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Conserved domains on  [gi|966929747|ref|XP_014987600|]
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kyphoscoliosis peptidase isoform X4 [Macaca mulatta]

Protein Classification

CYK3 family protein( domain architecture ID 11474529)

CYK3 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYK3 COG5279
Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle ...
 188-361 6.06e-52

Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 444090 [Multi-domain]  Cd Length: 250  Bit Score: 180.21  E-value: 6.06e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966929747 188 LDELVSDLLQEAHTDLERVRAIWIWICHHIEYDIAAAQEKDRQAFKPTDILRTQKTNCDGYAGLFERMCRIAGVQCMTVP 267
Cdd:COG5279   87 ESKDDDYIITPGMSDYEKVRAIHDWIVDNIEYDYEAYNSGKSDSHSAYGALKNGKGVCEGYAKLFKLLCNKAGIECYIVT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966929747 268 GYSKGFGYQTGqsfsgefDHAWNAVYLEGRWHLVDSTWGSGLVDTTTSKftflYNEFYFLTHPALFIEDHFPDNKNWQLL 347
Cdd:COG5279  167 GYARGSGGESG-------NHAWNAVKIDGKWYLVDATWDDGVPDNGGGD----VNYDYFLLSDEEFAKDHLPEDPKWQLL 235

                        170
                 ....*....|....
gi 966929747 348 KPPQSLRQFENNMY 361
Cdd:COG5279  236 DYPISKDEFANLYY 249
 
Name Accession Description Interval E-value
CYK3 COG5279
Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle ...
 188-361 6.06e-52

Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444090 [Multi-domain]  Cd Length: 250  Bit Score: 180.21  E-value: 6.06e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966929747 188 LDELVSDLLQEAHTDLERVRAIWIWICHHIEYDIAAAQEKDRQAFKPTDILRTQKTNCDGYAGLFERMCRIAGVQCMTVP 267
Cdd:COG5279   87 ESKDDDYIITPGMSDYEKVRAIHDWIVDNIEYDYEAYNSGKSDSHSAYGALKNGKGVCEGYAKLFKLLCNKAGIECYIVT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966929747 268 GYSKGFGYQTGqsfsgefDHAWNAVYLEGRWHLVDSTWGSGLVDTTTSKftflYNEFYFLTHPALFIEDHFPDNKNWQLL 347
Cdd:COG5279  167 GYARGSGGESG-------NHAWNAVKIDGKWYLVDATWDDGVPDNGGGD----VNYDYFLLSDEEFAKDHLPEDPKWQLL 235

                        170
                 ....*....|....
gi 966929747 348 KPPQSLRQFENNMY 361
Cdd:COG5279  236 DYPISKDEFANLYY 249
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 190-302 6.28e-16

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 73.98  E-value: 6.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966929747  190 ELVSDLLQEAHTDLERVRAIWIWICHHIEYDIAAAQEKDRQAfkpTDILRTQKTNCDGYAGLFERMCRIAGVQCMTVpgy 269
Cdd:pfam01841   2 ALADRITGGATDPLEKARAIYDYVRKNITYDLPGRSPGDGDA---EEFLFTGKGDCEDFASLFVALLRALGIPARYV--- 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 966929747  270 skgFGYQTGQSFSGEFD-HAWNAVYLEG-RWHLVD 302
Cdd:pfam01841  76 ---TGYLRGPDTVRGGDaHAWVEVYLPGyGWVPVD 107
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 237-305 3.10e-15

Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events.


Pssm-ID: 214673  Cd Length: 68  Bit Score: 70.49  E-value: 3.10e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966929747   237 ILRTQKTNCDGYAGLFERMCRIAGVQCMTVPGYSKGFGYQTGQSFSGEFdHAWNAVYLEGRWHLVDSTW 305
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLRSIWEA-HAWAEVYLEGGWVPVDPTP 68
 
Name Accession Description Interval E-value
CYK3 COG5279
Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle ...
 188-361 6.06e-52

Cytokinesis protein 3, contains TGc (transglutaminase/protease-like) domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444090 [Multi-domain]  Cd Length: 250  Bit Score: 180.21  E-value: 6.06e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966929747 188 LDELVSDLLQEAHTDLERVRAIWIWICHHIEYDIAAAQEKDRQAFKPTDILRTQKTNCDGYAGLFERMCRIAGVQCMTVP 267
Cdd:COG5279   87 ESKDDDYIITPGMSDYEKVRAIHDWIVDNIEYDYEAYNSGKSDSHSAYGALKNGKGVCEGYAKLFKLLCNKAGIECYIVT 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966929747 268 GYSKGFGYQTGqsfsgefDHAWNAVYLEGRWHLVDSTWGSGLVDTTTSKftflYNEFYFLTHPALFIEDHFPDNKNWQLL 347
Cdd:COG5279  167 GYARGSGGESG-------NHAWNAVKIDGKWYLVDATWDDGVPDNGGGD----VNYDYFLLSDEEFAKDHLPEDPKWQLL 235

                        170
                 ....*....|....
gi 966929747 348 KPPQSLRQFENNMY 361
Cdd:COG5279  236 DYPISKDEFANLYY 249
Transglut_core pfam01841
Transglutaminase-like superfamily; This family includes animal transglutaminases and other ...
 190-302 6.28e-16

Transglutaminase-like superfamily; This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.


Pssm-ID: 376628 [Multi-domain]  Cd Length: 108  Bit Score: 73.98  E-value: 6.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966929747  190 ELVSDLLQEAHTDLERVRAIWIWICHHIEYDIAAAQEKDRQAfkpTDILRTQKTNCDGYAGLFERMCRIAGVQCMTVpgy 269
Cdd:pfam01841   2 ALADRITGGATDPLEKARAIYDYVRKNITYDLPGRSPGDGDA---EEFLFTGKGDCEDFASLFVALLRALGIPARYV--- 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 966929747  270 skgFGYQTGQSFSGEFD-HAWNAVYLEG-RWHLVD 302
Cdd:pfam01841  76 ---TGYLRGPDTVRGGDaHAWVEVYLPGyGWVPVD 107
YebA COG1305
Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, ...
 188-304 1.30e-15

Transglutaminase-like enzyme, putative cysteine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440916 [Multi-domain]  Cd Length: 174  Bit Score: 75.04  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966929747 188 LDELVSDLLQEAHTDLERVRAIWIWICHHIEYDIAAAQEKDRqafkPTDILRTQKTNCDGYAGLFERMCRIAGVQCmtvp 267
Cdd:COG1305   63 LRALAAELTGGATTPYEKARALYDWVRDNIRYDPGSTGVGTT----ALETLERRRGVCRDFAHLLVALLRALGIPA---- 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 966929747 268 GYSKGFGYQTGQSFSGEFD--HAWNAVYLEGR-WHLVDST 304
Cdd:COG1305  135 RYVSGYLPGEPPPGGGRADdaHAWVEVYLPGAgWVPFDPT 174
TGc smart00460
Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish ...
 237-305 3.10e-15

Transglutaminase/protease-like homologues; Transglutaminases are enzymes that establish covalent links between proteins. A subset of transglutaminase homologues appear to catalyse the reverse reaction, the hydrolysis of peptide bonds. Proteins with this domain are both extracellular and intracellular, and it is likely that the eukaryotic intracellular proteins are involved in signalling events.


Pssm-ID: 214673  Cd Length: 68  Bit Score: 70.49  E-value: 3.10e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966929747   237 ILRTQKTNCDGYAGLFERMCRIAGVQCMTVPGYSKGFGYQTGQSFSGEFdHAWNAVYLEGRWHLVDSTW 305
Cdd:smart00460   1 LLKTKYGTCGEFAALFVALLRSLGIPARVVSGYLKAPDTIGGLRSIWEA-HAWAEVYLEGGWVPVDPTP 68
 
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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