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Conserved domains on  [gi|2462617658|ref|XP_054215695|]
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protein odd-skipped-related 2 isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5048 super family cl34881
FOG: Zn-finger [General function prediction only];
172-307 4.14e-04

FOG: Zn-finger [General function prediction only];


The actual alignment was detected with superfamily member COG5048:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462617658 172 FICKFCGRHFTKSYNLLIHERT--HTDE--RPYTCDI--CHKAFRRQDHLRDHRYIHSKEKPFKC--QECGKGFCQSRTL 243
Cdd:COG5048   290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNN 369

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462617658 244 AVHKTLHMQESPHKCPT-------CGRTFNQRSNLKTHLLTHT--DIKPYSCEQCGKVFRRNCDLRRHSLTHT 307
Cdd:COG5048   370 EPPQSLQQYKDLKNDKKsetlsnsCIRNFKRDSNLSLHIITHLsfRPYNCKNPPCSKSFNRHYNLIPHKKIHT 442
Zinc_peptidase_like super family cl14876
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
 18-124 7.41e-03

Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).


The actual alignment was detected with superfamily member cd05643:

Pssm-ID: 472712 [Multi-domain]  Cd Length: 290  Bit Score: 37.38  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462617658  18 LTNYSFLQAVNTFPATVDHLQGL---YGLSA-----VQTMHMNHWTLGYPNVHEITRSTITEMAAAQGLVDARFPFPALP 89
Cdd:cd05643     8 ISRYHRVQGSRGYVKAAEEVKELleeLGLEAklisdIYDGGERILTPQSPISWELIEGELNETLPILYAIIGKETPPEIA 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462617658  90 FTTHLFHPKQGA------------IAHVLPALHKDRPRFDFANLAVA 124
Cdd:cd05643    88 FVAHLCHPKPGAndnasgsallleVARVLAKLILNRPKRGICFLWVP 134
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
172-307 4.14e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462617658 172 FICKFCGRHFTKSYNLLIHERT--HTDE--RPYTCDI--CHKAFRRQDHLRDHRYIHSKEKPFKC--QECGKGFCQSRTL 243
Cdd:COG5048   290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNN 369

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462617658 244 AVHKTLHMQESPHKCPT-------CGRTFNQRSNLKTHLLTHT--DIKPYSCEQCGKVFRRNCDLRRHSLTHT 307
Cdd:COG5048   370 EPPQSLQQYKDLKNDKKsetlsnsCIRNFKRDSNLSLHIITHLsfRPYNCKNPPCSKSFNRHYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
214-237 9.34e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 9.34e-04
                          10        20
                  ....*....|....*....|....
gi 2462617658 214 HLRDHRYIHSKEKPFKCQECGKGF 237
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
M28_like cd05643
M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), ...
 18-124 7.41e-03

M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They typically have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This protein subfamily conserves some of the metal-coordinating residues of the typically co-catalytic M28 family which might suggest binding of a single metal ion.


Pssm-ID: 349895 [Multi-domain]  Cd Length: 290  Bit Score: 37.38  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462617658  18 LTNYSFLQAVNTFPATVDHLQGL---YGLSA-----VQTMHMNHWTLGYPNVHEITRSTITEMAAAQGLVDARFPFPALP 89
Cdd:cd05643     8 ISRYHRVQGSRGYVKAAEEVKELleeLGLEAklisdIYDGGERILTPQSPISWELIEGELNETLPILYAIIGKETPPEIA 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462617658  90 FTTHLFHPKQGA------------IAHVLPALHKDRPRFDFANLAVA 124
Cdd:cd05643    88 FVAHLCHPKPGAndnasgsallleVARVLAKLILNRPKRGICFLWVP 134
 
Name Accession Description Interval E-value
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
172-307 4.14e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462617658 172 FICKFCGRHFTKSYNLLIHERT--HTDE--RPYTCDI--CHKAFRRQDHLRDHRYIHSKEKPFKC--QECGKGFCQSRTL 243
Cdd:COG5048   290 IKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNN 369

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462617658 244 AVHKTLHMQESPHKCPT-------CGRTFNQRSNLKTHLLTHT--DIKPYSCEQCGKVFRRNCDLRRHSLTHT 307
Cdd:COG5048   370 EPPQSLQQYKDLKNDKKsetlsnsCIRNFKRDSNLSLHIITHLsfRPYNCKNPPCSKSFNRHYNLIPHKKIHT 442
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
251-312 4.22e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 41.61  E-value: 4.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462617658 251 MQESPHKCPTCGRTFNQRSNLKTHLLTHTDIKPYSC--EQCGKVFRRNCDLRRHSLTHTPRQDF 312
Cdd:COG5048    29 NAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSD 92
zf-H2C2_2 pfam13465
Zinc-finger double domain;
214-237 9.34e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.20  E-value: 9.34e-04
                          10        20
                  ....*....|....*....|....
gi 2462617658 214 HLRDHRYIHSKEKPFKCQECGKGF 237
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 256-278 1.04e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 1.04e-03
                          10        20
                  ....*....|....*....|...
gi 2462617658 256 HKCPTCGRTFNQRSNLKTHLLTH 278
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
186-211 1.15e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.15e-03
                          10        20
                  ....*....|....*....|....*.
gi 2462617658 186 NLLIHERTHTDERPYTCDICHKAFRR 211
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 196-280 1.98e-03

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.70  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462617658 196 DERPYTCDI--CHKAFRRQDHLRDHRyihskekpfKCQECGKGFCQSRTLAVHKTLHMQESPHKCPTCGRTFNQRSNLKT 273
Cdd:COG5189   346 DGKPYKCPVegCNKKYKNQNGLKYHM---------LHGHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*..
gi 2462617658 274 HLLTHTD 280
Cdd:COG5189   417 HRKHSHD 423
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 225-302 2.00e-03

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 39.70  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462617658 225 EKPFKCQ--ECGKGFCQSRTLAVHKtLHMQESPHKCPTcgrtfnqRSNLKTHLLTHTDiKPYSCEQCGKVFRRNCDLRRH 302
Cdd:COG5189   347 GKPYKCPveGCNKKYKNQNGLKYHM-LHGHQNQKLHEN-------PSPEKMNIFSAKD-KPYRCEVCDKRYKNLNGLKYH 417
zf-H2C2_2 pfam13465
Zinc-finger double domain;
270-295 3.00e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 3.00e-03
                          10        20
                  ....*....|....*....|....*.
gi 2462617658 270 NLKTHLLTHTDIKPYSCEQCGKVFRR 295
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 200-222 4.07e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.20  E-value: 4.07e-03
                          10        20
                  ....*....|....*....|...
gi 2462617658 200 YTCDICHKAFRRQDHLRDHRYIH 222
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
252-312 5.10e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.52  E-value: 5.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462617658 252 QESPHKCPTCGRTFNQRSNLKTHLLT--HT--DIKPYSC--EQCGKVFRRNCDLRRHSLTHTPRQDF 312
Cdd:COG5048   286 FSLPIKSKQCNISFSRSSPLTRHLRSvnHSgeSLKPFSCpySLCGKLFSRNDALKRHILLHTSISPA 352
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
196-296 6.30e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 38.14  E-value: 6.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462617658 196 DERPYTCDICHKAFRRQDHLRDHRYIHSKEKPFKC--QECGKGFCQSRTLAVHKTLHMQESPHKCPTCGRTFNQ-RSNLK 272
Cdd:COG5048    30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSkASSSS 109

                          90       100
                  ....*....|....*....|....
gi 2462617658 273 THLLTHTDIKPYSCEQCGKVFRRN 296
Cdd:COG5048   110 LSSSSSNSNDNNLLSSHSLPPSSR 133
M28_like cd05643
M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), ...
 18-124 7.41e-03

M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They typically have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This protein subfamily conserves some of the metal-coordinating residues of the typically co-catalytic M28 family which might suggest binding of a single metal ion.


Pssm-ID: 349895 [Multi-domain]  Cd Length: 290  Bit Score: 37.38  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462617658  18 LTNYSFLQAVNTFPATVDHLQGL---YGLSA-----VQTMHMNHWTLGYPNVHEITRSTITEMAAAQGLVDARFPFPALP 89
Cdd:cd05643     8 ISRYHRVQGSRGYVKAAEEVKELleeLGLEAklisdIYDGGERILTPQSPISWELIEGELNETLPILYAIIGKETPPEIA 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462617658  90 FTTHLFHPKQGA------------IAHVLPALHKDRPRFDFANLAVA 124
Cdd:cd05643    88 FVAHLCHPKPGAndnasgsallleVARVLAKLILNRPKRGICFLWVP 134
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 284-306 8.57e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.43  E-value: 8.57e-03
                          10        20
                  ....*....|....*....|...
gi 2462617658 284 YSCEQCGKVFRRNCDLRRHSLTH 306
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
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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