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Conserved domains on  [gi|1207114027|ref|XP_021336175.1|]
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paired box protein Pax-2a isoform X11 [Danio rerio]

Protein Classification

paired box protein Pax( domain architecture ID 13907029)

paired box protein Pax functions as a transcription factor, similar to human paired box protein Pax-5 that plays an essential role in commitment of lymphoid progenitors to the B-lymphocyte lineage

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAX smart00351
Paired Box domain;
19-143 6.30e-89

Paired Box domain;


:

Pssm-ID: 128645 [Multi-domain]  Cd Length: 125  Bit Score: 267.27  E-value: 6.30e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027   19 GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKV 98
Cdd:smart00351   1 GHGGVNQLGGVFVNGRPLPDEERQRIVELAQNGVRPCDISRQLCVSHGCVSKILGRYYETGSIRPGAIGGSKPKVATPKV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1207114027   99 VEKIAEYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIR 143
Cdd:smart00351  81 VKKIADYKQENPGIFAWEIRDRLLSEGVCDKDNVPSVSSINRILR 125
Pax2_C pfam12403
Paired-box protein 2 C terminal; This domain family is found in eukaryotes, and is ...
 352-443 1.14e-46

Paired-box protein 2 C terminal; This domain family is found in eukaryotes, and is approximately 110 amino acids in length. The family is found in association with pfam00292. This family is the C terminal of the paired-box protein 2 which is a transcription factor involved in embryonic development and organogenesis.


:

Pssm-ID: 463563  Cd Length: 113  Bit Score: 157.63  E-value: 1.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027 352 ASTPCYGAYAHHAPSYCQYTSQHIIAGREMASTTLPGYPPHVPPTGQGSYPTSTLAGMVPGSDFSGNPYSHPQYTTYNEA 431
Cdd:pfam12403   1 ASLASFSAFAHLGSSYGQFQSYSLVAGRDMASTTLPGYPPHVPPTGQGSYSTSTLAGMVPGSDYSGNPYSHPQYSSYNEA 80

                          90
                  ....*....|..
gi 1207114027 432 WRFSNPALLMPH 443
Cdd:pfam12403  81 WRFPNPSLLGSP 92
Zinc_peptidase_like super family cl14876
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
 218-338 9.29e-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 cd05679:

Pssm-ID: 472712 [Multi-domain]  Cd Length: 448  Bit Score: 38.25  E-value: 9.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027 218 SDSQGSVESLRKHLRADAFTQQQLEALDRVFerpSYPDVFPTSEHIKPEQANEYSLPALNPGLdevKPSLSTSVSSDLGS 297
Cdd:cd05679   324 TDPDTFIPAVRAHLDANGFDGVEVTASQMVF---AATRLDPDSPWVGWALASLQKTTGKKPAL---LPNLGGSLPNDVFS 397

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1207114027 298 SVsQSYPVVTESHSSSMCVKQEPHEASLAPFTPSSLAV-SGL 338
Cdd:cd05679   398 EV-LGLPTLWVPHSYPACSQHAPNEHILAPVMREALRVmAGL 438
 
Name Accession Description Interval E-value
PAX smart00351
Paired Box domain;
19-143 6.30e-89

Paired Box domain;


Pssm-ID: 128645 [Multi-domain]  Cd Length: 125  Bit Score: 267.27  E-value: 6.30e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027   19 GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKV 98
Cdd:smart00351   1 GHGGVNQLGGVFVNGRPLPDEERQRIVELAQNGVRPCDISRQLCVSHGCVSKILGRYYETGSIRPGAIGGSKPKVATPKV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1207114027   99 VEKIAEYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIR 143
Cdd:smart00351  81 VKKIADYKQENPGIFAWEIRDRLLSEGVCDKDNVPSVSSINRILR 125
PAX cd00131
Paired Box domain
 19-145 2.07e-84

Paired Box domain


Pssm-ID: 238076  Cd Length: 128  Bit Score: 255.81  E-value: 2.07e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027  19 GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKV 98
Cdd:cd00131     1 GQGGVNQLGGVFVNGRPLPDSIRQRIVELAQSGIRPCDISRQLRVSHGCVSKILNRYYETGSIRPGAIGGSKPRVATPEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1207114027  99 VEKIAEYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIRTK 145
Cdd:cd00131    81 VKKIEIYKQENPGMFAWEIRDRLLQEGVCDKSNVPSVSSINRILRNK 127
PAX pfam00292
'Paired box' domain;
19-143 1.59e-83

'Paired box' domain;


Pssm-ID: 366005  Cd Length: 125  Bit Score: 253.25  E-value: 1.59e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027  19 GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKV 98
Cdd:pfam00292   1 GHGGVNQLGGVFVNGRPLPDHIRQKIVELAHSGVRPCDISRQLRVSHGCVSKILGRYYETGSIRPGVIGGSKPKVATPEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1207114027  99 VEKIAEYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIR 143
Cdd:pfam00292  81 VTKIAEYKRENPSIFAWEIRDRLLKEGVCDNDTVPSVSSINRILR 125
Pax2_C pfam12403
Paired-box protein 2 C terminal; This domain family is found in eukaryotes, and is ...
 352-443 1.14e-46

Paired-box protein 2 C terminal; This domain family is found in eukaryotes, and is approximately 110 amino acids in length. The family is found in association with pfam00292. This family is the C terminal of the paired-box protein 2 which is a transcription factor involved in embryonic development and organogenesis.


Pssm-ID: 463563  Cd Length: 113  Bit Score: 157.63  E-value: 1.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027 352 ASTPCYGAYAHHAPSYCQYTSQHIIAGREMASTTLPGYPPHVPPTGQGSYPTSTLAGMVPGSDFSGNPYSHPQYTTYNEA 431
Cdd:pfam12403   1 ASLASFSAFAHLGSSYGQFQSYSLVAGRDMASTTLPGYPPHVPPTGQGSYSTSTLAGMVPGSDYSGNPYSHPQYSSYNEA 80

                          90
                  ....*....|..
gi 1207114027 432 WRFSNPALLMPH 443
Cdd:pfam12403  81 WRFPNPSLLGSP 92
Csa3 COG3415
CRISPR-associated protein Csa3, CARF domain [Defense mechanisms]; CRISPR-associated protein ...
 41-155 9.28e-08

CRISPR-associated protein Csa3, CARF domain [Defense mechanisms]; CRISPR-associated protein Csa3, CARF domain is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 442641 [Multi-domain]  Cd Length: 325  Bit Score: 53.70  E-value: 9.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027  41 RQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETG--SIKPGVIGGSKPKVaTPKVVEKIAEY-KRQNPTMFA-W- 115
Cdd:COG3415    28 RLRAVLLLAEGLSVREIAERLGVSRSTVYRWLKRYREGGlaGLKDRPRGGRPSKL-SDEQRERLLELlREKSPDQGSrWt 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1207114027 116 --EIRDRLLAE-GVcdndTVpSVSSINRI-----IRTKVQQPFHPSSD 155
Cdd:COG3415   107 laELAELLEEEfGV----EV-SPSTVRRLlkrlgLSYKKPRPRAPKQD 149
M20_dipept_like cd05679
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
 218-338 9.29e-03

uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.


Pssm-ID: 349928 [Multi-domain]  Cd Length: 448  Bit Score: 38.25  E-value: 9.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027 218 SDSQGSVESLRKHLRADAFTQQQLEALDRVFerpSYPDVFPTSEHIKPEQANEYSLPALNPGLdevKPSLSTSVSSDLGS 297
Cdd:cd05679   324 TDPDTFIPAVRAHLDANGFDGVEVTASQMVF---AATRLDPDSPWVGWALASLQKTTGKKPAL---LPNLGGSLPNDVFS 397

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1207114027 298 SVsQSYPVVTESHSSSMCVKQEPHEASLAPFTPSSLAV-SGL 338
Cdd:cd05679   398 EV-LGLPTLWVPHSYPACSQHAPNEHILAPVMREALRVmAGL 438
 
Name Accession Description Interval E-value
PAX smart00351
Paired Box domain;
19-143 6.30e-89

Paired Box domain;


Pssm-ID: 128645 [Multi-domain]  Cd Length: 125  Bit Score: 267.27  E-value: 6.30e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027   19 GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKV 98
Cdd:smart00351   1 GHGGVNQLGGVFVNGRPLPDEERQRIVELAQNGVRPCDISRQLCVSHGCVSKILGRYYETGSIRPGAIGGSKPKVATPKV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1207114027   99 VEKIAEYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIR 143
Cdd:smart00351  81 VKKIADYKQENPGIFAWEIRDRLLSEGVCDKDNVPSVSSINRILR 125
PAX cd00131
Paired Box domain
 19-145 2.07e-84

Paired Box domain


Pssm-ID: 238076  Cd Length: 128  Bit Score: 255.81  E-value: 2.07e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027  19 GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKV 98
Cdd:cd00131     1 GQGGVNQLGGVFVNGRPLPDSIRQRIVELAQSGIRPCDISRQLRVSHGCVSKILNRYYETGSIRPGAIGGSKPRVATPEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1207114027  99 VEKIAEYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIRTK 145
Cdd:cd00131    81 VKKIEIYKQENPGMFAWEIRDRLLQEGVCDKSNVPSVSSINRILRNK 127
PAX pfam00292
'Paired box' domain;
19-143 1.59e-83

'Paired box' domain;


Pssm-ID: 366005  Cd Length: 125  Bit Score: 253.25  E-value: 1.59e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027  19 GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKV 98
Cdd:pfam00292   1 GHGGVNQLGGVFVNGRPLPDHIRQKIVELAHSGVRPCDISRQLRVSHGCVSKILGRYYETGSIRPGVIGGSKPKVATPEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1207114027  99 VEKIAEYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIR 143
Cdd:pfam00292  81 VTKIAEYKRENPSIFAWEIRDRLLKEGVCDNDTVPSVSSINRILR 125
Pax2_C pfam12403
Paired-box protein 2 C terminal; This domain family is found in eukaryotes, and is ...
 352-443 1.14e-46

Paired-box protein 2 C terminal; This domain family is found in eukaryotes, and is approximately 110 amino acids in length. The family is found in association with pfam00292. This family is the C terminal of the paired-box protein 2 which is a transcription factor involved in embryonic development and organogenesis.


Pssm-ID: 463563  Cd Length: 113  Bit Score: 157.63  E-value: 1.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027 352 ASTPCYGAYAHHAPSYCQYTSQHIIAGREMASTTLPGYPPHVPPTGQGSYPTSTLAGMVPGSDFSGNPYSHPQYTTYNEA 431
Cdd:pfam12403   1 ASLASFSAFAHLGSSYGQFQSYSLVAGRDMASTTLPGYPPHVPPTGQGSYSTSTLAGMVPGSDYSGNPYSHPQYSSYNEA 80

                          90
                  ....*....|..
gi 1207114027 432 WRFSNPALLMPH 443
Cdd:pfam12403  81 WRFPNPSLLGSP 92
Csa3 COG3415
CRISPR-associated protein Csa3, CARF domain [Defense mechanisms]; CRISPR-associated protein ...
 41-155 9.28e-08

CRISPR-associated protein Csa3, CARF domain [Defense mechanisms]; CRISPR-associated protein Csa3, CARF domain is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 442641 [Multi-domain]  Cd Length: 325  Bit Score: 53.70  E-value: 9.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027  41 RQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETG--SIKPGVIGGSKPKVaTPKVVEKIAEY-KRQNPTMFA-W- 115
Cdd:COG3415    28 RLRAVLLLAEGLSVREIAERLGVSRSTVYRWLKRYREGGlaGLKDRPRGGRPSKL-SDEQRERLLELlREKSPDQGSrWt 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1207114027 116 --EIRDRLLAE-GVcdndTVpSVSSINRI-----IRTKVQQPFHPSSD 155
Cdd:COG3415   107 laELAELLEEEfGV----EV-SPSTVRRLlkrlgLSYKKPRPRAPKQD 149
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 33-82 1.27e-03

Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.


Pssm-ID: 238042 [Multi-domain]  Cd Length: 78  Bit Score: 37.66  E-value: 1.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1207114027  33 GRPLPDVVRQRIVE-LAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIK 82
Cdd:cd00090     1 LKALSDPTRLRILRlLLEGPLTVSELAERLGLSQSTVSRHLKKLEEAGLVE 51
M20_dipept_like cd05679
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
 218-338 9.29e-03

uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.


Pssm-ID: 349928 [Multi-domain]  Cd Length: 448  Bit Score: 38.25  E-value: 9.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114027 218 SDSQGSVESLRKHLRADAFTQQQLEALDRVFerpSYPDVFPTSEHIKPEQANEYSLPALNPGLdevKPSLSTSVSSDLGS 297
Cdd:cd05679   324 TDPDTFIPAVRAHLDANGFDGVEVTASQMVF---AATRLDPDSPWVGWALASLQKTTGKKPAL---LPNLGGSLPNDVFS 397

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1207114027 298 SVsQSYPVVTESHSSSMCVKQEPHEASLAPFTPSSLAV-SGL 338
Cdd:cd05679   398 EV-LGLPTLWVPHSYPACSQHAPNEHILAPVMREALRVmAGL 438
 
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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