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Conserved domains on  [gi|156843330|ref|XP_001644733|]
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uncharacterized protein Kpol_1024p29 [Vanderwaltozyma polyspora DSM 70294]

Protein Classification

ACE1-Sec16-like domain-containing protein( domain architecture ID 10173993)

ACE1-Sec16-like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
1107-1455 9.01e-46

Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site.


:

Pssm-ID: 187750 [Multi-domain]  Cd Length: 314  Bit Score: 168.21  E-value: 9.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330 1107 YPGPLDSFKKSKTQLSSWLSVVLENLTTTST------FSVLISLFKIWIDSSNVVQDIIHILsdenklQEAFDNIE---- 1176
Cdd:cd09233     1 FPGPLIKGKTKKKDVLKWLEEKIAELEENEGyldledKLLLWKLLKLLVRQNGKLVGTDIAE------QKALNRFRnlll 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330 1177 --HKKtiseskrdsrildtngkdkilkllllgkknEALEFSMENSDFTMALLIANTIDEASRHSVIMSYFENkinpvnte 1254
Cdd:cd09233    75 tgNRK------------------------------EALELALDNGLWAHALLLASSLGKETWAEVVSRFARS-------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330 1255 KKSINMLLLALFQVYSGDGTHLLNIAKENPETKDWYVKNWNSIVLILLKNCdmnagnisskpnSHQKVTSFLVGFSNFLR 1334
Cdd:cd09233   117 ESKLNDPLQTLYQLFSGNSPEAITELADNPAEAEWALGNWREHLAIILSNR------------TSNLDLEALVELGDLLA 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330 1335 NTGNILPSFIVCLISDMLNSGSENGIevDMLDSVFGKHTVSSSIISEIYSL--------IKISKNQNSDEFLLYSSSLEC 1406
Cdd:cd09233   185 QRGLVEAAHICYLLAGVPLGPYPSSP--SSCLLGGAVHNKSPRTFATPEAIqlteiyeyALSLGNPQFGLPHLQPYKLIH 262
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 156843330 1407 ARLFFDIGYHSKALEYVNYFVSIKDRLIANEIFVDTSLEQLKVISELVN 1455
Cdd:cd09233   263 AARLAELGLVSEALKYCEAIASSLKSLTKSPYYDPNLLAQLQDLSERLS 311
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
700-869 2.26e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.98  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330   700 SPVPTLPTASSIINNTNINIPvNPYASIPTQSKTPVNAIAIDMYSP--STGPTKSPLPSKNTQQIQTPYDASSNTDNSSI 777
Cdd:pfam05109  422 SKAPESTTTSPTLNTTGFAAP-NTTTGLPSSTHVPTNLTAPASTGPtvSTADVTSPTPAGTTSGASPVTPSPSPRDNGTE 500
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330   778 PVSTDRYAPMSNISskSPHPPVRSRKSSPVAPVNNSyISPSLIPNKLNGSIDNKINASLKPIPLVQ--------PANANI 849
Cdd:pfam05109  501 SKAPDMTSPTSAVT--TPTPNATSPTPAVTTPTPNA-TSPTLGKTSPTSAVTTPTPNATSPTPAVTtptpnatiPTLGKT 577
                          170       180
                   ....*....|....*....|
gi 156843330   850 SPNENYGIPAPYLKSPSLPE 869
Cdd:pfam05109  578 SPTSAVTTPTPNATSPTVGE 597
 
Name Accession Description Interval E-value
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
1107-1455 9.01e-46

Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site.


Pssm-ID: 187750 [Multi-domain]  Cd Length: 314  Bit Score: 168.21  E-value: 9.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330 1107 YPGPLDSFKKSKTQLSSWLSVVLENLTTTST------FSVLISLFKIWIDSSNVVQDIIHILsdenklQEAFDNIE---- 1176
Cdd:cd09233     1 FPGPLIKGKTKKKDVLKWLEEKIAELEENEGyldledKLLLWKLLKLLVRQNGKLVGTDIAE------QKALNRFRnlll 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330 1177 --HKKtiseskrdsrildtngkdkilkllllgkknEALEFSMENSDFTMALLIANTIDEASRHSVIMSYFENkinpvnte 1254
Cdd:cd09233    75 tgNRK------------------------------EALELALDNGLWAHALLLASSLGKETWAEVVSRFARS-------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330 1255 KKSINMLLLALFQVYSGDGTHLLNIAKENPETKDWYVKNWNSIVLILLKNCdmnagnisskpnSHQKVTSFLVGFSNFLR 1334
Cdd:cd09233   117 ESKLNDPLQTLYQLFSGNSPEAITELADNPAEAEWALGNWREHLAIILSNR------------TSNLDLEALVELGDLLA 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330 1335 NTGNILPSFIVCLISDMLNSGSENGIevDMLDSVFGKHTVSSSIISEIYSL--------IKISKNQNSDEFLLYSSSLEC 1406
Cdd:cd09233   185 QRGLVEAAHICYLLAGVPLGPYPSSP--SSCLLGGAVHNKSPRTFATPEAIqlteiyeyALSLGNPQFGLPHLQPYKLIH 262
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 156843330 1407 ARLFFDIGYHSKALEYVNYFVSIKDRLIANEIFVDTSLEQLKVISELVN 1455
Cdd:cd09233   263 AARLAELGLVSEALKYCEAIASSLKSLTKSPYYDPNLLAQLQDLSERLS 311
Sec16_C pfam12931
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ...
1210-1357 7.44e-11

Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal region is the part that binds to Sec23, a COPII vesicle coat protein. This association is part of the transport vesicle coat structure.


Pssm-ID: 432884  Cd Length: 279  Bit Score: 65.27  E-value: 7.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330  1210 EALEFSMENSDFTMALLIANTIDEASRHSVIMSYFENKINPVNTekkSINMLLLALFQVYSGDGTHLLNIAKENPETKDW 1289
Cdd:pfam12931   12 KALWLALDKKLWAHALLIASTLGKEKWKEVVQEFVRSEFKGSNN---KSGESLAALYQVFAGNSEEAVDELVPPSKNALW 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156843330  1290 YVKNWNSIVLILLKNCdmnagnissKPNSHQkvtsFLVGFSNFLRNTGNILPSFIVCLISDMLNSGSE 1357
Cdd:pfam12931   89 ALDNWRETLALVLSNR---------SPGDVE----ALLALGDLLAQYGRTEAAHICFLLAGLPLSQTV 143
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
700-869 2.26e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.98  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330   700 SPVPTLPTASSIINNTNINIPvNPYASIPTQSKTPVNAIAIDMYSP--STGPTKSPLPSKNTQQIQTPYDASSNTDNSSI 777
Cdd:pfam05109  422 SKAPESTTTSPTLNTTGFAAP-NTTTGLPSSTHVPTNLTAPASTGPtvSTADVTSPTPAGTTSGASPVTPSPSPRDNGTE 500
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330   778 PVSTDRYAPMSNISskSPHPPVRSRKSSPVAPVNNSyISPSLIPNKLNGSIDNKINASLKPIPLVQ--------PANANI 849
Cdd:pfam05109  501 SKAPDMTSPTSAVT--TPTPNATSPTPAVTTPTPNA-TSPTLGKTSPTSAVTTPTPNATSPTPAVTtptpnatiPTLGKT 577
                          170       180
                   ....*....|....*....|
gi 156843330   850 SPNENYGIPAPYLKSPSLPE 869
Cdd:pfam05109  578 SPTSAVTTPTPNATSPTVGE 597
 
Name Accession Description Interval E-value
ACE1-Sec16-like cd09233
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ...
1107-1455 9.01e-46

Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site.


Pssm-ID: 187750 [Multi-domain]  Cd Length: 314  Bit Score: 168.21  E-value: 9.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330 1107 YPGPLDSFKKSKTQLSSWLSVVLENLTTTST------FSVLISLFKIWIDSSNVVQDIIHILsdenklQEAFDNIE---- 1176
Cdd:cd09233     1 FPGPLIKGKTKKKDVLKWLEEKIAELEENEGyldledKLLLWKLLKLLVRQNGKLVGTDIAE------QKALNRFRnlll 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330 1177 --HKKtiseskrdsrildtngkdkilkllllgkknEALEFSMENSDFTMALLIANTIDEASRHSVIMSYFENkinpvnte 1254
Cdd:cd09233    75 tgNRK------------------------------EALELALDNGLWAHALLLASSLGKETWAEVVSRFARS-------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330 1255 KKSINMLLLALFQVYSGDGTHLLNIAKENPETKDWYVKNWNSIVLILLKNCdmnagnisskpnSHQKVTSFLVGFSNFLR 1334
Cdd:cd09233   117 ESKLNDPLQTLYQLFSGNSPEAITELADNPAEAEWALGNWREHLAIILSNR------------TSNLDLEALVELGDLLA 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330 1335 NTGNILPSFIVCLISDMLNSGSENGIevDMLDSVFGKHTVSSSIISEIYSL--------IKISKNQNSDEFLLYSSSLEC 1406
Cdd:cd09233   185 QRGLVEAAHICYLLAGVPLGPYPSSP--SSCLLGGAVHNKSPRTFATPEAIqlteiyeyALSLGNPQFGLPHLQPYKLIH 262
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 156843330 1407 ARLFFDIGYHSKALEYVNYFVSIKDRLIANEIFVDTSLEQLKVISELVN 1455
Cdd:cd09233   263 AARLAELGLVSEALKYCEAIASSLKSLTKSPYYDPNLLAQLQDLSERLS 311
Sec16_C pfam12931
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ...
1210-1357 7.44e-11

Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal region is the part that binds to Sec23, a COPII vesicle coat protein. This association is part of the transport vesicle coat structure.


Pssm-ID: 432884  Cd Length: 279  Bit Score: 65.27  E-value: 7.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330  1210 EALEFSMENSDFTMALLIANTIDEASRHSVIMSYFENKINPVNTekkSINMLLLALFQVYSGDGTHLLNIAKENPETKDW 1289
Cdd:pfam12931   12 KALWLALDKKLWAHALLIASTLGKEKWKEVVQEFVRSEFKGSNN---KSGESLAALYQVFAGNSEEAVDELVPPSKNALW 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156843330  1290 YVKNWNSIVLILLKNCdmnagnissKPNSHQkvtsFLVGFSNFLRNTGNILPSFIVCLISDMLNSGSE 1357
Cdd:pfam12931   89 ALDNWRETLALVLSNR---------SPGDVE----ALLALGDLLAQYGRTEAAHICFLLAGLPLSQTV 143
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
700-869 2.26e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 42.98  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330   700 SPVPTLPTASSIINNTNINIPvNPYASIPTQSKTPVNAIAIDMYSP--STGPTKSPLPSKNTQQIQTPYDASSNTDNSSI 777
Cdd:pfam05109  422 SKAPESTTTSPTLNTTGFAAP-NTTTGLPSSTHVPTNLTAPASTGPtvSTADVTSPTPAGTTSGASPVTPSPSPRDNGTE 500
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156843330   778 PVSTDRYAPMSNISskSPHPPVRSRKSSPVAPVNNSyISPSLIPNKLNGSIDNKINASLKPIPLVQ--------PANANI 849
Cdd:pfam05109  501 SKAPDMTSPTSAVT--TPTPNATSPTPAVTTPTPNA-TSPTLGKTSPTSAVTTPTPNATSPTPAVTtptpnatiPTLGKT 577
                          170       180
                   ....*....|....*....|
gi 156843330   850 SPNENYGIPAPYLKSPSLPE 869
Cdd:pfam05109  578 SPTSAVTTPTPNATSPTVGE 597
 
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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