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Conserved domains on  [gi|1046849933|ref|XP_017452883|]
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secernin-2 isoform X2 [Rattus norvegicus]

Protein Classification

peptidase C69 family protein( domain architecture ID 1903692)

peptidase C69 family protein such as dipeptidases that cleave a wide range of dipeptides, and secernins

MEROPS:  C69
PubMed:  18768474|31377195

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PepD super family cl41909
Dipeptidase [Amino acid transport and metabolism];
51-204 1.12e-18

Dipeptidase [Amino acid transport and metabolism];


The actual alignment was detected with superfamily member COG4690:

Pssm-ID: 477862  Cd Length: 469  Bit Score: 87.23  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046849933  51 PSWLWGAEMGANELGVCIG-------NEAVWTKEPVGEGeallGM---DLLRLALERSSTAQAAVHVIAGLLDRYGQGGS 120
Cdd:COG4690    72 DKDGIWGEAGINEAGVAMSatetittNERVLGADPLVED----GIgeeDLVTLVLPRIKTAREGVELLGELIEKYGTGEG 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046849933 121 credpepfcyhNTFLLADRTEAWVLETA-GRLWAAQRIQGGARNIS-NQLSIGtDISAEHPE-------LRSHAKAQGWW 191
Cdd:COG4690   148 -----------NGIAFADKDEVWYLETIgGHHWVAQRVPDDAYAVApNQFRID-EVDFDDPEnfmaskdLKEFAEENGLY 215
                         170
                  ....*....|....
gi 1046849933 192 SGQ-GVFDFAEVFS 204
Cdd:COG4690   216 DPEdGPFNFRKAYG 229
 
Name Accession Description Interval E-value
PepD COG4690
Dipeptidase [Amino acid transport and metabolism];
51-204 1.12e-18

Dipeptidase [Amino acid transport and metabolism];


Pssm-ID: 443725  Cd Length: 469  Bit Score: 87.23  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046849933  51 PSWLWGAEMGANELGVCIG-------NEAVWTKEPVGEGeallGM---DLLRLALERSSTAQAAVHVIAGLLDRYGQGGS 120
Cdd:COG4690    72 DKDGIWGEAGINEAGVAMSatetittNERVLGADPLVED----GIgeeDLVTLVLPRIKTAREGVELLGELIEKYGTGEG 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046849933 121 credpepfcyhNTFLLADRTEAWVLETA-GRLWAAQRIQGGARNIS-NQLSIGtDISAEHPE-------LRSHAKAQGWW 191
Cdd:COG4690   148 -----------NGIAFADKDEVWYLETIgGHHWVAQRVPDDAYAVApNQFRID-EVDFDDPEnfmaskdLKEFAEENGLY 215
                         170
                  ....*....|....
gi 1046849933 192 SGQ-GVFDFAEVFS 204
Cdd:COG4690   216 DPEdGPFNFRKAYG 229
Peptidase_C69 pfam03577
Peptidase family C69;
43-204 4.16e-07

Peptidase family C69;


Pssm-ID: 427375  Cd Length: 402  Bit Score: 51.64  E-value: 4.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046849933  43 THAVILSRPSWlwgAEMGANELGVCIGNEavwtkEPVGEGEALLGMD------------LLRLALERSSTAQAAVHVIAG 110
Cdd:pfam03577  68 TPNADLKDGIW---GEAGINSANVAMSAT-----ETITTNERVLGADpyvskggigeedIITLVLPYIQSAREGVERLGD 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046849933 111 LLDRYGQGGScredpepfcyhNTFLLADRTEAWVLET-AGRLWAAQRIQGGARNIS-NQLSIgTDISAEHPE-------L 181
Cdd:pfam03577 140 LLEQYGTYEG-----------NGVAFSDSNEIWWLETiGGHHWIAVRVPDDCYVVApNQLGI-DHFDFNDPDnymcspdL 207
                         170       180
                  ....*....|....*....|....
gi 1046849933 182 RSHAKAQGWWSG-QGVFDFAEVFS 204
Cdd:pfam03577 208 KEFIDENHLDPTvNKEFNFRKAFG 231
C45_proenzyme NF040521
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
54-263 2.99e-06

C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.


Pssm-ID: 468523 [Multi-domain]  Cd Length: 312  Bit Score: 48.44  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046849933  54 LWGAEMGANELGVCIGNEAVWTKEPVGEGealLGMDLL-RLALERSSTAQAAVHVIAGLldrygqggscredpePFCYHN 132
Cdd:NF040521  140 LPGRTDGMNEAGLAVTLNFLDGRKLPGVG---VPVHLLaRAILENCKTVDEAIALLKEI---------------PRASSF 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046849933 133 TFLLADRT-EAWVLETAGRlwaaqriQGGARNISNQLSIGTDiSAEHPELRSHakaqgwwsgqgvfdfaevfsltqQPVR 211
Cdd:NF040521  202 NLTLADASgRAASVEASPD-------RVVVVRPEDGLLVHTN-HFLSPELEEE-----------------------NRIA 250
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046849933 212 MEAAKARFRAgceMLQRQQGSITAEVMMDILR-NKESGICM----DSGGFRTTASMV 263
Cdd:NF040521  251 TPSSRERYER---LEELLKGKLDAEDAKALLSdGYPLPICRhpypDGDRFGTLATVV 304
 
Name Accession Description Interval E-value
PepD COG4690
Dipeptidase [Amino acid transport and metabolism];
51-204 1.12e-18

Dipeptidase [Amino acid transport and metabolism];


Pssm-ID: 443725  Cd Length: 469  Bit Score: 87.23  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046849933  51 PSWLWGAEMGANELGVCIG-------NEAVWTKEPVGEGeallGM---DLLRLALERSSTAQAAVHVIAGLLDRYGQGGS 120
Cdd:COG4690    72 DKDGIWGEAGINEAGVAMSatetittNERVLGADPLVED----GIgeeDLVTLVLPRIKTAREGVELLGELIEKYGTGEG 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046849933 121 credpepfcyhNTFLLADRTEAWVLETA-GRLWAAQRIQGGARNIS-NQLSIGtDISAEHPE-------LRSHAKAQGWW 191
Cdd:COG4690   148 -----------NGIAFADKDEVWYLETIgGHHWVAQRVPDDAYAVApNQFRID-EVDFDDPEnfmaskdLKEFAEENGLY 215
                         170
                  ....*....|....
gi 1046849933 192 SGQ-GVFDFAEVFS 204
Cdd:COG4690   216 DPEdGPFNFRKAYG 229
Peptidase_C69 pfam03577
Peptidase family C69;
43-204 4.16e-07

Peptidase family C69;


Pssm-ID: 427375  Cd Length: 402  Bit Score: 51.64  E-value: 4.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046849933  43 THAVILSRPSWlwgAEMGANELGVCIGNEavwtkEPVGEGEALLGMD------------LLRLALERSSTAQAAVHVIAG 110
Cdd:pfam03577  68 TPNADLKDGIW---GEAGINSANVAMSAT-----ETITTNERVLGADpyvskggigeedIITLVLPYIQSAREGVERLGD 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046849933 111 LLDRYGQGGScredpepfcyhNTFLLADRTEAWVLET-AGRLWAAQRIQGGARNIS-NQLSIgTDISAEHPE-------L 181
Cdd:pfam03577 140 LLEQYGTYEG-----------NGVAFSDSNEIWWLETiGGHHWIAVRVPDDCYVVApNQLGI-DHFDFNDPDnymcspdL 207
                         170       180
                  ....*....|....*....|....
gi 1046849933 182 RSHAKAQGWWSG-QGVFDFAEVFS 204
Cdd:pfam03577 208 KEFIDENHLDPTvNKEFNFRKAFG 231
C45_proenzyme NF040521
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
54-263 2.99e-06

C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.


Pssm-ID: 468523 [Multi-domain]  Cd Length: 312  Bit Score: 48.44  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046849933  54 LWGAEMGANELGVCIGNEAVWTKEPVGEGealLGMDLL-RLALERSSTAQAAVHVIAGLldrygqggscredpePFCYHN 132
Cdd:NF040521  140 LPGRTDGMNEAGLAVTLNFLDGRKLPGVG---VPVHLLaRAILENCKTVDEAIALLKEI---------------PRASSF 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046849933 133 TFLLADRT-EAWVLETAGRlwaaqriQGGARNISNQLSIGTDiSAEHPELRSHakaqgwwsgqgvfdfaevfsltqQPVR 211
Cdd:NF040521  202 NLTLADASgRAASVEASPD-------RVVVVRPEDGLLVHTN-HFLSPELEEE-----------------------NRIA 250
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046849933 212 MEAAKARFRAgceMLQRQQGSITAEVMMDILR-NKESGICM----DSGGFRTTASMV 263
Cdd:NF040521  251 TPSSRERYER---LEELLKGKLDAEDAKALLSdGYPLPICRhpypDGDRFGTLATVV 304
 
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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