|
Name |
Accession |
Description |
Interval |
E-value |
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
32-281 |
5.54e-102 |
|
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: 298.15 E-value: 5.54e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSG-TIRLFQETYGEIAIQDLRKRI 110
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 111 GILDSSQQENsIQRKLTVKDTILTGLFHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVN 190
Cdd:COG1119 81 GLVSPALQLR-FPRDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 191 EPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKNLEDL 270
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEA 239
|
250
....*....|.
4HZI_A 271 YDIPLQVQRIE 281
Cdd:COG1119 240 FGLPVEVERRD 250
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
34-288 |
8.67e-54 |
|
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: 175.62 E-value: 8.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGIL 113
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 dssQQENSIQRKLTVKDTILTGLFHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPD 193
Cdd:COG1120 81 ---PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 194 FLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKNLEDLYDI 273
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGV 237
|
250
....*....|....*..
4HZI_A 274 PLQVQRIENT--WSVIP 288
Cdd:COG1120 238 EARVIEDPVTgrPLVLP 254
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
32-279 |
7.07e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 172.97 E-value: 7.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETygeiaIQDLRKRIG 111
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 112 ILdsSQQEnSIQR--KLTVKDTILTGLFHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIV 189
Cdd:COG1121 79 YV--PQRA-EVDWdfPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 190 NEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGkVIHFGPIEECFTEKNLED 269
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGK-TILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSR 233
|
250
....*....|
4HZI_A 270 LYDIPLQVQR 279
Cdd:COG1121 234 AYGGPVALLA 243
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
34-271 |
6.50e-44 |
|
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: 149.62 E-value: 6.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQdLRKRIGIL 113
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 dssQQENSIQRKLTVKDTILtgLFHTIgyYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPD 193
Cdd:COG4555 80 ---PDERGLYDRLTVRENIR--YFAEL--YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 194 FLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIE---ECFTEKNLEDL 270
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDelrEEIGEENLEDA 231
|
.
4HZI_A 271 Y 271
Cdd:COG4555 232 F 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
46-271 |
1.26e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.67 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQdLRKRIGILdssQQENSIQRK 125
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV---PQEPALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 126 LTVKDTiltgLFHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLD 205
Cdd:COG1131 88 LTVREN----LRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
4HZI_A 206 LTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEEcFTEKNLEDLY 271
Cdd:COG1131 164 PEARRELWELLRELAAEGK-TVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE-LKARLLEDVF 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
35-267 |
3.36e-43 |
|
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: 147.48 E-value: 3.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYK-PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGIL 113
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 --DSSQQensiqrkL---TVKDTILTGLFHtIGYyrdpSPEE-ETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRS 187
Cdd:COG1122 81 fqNPDDQ-------LfapTVEEDVAFGPEN-LGL----PREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 188 IVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKNL 267
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
36-256 |
8.47e-43 |
|
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: 145.75 E-value: 8.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 36 SLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFqetyGEiAIQDLRKRIGILds 115
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF----GK-PLEKERKRIGYV-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 116 SQQEnSIQRK--LTVKDTILTGLFHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPD 193
Cdd:cd03235 74 PQRR-SIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
4HZI_A 194 FLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKeGKVIHFG 256
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
36-256 |
1.50e-38 |
|
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: 133.71 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 36 SLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILds 115
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 116 sqqensiqrkltvkdtiltglfhtigyyrdpspeeetktLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFL 195
Cdd:cd03214 79 ---------------------------------------PQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
4HZI_A 196 IMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
44-271 |
1.99e-38 |
|
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: 135.39 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 44 PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLF---QETYGEIAIQDLRKRIGILdsSQQEN 120
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdINKLKGKALRQLRRQIGMI--FQQFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 SIQRkLTVKDTILTGLFHTIGYYRD----PSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLI 196
Cdd:cd03256 89 LIER-LSVLENVLSGRLGRRSTWRSlfglFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
4HZI_A 197 MDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEEcFTEKNLEDLY 271
Cdd:cd03256 168 ADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVLDEIY 241
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
41-251 |
1.04e-37 |
|
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: 132.59 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 41 SYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGIL--DSSQQ 118
Cdd:cd03225 8 SYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVfqNPDDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 119 ensIQrKLTVKDTILTGLFHtigyYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMD 198
Cdd:cd03225 88 ---FF-GPTVEEEVAFGLEN----LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
4HZI_A 199 EPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGK 251
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
34-279 |
7.13e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 129.08 E-value: 7.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGIL 113
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 dssQQENSIQRKLTVKDTILTGLFHtigyYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLR------- 186
Cdd:COG4559 81 ---PQHSSLAFPFTVEEVVALGRAP----HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARvlaqlwe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 187 SIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYhSKKKFTSLYITHrpeeipD------FYSKAVLLKEGKVIHFGPIEE 260
Cdd:COG4559 154 PVDGGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLH------DlnlaaqYADRILLLHQGRLVAQGTPEE 226
|
250
....*....|....*....
4HZI_A 261 CFTEKNLEDLYDIPLQVQR 279
Cdd:COG4559 227 VLTDELLERVYGADLRVLA 245
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
35-252 |
2.17e-33 |
|
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: 120.20 E-value: 2.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIqDLRKRIGILd 114
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 115 ssQQENSIQRKLTVKDTIltglfhtigyyrdpspeeetktlqilkdsdllskkdqlynTLSSGEKKKILFLRSIVNEPDF 194
Cdd:cd03230 79 --PEEPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
4HZI_A 195 LIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKV 252
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEGK-TILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
35-237 |
3.73e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 120.69 E-value: 3.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILd 114
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 115 ssQQENSIqrkltVKDTILTGLFHTIGYY-RDPSPEEETKTLQILK-DSDLLSKKdqlYNTLSSGEKKKILFLRSIVNEP 192
Cdd:COG4619 80 --PQEPAL-----WGGTVRDNLPFPFQLReRKFDRERALELLERLGlPPDILDKP---VERLSGGERQRLALIRALLLQP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
4HZI_A 193 DFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEI 237
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQI 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
46-267 |
1.54e-32 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 122.91 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDsVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTI----RLFQETYGEIAIQDLRKRIGILdssQQENS 121
Cdd:TIGR02142 10 GDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngRTLFDSRKGIFLPPEKRRIGYV---FQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 122 IQRKLTVKDTILTGLFHTIGYYRDPSPEEETKTLQIlkdSDLLskkDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPC 201
Cdd:TIGR02142 86 LFPHLSVRGNLRYGMKRARPSERRISFERVIELLGI---GHLL---GRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
4HZI_A 202 SSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKNL 267
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
36-251 |
1.70e-32 |
|
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: 117.35 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 36 SLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILDS 115
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 116 sqqensiqrkltvkdtiltglfhtigyyrdpspeeetktlqilkdsdllskkdqlyntLSSGEKKKILFLRSIVNEPDFL 195
Cdd:cd00267 81 ----------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
4HZI_A 196 IMDEPCSSLDLTAREDFLGFLKEyHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGK 251
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRE-LAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
35-252 |
2.34e-32 |
|
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: 118.75 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKIS--YKPTGKT--ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQET---YGEIAIQDLR 107
Cdd:cd03255 1 IELKNLSktYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiskLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 108 -KRIGILdsSQQENSIQRkLTVKDTILTGLFhtigYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLR 186
Cdd:cd03255 81 rRHIGFV--FQSFNLLPD-LTALENVELPLL----LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
4HZI_A 187 SIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPeEIPDFYSKAVLLKEGKV 252
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
50-262 |
9.42e-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: 117.82 E-value: 9.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETygeiaIQDL---RKRIGILdssQQENSIQRKL 126
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKD-----ITNLppeKRDISYV---PQNYALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 127 TVKDTILTGLFHTigyyRDPSPEEETKTLQI---LKDSDLLSKKDQlynTLSSGEKKKILFLRSIVNEPDFLIMDEPCSS 203
Cdd:cd03299 87 TVYKNIAYGLKKR----KVDKKEIERKVLEIaemLGIDHLLNRKPE---TLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 204 LDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECF 262
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
27-260 |
3.25e-31 |
|
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: 122.64 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 27 FQGKInsllSLEKIS--YKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQ 104
Cdd:COG2274 470 LKGDI----ELENVSfrYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 105 DLRKRIGILDssqQENSIQRKlTVKDTILTGlfhtigyyrDPSPEEEtKTLQILKDSDLLSKKDQL---YNT-------- 173
Cdd:COG2274 546 SLRRQIGVVL---QDVFLFSG-TIRENITLG---------DPDATDE-EIIEAARLAGLHDFIEALpmgYDTvvgeggsn 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 174 LSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKkfTSLYITHRPEEIPDFySKAVLLKEGKVI 253
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRLA-DRIIVLDKGRIV 688
|
....*..
4HZI_A 254 HFGPIEE 260
Cdd:COG2274 689 EDGTHEE 695
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
46-256 |
1.16e-30 |
|
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: 114.15 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQdlRKRIGILdssQQENSIQRK 125
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV---FQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 126 LTVKDTILTGLFHTigyyRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLD 205
Cdd:cd03259 87 LTVAENIAFGLKLR----GVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
4HZI_A 206 LTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:cd03259 163 AKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
34-279 |
1.69e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 115.25 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGIL 113
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 dssQQENSIQRKLTVKDTILTGLfhtigyYRDPSPEEETKTL--QILKDSDLLSKKDQLYNTLSSGEKKKILFLR----- 186
Cdd:PRK13548 82 ---PQHSSLSFPFTVEEVVAMGR------APHGLSRAEDDALvaAALAQVDLAHLAGRDYPQLSGGEQQRVQLARvlaql 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 187 -SIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHrpeeipD------FYSKAVLLKEGKVIHFGPIE 259
Cdd:PRK13548 153 wEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLH------DlnlaarYADRIVLLHQGRLVADGTPA 226
|
250 260
....*....|....*....|
4HZI_A 260 ECFTEKNLEDLYDIPLQVQR 279
Cdd:PRK13548 227 EVLTPETLRRVYGADVLVQP 246
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
50-202 |
1.78e-30 |
|
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: 111.97 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILDssqQENSIQRKLTVK 129
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVF---QDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4HZI_A 130 DTILTGLfHTIGYYRDPSPEEETKTLQILKDSDLLSKK-DQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCS 202
Cdd:pfam00005 78 ENLRLGL-LLKGLSKREKDARAEEALEKLGLGDLADRPvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
35-251 |
1.69e-28 |
|
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: 107.66 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQE--TYGEIAIQDLRKRIGI 112
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdlTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 113 LdssQQENSIQRKLTVKDTILTGlfhtigyyrdpspeeetktlqilkdsdllskkdqlyntLSSGEKKKILFLRSIVNEP 192
Cdd:cd03229 81 V---FQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 193 DFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGK 251
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
47-256 |
1.77e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 108.52 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 47 KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAiqdlRKRIGILdssQQENSIQRKL 126
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYL---PEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 127 TVKDTILtglfhTIGYYRDPSPEEETK-TLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLD 205
Cdd:cd03269 86 KVIDQLV-----YLAQLKGLKKEEARRrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
4HZI_A 206 LTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:cd03269 161 PVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
35-253 |
4.04e-28 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 105.97 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQEtygEIAIQDLR--KRIGI 112
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK---EVSFASPRdaRRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 113 ldssqqensiqrkltvkdtiltGLFHtigyyrdpspeeetktlQilkdsdllskkdqlyntLSSGEKKKILFLRSIVNEP 192
Cdd:cd03216 78 ----------------------AMVY-----------------Q-----------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
4HZI_A 193 DFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVI 253
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGV-AVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
50-274 |
6.35e-28 |
|
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: 107.81 E-value: 6.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDlrKRIGILdssQQENSIQRKLTVK 129
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFV---FQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 130 DTILTGLFHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAR 209
Cdd:cd03296 93 DNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
4HZI_A 210 EDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEEcfteknledLYDIP 274
Cdd:cd03296 173 KELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE---------VYDHP 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
35-253 |
6.40e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 107.45 E-value: 6.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYK-PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEI---AIQDLRKRI 110
Cdd:COG2884 2 IRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 111 GILDssqQENSIQRKLTVKDTILTGLfHTIGYyrdPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVN 190
Cdd:COG2884 82 GVVF---QDFRLLPDRTVYENVALPL-RVTGK---SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
4HZI_A 191 EPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVI 253
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGT-TVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
35-256 |
1.71e-27 |
|
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: 105.74 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHcVLLGRNGAGKSTLVNLIYGMIWATSGTIRlFQETYGEIAIQDLRKRIGILd 114
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIR-IDGQDVLKQPQKLRRRIGYL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 115 ssQQENSIQRKLTVKD-----TILTGLfhtigyyrdPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIV 189
Cdd:cd03264 78 --PQEFGVYPNFTVREfldyiAWLKGI---------PSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 190 NEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKkfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
34-232 |
3.12e-27 |
|
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: 105.67 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYK-PTGK---TILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQE---TYGEIAIQDL 106
Cdd:cd03257 1 LLEVKNLSVSfPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 107 RKRIGIL--DSSqqeNSIQRKLTVKDTILTGLFHtigyYRDPSPEEETKTLQILKDSDLLSKKDQLY---NTLSSGEKKK 181
Cdd:cd03257 81 RKEIQMVfqDPM---SSLNPRMTIGEQIAEPLRI----HGKLSKKEARKEAVLLLLVGVGLPEEVLNrypHELSGGQRQR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
4HZI_A 182 ILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITH 232
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITH 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
41-251 |
4.48e-27 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 103.62 E-value: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 41 SYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILdssQQEn 120
Cdd:cd03228 9 SYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYV---PQD- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 siqrkltvkdtilTGLFH-TIgyyRDpspeeetktlqilkdsdllskkdqlyNTLSSGEKKKILFLRSIVNEPDFLIMDE 199
Cdd:cd03228 85 -------------PFLFSgTI---RE--------------------------NILSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
4HZI_A 200 PCSSLDLTAREDFLGFLKEYHSKKkfTSLYITHRPEEIPDFySKAVLLKEGK 251
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
37-260 |
4.51e-27 |
|
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: 104.89 E-value: 4.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 37 LEKIsYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrlfqeTYGEIAIQ----DLRKRIGI 112
Cdd:cd03263 6 LTKT-YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA-----YINGYSIRtdrkAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 113 ldsSQQENSIQRKLTVKDTIltgLFHTI--GYYRDPSPEEETKTLQILkdsDLLSKKDQLYNTLSSGEKKKILFLRSIVN 190
Cdd:cd03263 80 ---CPQFDALFDELTVREHL---RFYARlkGLPKSEIKEEVELLLRVL---GLTDKANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 191 EPDFLIMDEPCSSLDLTAREDFLGFLKEYhsKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
44-252 |
2.22e-26 |
|
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: 103.26 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 44 PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLF-QET--YGEIAIQDLRKRIGILdssQQEN 120
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgQDVsdLRGRAIPYLRRKIGVV---FQDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 SIQRKLTVKDTILTGLFHTigyyrDPSPEEETKTL-QILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDE 199
Cdd:cd03292 88 RLLPDRNVYENVAFALEVT-----GVPPREIRKRVpAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
4HZI_A 200 PCSSLDLTAREDFLGFLKEYHsKKKFTSLYITHrPEEIPDFYSKAVL-LKEGKV 252
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATH-AKELVDTTRHRVIaLERGKL 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
34-263 |
2.95e-26 |
|
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: 107.68 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISY-----KPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQE---TYGEIAIQD 105
Cdd:COG1123 260 LLEVRNLSKrypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 106 LRKRIGILdssQQ--ENSIQRKLTVKDTILTGL-FHTIGyyrdPSPEEETKTLQILK----DSDLLSKkdqlY-NTLSSG 177
Cdd:COG1123 340 LRRRVQMV---FQdpYSSLNPRMTVGDIIAEPLrLHGLL----SRAERRERVAELLErvglPPDLADR----YpHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 178 EKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHrpeeipD-----FYS-KAVLLKEGK 251
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISH------DlavvrYIAdRVAVMYDGR 482
|
250
....*....|..
4HZI_A 252 VIHFGPIEECFT 263
Cdd:COG1123 483 IVEDGPTEEVFA 494
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
32-254 |
3.99e-26 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 102.81 E-value: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKISYK-PTGK---TILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQE---TYGEIAIQ 104
Cdd:COG1136 2 SPLLELRNLTKSyGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 105 DLR-KRIGILdsSQQENSIQRkLTVKDTILTGLFhtigYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKIL 183
Cdd:COG1136 82 RLRrRHIGFV--FQFFNLLPE-LTALENVALPLL----LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4HZI_A 184 FLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPeEIPDFYSKAVLLKEGKVIH 254
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
32-263 |
5.56e-26 |
|
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: 106.91 E-value: 5.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLE--KISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWAT---SGTIRLFQETYGEIAIQDL 106
Cdd:COG1123 2 TPLLEVRdlSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 107 RKRIGIL--DSSQQENSiqrkLTVKDTILTGLFHTigyyRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILF 184
Cdd:COG1123 82 GRRIGMVfqDPMTQLNP----VTVGDQIAEALENL----GLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 185 LRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFT 263
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
38-260 |
6.10e-26 |
|
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: 102.06 E-value: 6.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 38 EKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFqetyGEIAIQD---LRKRIGILd 114
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVA----GHDVVREpreVRRRIGIV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 115 ssQQENSIQRKLTVKDTILtgLFHTIgyYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDF 194
Cdd:cd03265 79 --FQDLSVDDELTGWENLY--IHARL--YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
4HZI_A 195 LIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
34-262 |
6.15e-26 |
|
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: 102.27 E-value: 6.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKIS--YKPTGKTI--LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLF-QE--TYGEIAIQDL 106
Cdd:cd03258 1 MIELKNVSkvFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgTDltLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 107 RKRIGILdsSQQENSIQRKlTVKDTILTGLFHTigyyRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLR 186
Cdd:cd03258 81 RRRIGMI--FQHFNLLSSR-TVFENVALPLEIA----GVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
4HZI_A 187 SIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECF 262
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
34-239 |
6.36e-26 |
|
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: 101.40 E-value: 6.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETyGEIAIQDLRKRIGIL 113
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP-IRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 DssqQENSIQRKLTVKDTIltgLFHTIGYYRDPSPEEETKTLQILkdsDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPD 193
Cdd:COG4133 81 G---HADGLKPELTVRENL---RFWAALYGLRADREAIDEALEAV---GLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
4HZI_A 194 FLIMDEPCSSLDLTAREDFLGFLKEyHSKKKFTSLYITHRPEEIPD 239
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLELAA 196
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
53-256 |
1.07e-25 |
|
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: 101.22 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 53 VSFEIKTnEHCVLLGRNGAGKSTLVNLIYGMIWATSGTI----RLFQETYGEIAIQDLRKRIGILdssQQENSIQRKLTV 128
Cdd:cd03297 17 IDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngTVLFDSRKKINLPPQQRKIGLV---FQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 129 KDTILTGL-FHTIGYYRDpSPEEETKTLQIlkdSDLLSKKDQlynTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLT 207
Cdd:cd03297 93 RENLAFGLkRKRNREDRI-SVDELLDLLGL---DHLLNRYPA---QLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
4HZI_A 208 AREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
44-280 |
1.38e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.82 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 44 PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRL--FQETYGEIAIQDLRKRIGI--------- 112
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdgVDITDKKVKLSDIRKKVGLvfqypeyql 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 113 ---------------LDSSQQEnsIQRKltVKDTI-LTGLFHTIgyYRDPSPEEetktlqilkdsdllskkdqlyntLSS 176
Cdd:PRK13637 97 feetiekdiafgpinLGLSEEE--IENR--VKRAMnIVGLDYED--YKDKSPFE-----------------------LSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 177 GEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
250 260
....*....|....*....|....
4HZI_A 257 PIEECFteKNLEDLYDIPLQVQRI 280
Cdd:PRK13637 228 TPREVF--KEVETLESIGLAVPQV 249
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
41-234 |
1.98e-25 |
|
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: 100.74 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 41 SYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILdssQQEN 120
Cdd:cd03245 11 SYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYV---PQDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 SiqrkL---TVKDTILTGlfhtigyyrDPSPEEEtktlQILKDSDlLSKKDQLYNT---------------LSSGEKKKI 182
Cdd:cd03245 88 T----LfygTLRDNITLG---------APLADDE----RILRAAE-LAGVTDFVNKhpngldlqigergrgLSGGQRQAV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
4HZI_A 183 LFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKkfTSLYITHRP 234
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRP 199
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
36-253 |
2.22e-25 |
|
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: 100.02 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 36 SLEKISYK-PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQEtygEIAIQDLRKRIGILd 114
Cdd:cd03226 1 RIENISFSyKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERRKSIGYV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 115 sSQQENSIQRKLTVKDTILTGLfhtigyyrDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDF 194
Cdd:cd03226 77 -MQDVDYQLFTDSVREELLLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 195 LIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVI 253
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
36-282 |
3.04e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 100.93 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 36 SLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILds 115
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 116 sQQENSIQRKLTVKDTILTGLF-HTIGyyRdPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDF 194
Cdd:COG4604 81 -RQENHINSRLTVRELVAFGRFpYSKG--R-LTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 195 LIMDEPCSSLDLtaredflgflkeYHS-------------KKK----------FTSLYITHrpeeIpdfyskaVLLKEGK 251
Cdd:COG4604 157 VLLDEPLNNLDM------------KHSvqmmkllrrladeLGKtvvivlhdinFASCYADH----I-------VAMKDGR 213
|
250 260 270
....*....|....*....|....*....|.
4HZI_A 252 VIHFGPIEECFTEKNLEDLYDIPLQVQRIEN 282
Cdd:COG4604 214 VVAQGTPEEIITPEVLSDIYDTDIEVEEIDG 244
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
35-270 |
1.72e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 98.29 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKpTGKTILdSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIqDLRKrIGILd 114
Cdd:COG3840 2 LRLDDLTYR-YGDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERP-VSML- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 115 ssQQENSIQRKLTVKDTILTGLfhtigyyrDP----SPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVN 190
Cdd:COG3840 77 --FQENNLFPHLTVAQNIGLGL--------RPglklTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 191 EPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKNLEDL 270
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-260 |
1.76e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 99.80 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGeiaiQDLRKRIGILd 114
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGYL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 115 ssQQENSIQRKLTVKDTI-----LTGLfhtigyyrdPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIV 189
Cdd:COG4152 77 --PEERGLYPKMKVGEQLvylarLKGL---------SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4HZI_A 190 NEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGT-TVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDE 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
46-266 |
2.07e-24 |
|
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: 98.34 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQE---TYGEIAIQDLRKRIGIL-------DS 115
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisGLSEAELYRLRRRMGMLfqsgalfDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 116 sqqensiqrkLTVKDTILTGLF-HTigyyRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDF 194
Cdd:cd03261 92 ----------LTVFENVAFPLReHT----RLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
4HZI_A 195 LIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKN 266
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
35-260 |
3.89e-24 |
|
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: 97.61 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqetyGEIAIQDL----RKRI 110
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL-----DGQDITKLpmhkRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 111 GI--LdssQQENSIQRKLTVKDTILTGLfhtiGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSI 188
Cdd:cd03218 76 GIgyL---PQEASIFRKLTVEENILAVL----EIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4HZI_A 189 VNEPDFLIMDEPCSSLDLTAREDFLGFLKeyHSKKKFTSLYIT-HRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIK--ILKDRGIGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEE 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
34-260 |
7.18e-24 |
|
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: 97.18 E-value: 7.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKIS----YKPTGKTILDSVSFEIKTNEhCV-LLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRK 108
Cdd:COG1124 1 MLEVRNLSvsygQGGRRVPVLKDVSLEVAPGE-SFgLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 109 RIGILdsSQQ-ENSIQRKLTVKDTILTGL-FHTIgyyrdpsPEEETKTLQILK----DSDLLSKK-DQLyntlSSGEKKK 181
Cdd:COG1124 80 RVQMV--FQDpYASLHPRHTVDRILAEPLrIHGL-------PDREERIAELLEqvglPPSFLDRYpHQL----SGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 182 ILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
35-260 |
1.53e-23 |
|
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: 100.22 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYK-PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGIL 113
Cdd:COG4988 337 IELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 DssqqensiQR----KLTVKDTILTGLfhtigyyRDPSPEEetkTLQILKDSDLLSKKDQL---YNT--------LSSGE 178
Cdd:COG4988 417 P--------QNpylfAGTIRENLRLGR-------PDASDEE---LEAALEAAGLDEFVAALpdgLDTplgeggrgLSGGQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 179 KKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYhSKKKfTSLYITHRPEEIpDFYSKAVLLKEGKVIHFGPI 258
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGR-TVILITHRLALL-AQADRILVLDDGRIVEQGTH 555
|
..
4HZI_A 259 EE 260
Cdd:COG4988 556 EE 557
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-277 |
4.81e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 95.85 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKIS--YKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKR 109
Cdd:PRK13635 3 EEIIRVEHISfrYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 110 IGILdsSQQENSIQRKLTVKDTILTGLfHTIGYYRDPSPEEETKTLQILKDSDLLskkDQLYNTLSSGEKKKILFLRSIV 189
Cdd:PRK13635 83 VGMV--FQNPDNQFVGATVQDDVAFGL-ENIGVPREEMVERVDQALRQVGMEDFL---NREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 190 NEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPdFYSKAVLLKEGKVIHFGPIEECFteKNLED 269
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTPEEIF--KSGHM 233
|
....*...
4HZI_A 270 LYDIPLQV 277
Cdd:PRK13635 234 LQEIGLDV 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
35-247 |
6.40e-23 |
|
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: 94.08 E-value: 6.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISY----KPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFqetyGEiAIQDLRKRI 110
Cdd:cd03293 1 LEVRNVSKtyggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD----GE-PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 111 GILdssQQENSIQRKLTVKDTILTGLFHTigyyRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVN 190
Cdd:cd03293 76 GYV---FQQDALLPWLTVLDNVALGLELQ----GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
4HZI_A 191 EPDFLIMDEPCSSLD-LTA---REDFLGFLKEYhskkKFTSLYITHRPEEipdfyskAVLL 247
Cdd:cd03293 149 DPDVLLLDEPFSALDaLTReqlQEELLDIWRET----GKTVLLVTHDIDE-------AVFL 198
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
35-256 |
7.55e-23 |
|
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: 93.47 E-value: 7.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqetyGEIAIQDLR--KR-IG 111
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYI-----GGRDVTDLPpkDRdIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 112 ILdssQQENSIQRKLTVKDTILTGLfHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQlynTLSSGEKKKILFLRSIVNE 191
Cdd:cd03301 76 MV---FQNYALYPHMTVYDNIAFGL-KLRKVPKDEIDERVREVAELLQIEHLLDRKPK---QLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
4HZI_A 192 PDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
35-260 |
8.38e-23 |
|
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: 93.78 E-value: 8.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWA-----TSGTIRLFQETYGEIAIQD--LR 107
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVleLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 108 KRIGILdsSQQENSIqrKLTVKDTILTGLFHtigyyRDPSPEEETKTL--QILKDSDLLSK-KDQLYNT-LSSGEKKKIL 183
Cdd:cd03260 81 RRVGMV--FQKPNPF--PGSIYDNVAYGLRL-----HGIKLKEELDERveEALRKAALWDEvKDRLHALgLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 184 FLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYhsKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
46-268 |
8.95e-23 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 94.95 E-value: 8.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGeiaiQDLRKRIGILDSSQQENSIQRK 125
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLVAYVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 126 LTVKDTILTGLFHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLD 205
Cdd:PRK15056 95 VLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
4HZI_A 206 LTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKeGKVIHFGPIEECFTEKNLE 268
Cdd:PRK15056 175 VKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLE 235
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
33-260 |
9.54e-23 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 95.94 E-value: 9.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 33 SLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQdlRKRIGI 112
Cdd:COG3842 4 PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 113 LdssQQENSIQRKLTVKDTILTGLfhtigYYRDPSPEE-ETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNE 191
Cdd:COG3842 82 V---FQDYALFPHLTVAENVAFGL-----RMRGVPKAEiRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
4HZI_A 192 PDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEE---IPDfysKAVLLKEGKVIHFGPIEE 260
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEalaLAD---RIAVMNDGRIEQVGTPEE 222
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
32-205 |
9.93e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.94 E-value: 9.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKI--SYKptGKTILDSVSFEIKTNEhCV-LLGRNGAGKSTLVNLIYGMIWATSGTIRLfqetyGEIAIQDL-- 106
Cdd:COG1137 1 MMTLEAENLvkSYG--KRTVVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPDSGRIFL-----DGEDITHLpm 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 107 --RKRIGI--LdssQQENSIQRKLTVKDTILtglfhTIGYYRDPSPEEETKTL-QILKDSDLLSKKDQLYNTLSSGEKKK 181
Cdd:COG1137 73 hkRARLGIgyL---PQEASIFRKLTVEDNIL-----AVLELRKLSKKEREERLeELLEEFGITHLRKSKAYSLSGGERRR 144
|
170 180
....*....|....*....|....
4HZI_A 182 ILFLRSIVNEPDFLIMDEPCSSLD 205
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVD 168
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
41-267 |
1.09e-22 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 93.83 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 41 SYKPtGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILDssqqen 120
Cdd:cd03253 9 AYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVP------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 siqrkltvKDTIL--TGLFHTIGYYR-DPSPEEETKTLQILKDSDLLSKKDQLYNT--------LSSGEKKKILFLRSIV 189
Cdd:cd03253 82 --------QDTVLfnDTIGYNIRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTivgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
4HZI_A 190 NEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKkfTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGPIEECFTEKNL 267
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKGGL 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
41-260 |
2.10e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 96.77 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 41 SYkPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILdssQQEn 120
Cdd:COG1132 348 SY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVV---PQD- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 siqrkltvkdtilTGLFHT-----IGYYRDPSPEEE----TKTLQIlkdSDLLSKKDQLYNT--------LSSGEKKKIL 183
Cdd:COG1132 423 -------------TFLFSGtirenIRYGRPDATDEEveeaAKAAQA---HEFIEALPDGYDTvvgergvnLSGGQRQRIA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 184 FLRSIVNEPDFLIMDEPCSSLD-LTAREDFLGFLKEYHSKkkfTSLYITHRPEEIPDfyskA---VLLKEGKVIHFGPIE 259
Cdd:COG1132 487 IARALLKDPPILILDEATSALDtETEALIQEALERLMKGR---TTIVIAHRLSTIRN----AdriLVLDDGRIVEQGTHE 559
|
.
4HZI_A 260 E 260
Cdd:COG1132 560 E 560
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
42-264 |
2.84e-22 |
|
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: 93.48 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 42 YKPTGKTI-LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDL----RKRIGILdss 116
Cdd:cd03294 31 LKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMV--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 117 QQENSIQRKLTVKDTILTGLfHTIGYyrdPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLI 196
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGL-EVQGV---PRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
4HZI_A 197 MDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTE 264
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
29-256 |
3.50e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 92.40 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 29 GKINSLLSLEKISYKPtgKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQdLRK 108
Cdd:cd03267 18 GLIGSLKSLFKRKYRE--VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK-FLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 109 RIGILDSsqQENSIQRKLTVKDTILtgLFHTIgyYRDPsPEEETKTLQILkdSDLLSKKDQLYN---TLSSGEKKKILFL 185
Cdd:cd03267 95 RIGVVFG--QKTQLWWDLPVIDSFY--LLAAI--YDLP-PARFKKRLDEL--SELLDLEELLDTpvrQLSLGQRMRAEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4HZI_A 186 RSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
35-263 |
7.44e-22 |
|
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: 91.59 E-value: 7.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYK-PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGIL 113
Cdd:cd03295 1 IEFENVTKRyGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 dssqqensIQR-----KLTVKDTIltGLFHTIGYYrdPSPEEETKTLQILKDSDLLSKK--DQLYNTLSSGEKKKILFLR 186
Cdd:cd03295 81 --------IQQiglfpHMTVEENI--ALVPKLLKW--PKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 187 SIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFT 263
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
35-274 |
8.87e-22 |
|
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: 91.14 E-value: 8.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqetyGEIAIQDL---RKRIG 111
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL-----DGKDITNLpphKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 112 ILdssQQENSIQRKLTVKDTILTGLfhtigyYRDPSPEEETK-----TLQILKDSDLLSKK-DQLyntlSSGEKKKILFL 185
Cdd:cd03300 76 TV---FQNYALFPHLTVFENIAFGL------RLKKLPKAEIKervaeALDLVQLEGYANRKpSQL----SGGQQQRVAIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 186 RSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGpieecftek 265
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG--------- 213
|
....*....
4HZI_A 266 NLEDLYDIP 274
Cdd:cd03300 214 TPEEIYEEP 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
41-266 |
9.43e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.98 E-value: 9.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 41 SYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILDSSQQEN 120
Cdd:PRK13632 16 SYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPDNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 SIqrKLTVKDTILTGLFHtigyyRDPSPEEETKtlqILKDS-------DLLSKKDQlynTLSSGEKKKILFLRSIVNEPD 193
Cdd:PRK13632 96 FI--GATVEDDIAFGLEN-----KKVPPKKMKD---IIDDLakkvgmeDYLDKEPQ---NLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
4HZI_A 194 FLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEI--PDfysKAVLLKEGKVIHFGPIEECFTEKN 266
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAilAD---KVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
35-256 |
1.37e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.18 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQdLRKRIGILd 114
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGVV- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 115 ssQQENSIQRKLTVKDTILtgLFHTigYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDF 194
Cdd:PRK13537 86 --PQFDNLDPDFTVRENLL--VFGR--YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
4HZI_A 195 LIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
61-256 |
1.75e-21 |
|
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: 89.86 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 61 EHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGeiAIQDLRKRIGILdssQQENSIQRKLTVkdtiltglFHTI 140
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSML---FQENNLFAHLTV--------EQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 141 GYYRDPS----PEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFL 216
Cdd:cd03298 92 GLGLSPGlkltAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
4HZI_A 217 KEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
46-253 |
2.07e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.20 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAiQDLRKRIGILdssQQENSIQRK 125
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVV---PQFDNLDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 126 LTVKDTILtglfhTIG-YYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSL 204
Cdd:PRK13536 129 FTVRENLL-----VFGrYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
4HZI_A 205 DLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVI 253
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
37-264 |
2.10e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.45 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 37 LEKISyKPTGKT-ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDlrKRIGILds 115
Cdd:PRK10851 5 IANIK-KSFGRTqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 116 sQQENSIQRKLTVKDTILTGLfhTIGYYRD-PSPEE-ETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPD 193
Cdd:PRK10851 80 -FQHYALFRHMTVFDNIAFGL--TVLPRRErPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4HZI_A 194 FLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTE 264
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWRE 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
32-275 |
3.71e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.20 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKISYKPTGKT--ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKR 109
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 110 IGILDSSQQENSIQRklTVKDTILTGL-FHTIgyyrdPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSI 188
Cdd:PRK13648 85 IGIVFQNPDNQFVGS--IVKYDVAFGLeNHAV-----PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 189 VNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGPIEECFteKNLE 268
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF--DHAE 234
|
....*..
4HZI_A 269 DLYDIPL 275
Cdd:PRK13648 235 ELTRIGL 241
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
40-257 |
4.13e-21 |
|
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: 89.09 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 40 ISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILdssQQE 119
Cdd:cd03244 10 LRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISII---PQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 120 NsiqrkltvkdTILTGlfhTIGYYRDP---SPEEEtkTLQILKDSDL----LSKKDQLY-------NTLSSGEKKKILFL 185
Cdd:cd03244 87 P----------VLFSG---TIRSNLDPfgeYSDEE--LWQALERVGLkefvESLPGGLDtvveeggENLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 186 RSIVNEPDFLIMDEPCSSLDL--------TAREDFlgflkeyhskKKFTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGP 257
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPetdaliqkTIREAF----------KDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
35-232 |
1.40e-20 |
|
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: 85.58 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETygeiaiqdlrkrigild 114
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 115 ssqqensiqrkltvkdtiltglfhTIGYYrdpspeeetktlqilkdsdllskkDQlyntLSSGEKKKILFLRSIVNEPDF 194
Cdd:cd03221 64 ------------------------KIGYF------------------------EQ----LSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*...
4HZI_A 195 LIMDEPCSSLDLTAREDFLGFLKEYHSkkkfTSLYITH 232
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYPG----TVILVSH 125
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
47-239 |
1.68e-20 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 90.84 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 47 KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYG-MIWATSGTIRLF--QETYGEiAIQDLRKRIGILdSSQQENSIQ 123
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDLTLFgrRRGSGE-TIWDIKKHIGYV-SSSLHLDYR 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 124 RKLTVKDTILTGLFHTIGYYRDPSPEEETKTLQILkdsDLL----SKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDE 199
Cdd:PRK10938 351 VSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWL---DILgidkRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDE 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
4HZI_A 200 PCSSLDLTAREDFLGFLK----EYHSKKKFTSLY-------ITHRPEEIPD 239
Cdd:PRK10938 428 PLQGLDPLNRQLVRRFVDvlisEGETQLLFVSHHaedapacITHRLEFVPD 478
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
35-260 |
2.13e-20 |
|
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: 87.10 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKIS--YKPTgkTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFqetyGEiAIQDL----RK 108
Cdd:cd03224 1 LEVENLNagYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD----GR-DITGLppheRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 109 RIGILdSSQQENSIQRKLTVKDTILTGlfhtiGYYRDPSPEEET--KTLQ---ILKDsdllsKKDQLYNTLSSGEKKKIL 183
Cdd:cd03224 74 RAGIG-YVPEGRRIFPELTVEENLLLG-----AYARRRAKRKARleRVYElfpRLKE-----RRKQLAGTLSGGEQQMLA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 184 FLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHsKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
41-260 |
2.94e-20 |
|
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: 87.29 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 41 SYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILdsSQqen 120
Cdd:cd03251 9 RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLV--SQ--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 siqrkltvkDTIL--TGLFHTIGYYR-DPSPEEETKTLQILKDSDLLSKKDQLYNT--------LSSGEKKKILFLRSIV 189
Cdd:cd03251 84 ---------DVFLfnDTVAENIAYGRpGATREEVEEAARAANAHEFIMELPEGYDTvigergvkLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4HZI_A 190 NEPDFLIMDEPCSSLDlTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGPIEE 260
Cdd:cd03251 155 KDPPILILDEATSALD-TESERLVQAALERLMKNR-TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEE 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
50-260 |
5.16e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.69 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNE-HCvLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQD-LRKRIGILdssQQENSIQRKLT 127
Cdd:COG1129 20 LDGVSLELRPGEvHA-LLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAII---HQELNLVPNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 128 VKDTILTGLFHTIGYYRDPSpEEETKTLQILK----DSDLlskkDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSS 203
Cdd:COG1129 96 VAENIFLGREPRRGGLIDWR-AMRRRARELLArlglDIDP----DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 204 LDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:COG1129 171 LTEREVERLFRIIRRLKAQGV-AIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAE 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
41-260 |
8.06e-20 |
|
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: 85.74 E-value: 8.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 41 SYKPtGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILdssqqen 120
Cdd:cd03254 11 SYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 sIQRKLTVKDTIltglFHTIGYYRDPSPEEET-KTLQILKDSDLLSKKDQLYNT--------LSSGEKKKILFLRSIVNE 191
Cdd:cd03254 83 -LQDTFLFSGTI----MENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTvlgenggnLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 192 PDFLIMDEPCSSLDLTAREDFLGFLKEYhsKKKFTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGPIEE 260
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDE 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
41-256 |
8.42e-20 |
|
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: 85.50 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 41 SYKPTGKTI--LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrlfqETYGEIAIQD---LRKRIGILDS 115
Cdd:cd03266 10 RFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA----TVDGFDVVKEpaeARRRLGFVSD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 116 SQqenSIQRKLTVKDTILT-GLFHtiGYYRDPSPEEETKTLQILKDSDLLSKKDQlynTLSSGEKKKILFLRSIVNEPDF 194
Cdd:cd03266 86 ST---GLYDRLTARENLEYfAGLY--GLKGDELTARLEELADRLGMEELLDRRVG---GFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
4HZI_A 195 LIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
50-218 |
8.55e-20 |
|
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: 85.95 E-value: 8.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFqetyGEiAIQDL----RKRIGILDSSQQeNSIQRK 125
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD----GE-DITGLppheIARLGIGRTFQI-PRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 126 LTVKDTILTGLF----HTIGYYRDPSPEEET--KTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDE 199
Cdd:cd03219 90 LTVLENVMVAAQartgSGLLLARARREEREAreRAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170
....*....|....*....
4HZI_A 200 PCSSLDLTAREDFLGFLKE 218
Cdd:cd03219 170 PAAGLNPEETEELAELIRE 188
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
34-219 |
1.16e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.58 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqetyGEiaiqdlRKRIGIL 113
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-----GE------TVKIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 DssQQENSIQRKLTVKDTIltglfhtigyyRDPSPEEETKTL-QILKdsDLLSKKDQLY---NTLSSGEKKKILFLRSIV 189
Cdd:COG0488 384 D--QHQEELDPDKTVLDEL-----------RDGAPGGTEQEVrGYLG--RFLFSGDDAFkpvGVLSGGEKARLALAKLLL 448
|
170 180 190
....*....|....*....|....*....|
4HZI_A 190 NEPDFLIMDEPCSSLDLTAREDFLGFLKEY 219
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALDDF 478
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
50-253 |
1.29e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.55 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNE-HCvLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQEtygEIAIQD----LRKRIGILdssQQENSIQR 124
Cdd:COG3845 21 NDDVSLTVRPGEiHA-LLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRSprdaIALGIGMV---HQHFMLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 125 KLTVKDTILTGLFHTIGYYRDPSPEEEtktlQILKdsdlLSKK-------DQLYNTLSSGEKKKILFLRSIVNEPDFLIM 197
Cdd:COG3845 94 NLTVAENIVLGLEPTKGGRLDRKAARA----RIRE----LSERygldvdpDAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
4HZI_A 198 DEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVI 253
Cdd:COG3845 166 DEPTAVLTPQEADELFEILRRLAAEGK-SIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
32-293 |
1.73e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.01 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKIS--YKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIW---ATSGTIRLFQETYGEIAIQDL 106
Cdd:PRK13640 3 DNIVEFKHVSftYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLpddNPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 107 RKRIGILdsSQQENSIQRKLTVKDTILTGLFHTigyyRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLR 186
Cdd:PRK13640 83 REKVGIV--FQNPDNQFVGATVGDDVAFGLENR----AVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 187 SIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEiPDFYSKAVLLKEGKVIHFGPIEECFTEKN 266
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
250 260 270
....*....|....*....|....*....|..
4HZI_A 267 L--EDLYDIPLQ---VQRIENTWSVIPKQKRT 293
Cdd:PRK13640 236 MlkEIGLDIPFVyklKNKLKEKGISVPQEINT 267
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
32-280 |
2.37e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.67 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKISYK-PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrLFQET---YGEIAIQDLR 107
Cdd:PRK13636 3 DYILKVEELNYNySDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKpidYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 108 KRIGIL--DSSQQENSIqrklTVKDTILTGLFHTigyyRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFL 185
Cdd:PRK13636 82 ESVGMVfqDPDNQLFSA----SVYQDVSFGAVNL----KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 186 RSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEK 265
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
250
....*....|....*
4HZI_A 266 nlEDLYDIPLQVQRI 280
Cdd:PRK13636 234 --EMLRKVNLRLPRI 246
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
46-232 |
2.75e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqetygeiaiqDLRKRIGILDssqQENSIQRK 125
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-----------PKGLRIGYLP---QEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 126 LTVKDTILTGL---------FHTIgYYRDPSPEE--------------------ETKTLQIL-----KDSDLlskkDQLY 171
Cdd:COG0488 76 LTVLDTVLDGDaelraleaeLEEL-EAKLAEPDEdlerlaelqeefealggweaEARAEEILsglgfPEEDL----DRPV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
4HZI_A 172 NTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREdFL-GFLKEYhskkKFTSLYITH 232
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE-WLeEFLKNY----PGTVLVVSH 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
33-271 |
2.76e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.56 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 33 SLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQEtygEIAIQDL----RK 108
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE---DISLLPLharaRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 109 RIGILdssQQENSIQRKLTVKDTILTglfhTIGYYRDPSPEE-ETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRS 187
Cdd:PRK10895 79 GIGYL---PQEASIFRRLSVYDNLMA----VLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 188 IVNEPDFLIMDEPCSSLDLTAREDFLGFLKeyHSKKKFTSLYIT-HRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKN 266
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKRIIE--HLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
....*
4HZI_A 267 LEDLY 271
Cdd:PRK10895 230 VKRVY 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
34-260 |
3.09e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.25 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTIldSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQdlRKRIGIL 113
Cdd:PRK10771 1 MLKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 dssQQENSIQRKLTVKDTILTGLfhtigyyrDP----SPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIV 189
Cdd:PRK10771 77 ---FQENNLFSHLTVAQNIGLGL--------NPglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4HZI_A 190 NEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
39-256 |
3.11e-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: 83.62 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 39 KISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILdssQQ 118
Cdd:cd03369 13 SVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTII---PQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 119 EnsiqrkltvkDTILTGlfhTIGYYRDpsPEEETKTLQILKdsdLLSKKDQLYNtLSSGEKKKILFLRSIVNEPDFLIMD 198
Cdd:cd03369 90 D----------PTLFSG---TIRSNLD--PFDEYSDEEIYG---ALRVSEGGLN-LSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
4HZI_A 199 EPCSSLDL--------TAREDFlgflkeyhskKKFTSLYITHRPEEIPDfYSKAVLLKEGKVIHFG 256
Cdd:cd03369 151 EATASIDYatdaliqkTIREEF----------TNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
34-267 |
6.08e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.47 E-value: 6.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTG-KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGI 112
Cdd:PRK13652 3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 113 LdsSQQENSIQRKLTVKDTILTGLFHtIGYYRDPSPEEETKTLQILKDSDLLskkDQLYNTLSSGEKKKILFLRSIVNEP 192
Cdd:PRK13652 83 V--FQNPDDQIFSPTVEQDIAFGPIN-LGLDEETVAHRVSSALHMLGLEELR---DRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
4HZI_A 193 DFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKNL 267
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-260 |
1.32e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.61 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKR-IGI 112
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 113 LdssQQENSIQRKLTVKDTILTGLFHTIGYYRDPS---PEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIV 189
Cdd:PRK09700 85 I---YQELSVIDELTVLENLYIGRHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
4HZI_A 190 NEPDFLIMDEPCSSldLTARE-DFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:PRK09700 162 LDAKVIIMDEPTSS--LTNKEvDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
48-260 |
1.44e-18 |
|
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: 82.78 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 48 TILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFqetyGEiAIQDL----RKRIGILDSSQQeNSIQ 123
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD----GR-DITGLpphrIARLGIARTFQN-PRLF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 124 RKLTVKDTILTGLFHTIGY-----------YRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEP 192
Cdd:COG0411 92 PELTVLENVLVAAHARLGRgllaallrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
4HZI_A 193 DFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:COG0411 172 KLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
35-252 |
1.73e-18 |
|
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: 80.72 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTG--KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGI 112
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 113 LdssQQEnsiqrkltvkDTILTGlfhTIgyyRDpspeeetktlqilkdsdllskkdqlyNTLSSGEKKKILFLRSIVNEP 192
Cdd:cd03246 81 L---PQD----------DELFSG---SI---AE--------------------------NILSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
4HZI_A 193 DFLIMDEPCSSLDlTAREDFLGFLKEYHSKKKFTSLYITHRPE--EIPDfysKAVLLKEGKV 252
Cdd:cd03246 116 RILVLDEPNSHLD-VEGERALNQAIAALKAAGATRIVIAHRPEtlASAD---RILVLEDGRV 173
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
35-266 |
2.15e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 82.95 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISY-----KPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETY----GEIAIQD 105
Cdd:PRK13641 3 IKFENVDYiyspgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 106 LRKRIGiLDSSQQENSIQRKLTVKDTILTGLfhTIGYYRDpspEEETKTLQILK----DSDLLSKKDqlyNTLSSGEKKK 181
Cdd:PRK13641 83 LRKKVS-LVFQFPEAQLFENTVLKDVEFGPK--NFGFSED---EAKEKALKWLKkvglSEDLISKSP---FELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 182 ILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHsKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEEC 261
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
....*
4HZI_A 262 FTEKN 266
Cdd:PRK13641 233 FSDKE 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
34-264 |
2.70e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.86 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISY-----KPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIR----LFQETYGEIAIQ 104
Cdd:PRK13643 1 MIKFEKVNYtyqpnSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdiVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 105 DLRKRIGILdSSQQENSIQRKLTVKDTILTGlfHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLynTLSSGEKKKILF 184
Cdd:PRK13643 81 PVRKKVGVV-FQFPESQLFEETVLKDVAFGP--QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPF--ELSGGQMRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 185 LRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTE 264
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
46-253 |
2.71e-18 |
|
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: 81.11 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAiqDLRKRIG-ILDS-------SQ 117
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGaLIEApgfypnlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 118 QENsiqrkLTVKDTILtGLfhtigyyrdpsPEEETKtlQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIM 197
Cdd:cd03268 90 REN-----LRLLARLL-GI-----------RKKRID--EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 198 DEPCSSLD----LTAREDFLGflkeyHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVI 253
Cdd:cd03268 151 DEPTNGLDpdgiKELRELILS-----LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
34-270 |
3.29e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.34 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYK-PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIA-IQDLRKRIG 111
Cdd:PRK13644 1 MIRLENVSYSyPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 112 ILDSSQQENSIQRklTVKDTILTGLFHTIgyyrDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNE 191
Cdd:PRK13644 81 IVFQNPETQFVGR--TVEEDLAFGPENLC----LPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 192 PDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGPIEECFTEKNLEDL 270
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
47-260 |
4.21e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.28 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 47 KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRlfqeTYGEIAiqdlrkriGILDSSQqenSIQRKL 126
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE----VNGRVS--------ALLELGA---GFHPEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 127 TVKDTI-LTGLFHtiGYYRdpspeEETKTL--QILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSS 203
Cdd:COG1134 104 TGRENIyLNGRLL--GLSR-----KEIDEKfdEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 204 LDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:COG1134 177 GDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
65-260 |
4.71e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.00 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 65 LLGRNGAGKSTLVNLIYGMIWATSGTI----RLFQETYGEIAIQDLRKRIGILdssQQENSIQRKLTVKDTILTGLFHTi 140
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIvlngRVLFDAEKGICLPPEKRRIGYV---FQDARLFPHYKVRGNLRYGMAKS- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 141 gyyrdpSPEEETKTLQILKDSDLLskkDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYH 220
Cdd:PRK11144 105 ------MVAQFDKIVALLGIEPLL---DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
4HZI_A 221 SKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:PRK11144 176 REINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
35-272 |
5.89e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 5.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGild 114
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 115 SSQQENSIQRKLTVKDTILTGLFHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDF 194
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
4HZI_A 195 LIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKNLEDLYD 272
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFD 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
47-278 |
8.04e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 81.32 E-value: 8.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 47 KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILdsSQQENSIQRKL 126
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMV--FQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 127 TVKDTILTGLfHTIGYYRDPSPEEETKTLQILKDSDLlskKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDL 206
Cdd:PRK13650 98 TVEDDVAFGL-ENKGIPHEEMKERVNEALELVGMQDF---KEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4HZI_A 207 TAREDFLGFLKEYHSKKKFTSLYITHRPEEIPdFYSKAVLLKEGKVIHFGPIEECFTEKN-LEDL-YDIPLQVQ 278
Cdd:PRK13650 174 EGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNdLLQLgLDIPFTTS 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
35-260 |
1.25e-17 |
|
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: 82.54 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGM--IWATSGTIrLFQ----ETYGEIAIQ---- 104
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRI-IYHvalcEKCGYVERPskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 105 --------------------------DLRKRIGILdsSQQENSIQRKLTVKDTILTGLfHTIGYyrdPSPEEETKTLQIL 158
Cdd:TIGR03269 80 epcpvcggtlepeevdfwnlsdklrrRIRKRIAIM--LQRTFALYGDDTVLDNVLEAL-EEIGY---EGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 159 KDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIP 238
Cdd:TIGR03269 154 EMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|..
4HZI_A 239 DFYSKAVLLKEGKVIHFGPIEE 260
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDE 255
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
47-271 |
2.32e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.03 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 47 KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILdssQQENSIQRKL 126
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLL---AQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 127 TVKDTILTGLFHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDL 206
Cdd:PRK10253 97 TVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
4HZI_A 207 TAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKNLEDLY 271
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
31-277 |
4.18e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 79.37 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 31 INSLLSLEKISYKPTGKT---ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLR 107
Cdd:PRK13642 1 MNKILEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 108 KRIGILDSSQQENSIqrKLTVKDTILTGLFHTigyyRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRS 187
Cdd:PRK13642 81 RKIGMVFQNPDNQFV--GATVEDDVAFGMENQ----GIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 188 IVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGPIEECFTEKnl 267
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATS-- 231
|
250
....*....|
4HZI_A 268 EDLYDIPLQV 277
Cdd:PRK13642 232 EDMVEIGLDV 241
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
42-267 |
4.52e-17 |
|
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: 78.30 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 42 YKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILdssQQENS 121
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVV---LQENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 122 IQRKlTVKDTILTGlfhtigyyrDPSP--EEETKTLQILKDSDLLSKKDQLYNT--------LSSGEKKKILFLRSIVNE 191
Cdd:cd03252 87 LFNR-SIRDNIALA---------DPGMsmERVIEAAKLAGAHDFISELPEGYDTivgeqgagLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
4HZI_A 192 PDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKkfTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGPIEECFTEKNL 267
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGL 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
35-259 |
4.66e-17 |
|
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: 77.57 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGM--IWATSGTIRLFQETYGEIAIQDlRKRIGI 112
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 113 LDSSQqensiqrkltvkdtiltglfhtigyyrdpSPEEetktLQILKDSDLLSKKDQlynTLSSGEKKKILFLRSIVNEP 192
Cdd:cd03217 80 FLAFQ-----------------------------YPPE----IPGVKNADFLRYVNE---GFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4HZI_A 193 DFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPE----EIPDFyskAVLLKEGKVIHFGPIE 259
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGK-SVLIITHYQRlldyIKPDR---VHVLYDGRIVKSGDKE 190
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
33-263 |
6.59e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.58 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 33 SLLSLEKIS--YKPTG-------KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEI-- 101
Cdd:PRK10419 2 TLLNVSGLShhYAHGGlsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 102 -AIQDLRKRIGIL--DSSQQENSiqRKlTVKDTILTGLFHTIGYyrDPSpEEETKTLQILKDSDL-LSKKDQLYNTLSSG 177
Cdd:PRK10419 82 aQRKAFRRDIQMVfqDSISAVNP--RK-TVREIIREPLRHLLSL--DKA-ERLARASEMLRAVDLdDSVLDKRPPQLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 178 EKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGP 257
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
....*.
4HZI_A 258 IEECFT 263
Cdd:PRK10419 236 VGDKLT 241
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
41-253 |
6.69e-17 |
|
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: 76.58 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 41 SYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrLFQETYGEIAIQDLRKRIGILDssqqen 120
Cdd:cd03247 9 SYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-TLDGVPVSDLEKALSSLISVLN------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 siQRKLTVKDTILtglfhtigyyrdpspeeetktlqilkdsdllskkDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEP 200
Cdd:cd03247 82 --QRPYLFDTTLR----------------------------------NNLGRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
4HZI_A 201 CSSLDLTAREDFLGFLKEyHSKKKfTSLYITHRPEEIPDFySKAVLLKEGKVI 253
Cdd:cd03247 126 TVGLDPITERQLLSLIFE-VLKDK-TLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
47-256 |
1.14e-16 |
|
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: 77.19 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 47 KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrlfqETYGEIAiqdlrkriGILDSSqqeNSIQRKL 126
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV----TVRGRVS--------SLLGLG---GGFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 127 TVKDTI-LTGLFHtiGYYRDpspEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLD 205
Cdd:cd03220 100 TGRENIyLNGRLL--GLSRK---EIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
4HZI_A 206 LTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:cd03220 175 AAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
32-256 |
1.18e-16 |
|
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: 76.93 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKISYKPTGKT----ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMI---WATSGTIRLFQEtygEIAIQ 104
Cdd:cd03234 1 QRVLPWWDVGLKAKNWNkyarILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQ---PRKPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 105 DLRKRIGILDssqQENSIQRKLTVKDTIL-TGLFHTIGYYRDPSPEEETKTLqILKDSDLLSKKDQLYNTLSSGEKKKIL 183
Cdd:cd03234 78 QFQKCVAYVR---QDDILLPGLTVRETLTyTAILRLPRKSSDAIRKKRVEDV-LLRDLALTRIGGNLVKGISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
4HZI_A 184 FLRSIVNEPDFLIMDEPCSSLD-LTAReDFLGFLKEYHSKKKFTSLYItHRP-EEIPDFYSKAVLLKEGKVIHFG 256
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDsFTAL-NLVSTLSQLARRNRIVILTI-HQPrSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
46-232 |
2.12e-16 |
|
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: 76.03 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYG--EIAIQDLRKRIGILdsSQQENSIQ 123
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQKVGMV--FQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 124 RkLTVKDTILTGLFHTIGYYRDpspEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSS 203
Cdd:cd03262 90 H-LTVLENITLAPIKVKGMSKA---EAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180
....*....|....*....|....*....
4HZI_A 204 LDLTAREDFLGFLKEYhSKKKFTSLYITH 232
Cdd:cd03262 166 LDPELVGEVLDVMKDL-AEEGMTMVVVTH 193
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
35-260 |
2.34e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 75.98 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMI---WATSGTIRLfqetyGEIAIQDL---RK 108
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLspaFSASGEVLL-----NGRRLTALpaeQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 109 RIGILdssQQENSIQRKLTVKDTILTGLFHTIGyyrdpSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSI 188
Cdd:COG4136 77 RIGIL---FQDDLLFPHLSVGENLAFALPPTIG-----RAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
4HZI_A 189 VNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDfyskavllkEGKVIHFGPIEE 260
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA---------AGRVLDLGNWQH 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
52-256 |
3.78e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.37 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 52 SVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRL--FQETYGEIAIQDLRKRIGILDSSQQENSIQRKLTVK 129
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddHPLHFGDYSYRSQRIRMIFQDPSTSLNPRQRISQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 130 DTIL---TGLfhtigyyrdPSPEEETKTLQILKDSDLLSKKDQLY-NTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLD 205
Cdd:PRK15112 111 DFPLrlnTDL---------EPEQREKQIIETLRQVGLLPDHASYYpHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
4HZI_A 206 LTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERG 232
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
42-260 |
8.83e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.19 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 42 YKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIwATSGTIRLFQETYGEIAIQDLRKRIGILdsSQqeNS 121
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWV--GQ--NP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 122 IQRKLTVKDTILTGlfhtigyyrDP--SPEEETKTLQILKDSDLLSKKDQLYNT--------LSSGEKKKILFLRSIVNE 191
Cdd:PRK11174 433 QLPHGTLRDNVLLG---------NPdaSDEQLQQALENAWVSEFLPLLPQGLDTpigdqaagLSVGQAQRLALARALLQP 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 192 PDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKkfTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGPIEE 260
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAE 569
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
32-280 |
9.06e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.51 E-value: 9.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKISYK------PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQ-ETYGEIAIQ 104
Cdd:PRK13633 2 NEMIKCKNVSYKyesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 105 DLRKRIGILdSSQQENSIQRKLTVKDTILTGlfHTIGYyrdPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILF 184
Cdd:PRK13633 82 DIRNKAGMV-FQNPDNQIVATIVEEDVAFGP--ENLGI---PPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 185 LRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGPIEECFte 264
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF-- 232
|
250
....*....|....*.
4HZI_A 265 KNLEDLYDIPLQVQRI 280
Cdd:PRK13633 233 KEVEMMKKIGLDVPQV 248
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
31-256 |
9.26e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.54 E-value: 9.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 31 INSLLSLEKISYK-PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKR 109
Cdd:PRK13647 1 MDNIIEVEDLHFRyKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 110 IGIL--DSSQQENSiqrkLTVKDTILTGLFHtIGYYRDpspEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRS 187
Cdd:PRK13647 81 VGLVfqDPDDQVFS----STVWDDVAFGPVN-MGLDKD---EVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 188 IVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
37-267 |
9.61e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.81 E-value: 9.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 37 LEKISYKPTGKT-----ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGtirlfQETYGEIAI-------- 103
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETG-----QTIVGDYAIpanlkkik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 104 --QDLRKRIGILDSSQQENSIQRklTVKDTILTGLFHtIGYYRDPSPEEETKTLQILKDSDLLSKKDQLynTLSSGEKKK 181
Cdd:PRK13645 84 evKRLRKEIGLVFQFPEYQLFQE--TIEKDIAFGPVN-LGENKQEAYKKVPELLKLVQLPEDYVKRSPF--ELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 182 ILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEEC 261
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
....*.
4HZI_A 262 FTEKNL 267
Cdd:PRK13645 239 FSNQEL 244
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
47-279 |
1.47e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.67 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 47 KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILdssQQENSIQRKL 126
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL---PQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 127 TVKDtiltglfhTIGYYRDP--------SPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMD 198
Cdd:PRK11231 92 TVRE--------LVAYGRSPwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 199 EPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKNLEDLYDIPLQVQ 278
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAEIH 242
|
.
4HZI_A 279 R 279
Cdd:PRK11231 243 P 243
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
50-239 |
1.52e-15 |
|
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: 76.56 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILDssqqensiQRKLTVK 129
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVP--------QHPFLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 130 DTILTGLFHtigYYRDPSPEEETKTLQILKDSDLLSKKDQLYNT--------LSSGEKKKILFLRSIVNEPDFLIMDEPC 201
Cdd:TIGR02857 410 GTIAENIRL---ARPDASDAEIREALERAGLDEFVAALPQGLDTpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190
....*....|....*....|....*....|....*...
4HZI_A 202 SSLDLTAREDFLGFLKEYHSKKkfTSLYITHRPEEIPD 239
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAAL 522
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-260 |
2.09e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.12 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 29 GKINSLLSLekisYKPTGKTI--LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFqetyGEIAIQD- 105
Cdd:COG4586 19 GLKGALKGL----FRREYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL----GYVPFKRr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 106 --LRKRIGIL---------DssqqensiqrkLTVKDTILtgLFHTIgyYRDPsPEEETKTLQILkdSDLLSKKDQLY--- 171
Cdd:COG4586 91 keFARRIGVVfgqrsqlwwD-----------LPAIDSFR--LLKAI--YRIP-DAEYKKRLDEL--VELLDLGELLDtpv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 172 NTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGK 251
Cdd:COG4586 153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGR 232
|
....*....
4HZI_A 252 VIHFGPIEE 260
Cdd:COG4586 233 IIYDGSLEE 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
47-263 |
2.39e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 47 KTILDSVSFEIKTNEHCVLLGRNGAGKST----LVNLI--YGMIWATSGTIRLFQETygeiAIQDLRKRIGILdsSQQEN 120
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsQGEIWFDGQPLHNLNRR----QLLPVRHRIQVV--FQDPN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 S-IQRKLTVKDTILTGL-FHtigyYRDPSPEE-ETKTLQILKDSDLLSKKDQLYNT-LSSGEKKKILFLRSIVNEPDFLI 196
Cdd:PRK15134 373 SsLNPRLNVLQIIEEGLrVH----QPTLSAAQrEQQVIAVMEEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 197 MDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFT 263
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
34-267 |
2.65e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 74.34 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYK-PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQET--YGEIAIQDLRKRI 110
Cdd:PRK13639 1 ILETRDLKYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 111 GILdsSQQENSIQRKLTVKDTILTGLFHtIGYyrdPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVN 190
Cdd:PRK13639 81 GIV--FQNPDDQLFAPTVEEDVAFGPLN-LGL---SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 191 EPDFLIMDEPCSSLDLTAREDFLGFLKEYhSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKNL 267
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
54-275 |
3.12e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 75.44 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 54 SFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSG--------TIRLFQETYGEIAIQDLRKRIGILDSSQQENSiqrK 125
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshITRLSFEQLQKLVSDEWQRNNTDMLSPGEDDT---G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 126 LTVKDTILTGLfhtigyyRDPSP-EEETKTLQIlkdSDLLSKKdqlYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSL 204
Cdd:PRK10938 100 RTTAEIIQDEV-------KDPARcEQLAQQFGI---TALLDRR---FKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 205 DLTAREDFLGFLKEYHsKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTE------KNLEDLYDIPL 275
Cdd:PRK10938 167 DVASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQalvaqlAHSEQLEGVQL 242
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
31-281 |
3.45e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.89 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 31 INSLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGT---IRLFQETY---GEIAiQ 104
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVqreGRLA-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 105 DLRKRIGILDSSQQENSIQRKLTVKDTILTGLFHTIGYYRDP----SPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKK 180
Cdd:PRK09984 80 DIRKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 181 KILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
250 260
....*....|....*....|.
4HZI_A 261 cFTEKNLEDLYDiplQVQRIE 281
Cdd:PRK09984 240 -FDNERFDHLYR---SINRVE 256
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
39-256 |
3.88e-15 |
|
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: 72.20 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 39 KISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMiwatsgtiRLFQETYGEIAI-------QDLRKRIG 111
Cdd:cd03213 14 KSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGR--------RTGLGVSGEVLIngrpldkRSFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 112 ILDssqQENSIQRKLTVKDTIltglfhtigYYrdpspeeetktlqilkdSDLLSKkdqlyntLSSGEKKKILFLRSIVNE 191
Cdd:cd03213 86 YVP---QDDILHPTLTVRETL---------MF-----------------AAKLRG-------LSGGERKRVSIALELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
4HZI_A 192 PDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRP-EEIPDFYSKAVLLKEGKVIHFG 256
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLRRLADTGR-TIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
35-259 |
4.06e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.23 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKIS-YKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGmIW-ATSGTIR-------LF--QETYgeIAI 103
Cdd:COG4178 363 LALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWpYGSGRIArpagarvLFlpQRPY--LPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 104 QDLRkrigildssqqensiqrkltvkDTILtglfhtigYYRDPSPEEETKTLQILKD---SDLLSKKDQLYN---TLSSG 177
Cdd:COG4178 440 GTLR----------------------EALL--------YPATAEAFSDAELREALEAvglGHLAERLDEEADwdqVLSLG 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 178 EKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEyhSKKKFTSLYITHRPeEIPDFYSKAVLLKEGKVIHFGP 257
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRS-TLAAFHDRVLELTGDGSWQLLP 566
|
..
4HZI_A 258 IE 259
Cdd:COG4178 567 AE 568
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
34-250 |
5.00e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.20 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqetyGEIAIQDLRKRIGIL 113
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL-----DGKPVEGPGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 dssQQENSIQRKLTVKDTILTGLfHTIGYyrdPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPD 193
Cdd:PRK11248 76 ---FQNEGLLPWRNVQDNVAFGL-QLAGV---EKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
4HZI_A 194 FLIMDEPCSSLDLTAREDFLG-FLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEG 250
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTlLLKLWQETGK-QVLLITHDIEEAVFMATELVLLSPG 205
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
35-234 |
6.39e-15 |
|
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: 74.70 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYK-PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGIL 113
Cdd:TIGR02868 335 LELRDLSAGyPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 -------DSSQQEN-SIQRKltvkdtiltglfhtigyyrDPSPEEETKTLQILKDSDLLSKKDQLYNT--------LSSG 177
Cdd:TIGR02868 415 aqdahlfDTTVRENlRLARP-------------------DATDEELWAALERVGLADWLRALPDGLDTvlgeggarLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 178 EKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKkfTSLYITHRP 234
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
33-200 |
9.20e-15 |
|
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: 71.94 E-value: 9.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 33 SLLSLEKIS--YKPTgkTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFqetyGEiAIQDL---- 106
Cdd:COG0410 2 PMLEVENLHagYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD----GE-DITGLpphr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 107 RKRIGIldsSQ--QENSIQRKLTVKDTILTGLfhtigyYRDPSPEEETKTLQ-------ILKDsdllsKKDQLYNTLSSG 177
Cdd:COG0410 75 IARLGI---GYvpEGRRIFPSLTVEENLLLGA------YARRDRAEVRADLErvyelfpRLKE-----RRRQRAGTLSGG 140
|
170 180
....*....|....*....|...
4HZI_A 178 EKKKILFLRSIVNEPDFLIMDEP 200
Cdd:COG0410 141 EQQMLAIGRALMSRPKLLLLDEP 163
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
35-259 |
9.89e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.02 E-value: 9.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNE-HcVLLGRNGAGKSTLVNLIYGmIWA---TSGTIRLFQETYGEIAIQDlRKRI 110
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEvH-AIMGPNGSGKSTLAKVLMG-HPKyevTSGSILLDGEDILELSPDE-RARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 111 GILDSSQQENSIqRKLTVKDTILTGLFHTIGyyRDPSPEEETKTLQ----ILK-DSDLLSKkdQLYNTLSSGEKKKILFL 185
Cdd:COG0396 78 GIFLAFQYPVEI-PGVSVSNFLRTALNARRG--EELSAREFLKLLKekmkELGlDEDFLDR--YVNEGFSGGEKKRNEIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 186 RSIVNEPDFLIMDEPCSSLDLtareDFL-----GFlKEYHSKKKfTSLYITHRP---EEI-PDFyskAVLLKEGKVIHFG 256
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLDI----DALrivaeGV-NKLRSPDR-GILIITHYQrilDYIkPDF---VHVLVDGRIVKSG 223
|
...
4HZI_A 257 PIE 259
Cdd:COG0396 224 GKE 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
50-283 |
1.64e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.41 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIwATSGTIRLFQETYGEIAIQDLRKRIGILdSSQQENSIQrkLTVk 129
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYL-SQQQSPPFA--MPV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 130 dtiltglFHTIG-YYRDPSPEEETKTL-----QILKDSDLLSKkdQLyNTLSSGEKKKIL----FL---RSIVNEPDFLI 196
Cdd:COG4138 87 -------FQYLAlHQPAGASSEAVEQLlaqlaEALGLEDKLSR--PL-TQLSGGEWQRVRlaavLLqvwPTINPEGQLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 197 MDEPCSSLDLTAREDFLGFLKEyhskkkFTSLYIT-----HrpeeipD------FYSKAVLLKEGKVIHFGPIEECFTEK 265
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRE------LCQQGITvvmssH------DlnhtlrHADRVWLLKQGKLVASGETAEVMTPE 224
|
250
....*....|....*...
4HZI_A 266 NLEDLYDIPLQVQRIENT 283
Cdd:COG4138 225 NLSEVFGVKFRRLEVEGH 242
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
11-260 |
2.44e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 72.76 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 11 LESTSLYKKAGSENLYFQGKINSLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGT 90
Cdd:PRK10070 5 LEIKNLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 91 IRLFQETYGEIAIQDLR----KRIGILdssQQENSIQRKLTVKDTILTGLfHTIGYyrdPSPEEETKTLQILKDSDLLSK 166
Cdd:PRK10070 85 VLIDGVDIAKISDAELRevrrKKIAMV---FQSFALMPHMTVLDNTAFGM-ELAGI---NAEERREKALDALRQVGLENY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 167 KDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVL 246
Cdd:PRK10070 158 AHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAI 237
|
250
....*....|....
4HZI_A 247 LKEGKVIHFGPIEE 260
Cdd:PRK10070 238 MQNGEVVQVGTPDE 251
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
32-237 |
2.72e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.51 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKrig 111
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 112 ildssQQENSIQRKLTVKDTILTGLfhtIGYY--RDPSPeEETKTLQILKDSDL-LSKKDQLYNTLSSGEKKKILFLRSI 188
Cdd:PRK10247 82 -----QVSYCAQTPTLFGDTVYDNL---IFPWqiRNQQP-DPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
4HZI_A 189 VNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEI 237
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEI 201
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
42-262 |
3.59e-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: 72.74 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 42 YKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYgEIAIQDLRKRIGIldsSQQENS 121
Cdd:TIGR01257 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGM---CPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 122 IQRKLTVKDTIltgLFHtiGYYRDPSPEEETKTLQ-ILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEP 200
Cdd:TIGR01257 1014 LFHHLTVAEHI---LFY--AQLKGRSWEEAQLEMEaMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
4HZI_A 201 CSSLDLTAREDFLGFLKEYHSKKkfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGP---IEECF 262
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRLYCSGTplfLKNCF 1151
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
33-264 |
7.61e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.78 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 33 SLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqetyGEIAI--------- 103
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-----GDITIdtarslsqq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 104 ----QDLRKRIGIL--------DSSQQENSIQRKLTVKdtiltglfhtigyyRDPSPEEETKTLQILKDSDLLSKKDQLY 171
Cdd:PRK11264 77 kgliRQLRQHVGFVfqnfnlfpHRTVLENIIEGPVIVK--------------GEPKEEATARARELLAKVGLAGKETSYP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 172 NTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGK 251
Cdd:PRK11264 143 RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGR 221
|
250
....*....|...
4HZI_A 252 VIHFGPIEECFTE 264
Cdd:PRK11264 222 IVEQGPAKALFAD 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
32-266 |
9.26e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.52 E-value: 9.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKISyKPTGK-TILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQdlRKRI 110
Cdd:PRK11432 4 KNFVVLKNIT-KRFGSnTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 111 GILdssQQENSIQRKLTVKDTILTGLfHTIGYyrdPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVN 190
Cdd:PRK11432 81 CMV---FQSYALFPHMSLGENVGYGL-KMLGV---PKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
4HZI_A 191 EPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKN 266
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
49-263 |
1.00e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.17 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 49 ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMI-----WATSGTIRLFQETYGEIAIQDLRKRIGILdsSQQENSIQ 123
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELRRRVQMV--FQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 124 rKLTVKDTILTGLfhTIGYYRDPSPEEETKTLQILKDSDLLSK-KDQL---YNTLSSGEKKKILFLRSIVNEPDFLIMDE 199
Cdd:PRK14247 96 -NLSIFENVALGL--KLNRLVKSKKELQERVRWALEKAQLWDEvKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
4HZI_A 200 PCSSLDL--TAREDFLgFLKeyhSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFT 263
Cdd:PRK14247 173 PTANLDPenTAKIESL-FLE---LKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
36-277 |
1.81e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.66 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 36 SLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILds 115
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 116 sQQENSIQRKLTVKDTILTGLF--H-TIGYYR--DPSPEEETKTLQILKdsdllSKKDQLYNTLSSGEKKKILFLRSIVN 190
Cdd:PRK10575 91 -PQQLPAAEGMTVRELVAIGRYpwHgALGRFGaaDREKVEEAISLVGLK-----PLAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 191 EPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKNLEDL 270
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQI 244
|
....*..
4HZI_A 271 YDIPLQV 277
Cdd:PRK10575 245 YGIPMGI 251
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
49-264 |
2.14e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.12 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 49 ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRL------FQETYGEIAIQDLRKRIGILdsSQQENsI 122
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdFSKTPSDKAIRELRRNVGMV--FQQYN-L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 123 QRKLTVKDTILTGLFHTIGYYRDpspEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCS 202
Cdd:PRK11124 94 WPHLTVQQNLIEAPCRVLGLSKD---QALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
4HZI_A 203 SLD--LTARedFLGFLKEYhSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIeECFTE 264
Cdd:PRK11124 171 ALDpeITAQ--IVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQ 230
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-263 |
2.45e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.52 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 30 KINSLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATS-----GTIRLFQETYGE--IA 102
Cdd:PRK14258 3 KLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 103 IQDLRKRIGILdsSQQENSIqrKLTVKDTILTGLfHTIGYYrdPSPEEETKTLQILKDSDLLSK-KDQLYNT---LSSGE 178
Cdd:PRK14258 83 LNRLRRQVSMV--HPKPNLF--PMSVYDNVAYGV-KIVGWR--PKLEIDDIVESALKDADLWDEiKHKIHKSaldLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 179 KKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEI---PDF--YSKAVLLKEGKVI 253
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVsrlSDFtaFFKGNENRIGQLV 235
|
250
....*....|
4HZI_A 254 HFGPIEECFT 263
Cdd:PRK14258 236 EFGLTKKIFN 245
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
46-240 |
2.64e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.21 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqeTYGEIAIQDLRKRIGILDSSqqeNSIQRK 125
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKL---DGGDIDDPDVAEACHYLGHR---NAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 126 LTVKDTIL--TGLFHTigyyRDPSPEEetkTLQILKDSDLLskkDQLYNTLSSGEKKKILFLRSIV-NEPDFLImDEPCS 202
Cdd:PRK13539 88 LTVAENLEfwAAFLGG----EELDIAA---ALEAVGLAPLA---HLPFGYLSAGQKRRVALARLLVsNRPIWIL-DEPTA 156
|
170 180 190
....*....|....*....|....*....|....*...
4HZI_A 203 SLDLTAREDFLGfLKEYHSKKKFTSLYITHRPEEIPDF 240
Cdd:PRK13539 157 ALDAAAVALFAE-LIRAHLAQGGIVIAATHIPLGLPGA 193
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
46-263 |
2.74e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.58 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMI-----WATSGTIRLF-QETYGEIAIQDLRKRIGILdsSQQE 119
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGgRSIFNYRDVLEFRRRVGML--FQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 120 NSIqrKLTVKDTILTGL-FHTIgyyrdpSPEEETKTLQILKDSDL---LSKKDQLYNT---LSSGEKKKILFLRSIVNEP 192
Cdd:PRK14271 111 NPF--PMSIMDNVLAGVrAHKL------VPRKEFRGVAQARLTEVglwDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4HZI_A 193 DFLIMDEPCSSLDLTAREDFLGFLKEYhsKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFT 263
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
29-205 |
3.85e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.22 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 29 GKINSLLSLEKISYKPTGKT-ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLR 107
Cdd:PRK13657 329 GRVKGAVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 108 KRIGILdsSQQENSIQRklTVKDTILTGlfhtigyYRDPSPEEETKTLQILKDSDLLSKKDQLYNT--------LSSGEK 179
Cdd:PRK13657 409 RNIAVV--FQDAGLFNR--SIEDNIRVG-------RPDATDEEMRAAAERAQAHDFIERKPDGYDTvvgergrqLSGGER 477
|
170 180
....*....|....*....|....*.
4HZI_A 180 KKILFLRSIVNEPDFLIMDEPCSSLD 205
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALD 503
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
33-267 |
3.85e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.82 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 33 SLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQdlrKRIgi 112
Cdd:PRK09452 13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE---NRH-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 113 LDSSQQENSIQRKLTVKDTILTGLfhtiGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEP 192
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGL----RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
4HZI_A 193 DFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTE-KNL 267
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEpKNL 239
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
53-277 |
5.07e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 67.74 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 53 VSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqetyGEIAIQ---------DLRKRIGIL---DSSQ--Q 118
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-----GERVITagkknkklkPLRKKVGIVfqfPEHQlfE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 119 EnsiqrklTVKDTILTGlfhtigyyrdPS----PEEETKTL--QILK----DSDLLSKKDqlyNTLSSGEKKKILFLRSI 188
Cdd:PRK13634 101 E-------TVEKDICFG----------PMnfgvSEEDAKQKarEMIElvglPEELLARSP---FELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 189 VNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKnlE 268
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP--D 238
|
....*....
4HZI_A 269 DLYDIPLQV 277
Cdd:PRK13634 239 ELEAIGLDL 247
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
31-206 |
5.53e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.06 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 31 INSLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRlfqetygeiaiQDLRKRI 110
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 111 GIldssqqensIQRKLTVKDTiltgLFHTIGYYRDPSPE-EETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIV 189
Cdd:PRK09544 70 GY---------VPQKLYLDTT----LPLTVNRFLRLRPGtKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALL 136
|
170
....*....|....*..
4HZI_A 190 NEPDFLIMDEPCSSLDL 206
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDV 153
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
35-263 |
6.99e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 67.80 E-value: 6.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKIS--YKPTGKTI--LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQE---TYGEIAIQDLR 107
Cdd:COG1135 2 IELENLSktFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 108 KRIG-IldsSQQENSIQRKlTVKDTI-----LTGLfhtigyyrdPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKK 181
Cdd:COG1135 82 RKIGmI---FQHFNLLSSR-TVAENValpleIAGV---------PKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 182 ILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPE---EIPDfysKAVLLKEGKVIHFGPI 258
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDvvrRICD---RVAVLENGRIVEQGPV 225
|
....*
4HZI_A 259 EECFT 263
Cdd:COG1135 226 LDVFA 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
50-260 |
1.05e-12 |
|
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: 65.95 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqetYGEIAIQDLRKRIGILdssqQENSIQRKLTVK 129
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL----EGKQITEPGPDRMVVF----QNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 130 DTILTGLFHTIgyyRD-PSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTA 208
Cdd:TIGR01184 73 ENIALAVDRVL---PDlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
4HZI_A 209 REDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILE 201
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
49-233 |
1.18e-12 |
|
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: 65.96 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 49 ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRL-------FQETYgeiaiqdLRKRIGILdsSQQENS 121
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdgkpisqYEHKY-------LHSKVSLV--GQEPVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 122 IQRklTVKDTILTGLfhtigyyRDPSPEEETKTLQILKDSDLLSKKDQLYNT--------LSSGEKKKILFLRSIVNEPD 193
Cdd:cd03248 100 FAR--SLQDNIAYGL-------QSCSFECVKEAAQKAHAHSFISELASGYDTevgekgsqLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
4HZI_A 194 FLIMDEPCSSLDLTAREDFLGFLKEYHSKKkfTSLYITHR 233
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHR 208
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
44-256 |
1.34e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.65 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 44 PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTI-------------RLFQETYGEIAIQ------ 104
Cdd:PRK13651 17 PTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktKEKEKVLEKLVIQktrfkk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 105 -----DLRKRIGILDSSQQ----ENSIQrkltvKDTIltglFHTIGYYRDPSpEEETKTLQILK----DSDLLSKKDqlY 171
Cdd:PRK13651 97 ikkikEIRRRVGVVFQFAEyqlfEQTIE-----KDII----FGPVSMGVSKE-EAKKRAAKYIElvglDESYLQRSP--F 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 172 NtLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGK 251
Cdd:PRK13651 165 E-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGK 242
|
....*
4HZI_A 252 VIHFG 256
Cdd:PRK13651 243 IIKDG 247
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
34-232 |
1.37e-12 |
|
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: 67.00 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLE--KISYKPTGKTI--LDSVSFEIKTNEhCV-LLGRNGAGKSTLVNLIYGMI---WATSGTIRLFQE---TYGEIA 102
Cdd:COG0444 1 LLEVRnlKVYFPTRRGVVkaVDGVSFDVRRGE-TLgLVGESGSGKSTLARAILGLLpppGITSGEILFDGEdllKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 103 IQDLR-KRIGILdssQQE--NSIQRKLTVKDTILTGLFHtigyYRDPSPEE-ETKTLQILKDSDLLSKKDQLYN---TLS 175
Cdd:COG0444 80 LRKIRgREIQMI---FQDpmTSLNPVMTVGDQIAEPLRI----HGGLSKAEaRERAIELLERVGLPDPERRLDRyphELS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 176 SGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITH 232
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITH 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
50-264 |
2.27e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.13 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqeTYGEIAIQ------DLRKR----IGILdssQQE 119
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV---RVGDEWVDmtkpgpDGRGRakryIGIL---HQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 120 NSiqrkLTVKDTILTGLFHTIGYyrdPSPEE--ETKTLQILKDSDLLSKK-----DQLYNTLSSGEKKKILFLRSIVNEP 192
Cdd:TIGR03269 374 YD----LYPHRTVLDNLTEAIGL---ELPDElaRMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
4HZI_A 193 DFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTE 264
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
46-232 |
2.29e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.90 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQD---LRKRIGILdssQQENSI 122
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMI---FQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 123 QRKLTVKDTILTGLFhtigyYRDPSPEE-ETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPC 201
Cdd:PRK10908 91 LMDRTVYDNVAIPLI-----IAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190
....*....|....*....|....*....|.
4HZI_A 202 SSLDLTAREDFLGFLKEYhSKKKFTSLYITH 232
Cdd:PRK10908 166 GNLDDALSEGILRLFEEF-NRVGVTVLMATH 195
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
49-205 |
2.39e-12 |
|
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: 65.25 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 49 ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLI---YGmiwATSGTIRLFQETYGEIAIQDLRKRIGILdssQQE-----N 120
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfYD---PTSGEILLDGVDIRDLNLRWLRSQIGLV---SQEpvlfdG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 SIQrkltvkdtiltglfHTIGYYRDPSPEEETKtlQILKDS---DLLSKKDQLYNT--------LSSGEKKKILFLRSIV 189
Cdd:cd03249 92 TIA--------------ENIRYGKPDATDEEVE--EAAKKAnihDFIMSLPDGYDTlvgergsqLSGGQKQRIAIARALL 155
|
170
....*....|....*.
4HZI_A 190 NEPDFLIMDEPCSSLD 205
Cdd:cd03249 156 RNPKILLLDEATSALD 171
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
34-253 |
3.08e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.77 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKIS--YKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIG 111
Cdd:PRK11160 338 SLTLNNVSftYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 112 ILDssqqensiQR----KLTVKDTILTGlfhtigyyrDPSPEEEtKTLQILKD---SDLLSKKDQLyNT--------LSS 176
Cdd:PRK11160 418 VVS--------QRvhlfSATLRDNLLLA---------APNASDE-ALIEVLQQvglEKLLEDDKGL-NAwlgeggrqLSG 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 177 GEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEyHSKKKfTSLYITHRPEEIPDFySKAVLLKEGKVI 253
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE-HAQNK-TVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
47-268 |
3.58e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.07 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 47 KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNL------IYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILdsSQQEN 120
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMV--FQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 SIQRkLTVKDTILTGL-FHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDE 199
Cdd:PRK14246 101 PFPH-LSIYDNIAYPLkSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 200 PCSSLDLTAREDFLGFLKEYhsKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKNLE 268
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNE 246
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
49-267 |
4.11e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.28 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 49 ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILdssQQENSIQRKlTV 128
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALV---GQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 129 KDTILTGLfhtigyyRDPSPEEETKTLQILKDSDLLSKKDQLYNT--------LSSGEKKKILFLRSIVNEPDFLIMDEP 200
Cdd:TIGR00958 572 RENIAYGL-------TDTPDEEIMAAAKAANAHDFIMEFPNGYDTevgekgsqLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 201 CSSLDlTAREDFLGFLKEYHSKkkfTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGPIEECFTEKNL 267
Cdd:TIGR00958 645 TSALD-AECEQLLQESRSRASR---TVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
47-235 |
4.45e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 47 KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIwatsgtirLFQETYGEIAIQDlrkrigildssqqeNSIQRKL 126
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL--------KGTPVAGCVDVPD--------------NQFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 127 TVKDTIltglfhtigyYRDPSPEEETKTLQILKDSD--LLSKKdqlYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSL 204
Cdd:COG2401 101 SLIDAI----------GRKGDFKDAVELLNAVGLSDavLWLRR---FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190
....*....|....*....|....*....|..
4HZI_A 205 D-LTAREDFLGFLKEYHSKKKfTSLYITHRPE 235
Cdd:COG2401 168 DrQTAKRVARNLQKLARRAGI-TLVVATHHYD 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
34-260 |
5.80e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 5.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEiAIQDLRKRIGIL 113
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR-LTPAKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 dSSQQENSIQRKLTVKDTILTGLfhtigyyrdPSPEEETKTL-QILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEP 192
Cdd:PRK15439 90 -LVPQEPLLFPNLSVKENILFGL---------PKRQASMQKMkQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
4HZI_A 193 DFLIMDEPCSSLDLTAREDFLGFLKEYHSkKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
35-235 |
6.53e-12 |
|
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: 62.56 E-value: 6.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYK-PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGmIWatsgtirlfqeTYGEiaiqdlrkriGIL 113
Cdd:cd03223 1 IELENLSLAtPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LW-----------PWGS----------GRI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 DSSQQENSI---QRKltvkdtiltglFHTIGyyrdpspeeetkTLqilkdsdllskKDQL----YNTLSSGEKKKILFLR 186
Cdd:cd03223 59 GMPEGEDLLflpQRP-----------YLPLG------------TL-----------REQLiypwDDVLSGGEQQRLAFAR 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
4HZI_A 187 SIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEyhskKKFTSLYITHRPE 235
Cdd:cd03223 105 LLLHKPKFVFLDEATSALDEESEDRLYQLLKE----LGITVISVGHRPS 149
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
49-262 |
1.29e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 49 ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLI-------YGMIWATSGTIRLFQETYGEIAIQD------LRKRIGILds 115
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsEGSIVVNGQTINLVRDKDGQLKVADknqlrlLRTRLTMV-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 116 sQQENSIQRKLTVKDTILTGLFHTIGYYRDPSPEEETKTLQILKDSDllSKKDQLYNTLSSGEKKKILFLRSIVNEPDFL 195
Cdd:PRK10619 98 -FQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDE--RAQGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 196 IMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECF 262
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
41-233 |
1.43e-11 |
|
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: 64.46 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 41 SYKPtGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRlfqetygeIAIQDLRkrigilDSSQQen 120
Cdd:COG5265 366 GYDP-ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIL--------IDGQDIR------DVTQA-- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 SIQRKLTV--KDTIL--TGLFHTIGYYRDPSPEEE----TKTLQIlkdSDLLSKKDQLYNT--------LSSGEKKKILF 184
Cdd:COG5265 429 SLRAAIGIvpQDTVLfnDTIAYNIAYGRPDASEEEveaaARAAQI---HDFIESLPDGYDTrvgerglkLSGGEKQRVAI 505
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
4HZI_A 185 LRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYhSKKKfTSLYITHR 233
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGR-TTLVIAHR 552
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
49-251 |
1.51e-11 |
|
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: 62.49 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 49 ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqetYGEIAIqdlrkrigildSSQQ---ENSiqrk 125
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV----PGSIAY-----------VSQEpwiQNG---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 126 lTVKDTILTGLFHTIGYYRdpspeeetKTL---QILKDSDLLSKKDQLY-----NTLSSGEKKKILFLRSIVNEPDFLIM 197
Cdd:cd03250 81 -TIRENILFGKPFDEERYE--------KVIkacALEPDLEILPDGDLTEigekgINLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 198 DEPCSSLD-LTAREDF----LGFLKeyhsKKKfTSLYITHRPEEIPDFySKAVLLKEGK 251
Cdd:cd03250 152 DDPLSAVDaHVGRHIFenciLGLLL----NNK-TRILVTHQLQLLPHA-DQIVVLDNGR 204
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
35-252 |
1.61e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.16 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqetyGEIAIQDLRKRIGILd 114
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-----GTAPLAEAREDTRLM- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 115 ssQQENSIQRKLTVKDTILTGLfhtIGYYRDpspeeetKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDF 194
Cdd:PRK11247 87 --FQDARLLPWKKVIDNVGLGL---KGQWRD-------AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
4HZI_A 195 LIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKV 252
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
49-232 |
2.51e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.14 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 49 ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrLFQ----ETYGEIAIQDLRKR-IGILdssQQENSIQ 123
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-IFNgqpmSKLSSAAKAELRNQkLGFI---YQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 124 RKLTVKDTILTGLFhtIGyyRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSS 203
Cdd:PRK11629 100 PDFTALENVAMPLL--IG--KKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180
....*....|....*....|....*....
4HZI_A 204 LDLTAREDFLGFLKEYHSKKKFTSLYITH 232
Cdd:PRK11629 176 LDARNADSIFQLLGELNRLQGTAFLVVTH 204
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
50-266 |
2.82e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.76 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrlfqetygeiaiqDLRKRIGILDSSQQENSiqrKLTVK 129
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-------------DIKGSAALIAISSGLNG---QLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 130 DTI-LTGLFHTIgyyrdpsPEEETK--TLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDL 206
Cdd:PRK13545 104 ENIeLKGLMMGL-------TKEKIKeiIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 207 TAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKN 266
Cdd:PRK13545 177 TFTKKCLDKMNEFKEQGK-TIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYD 235
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
46-281 |
3.32e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWAT--------SGTIRLFQETYGEIAIQDLRKRIGILDSSQ 117
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 118 QENSiqrKLTVKDTILTGLFHTIGYYRDPSPEEETKTLQILK--DSDLLSKKDqlYNTLSSGEKKKILFLRSIVN----- 190
Cdd:PRK13547 93 QPAF---AFSAREIVLLGRYPHARRAGALTHRDGEIAWQALAlaGATALVGRD--VTTLSGGELARVQFARVLAQlwpph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 191 ----EPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKN 266
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAH 247
|
250
....*....|....*
4HZI_A 267 LEDLYDIPlqVQRIE 281
Cdd:PRK13547 248 IARCYGFA--VRLVD 260
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-93 |
5.22e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 61.64 E-value: 5.22e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
4HZI_A 35 LSLEKIS---YKPTG--KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRL 93
Cdd:COG1101 2 LELKNLSktfNPGTVneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILI 65
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
48-294 |
5.53e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.18 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 48 TILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRL--------FQETYGEIA--------IQDLRKRIG 111
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkKNNHELITNpyskkiknFKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 112 ILdsSQQENSIQRKLTVKDTILTGLFhTIGYYRDPSPEEETKTLQILK-DSDLLskkDQLYNTLSSGEKKKILFLRSIVN 190
Cdd:PRK13631 120 MV--FQFPEYQLFKDTIEKDIMFGPV-ALGVKKSEAKKLAKFYLNKMGlDDSYL---ERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 191 EPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKNLEDL 270
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIINS 272
|
250 260
....*....|....*....|....*.
4HZI_A 271 YDI--PLQVQRIENTWSVIPKQKRTY 294
Cdd:PRK13631 273 TSIqvPRVIQVINDLIKKDPKYKKLY 298
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
46-210 |
7.17e-11 |
|
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: 60.91 E-value: 7.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTI--LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrLFQETYGEI--------AIQDLRKR-IGILd 114
Cdd:COG4778 21 GKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSI-LVRHDGGWVdlaqasprEILALRRRtIGYV- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 115 sSQQENSIQRKLTVkDTILTGLFHtIGYYRDpspEEETKTLQILKDSDLLSKKDQLY-NTLSSGEKKKILFLRSIVNEPD 193
Cdd:COG4778 99 -SQFLRVIPRVSAL-DVVAEPLLE-RGVDRE---EARARARELLARLNLPERLWDLPpATFSGGEQQRVNIARGFIADPP 172
|
170
....*....|....*..
4HZI_A 194 FLIMDEPCSSLDLTARE 210
Cdd:COG4778 173 LLLLDEPTASLDAANRA 189
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
34-232 |
8.09e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.16 E-value: 8.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQEtygeiAIQDLR----KR 109
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ-----HIEGLPghqiAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 110 IGILDSSQQ----------EN-SIQRKLTVKDTILTGLFHTIGYYRDPSpEEETKTLQILKDSDLLSKKDQLYNTLSSGE 178
Cdd:PRK11300 80 MGVVRTFQHvrlfremtviENlLVAQHQQLKTGLFSGLLKTPAFRRAES-EALDRAATWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
4HZI_A 179 KKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITH 232
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEH 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
34-263 |
8.64e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 61.74 E-value: 8.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKIsYKPTGKTI--LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQE---TYGEIAIQDLRK 108
Cdd:PRK11153 4 LKNISKV-FPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltALSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 109 RIGI------LDSSQqensiqrklTVKDTI-----LTGLfhtigyyrdPSPEEETKTLQILKDSDLLSKKDQLYNTLSSG 177
Cdd:PRK11153 83 QIGMifqhfnLLSSR---------TVFDNValpleLAGT---------PKAEIKARVTELLELVGLSDKADRYPAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 178 EKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGP 257
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
....*.
4HZI_A 258 IEECFT 263
Cdd:PRK11153 225 VSEVFS 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
32-200 |
1.15e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.28 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrlfqeTYGEIAIQD------ 105
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI-----VFDGKDITDwqtaki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 106 LRKRIGILDSSQQENSiqrKLTVKDTILTGlfhtiGYYRDPSPEEEtktlQILKDSDLL----SKKDQLYNTLSSGEKKK 181
Cdd:PRK11614 78 MREAVAIVPEGRRVFS---RMTVEENLAMG-----GFFAERDQFQE----RIKWVYELFprlhERRIQRAGTMSGGEQQM 145
|
170
....*....|....*....
4HZI_A 182 ILFLRSIVNEPDFLIMDEP 200
Cdd:PRK11614 146 LAIGRALMSQPRLLLLDEP 164
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
50-260 |
1.32e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 60.60 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrlfqETYGEIAIqdlrkrIGIldssqqENSIQRKLTVK 129
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----DRNGEVSV------IAI------SAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 130 DTILTGLFhTIGYYRdpspeEETKTL--QILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLT 207
Cdd:PRK13546 104 ENIEFKML-CMGFKR-----KEIKAMtpKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
4HZI_A 208 AREDFLGFLKEYHSKKKfTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNK-TIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDD 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
44-278 |
1.38e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.56 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 44 PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETY----GEIAIQDLRKRIGIL----DS 115
Cdd:PRK13646 17 PYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRPVRKRIGMVfqfpES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 116 SQQENSIQRKL------------TVKDTILTgLFHTIGYYRDpspeeetktlqILKDSDLlskkdqlynTLSSGEKKKIL 183
Cdd:PRK13646 97 QLFEDTVEREIifgpknfkmnldEVKNYAHR-LLMDLGFSRD-----------VMSQSPF---------QMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 184 FLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFT 263
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
250
....*....|....*..
4HZI_A 264 EKN-LEDLY-DIPLQVQ 278
Cdd:PRK13646 236 DKKkLADWHiGLPEIVQ 252
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
43-260 |
1.45e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.60 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 43 KPTgKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWA---TSGTIRLfqetYGE-IAIQDLRKRIGILdssQQ 118
Cdd:TIGR00955 35 RPR-KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLL----NGMpIDAKEMRAISAYV---QQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 119 ENSIQRKLTVKDTiLTGLFHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNT------LSSGEKKKILFLRSIVNEP 192
Cdd:TIGR00955 107 DDLFIPTLTVREH-LMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 193 DFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYItHRPE-EIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTI-HQPSsELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
46-263 |
1.56e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 60.05 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLV---N----LIYGMiwATSGTIRLF-QETYG-EIAIQDLRKRIGILdsS 116
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNrmndLIPGA--RVEGEILLDgEDIYDpDVDVVELRRRVGMV--F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 117 QQEN----SIqrkltvKDTILTGLfhTIGYYRDPSpEEETKTLQILKDSDLLSK-KDQLY---NTLSSGEKKKILFLRSI 188
Cdd:COG1117 99 QKPNpfpkSI------YDNVAYGL--RLHGIKSKS-ELDEIVEESLRKAALWDEvKDRLKksaLGLSGGQQQRLCIARAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 189 VNEPDFLIMDEPCSSLD--LTAR-EDFLGFLkeyhsKKKFTSLYITHRPEE---IPDfysKAVLLKEGKVIHFGPIEECF 262
Cdd:COG1117 170 AVEPEVLLMDEPTSALDpiSTAKiEELILEL-----KKDYTIVIVTHNMQQaarVSD---YTAFFYLGELVEFGPTEQIF 241
|
.
4HZI_A 263 T 263
Cdd:COG1117 242 T 242
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
47-256 |
1.91e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 47 KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETyGEIAIQDLrKRIGILdssQQENSIQRKL 126
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQIL-KRTGFV---TQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 127 TVKDT-ILTGLFHTigyyrdpsPEEETKTLQILKDSDLLSK-----------KDQLYNTLSSGEKKKILFLRSIVNEPDF 194
Cdd:PLN03211 156 TVRETlVFCSLLRL--------PKSLTKQEKILVAESVISElgltkcentiiGNSFIRGISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
4HZI_A 195 LIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRP-EEIPDFYSKAVLLKEGKVIHFG 256
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGK-TIVTSMHQPsSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
35-280 |
3.41e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 59.37 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISY-----KPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIA----IQD 105
Cdd:PRK13649 3 INLQNVSYtyqagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 106 LRKRIGiLDSSQQENSIQRKLTVKDTILTGLFHTIgyyrdpSPEEETKT----LQILKDSDLLSKKDQLynTLSSGEKKK 181
Cdd:PRK13649 83 IRKKVG-LVFQFPESQLFEETVLKDVAFGPQNFGV------SQEEAEALarekLALVGISESLFEKNPF--ELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 182 ILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHsKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEEC 261
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
250
....*....|....*....
4HZI_A 262 FTEknLEDLYDIPLQVQRI 280
Cdd:PRK13649 233 FQD--VDFLEEKQLGVPKI 249
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
50-263 |
4.26e-10 |
|
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: 60.08 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIwATSGTIRLFQE---TYGEIAIQDLRKRIGI--------LDSsqq 118
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQdldGLSRRALRPLRRRMQVvfqdpfgsLSP--- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 119 ensiqrKLTVKDTILTGL-FHTIGyyrdPSPEE-ETKTLQILK----DSDLLSKkdqlY-NTLSSGEKKKILFLRSIVNE 191
Cdd:COG4172 378 ------RMTVGQIIAEGLrVHGPG----LSAAErRARVAEALEevglDPAARHR----YpHEFSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 192 PDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHrpeeipDFyskAVL---------LKEGKVIHFGPIEECF 262
Cdd:COG4172 444 PKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISH------DL---AVVralahrvmvMKDGKVVEQGPTEQVF 514
|
.
4HZI_A 263 T 263
Cdd:COG4172 515 D 515
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
34-266 |
5.75e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.46 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQetygeiaiQDL------R 107
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--------VDLshvppyQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 108 KRIGILdssQQENSIQRKLTVKDTILTGLfhtigyYRDPSPEEETKT-----LQILKDSDLLSKKDqlyNTLSSGEKKKI 182
Cdd:PRK11607 91 RPINMM---FQSYALFPHMTVEQNIAFGL------KQDKLPKAEIASrvnemLGLVHMQEFAKRKP---HQLSGGQRQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 183 LFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECF 262
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
....
4HZI_A 263 TEKN 266
Cdd:PRK11607 239 EHPT 242
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
44-232 |
5.86e-10 |
|
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: 59.56 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 44 PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGmiwatsgtirLFQETYGEIAIQDLRKrIGILdssQQENSIQ 123
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------VDKDFNGEARPQPGIK-VGYL---PQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 124 RKLTVKDTILTGLFHTIGY----------YRDPSPE-----EETKTLQILKDS----DLLSK------------KDQLYN 172
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKDAldrfneisakYAEPDADfdklaAEQAELQEIIDAadawDLDSQleiamdalrcppWDADVT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 173 TLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYhskkKFTSLYITH 232
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY----PGTVVAVTH 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-255 |
6.00e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 33 SLLSLE----KISYKPtgktILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIygmiwatSGTIRLFQetyGEIAI-QDLr 107
Cdd:PRK11147 2 SLISIHgawlSFSDAP----LLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDD---GRIIYeQDL- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 108 krigILDSSQQENSIQRKLTVKDTILTGLFHTIGYYR-----------DPSPE--EETKTLQILKD-----------SDL 163
Cdd:PRK11147 67 ----IVARLQQDPPRNVEGTVYDFVAEGIEEQAEYLKryhdishlvetDPSEKnlNELAKLQEQLDhhnlwqlenriNEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 164 LSK----KDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYhskkKFTSLYITHRPEEIPD 239
Cdd:PRK11147 143 LAQlgldPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF----QGSIIFISHDRSFIRN 218
|
250
....*....|....*.
4HZI_A 240 FYSKAVLLKEGKVIHF 255
Cdd:PRK11147 219 MATRIVDLDRGKLVSY 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
24-256 |
6.15e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 59.65 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 24 NLYFQGKINslLSLEKISYK-PTGKTIldsvsfeiktnehcVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIA 102
Cdd:PRK11176 348 TFTYPGKEV--PALRNINFKiPAGKTV--------------ALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 103 IQDLRKRIGILdsSQQENsiqrklTVKDTILtglfHTIGYYRDP--SPEEETKTLQILKDSDLLSKKDQLYNT------- 173
Cdd:PRK11176 412 LASLRNQVALV--SQNVH------LFNDTIA----NNIAYARTEqySREQIEEAARMAYAMDFINKMDNGLDTvigengv 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 174 -LSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYhsKKKFTSLYITHRPEEIpdfySKA---VLLKE 249
Cdd:PRK11176 480 lLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTI----EKAdeiLVVED 553
|
....*..
4HZI_A 250 GKVIHFG 256
Cdd:PRK11176 554 GEIVERG 560
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
34-269 |
6.95e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGM-----IWATSGTIrlfqeTYGEIAIQ---- 104
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSI-----VYNGHNIYsprt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 105 ---DLRKRIGILdsSQQENSIqrKLTVKDTILTGLfhTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNT---LSSGE 178
Cdd:PRK14239 80 dtvDLRKEIGMV--FQQPNPF--PMSIYENVVYGL--RLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSalgLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 179 KKKILFLRSIVNEPDFLIMDEPCSSLD-LTAR--EDFLgflkeYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHF 255
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDpISAGkiEETL-----LGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEY 228
|
250
....*....|....*..
4HZI_A 256 GPIEECFTE---KNLED 269
Cdd:PRK14239 229 NDTKQMFMNpkhKETED 245
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
42-267 |
8.10e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 42 YKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIwATSGTIRLFQETYGEIAIQDLRKRIGILDSsqqens 121
Cdd:TIGR01271 1227 YTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIPQ------ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 122 iqrkltvKDTILTGLFHtigyyRDPSPEEETKTLQILKDSD---LLSKKDQLYN-----------TLSSGEKKKILFLRS 187
Cdd:TIGR01271 1300 -------KVFIFSGTFR-----KNLDPYEQWSDEEIWKVAEevgLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARS 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 188 IVNEPDFLIMDEPCSSLDLTAREDFLGFLKeyHSKKKFTSLYITHRPEEIPDFYSkAVLLKEGKVIHFGPIEECFTEKNL 267
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKTLK--QSFSNCTVILSEHRVEALLECQQ-FLVIEGSSVKQYDSIQKLLNETSL 1444
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
42-259 |
1.12e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.50 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 42 YKPTGKT-ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqetyGEIAIQDL--RKR-IGILdssQ 117
Cdd:PRK11000 10 TKAYGDVvISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-----GEKRMNDVppAERgVGMV---F 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 118 QENSIQRKLTVKDTILTG--LFHTIGYYRDPSPEEETKTLQIlkdSDLLSKKDQlynTLSSGEKKKILFLRSIVNEPDFL 195
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGlkLAGAKKEEINQRVNQVAEVLQL---AHLLDRKPK---ALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
4HZI_A 196 IMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG-PIE 259
Cdd:PRK11000 156 LLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGkPLE 220
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
46-234 |
1.40e-09 |
|
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: 56.73 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGeiaiqdlrkrigildssQQENSIQRK 125
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-----------------FQRDSIARG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 126 LT-------VKdTILTGLFHTIGYYRDPSPEEetkTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMD 198
Cdd:cd03231 75 LLylghapgIK-TTLSVLENLRFWHADHSDEQ---VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190
....*....|....*....|....*....|....*.
4HZI_A 199 EPCSSLDLTAREDFLGFLKEyHSKKKFTSLYITHRP 234
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAG-HCARGGMVVLTTHQD 185
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
40-267 |
1.54e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 57.56 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 40 ISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWaTSGTIRLFQETYGEIAIQDLRKRIGIldssqqe 119
Cdd:cd03289 10 AKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 120 nsiqrkLTVKDTILTGLFHtigyyRDPSPEEETKTLQILKDSDLLSKK-------DQLYNT-------LSSGEKKKILFL 185
Cdd:cd03289 82 ------IPQKVFIFSGTFR-----KNLDPYGKWSDEEIWKVAEEVGLKsvieqfpGQLDFVlvdggcvLSHGHKQLMCLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 186 RSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKeyHSKKKFTSLYITHRPEEIPDFySKAVLLKEGKVIHFGPIEECFTEK 265
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLEC-QRFLVIEENKVRQYDSIQKLLNEK 227
|
..
4HZI_A 266 NL 267
Cdd:cd03289 228 SH 229
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
50-281 |
1.82e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.86 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIwATSGTIRLFQETYGEIAIQDLRKRIGILdsSQQENSiqrkltvk 129
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYL--SQQQTP-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 130 dTILTGLFHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLY---NTLSSGEKKKI----LFL---RSIVNEPDFLIMDE 199
Cdd:PRK03695 81 -PFAMPVFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLGrsvNQLSGGEWQRVrlaaVVLqvwPDINPAGQLLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 200 PCSSLDLtAREDFLgflkeYHSKKKFTSLYIT-----HRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEKNLEDLYDIP 274
Cdd:PRK03695 160 PMNSLDV-AQQAAL-----DRLLSELCQQGIAvvmssHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVN 233
|
....*..
4HZI_A 275 LQVQRIE 281
Cdd:PRK03695 234 FRRLDVE 240
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
41-205 |
2.13e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.19 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 41 SYKpTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILdssQQEn 120
Cdd:PRK10790 349 AYR-DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV---QQD- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 siqrKLTVKDTILTGLfhTIGyyRDPSPEEETKTLQILKDSDLL-SKKDQLY-------NTLSSGEKKKILFLRSIVNEP 192
Cdd:PRK10790 424 ----PVVLADTFLANV--TLG--RDISEEQVWQALETVQLAELArSLPDGLYtplgeqgNNLSVGQKQLLALARVLVQTP 495
|
170
....*....|...
4HZI_A 193 DFLIMDEPCSSLD 205
Cdd:PRK10790 496 QILILDEATANID 508
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
39-256 |
2.18e-09 |
|
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: 56.12 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 39 KISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMI---WATSGTIRLFQETYGEIAIQDLRKrigILDS 115
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTegnVSVEGDIHYNGIPYKEFAEKYPGE---IIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 116 SQQENSIQrKLTVKDTIltglfhtigyyrdpspeeetktlqilkDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFL 195
Cdd:cd03233 89 SEEDVHFP-TLTVRETL---------------------------DFALRCKGNEFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
4HZI_A 196 IMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRP-EEIPDFYSKAVLLKEGKVIHFG 256
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQAsDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
32-216 |
2.19e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.87 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQetygeiaiqdlrkriG 111
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK---------------G 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 112 IldssqqensiqrKLtvkdtiltGLF--HTIGYYR-DPSPEE------ETKTLQILKD--------SDLLSKKDQLYntl 174
Cdd:PRK10636 375 I------------KL--------GYFaqHQLEFLRaDESPLQhlarlaPQELEQKLRDylggfgfqGDKVTEETRRF--- 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
4HZI_A 175 SSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTARE-------DFLGFL 216
Cdd:PRK10636 432 SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQaltealiDFEGAL 480
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
48-260 |
3.54e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 56.25 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 48 TILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRL--FQETYGEIAIQDLRKRIGILdsSQQENsIQRK 125
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdgLKVNDPKVDERLIRQEAGMV--FQQFY-LFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 126 LTVKDTILTGLFHTIGYYRDpspEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLD 205
Cdd:PRK09493 92 LTALENVMFGPLRVRGASKE---EAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
4HZI_A 206 LTAREDFLGFLKEYhSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:PRK09493 169 PELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
34-292 |
3.60e-09 |
|
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: 57.14 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGM----IWatSGTIRLFQETYGEIAIQDL-RK 108
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgTW--DGEIYWSGSPLKASNIRDTeRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 109 RIGILdssQQENSIQRKLTVKDTILTG--LFHTIGYYRDPS----PEEETKTLQILKDSDLLSKKDqlyntLSSGEKKKI 182
Cdd:TIGR02633 79 GIVII---HQELTLVPELSVAENIFLGneITLPGGRMAYNAmylrAKNLLRELQLDADNVTRPVGD-----YGGGQQQLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 183 LFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYhSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECF 262
Cdd:TIGR02633 151 EIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMS 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
4HZI_A 263 TE--------KNLEDLY-----DIPLQVQRIEN--TWSVI-PKQKR 292
Cdd:TIGR02633 230 EDdiitmmvgREITSLYphephEIGDVILEARNltCWDVInPHRKR 275
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
51-212 |
4.27e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.44 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 51 DSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQEtygEIAIQDL--RKRIGILdssQQENSIQRKLTV 128
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---PVDAGDIatRRRVGYM---SQAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 129 KDTIL--TGLFHTigyyrdpsPEEETKTL--QILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSL 204
Cdd:NF033858 357 RQNLElhARLFHL--------PAAEIAARvaEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
....*...
4HZI_A 205 DLTAREDF 212
Cdd:NF033858 429 DPVARDMF 436
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
47-260 |
6.22e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 47 KTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLI----YGMIWATSGTIrlfqeTYGEIAIQDLRK--RIGILDSSQQEN 120
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVI-----TYDGITPEEIKKhyRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 SIQRkLTVKDTIltglfHTIGYYRDPS--PEEETKTLQILKDSDLLSKK---DQLYNT---------LSSGEKKKILFLR 186
Cdd:TIGR00956 149 HFPH-LTVGETL-----DFAARCKTPQnrPDGVSREEYAKHIADVYMATyglSHTRNTkvgndfvrgVSGGERKRVSIAE 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
4HZI_A 187 SIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRP-EEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCsQDAYELFDKVIVLYEGYQIYFGPADK 297
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
35-268 |
7.69e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRlfqetYGEIAiqdlrkRIGIL- 113
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-----WSENA------NIGYYa 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 -DSSQQ-ENSIQrkltvkdtiltgLFHTIGYYRDPSPEEET--KTL-QILKDSDLLSKKdqlYNTLSSGEKKKILFLRSI 188
Cdd:PRK15064 389 qDHAYDfENDLT------------LFDWMSQWRQEGDDEQAvrGTLgRLLFSQDDIKKS---VKVLSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 189 VNEPDFLIMDEPCSSLDLTAREDFLGFLKEYhskkKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHF-GPIEECFTEKNL 267
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESIESLNMALEKY----EGTLIFVSHDREFVSSLATRIIEITPDGVVDFsGTYEEYLRSQGI 529
|
.
4HZI_A 268 E 268
Cdd:PRK15064 530 E 530
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
40-260 |
8.82e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 8.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 40 ISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILDSSQqe 119
Cdd:PLN03232 1242 LRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSP-- 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 120 nsiqrkltvkdTILTGlfhTIGYYRDPSPEEETKTL-QILKDSDLlskKDQLYN--------------TLSSGEKKKILF 184
Cdd:PLN03232 1320 -----------VLFSG---TVRFNIDPFSEHNDADLwEALERAHI---KDVIDRnpfgldaevseggeNFSVGQRQLLSL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 185 LRSIVNEPDFLIMDEPCSSLDL--------TAREDFlgflkeyhskKKFTSLYITHRPEEIPDFySKAVLLKEGKVIHFG 256
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVrtdsliqrTIREEF----------KSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYD 1451
|
....
4HZI_A 257 PIEE 260
Cdd:PLN03232 1452 SPQE 1455
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
50-265 |
8.94e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 8.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrLF--QETYGEIAIQDLRKRIGILdssQQENSIQRKLT 127
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI-LFqgKEIDFKSSKEALENGISMV---HQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 128 VKDTILTGLFHTIGYYRDPSPE-EETKTlqILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSldL 206
Cdd:PRK10982 90 VMDNMWLGRYPTKGMFVDQDKMyRDTKA--IFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS--L 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 207 TARE-DFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECFTEK 265
Cdd:PRK10982 166 TEKEvNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDK 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-205 |
9.82e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 29 GKInsLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqETYGEIAIQDLRK 108
Cdd:PRK11147 316 GKI--VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC--GTKLEVAYFDQHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 109 RIGILDSSQQENSIQRKLTVkdTILTGLFHTIGYYRDpspeeetktlqilkdsDLLSKKDQL--YNTLSSGEKKKILFLR 186
Cdd:PRK11147 392 AELDPEKTVMDNLAEGKQEV--MVNGRPRHVLGYLQD----------------FLFHPKRAMtpVKALSGGERNRLLLAR 453
|
170
....*....|....*....
4HZI_A 187 SIVNEPDFLIMDEPCSSLD 205
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLD 472
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
42-260 |
9.86e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.28 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 42 YKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILDSSQqens 121
Cdd:PLN03130 1247 YRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAP---- 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 122 iqrkltvkdTILTGlfhTIGYYRDPSPEEetktlqilKDSDLLSK------KDQLY-NTL-------------SSGEKKK 181
Cdd:PLN03130 1323 ---------VLFSG---TVRFNLDPFNEH--------NDADLWESlerahlKDVIRrNSLgldaevseagenfSVGQRQL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 182 ILFLRSIVNEPDFLIMDEPCSSLDL--------TAREDFlgflkeyhskKKFTSLYITHRPEEIPDfYSKAVLLKEGKVI 253
Cdd:PLN03130 1383 LSLARALLRRSKILVLDEATAAVDVrtdaliqkTIREEF----------KSCTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
|
....*..
4HZI_A 254 HFGPIEE 260
Cdd:PLN03130 1452 EFDTPEN 1458
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
53-258 |
1.90e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.06 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 53 VSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQD-LRKRIGILDSSQQENSIQRKLTVKDT 131
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 132 ILTGLFHTIGYYRDPSPEEET-----KTLQILkdsdlLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDL 206
Cdd:PRK15439 362 VCALTHNRRGFWIKPARENAVleryrRALNIK-----FNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
4HZI_A 207 TAREDFLGFLKEYhSKKKFTSLYITHRPEEIPDFySKAVLlkegkVIHFGPI 258
Cdd:PRK15439 437 SARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQM-ADRVL-----VMHQGEI 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
53-209 |
2.11e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 53 VSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQEtygEIAIQD----LRKRIGILDSSQQEN------SI 122
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRSpldaVKKGMAYITESRRDNgffpnfSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 123 QRKLTVKDTI-LTGLFHTIGYYrdpSPEEETKTLQilKDSDLLSKK----DQLYNTLSSGEKKKILFLRSIVNEPDFLIM 197
Cdd:PRK09700 359 AQNMAISRSLkDGGYKGAMGLF---HEVDEQRTAE--NQRELLALKchsvNQNITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170
....*....|..
4HZI_A 198 DEPCSSLDLTAR 209
Cdd:PRK09700 434 DEPTRGIDVGAK 445
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
46-265 |
2.21e-08 |
|
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: 55.30 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrlfqetygeiaiqdlrKRIGILDSSQQENSIQRK 125
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------------KHSGRISFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 126 lTVKDTILTGLfhTIGYYRDPSPeeeTKTLQILKDSDLLSKKDQLY-----NTLSSGEKKKILFLRSIVNEPDFLIMDEP 200
Cdd:TIGR01271 502 -TIKDNIIFGL--SYDEYRYTSV---IKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
4HZI_A 201 CSSLD-LTAREDFLGFLKEYHSKKkfTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGPIEECFTEK 265
Cdd:TIGR01271 576 FTHLDvVTEKEIFESCLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-209 |
3.89e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.63 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 29 GKINSLLSLEKIS--YKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYgEIAIQDL 106
Cdd:TIGR01257 1932 GNKTDILRLNELTkvYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 107 RKRIGIldsSQQENSIqrkltvkDTILTGLFHTIGYYR---DPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKIL 183
Cdd:TIGR01257 2011 HQNMGY---CPQFDAI-------DDLLTGREHLYLYARlrgVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLS 2080
|
170 180
....*....|....*....|....*.
4HZI_A 184 FLRSIVNEPDFLIMDEPCSSLDLTAR 209
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
40-267 |
4.77e-08 |
|
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: 54.18 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 40 ISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILDssqqe 119
Cdd:TIGR00957 1292 LRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIP----- 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 120 nsiqrkltvKDTIL-TGlfhTIGYYRDP----SPEEETKTLQILKDSDLLSKKDQLYN--------TLSSGEKKKILFLR 186
Cdd:TIGR00957 1367 ---------QDPVLfSG---SLRMNLDPfsqySDEEVWWALELAHLKTFVSALPDKLDhecaeggeNLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 187 SIVNEPDFLIMDEPCSSLDL--------TAREDFlgflkeyhskKKFTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGPI 258
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLetdnliqsTIRTQF----------EDCTVLTIAHRLNTIMD-YTRVIVLDKGEVAEFGAP 1503
|
....*....
4HZI_A 259 EECFTEKNL 267
Cdd:TIGR00957 1504 SNLLQQRGI 1512
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
34-267 |
8.81e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIR-LFQET--YGEIAIQDlrKRI 110
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVtfNGPKSSQE--AGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 111 GILdssQQENSIQRKLTVKDTIL-----TGLFHTIGYYRdpSPEEETKTLQILKdsdLLSKKDQLYNTLSSGEKKKILFL 185
Cdd:PRK10762 82 GII---HQELNLIPQLTIAENIFlgrefVNRFGRIDWKK--MYAEADKLLARLN---LRFSSDKLVGELSIGEQQMVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 186 RSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTsLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEEcFTEK 265
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGI-VYISHRLKEIFEICDDVTVFRDGQFIAEREVAD-LTED 231
|
..
4HZI_A 266 NL 267
Cdd:PRK10762 232 SL 233
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
35-199 |
8.88e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYK-PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGil 113
Cdd:PRK10522 323 LELRNVTFAyQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 dssqqensiqrkltvkdTILTG--LF-HTIGYYRDPSPEEETKT-LQILKDSDLLSKKD-QLYNT-LSSGEKKKILFLRS 187
Cdd:PRK10522 401 -----------------AVFTDfhLFdQLLGPEGKPANPALVEKwLERLKMAHKLELEDgRISNLkLSKGQKKRLALLLA 463
|
170
....*....|..
4HZI_A 188 IVNEPDFLIMDE 199
Cdd:PRK10522 464 LAEERDILLLDE 475
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
50-232 |
1.85e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.32 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLV---NLIYGMIWATSGTIRLF---QETY-GEIAIQDLRKRIGILdsSQQENSI 122
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGFRVEGKVTfhgKNLYaPDVDPVEVRRRIGMV--FQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 123 QRklTVKDTILTGLfHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCS 202
Cdd:PRK14243 104 PK--SIYDNIAYGA-RINGYKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190
....*....|....*....|....*....|...
4HZI_A 203 SLD--LTAR-EDFLGFLKEyhskkKFTSLYITH 232
Cdd:PRK14243 181 ALDpiSTLRiEELMHELKE-----QYTIIIVTH 208
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
56-251 |
2.00e-07 |
|
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: 50.87 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 56 EIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETygeIAIQdlrkrigildssQQENSIQRKLTVKDTI--L 133
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---VSYK------------PQYIKADYEGTVRDLLssI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 134 TGLFHTIGYYRdpspeeeTKTLQILKDSDLLskkDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFL 213
Cdd:cd03237 86 TKDFYTHPYFK-------TEIAKPLQIEQIL---DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
4HZI_A 214 GFLKEYHSKKKFTSLYITHrpeeipDFY-----SKAVLLKEGK 251
Cdd:cd03237 156 KVIRRFAENNEKTAFVVEH------DIImidylADRLIVFEGE 192
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
46-232 |
2.11e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.38 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKT-ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGmiwatsgtirLFQETYGEIAIQDlrKRIGILDSSQ------- 117
Cdd:PRK11650 15 GKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG----------LERITSGEIWIGG--RVVNELEPADrdiamvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 118 QENSIQRKLTVKDTILTGL----FhtigyyrdpsPEEE-----TKTLQILKDSDLLSKKDQlynTLSSGEKKKILFLRSI 188
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLkirgM----------PKAEieervAEAARILELEPLLDRKPR---ELSGGQRQRVAMGRAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
4HZI_A 189 VNEPDFLIMDEPCSSLDLTAR-----EdflgfLKEYHSKKKFTSLYITH 232
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRvqmrlE-----IQRLHRRLKTTSLYVTH 193
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
34-200 |
2.62e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.56 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISykptGKTILDSVSFEIKTNEhcVL--LGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYgEI-----AIQ-- 104
Cdd:COG1129 256 VLEVEGLS----VGGVVRDVSFSVRAGE--ILgiAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIrsprdAIRag 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 105 ------DlRKRIGI-LDSSQQENSIqrkLTVKDTILTGLFhtigyyRDPSPEEET-----KTLQIlKDSDLlskkDQLYN 172
Cdd:COG1129 329 iayvpeD-RKGEGLvLDLSIRENIT---LASLDRLSRGGL------LDRRRERALaeeyiKRLRI-KTPSP----EQPVG 393
|
170 180
....*....|....*....|....*...
4HZI_A 173 TLSSGEKKKILFLRSIVNEPDFLIMDEP 200
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
34-233 |
3.37e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.95 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGeiaiQDLRKRIGIL 113
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 DSSQQENSIQRKLTVKDTILTGLFHTIGYYrdpspeEETKTLQILKDSDLLskkDQLYNTLSSGEKKKILFLRSIVNEPD 193
Cdd:PRK13540 77 CFVGHRSGINPYLTLRENCLYDIHFSPGAV------GITELCRLFSLEHLI---DYPCGLLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
4HZI_A 194 FLIMDEPCSSLDLTAREDFLGFLKEyHSKKKFTSLYITHR 233
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSHQ 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
50-209 |
4.35e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQET-----------YGEIAIQDLRKRIG-ILDSSQ 117
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEvvtrspqdglaNGIVYISEDRKRDGlVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 118 QEN--------------SIQRK---LTVKDTIltGLFHTigyyRDPSpeeetktlqilkdsdllskKDQLYNTLSSGEKK 180
Cdd:PRK10762 348 KENmsltalryfsraggSLKHAdeqQAVSDFI--RLFNI----KTPS-------------------MEQAIGLLSGGNQQ 402
|
170 180
....*....|....*....|....*....
4HZI_A 181 KILFLRSIVNEPDFLIMDEPCSSLDLTAR 209
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDVGAK 431
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
46-260 |
5.06e-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: 49.86 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 46 GKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrlfqetygeiaiqdlrKRIGILDSSQQENSIQRK 125
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----------------KHSGRISFSSQFSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 126 lTVKDTILTGLfhTIGYYRDPSPeeeTKTLQILKDSDLLSKKDQLYN-----TLSSGEKKKILFLRSIVNEPDFLIMDEP 200
Cdd:cd03291 113 -TIKENIIFGV--SYDEYRYKSV---VKACQLEEDITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
4HZI_A 201 CSSLDL-TAREDFLGFLKEYHSKKkfTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGPIEE 260
Cdd:cd03291 187 FGYLDVfTEKEIFESCVCKLMANK--TRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSE 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
53-262 |
6.37e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 53 VSFEIKTNEHCVLLGRNGAGKS-TLVNLIygmiwatsgtiRLFQETYGEIAIQD--LRKR----IGILDSSQ-------- 117
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSvTALALM-----------RLLEQAGGLVQCDKmlLRRRsrqvIELSEQSAaqmrhvrg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 118 -------QE--NSIQRKLTVKDTILTGLFHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRSI 188
Cdd:PRK10261 104 admamifQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4HZI_A 189 VNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECF 262
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIF 257
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
44-234 |
7.05e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.52 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 44 PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIyGMIWATSGTI-------RLF---QETYgeIAIQDLRKRIGIL 113
Cdd:TIGR00954 462 PNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYGGRltkpakgKLFyvpQRPY--MTLGTLRDQIIYP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 DSSqqENSIQRKLTVKDTIltglfhtigyyrdpspeeetKTLQILKDSDLLSKKDQL------YNTLSSGEKKKILFLRS 187
Cdd:TIGR00954 539 DSS--EDMKRRGLSDKDLE--------------------QILDNVQLTHILEREGGWsavqdwMDVLSGGEKQRIAMARL 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
4HZI_A 188 IVNEPDFLIMDEPCSSLDLtareDFLGFLKEYHSKKKFTSLYITHRP 234
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSV----DVEGYMYRLCREFGITLFSVSHRK 639
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
32-256 |
7.72e-07 |
|
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: 48.39 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKISY----KPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMiwATSGTIRlfqetyGEIAI---- 103
Cdd:cd03232 1 GSVLTWKNLNYtvpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGR--KTAGVIT------GEILIngrp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 104 --QDLRKRIGILdssQQENSIQRKLTVKDTIltgLFHtiGYYRDPSPEEetktlqilkdsdllskkdqlyntlssgekKK 181
Cdd:cd03232 73 ldKNFQRSTGYV---EQQDVHSPNLTVREAL---RFS--ALLRGLSVEQ-----------------------------RK 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 182 ILflrSI----VNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRP-EEIPDFYSKAVLLKE-GKVIHF 255
Cdd:cd03232 116 RL---TIgvelAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQ-AILCTIHQPsASIFEKFDRLLLLKRgGKTVYF 191
|
.
4HZI_A 256 G 256
Cdd:cd03232 192 G 192
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
53-209 |
1.43e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 53 VSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETygeIAIQDL--------------RKRIGILD-SSQ 117
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKP---IDIRSPrdairagimlcpedRKAEGIIPvHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 118 QEN---SIQRKltvkdtiltglFHTIGYYRDPSPEEETKTLQIlkdsDLLSKK----DQLYNTLSSGEKKKILFLRSIVN 190
Cdd:PRK11288 349 ADNiniSARRH-----------HLRAGCLINNRWEAENADRFI----RSLNIKtpsrEQLIMNLSGGNQQKAILGRWLSE 413
|
170
....*....|....*....
4HZI_A 191 EPDFLIMDEPCSSLDLTAR 209
Cdd:PRK11288 414 DMKVILLDEPTRGIDVGAK 432
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
50-262 |
1.43e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrLFQ----ETYGEIAIQDLRKRIGILDSSQQEnSIQRK 125
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI-IFNgqriDTLSPGKLQALRRDIQFIFQDPYA-SLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 126 LTVKDTILTGL-FHTIGyyrdPSPEEETKTLQILKDSDLLSKKDQLY-NTLSSGEKKKILFLRSIVNEPDFLIMDEPCSS 203
Cdd:PRK10261 418 QTVGDSIMEPLrVHGLL----PGKAAAARVAWLLERVGLLPEHAWRYpHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 204 LDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEECF 262
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF 552
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
44-210 |
1.63e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 44 PTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrlfqetygeiaIQDLRKRIGILDssqqensiQ 123
Cdd:PLN03073 519 PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------FRSAKVRMAVFS--------Q 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 124 RKLTVKDTILTGLFHTIGYYrdPS-PEEETKT-LQILKDSDLLSKkdQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPC 201
Cdd:PLN03073 580 HHVDGLDLSSNPLLYMMRCF--PGvPEQKLRAhLGSFGVTGNLAL--QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
....*....
4HZI_A 202 SSLDLTARE 210
Cdd:PLN03073 656 NHLDLDAVE 664
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
35-272 |
2.36e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 35 LSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRL------FQETYGEIAiqdlrK 108
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdgqemrFASTTAALA-----A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 109 RIGILdssQQENSIQRKLTVKDTILTGLFHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLyNTLSSGEKKKILFLRSI 188
Cdd:PRK11288 80 GVAII---YQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPL-KYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 189 VNEPDFLIMDEPCSSldLTARE-DFL-GFLKEYHSKKKFTsLYITHRPEEIPDFYSKAVLLKEG-KVIHFGPIEE----- 260
Cdd:PRK11288 156 ARNARVIAFDEPTSS--LSAREiEQLfRVIRELRAEGRVI-LYVSHRMEEIFALCDAITVFKDGrYVATFDDMAQvdrdq 232
|
250
....*....|....*
4HZI_A 261 ---CFTEKNLEDLYD 272
Cdd:PRK11288 233 lvqAMVGREIGDIYG 247
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
174-232 |
2.57e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 2.57e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 174 LSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITH 232
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITH 215
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-267 |
3.60e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKISYKPTgktiLDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIwatsgtirlfqeTYGEIAIQDLRkriG 111
Cdd:PLN03232 619 NGYFSWDSKTSKPT----LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL------------SHAETSSVVIR---G 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 112 ILDSSQQENSIQRKlTVKDTILTGL-FHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNtLSSGEKKKILFLRSIVN 190
Cdd:PLN03232 680 SVAYVPQVSWIFNA-TVRENILFGSdFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVN-ISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
4HZI_A 191 EPDFLIMDEPCSSLDL-TAREDFLGFLKEYHSKKkfTSLYITHRPEEIPdFYSKAVLLKEGKVIHFGPIEECFTEKNL 267
Cdd:PLN03232 758 NSDIYIFDDPLSALDAhVAHQVFDSCMKDELKGK--TRVLVTNQLHFLP-LMDRIILVSEGMIKEEGTFAELSKSGSL 832
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
34-262 |
3.83e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 47.31 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrLFQetyGEIAiqDLRKRiGIL 113
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQ---GKPL--DYSKR-GLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 114 DSSQQENSI------QRKLTVKDTILTGLFHTIGYyrdpsPEEET--KTLQILKDSDLLSKKDQLYNTLSSGEKKKILFL 185
Cdd:PRK13638 74 ALRQQVATVfqdpeqQIFYTDIDSDIAFSLRNLGV-----PEAEItrRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
4HZI_A 186 RSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYiTHRPEEIPDFYSKAVLLKEGKVIHFGPIEECF 262
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIS-SHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
41-257 |
5.44e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.40 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 41 SYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRKRIGILDssqqen 120
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVS------ 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 121 siQRKLTVKDTILtglfHTIGYYR-DPSPE--EETKTLQILKDsDLLsKKDQLYNT--------LSSGEKKKILFLRSIV 189
Cdd:PRK10789 396 --QTPFLFSDTVA----NNIALGRpDATQQeiEHVARLASVHD-DIL-RLPQGYDTevgergvmLSGGQKQRISIARALL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
4HZI_A 190 NEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKkfTSLYITHRPEEIPDfYSKAVLLKEGKVIHFGP 257
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTE-ASEILVMQHGHIAQRGN 532
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
34-265 |
5.74e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIwaTSGTIRlfqetyGEIAI--QDLRKRiG 111
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY--PHGTYE------GEIIFegEELQAS-N 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 112 ILDSSQ-------QENSIQRKLTVKDTILTGlfHTI---GYYRDPSPEEETKTLqiLKDSDLLSKKDQLYNTLSSGEKKK 181
Cdd:PRK13549 76 IRDTERagiaiihQELALVKELSVLENIFLG--NEItpgGIMDYDAMYLRAQKL--LAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 182 ILFLRSIVNEPDFLIMDEPCSSldLTARE-----DFLGFLKeyhsKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFG 256
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTAS--LTESEtavllDIIRDLK----AHGIACIYISHKLNEVKAISDTICVIRDGRHIGTR 225
|
....*....
4HZI_A 257 PIEECFTEK 265
Cdd:PRK13549 226 PAAGMTEDD 234
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
45-238 |
1.69e-05 |
|
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: 45.01 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 45 TGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGE--IAIQDLRKRIGILDSSQQENSI 122
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEpsFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 123 QRklTVKDTILTGLFHTIGYYRDPSpeeETKTLQilKDSDLLSKKDQLYN-----TLSSGEKKKILFLRSIVNEPDFLIM 197
Cdd:cd03290 92 NA--TVEENITFGSPFNKQRYKAVT---DACSLQ--PDIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
4HZI_A 198 DEPCSSLDL-----TAREDFLGFLKEyhskKKFTSLYITHRPEEIP 238
Cdd:cd03290 165 DDPFSALDIhlsdhLMQEGILKFLQD----DKRTLVLVTHKLQYLP 206
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
32-260 |
1.75e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.14 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 32 NSLLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDL---RK 108
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 109 RIGILdssQQENSIQRKLTVKDTILTGLF-HTigyyRDPSPEEETKTLQILKDSDLLSKKDQLYNTLSSGEKKKILFLRS 187
Cdd:PRK11831 85 RMSML---FQSGALFTDMNVFDNVAYPLReHT----QLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4HZI_A 188 IVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFYSKAVLLKEGKVIHFGPIEE 260
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
43-260 |
3.07e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 43 KPTgktiLDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGT---IRlfqetyGEIAIqdlrkrigILDSSQQE 119
Cdd:PLN03130 630 RPT----LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDAsvvIR------GTVAY--------VPQVSWIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 120 NSiqrklTVKDTILTGL-FHTIGYYRDPSPEEETKTLQILKDSDLLSKKDQLYNtLSSGEKKKILFLRSIVNEPDFLIMD 198
Cdd:PLN03130 692 NA-----TVRDNILFGSpFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFD 765
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
4HZI_A 199 EPCSSLDL-TAREDFLGFLKEYHSKKkfTSLYITHRPEEIPDFySKAVLLKEGKVIHFGPIEE 260
Cdd:PLN03130 766 DPLSALDAhVGRQVFDKCIKDELRGK--TRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEE 825
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
34-206 |
3.31e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.07 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLfqetYGEIAIQDLRKR---- 109
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI----DGKTATRGDRSRfmay 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 110 IGILDSSQQENSIQRKLtvkdTILTGLFhtiGYYRDPSPeeeTKTLQILkdsDLLSKKDQLYNTLSSGEKKKILFLRSIV 189
Cdd:PRK13543 87 LGHLPGLKADLSTLENL----HFLCGLH---GRRAKQMP---GSALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWL 153
|
170
....*....|....*..
4HZI_A 190 NEPDFLIMDEPCSSLDL 206
Cdd:PRK13543 154 SPAPLWLLDEPYANLDL 170
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
49-205 |
3.77e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 49 ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYgmiwatsgtiRLFQETYGEIAIQD-----------LRKRIGI----- 112
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIE----------RLYDPTEGDIIINDshnlkdinlkwWRSKIGVvsqdp 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 113 -LDSSQQENSIQRKL-TVKD--------------------------TILTGLFHTIGYYRDPSPE-EETKTLQILKDSDL 163
Cdd:PTZ00265 470 lLFSNSIKNNIKYSLySLKDlealsnyynedgndsqenknkrnscrAKCAGDLNDMSNTTDSNELiEMRKNYQTIKDSEV 549
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
4HZI_A 164 LSKKDQL------------YNTL--------SSGEKKKILFLRSIVNEPDFLIMDEPCSSLD 205
Cdd:PTZ00265 550 VDVSKKVlihdfvsalpdkYETLvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
162-262 |
1.03e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 162 DLLSKKDQLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEIPDFY 241
Cdd:PRK11022 142 DPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAA 221
|
90 100
....*....|....*....|.
4HZI_A 242 SKAVLLKEGKVIHFGPIEECF 262
Cdd:PRK11022 222 HKIIVMYAGQVVETGKAHDIF 242
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
31-235 |
1.74e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 42.79 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 31 INSLLSLEKI--SYkPTGKT---ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRlfqetygeIAIQD 105
Cdd:PRK10535 1 MTALLELKDIrrSY-PSGEEqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYR--------VAGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 106 lrkrIGILDSSQ-------------QENSIQRKLTVKDTILTGLFhtigYYRDPSPEEETKTLQILKDSDLLSKKDQLYN 172
Cdd:PRK10535 72 ----VATLDADAlaqlrrehfgfifQRYHLLSHLTAAQNVEVPAV----YAGLERKQRLLRAQELLQRLGLEDRVEYQPS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
4HZI_A 173 TLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKfTSLYITHRPE 235
Cdd:PRK10535 144 QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQ 205
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
50-260 |
9.03e-04 |
|
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: 40.70 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 50 LDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIwatsgtirlfQETYGEIAIQdlrkriGILDSSQQENSIQRKlTVK 129
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEM----------DKVEGHVHMK------GSVAYVPQQAWIQND-SLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 130 DTILTGLFHTIGYYRdpspeEETKTLQILKDSDLLSKKDQLY-----NTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSL 204
Cdd:TIGR00957 717 ENILFGKALNEKYYQ-----QVLEACALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 205 DL-TAREDFLGFLKEYHSKKKFTSLYITHRPEEIP--DFyskAVLLKEGKVIHFGPIEE 260
Cdd:TIGR00957 792 DAhVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPqvDV---IIVMSGGKISEMGSYQE 847
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
65-258 |
1.17e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.60 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 65 LLGRNGAGKSTLVNLIYGMiwATSGTIRlfqetyGEIAIQDLRKR----IGILDSSQQENSIQRKLTVKDTILTGLFHTI 140
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGR--KTGGYIE------GDIRISGFPKKqetfARISGYCEQNDIHSPQVTVRESLIYSAFLRL 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 141 GyyRDPSPEEETKTL-QILKDSDLLSKKDQLYNT-----LSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLG 214
Cdd:PLN03140 983 P--KEVSKEEKMMFVdEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMR 1060
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
4HZI_A 215 FLKEYHSKKKfTSLYITHRPE-EIPDFYSKAVLLKE-GKVIHFGPI 258
Cdd:PLN03140 1061 TVRNTVDTGR-TVVCTIHQPSiDIFEAFDELLLMKRgGQVIYSGPL 1105
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
37-235 |
1.65e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 37 LEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLvnLIYGMIWATSGTIR------LFQETYGE--IAIQ---- 104
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTF--LRYMAMHAIDGIPKncqilhVEQEVVGDdtTALQcvln 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 105 -DLrKRIGILDSSQQENSIQRKLTVKDTILTGLFHTI-GYYRDPSPEE----------------ETKTLQILK----DSD 162
Cdd:PLN03073 258 tDI-ERTQLLEEEAQLVAQQRELEFETETGKGKGANKdGVDKDAVSQRleeiykrlelidaytaEARAASILAglsfTPE 336
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4HZI_A 163 LLSKKDqlyNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAredfLGFLKEYHSKKKFTSLYITHRPE 235
Cdd:PLN03073 337 MQVKAT---KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA----VLWLETYLLKWPKTFIVVSHARE 402
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
34-210 |
1.77e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 39.62 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYK-PTGKTILDSVSFEIKTNEhcVL--LGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRK-- 108
Cdd:COG3845 257 VLEVENLSVRdDRGVPALKDVSLEVRAGE--ILgiAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRlg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 109 -------RIG---ILDSSQQENSIqrkltvkdtiltglfhtIGYYRDP---------SPEEETKTLQILKDSDLLSKK-D 168
Cdd:COG3845 335 vayipedRLGrglVPDMSVAENLI-----------------LGRYRRPpfsrggfldRKAIRAFAEELIEEFDVRTPGpD 397
|
170 180 190 200
....*....|....*....|....*....|....*....|..
4HZI_A 169 QLYNTLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTARE 210
Cdd:COG3845 398 TPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIE 439
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
173-237 |
2.23e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.63 E-value: 2.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
4HZI_A 173 TLSSGEKKKILFLRSIVNEPDFLIMDEPCSSLDLTAREDFLGFLKEYHSKKKFTSLYITHRPEEI 237
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-238 |
3.11e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 37.93 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 34 LLSLEKISYKPTGKTILDsVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIrlfqeTYGEIAIQDLRK----R 109
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI-----YYKNCNINNIAKpyctY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 110 IGildssqQENSIQRKLTVKDTILtglFHTIGYyrdPSPEEETKTLQILKDSDLLSKKdqLYNtLSSGEKKKILFLRSIV 189
Cdd:PRK13541 75 IG------HNLGLKLEMTVFENLK---FWSEIY---NSAETLYAAIHYFKLHDLLDEK--CYS-LSSGMQKIVAIARLIA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
4HZI_A 190 NEPDFLIMDEPCSSLDLTAReDFLGFLKEYHSKKKFTSLYITHRPEEIP 238
Cdd:PRK13541 140 CQSDLWLLDEVETNLSKENR-DLLNNLIVMKANSGGIVLLSSHLESSIK 187
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
49-108 |
6.42e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.22 E-value: 6.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
4HZI_A 49 ILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIRLFQETYGEIAIQDLRK 108
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
34-92 |
6.95e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 37.21 E-value: 6.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
4HZI_A 34 LLSLEKISYKPTGKTILDSVSFEIKTNEHCVLLGRNGAGKSTLVNLIYGMIWATSGTIR 92
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| |
