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Conserved domains on  [gi|1938945303]
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Chain d, V-type proton ATPase subunit d

Protein Classification

V0D/AC39 family V-type ATPase subunit( domain architecture ID 10488051)

V0D/AC39 family V-type ATPase subunit such as Deinococcus radiodurans V-type ATPase subunit C, and eukaryotic V-type proton ATPase subunit d that is part of the integral membrane V0 proton pore complex of vacuolar ATPase, which is responsible for acidifying a variety of intracellular compartments in cells and providing the energy required for transport in the vacuolar system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
vATP-synt_AC39 pfam01992
ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP ...
13-338 8.93e-97

ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP synthase, and the C subunit from archaebacterial ATP synthase. The family also includes subunit C from the Sodium transporting ATP synthase from Enterococcus hirae.


:

Pssm-ID: 426553  Cd Length: 333  Bit Score: 290.33  E-value: 8.93e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  13 IEGVVRGYRNGLLSNNQYINLTQCDTLEDLKLQLSSTDYGNFLSSVSSeSLTTSLIQEYASSKLYHEFNYIRDQSSGSTR 92
Cdd:pfam01992   1 LNARVRAMESKLLTEEDYERLLQCESLEEAVRYLKETGYGDFLADEES-PLHRGDIEKALRRELAKTFEKLRRFAPGLSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  93 KFMDYITYGYMIDNVALMITGTIHDRDKGEILQRCHPLGWFDTLP--TLSVATDLESLYETVLvDTPLAPYFKNCFDTAE 170
Cdd:pfam01992  80 EFLDLYLYRYDIHNLKLLLRGKLSGLDLEELLEFLIPLGTLSALDldKLIEAKDVEELVEALL-GTPYAEALEEALDELE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 171 ELDDmnIEIIRNKLYKAYLEDFYNFVtEEIPEPAKECMQTLLGFEADRRSINIALNSLQSSDIDPDLKSDLLPNIGKLYP 250
Cdd:pfam01992 159 ETGD--LQLIENALDKAYYEDLYKFC-KKLGGKTAEILREYLGFEIDLRNIKIILRSKKYGKLSPEDIYKLLIPGGSLSP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 251 LATFHLAQAQDFEGVRAALANvYEYRGFLETGN---------LEDHFYQLEMELCRD-AFTQQFAISTVWAWMKSKEQEV 320
Cdd:pfam01992 236 EELKALAEAEDVEEVLAALEG-TPYGELLSEALeeltgslsaLERALDNYLLELAKKlARYQPFSIGPVLAYLKLKEQEI 314
                         330
                  ....*....|....*....
gi 1938945303 321 RNITWIAECIAQN-QRERI 338
Cdd:pfam01992 315 RNLRIIAEGKRYGlPPEEI 333
 
Name Accession Description Interval E-value
vATP-synt_AC39 pfam01992
ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP ...
13-338 8.93e-97

ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP synthase, and the C subunit from archaebacterial ATP synthase. The family also includes subunit C from the Sodium transporting ATP synthase from Enterococcus hirae.


Pssm-ID: 426553  Cd Length: 333  Bit Score: 290.33  E-value: 8.93e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  13 IEGVVRGYRNGLLSNNQYINLTQCDTLEDLKLQLSSTDYGNFLSSVSSeSLTTSLIQEYASSKLYHEFNYIRDQSSGSTR 92
Cdd:pfam01992   1 LNARVRAMESKLLTEEDYERLLQCESLEEAVRYLKETGYGDFLADEES-PLHRGDIEKALRRELAKTFEKLRRFAPGLSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  93 KFMDYITYGYMIDNVALMITGTIHDRDKGEILQRCHPLGWFDTLP--TLSVATDLESLYETVLvDTPLAPYFKNCFDTAE 170
Cdd:pfam01992  80 EFLDLYLYRYDIHNLKLLLRGKLSGLDLEELLEFLIPLGTLSALDldKLIEAKDVEELVEALL-GTPYAEALEEALDELE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 171 ELDDmnIEIIRNKLYKAYLEDFYNFVtEEIPEPAKECMQTLLGFEADRRSINIALNSLQSSDIDPDLKSDLLPNIGKLYP 250
Cdd:pfam01992 159 ETGD--LQLIENALDKAYYEDLYKFC-KKLGGKTAEILREYLGFEIDLRNIKIILRSKKYGKLSPEDIYKLLIPGGSLSP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 251 LATFHLAQAQDFEGVRAALANvYEYRGFLETGN---------LEDHFYQLEMELCRD-AFTQQFAISTVWAWMKSKEQEV 320
Cdd:pfam01992 236 EELKALAEAEDVEEVLAALEG-TPYGELLSEALeeltgslsaLERALDNYLLELAKKlARYQPFSIGPVLAYLKLKEQEI 314
                         330
                  ....*....|....*....
gi 1938945303 321 RNITWIAECIAQN-QRERI 338
Cdd:pfam01992 315 RNLRIIAEGKRYGlPPEEI 333
NtpC COG1527
Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]; Archaeal ...
17-342 2.10e-24

Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441136  Cd Length: 348  Bit Score: 101.96  E-value: 2.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  17 VRGYRNGLLSNNQYINLTQCDTLEDLKLQLSSTDYGNFLSSVSSESLTTSLIqEYA-SSKLYHEFNYIRDQSSGSTRKFM 95
Cdd:COG1527    14 IRAMESKLLKEEDYERLLEAESLEEIARFLKETGYGEELDELAERESGRDLL-EKAlNRNLAKTYRKLLEFAPGELKEFV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  96 DYITYGYMIDNVALMITGTIHDRDKGEILQRCHPLGWFDTLP--TLSVATDLESLYEtVLVDTPLAPYFKNCFDTAEELD 173
Cdd:COG1527    93 KLYLLRYDIHNLKVILRGKYSGEDLEEIRELLIPAGELSEEDlkKLLEAKSVEELVE-ALEGTPYYEALEEALEEYEETG 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 174 DmnIEIIRNKLYKAYLEDFYNFVteEIPEPAKECMQTLLGFEADRRSINIALNsLQSSDIDPDLKSDLLPNIGKLYPLAT 253
Cdd:COG1527   172 D--LFPIENALDRAYYENLLELA--KKKGKDRKLLLEYLGTEIDLLNLRTILR-LKRYGLSPEEIEAYLIPGGYRISEKE 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 254 F-HLAQAQDFEGVRAALAN------VYEYRGFLETGNL---EDHFYQLEMELCRDAF-TQQFAISTVWAWMKSKEQEVRN 322
Cdd:COG1527   247 LkELAEAEDVEELLEALEGtpygklLSELEELEETGSLsefERALDRYLLEYAKKLSkYYPFSIGPVLAYLLAKENEVKN 326
                         330       340
                  ....*....|....*....|.
gi 1938945303 323 ITWIAECIAQN-QRERINNYI 342
Cdd:COG1527   327 LRIIAEGKRYGlSPEEIRERL 347
PRK01198 PRK01198
V-type ATP synthase subunit C; Provisional
17-327 4.91e-14

V-type ATP synthase subunit C; Provisional


Pssm-ID: 234917  Cd Length: 352  Bit Score: 72.21  E-value: 4.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  17 VRGYRNGLLSNNQYINLTQCDTLEDLKLQLSSTDYGNFLSSVSSESLTTSLIqEYA-SSKLYHEFNYIRDQSSGSTRKFM 95
Cdd:PRK01198   18 VRVREAKLLDREKYERLLEMKSLEEIIRFLEETEYKEEIDELGSRYSGPDLI-EKAlNRNLAKTYELLLEISPGRLKELV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  96 DYITYGYMIDNVALMITGTIHDRDKGEILQRCHPLGWFD--TLPTLSVATDLESLyETVLVDTPLAPYFKNCFDTAEEld 173
Cdd:PRK01198   97 DVYLRKWDIHNIKTLLRGKILGLDAEEIEELLIPAGELDleKLKELLEAKSVEEI-VKILEGTEYYEVLEEALEDYEE-- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 174 DMNIEIIRNKLYKAYLED-FYNFVTEEIPE-PAKEcmqtLLGFEADRRSINIALNsLQSSDIDPDLKSDLLPNIGKLYPl 251
Cdd:PRK01198  174 TGDLQPIENALDKYYYENlLEIASPKDIDEkLLLE----YVRTEIDITNIKTLLR-LKAQGLSADFIEKVLIPGGSLDE- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 252 ATFHLAQAQDFEGVRAALANvYEY----RGFLETGNLEDHFYQLEMELcrDAFTQQ----------FAISTVWAWMKSKE 317
Cdd:PRK01198  248 EKLKELLAEDIEELVSALEG-TKYgdvlSEALEEYEETGSLSVFEKAL--DNYLLEymkklskrypFSVEPILGYILAKE 324
                         330
                  ....*....|
gi 1938945303 318 QEVRNITWIA 327
Cdd:PRK01198  325 REVKNLRIIA 334
AhaC TIGR02923
ATP synthase A1, C subunit; The A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
17-327 1.92e-13

ATP synthase A1, C subunit; The A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The C subunit is part of the hydrophilic A1 "stalk" complex (AhaABCDEFG), which is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex.


Pssm-ID: 274352  Cd Length: 343  Bit Score: 70.17  E-value: 1.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  17 VRGYRNGLLSNNQYINLTQCDTLEDLKLQLSSTDYGNFLSSVSSESLTTSLIQEYASSKLYHEFNYIRDQSSGSTRKFMD 96
Cdd:TIGR02923  12 VRAMESRLLKEEDFNELLEMRGTDEIVRFLEETDYKKELDELGSKSYGVDLIEHALDANLAKTYEKLFRISPGASRDLIR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  97 YITYGYMIDNVALMITGTIHDRDKGEILQRCHPLGWF--DTLPTLSVATDLESLYEtVLVDTPLAPYFKNCFDtaeelDD 174
Cdd:TIGR02923  92 LYLKKWDVWNIKTLIRAKYANASAEEVEDLLIPAGEFleKRIKELAEAKTIEEIVE-ALEGTPYYGPLQEALA-----GN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 175 MNIEIIRNKLYKAYLEDFYNFVteeiPEP---AKECMQTLLGFEADRRSINIALNsLQSSDIDPDLKSDLLpnIGKLYPL 251
Cdd:TIGR02923 166 GDLSPIENELDRMYYEKLLKYV----GSPsddETKLFTEFIKTEVDIRNLKTLLR-LKAAGLSPDEIMPYT--IPGGYEL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 252 ATFHLAQ---AQDFEGVRAALANvYEYRGFLeTGNLE---DHFYQLEMELCRD--------AFTQQFAISTVWAWMKSKE 317
Cdd:TIGR02923 239 DEEKLAPlahIESIDEVVSALDG-TKYGEDI-SEVLSeeeKSVAVFERALDEYlikmatklSLRYPLSVGPVLGYILKKE 316
                         330
                  ....*....|
gi 1938945303 318 QEVRNITWIA 327
Cdd:TIGR02923 317 REVRNLRAIA 326
 
Name Accession Description Interval E-value
vATP-synt_AC39 pfam01992
ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP ...
13-338 8.93e-97

ATP synthase (C/AC39) subunit; This family includes the AC39 subunit from vacuolar ATP synthase, and the C subunit from archaebacterial ATP synthase. The family also includes subunit C from the Sodium transporting ATP synthase from Enterococcus hirae.


Pssm-ID: 426553  Cd Length: 333  Bit Score: 290.33  E-value: 8.93e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  13 IEGVVRGYRNGLLSNNQYINLTQCDTLEDLKLQLSSTDYGNFLSSVSSeSLTTSLIQEYASSKLYHEFNYIRDQSSGSTR 92
Cdd:pfam01992   1 LNARVRAMESKLLTEEDYERLLQCESLEEAVRYLKETGYGDFLADEES-PLHRGDIEKALRRELAKTFEKLRRFAPGLSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  93 KFMDYITYGYMIDNVALMITGTIHDRDKGEILQRCHPLGWFDTLP--TLSVATDLESLYETVLvDTPLAPYFKNCFDTAE 170
Cdd:pfam01992  80 EFLDLYLYRYDIHNLKLLLRGKLSGLDLEELLEFLIPLGTLSALDldKLIEAKDVEELVEALL-GTPYAEALEEALDELE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 171 ELDDmnIEIIRNKLYKAYLEDFYNFVtEEIPEPAKECMQTLLGFEADRRSINIALNSLQSSDIDPDLKSDLLPNIGKLYP 250
Cdd:pfam01992 159 ETGD--LQLIENALDKAYYEDLYKFC-KKLGGKTAEILREYLGFEIDLRNIKIILRSKKYGKLSPEDIYKLLIPGGSLSP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 251 LATFHLAQAQDFEGVRAALANvYEYRGFLETGN---------LEDHFYQLEMELCRD-AFTQQFAISTVWAWMKSKEQEV 320
Cdd:pfam01992 236 EELKALAEAEDVEEVLAALEG-TPYGELLSEALeeltgslsaLERALDNYLLELAKKlARYQPFSIGPVLAYLKLKEQEI 314
                         330
                  ....*....|....*....
gi 1938945303 321 RNITWIAECIAQN-QRERI 338
Cdd:pfam01992 315 RNLRIIAEGKRYGlPPEEI 333
NtpC COG1527
Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]; Archaeal ...
17-342 2.10e-24

Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit C/Vma6 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441136  Cd Length: 348  Bit Score: 101.96  E-value: 2.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  17 VRGYRNGLLSNNQYINLTQCDTLEDLKLQLSSTDYGNFLSSVSSESLTTSLIqEYA-SSKLYHEFNYIRDQSSGSTRKFM 95
Cdd:COG1527    14 IRAMESKLLKEEDYERLLEAESLEEIARFLKETGYGEELDELAERESGRDLL-EKAlNRNLAKTYRKLLEFAPGELKEFV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  96 DYITYGYMIDNVALMITGTIHDRDKGEILQRCHPLGWFDTLP--TLSVATDLESLYEtVLVDTPLAPYFKNCFDTAEELD 173
Cdd:COG1527    93 KLYLLRYDIHNLKVILRGKYSGEDLEEIRELLIPAGELSEEDlkKLLEAKSVEELVE-ALEGTPYYEALEEALEEYEETG 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 174 DmnIEIIRNKLYKAYLEDFYNFVteEIPEPAKECMQTLLGFEADRRSINIALNsLQSSDIDPDLKSDLLPNIGKLYPLAT 253
Cdd:COG1527   172 D--LFPIENALDRAYYENLLELA--KKKGKDRKLLLEYLGTEIDLLNLRTILR-LKRYGLSPEEIEAYLIPGGYRISEKE 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 254 F-HLAQAQDFEGVRAALAN------VYEYRGFLETGNL---EDHFYQLEMELCRDAF-TQQFAISTVWAWMKSKEQEVRN 322
Cdd:COG1527   247 LkELAEAEDVEELLEALEGtpygklLSELEELEETGSLsefERALDRYLLEYAKKLSkYYPFSIGPVLAYLLAKENEVKN 326
                         330       340
                  ....*....|....*....|.
gi 1938945303 323 ITWIAECIAQN-QRERINNYI 342
Cdd:COG1527   327 LRIIAEGKRYGlSPEEIRERL 347
PRK01198 PRK01198
V-type ATP synthase subunit C; Provisional
17-327 4.91e-14

V-type ATP synthase subunit C; Provisional


Pssm-ID: 234917  Cd Length: 352  Bit Score: 72.21  E-value: 4.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  17 VRGYRNGLLSNNQYINLTQCDTLEDLKLQLSSTDYGNFLSSVSSESLTTSLIqEYA-SSKLYHEFNYIRDQSSGSTRKFM 95
Cdd:PRK01198   18 VRVREAKLLDREKYERLLEMKSLEEIIRFLEETEYKEEIDELGSRYSGPDLI-EKAlNRNLAKTYELLLEISPGRLKELV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  96 DYITYGYMIDNVALMITGTIHDRDKGEILQRCHPLGWFD--TLPTLSVATDLESLyETVLVDTPLAPYFKNCFDTAEEld 173
Cdd:PRK01198   97 DVYLRKWDIHNIKTLLRGKILGLDAEEIEELLIPAGELDleKLKELLEAKSVEEI-VKILEGTEYYEVLEEALEDYEE-- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 174 DMNIEIIRNKLYKAYLED-FYNFVTEEIPE-PAKEcmqtLLGFEADRRSINIALNsLQSSDIDPDLKSDLLPNIGKLYPl 251
Cdd:PRK01198  174 TGDLQPIENALDKYYYENlLEIASPKDIDEkLLLE----YVRTEIDITNIKTLLR-LKAQGLSADFIEKVLIPGGSLDE- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 252 ATFHLAQAQDFEGVRAALANvYEY----RGFLETGNLEDHFYQLEMELcrDAFTQQ----------FAISTVWAWMKSKE 317
Cdd:PRK01198  248 EKLKELLAEDIEELVSALEG-TKYgdvlSEALEEYEETGSLSVFEKAL--DNYLLEymkklskrypFSVEPILGYILAKE 324
                         330
                  ....*....|
gi 1938945303 318 QEVRNITWIA 327
Cdd:PRK01198  325 REVKNLRIIA 334
AhaC TIGR02923
ATP synthase A1, C subunit; The A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
17-327 1.92e-13

ATP synthase A1, C subunit; The A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The C subunit is part of the hydrophilic A1 "stalk" complex (AhaABCDEFG), which is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex.


Pssm-ID: 274352  Cd Length: 343  Bit Score: 70.17  E-value: 1.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  17 VRGYRNGLLSNNQYINLTQCDTLEDLKLQLSSTDYGNFLSSVSSESLTTSLIQEYASSKLYHEFNYIRDQSSGSTRKFMD 96
Cdd:TIGR02923  12 VRAMESRLLKEEDFNELLEMRGTDEIVRFLEETDYKKELDELGSKSYGVDLIEHALDANLAKTYEKLFRISPGASRDLIR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303  97 YITYGYMIDNVALMITGTIHDRDKGEILQRCHPLGWF--DTLPTLSVATDLESLYEtVLVDTPLAPYFKNCFDtaeelDD 174
Cdd:TIGR02923  92 LYLKKWDVWNIKTLIRAKYANASAEEVEDLLIPAGEFleKRIKELAEAKTIEEIVE-ALEGTPYYGPLQEALA-----GN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 175 MNIEIIRNKLYKAYLEDFYNFVteeiPEP---AKECMQTLLGFEADRRSINIALNsLQSSDIDPDLKSDLLpnIGKLYPL 251
Cdd:TIGR02923 166 GDLSPIENELDRMYYEKLLKYV----GSPsddETKLFTEFIKTEVDIRNLKTLLR-LKAAGLSPDEIMPYT--IPGGYEL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938945303 252 ATFHLAQ---AQDFEGVRAALANvYEYRGFLeTGNLE---DHFYQLEMELCRD--------AFTQQFAISTVWAWMKSKE 317
Cdd:TIGR02923 239 DEEKLAPlahIESIDEVVSALDG-TKYGEDI-SEVLSeeeKSVAVFERALDEYlikmatklSLRYPLSVGPVLGYILKKE 316
                         330
                  ....*....|
gi 1938945303 318 QEVRNITWIA 327
Cdd:TIGR02923 317 REVRNLRAIA 326
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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