERRRRIDELLRAtglapfADR---PAGKLSGGMKQKLG 146
|
170
....*....|....*...
gi 1626716271 140 IARTLLNDPQLILLDEPT 157
Cdd:NF033858 147 LCCALIHDPDLLILDEPT 164
|
|
| |
