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Conserved domains on  [gi|1207114025|ref|XP_021336174.1|]
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paired box protein Pax-2a isoform X10 [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;
19-150 3.17e-86

Paired Box domain;


:

Pssm-ID: 128645 [Multi-domain]  Cd Length: 125  Bit Score: 260.33  E-value: 3.17e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025   19 GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGsyqkdliRYYETGSIKPGVIGGSKP 98
Cdd:smart00351   1 GHGGVNQLGGVFVNGRPLPDEERQRIVELAQNGVRPCDISRQLCVSHGCVSKILG-------RYYETGSIRPGAIGGSKP 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207114025   99 KVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIR 150
Cdd:smart00351  74 KVATPKVVKKIADYKQENPGIFAWEIRDRLLSEGVCDKDNVPSVSSINRILR 125
Pax2_C pfam12403
Paired-box protein 2 C terminal; This domain family is found in eukaryotes, and is ...
 359-450 6.61e-47

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: 158.40  E-value: 6.61e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025 359 ASTPCYGAYAHHAPSYCQYTSQHIIAGREMASTTLPGYPPHVPPTGQGSYPTSTLAGMVPGSDFSGNPYSHPQYTTYNEA 438
Cdd:pfam12403   1 ASLASFSAFAHLGSSYGQFQSYSLVAGRDMASTTLPGYPPHVPPTGQGSYSTSTLAGMVPGSDYSGNPYSHPQYSSYNEA 80

                          90
                  ....*....|..
gi 1207114025 439 WRFSNPALLMPH 450
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 ...
 225-345 8.32e-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: 38.63  E-value: 8.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025 225 SDSQGSVESLRKHLRADAFTQQQLEALDRVFerpSYPDVFPTSEHIKPEQANEYSLPALNPGLdevKPSLSTSVSSDLGS 304
Cdd:cd05679   324 TDPDTFIPAVRAHLDANGFDGVEVTASQMVF---AATRLDPDSPWVGWALASLQKTTGKKPAL---LPNLGGSLPNDVFS 397

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1207114025 305 SVsQSYPVVTESHSSSMCVKQEPHEASLAPFTPSSLAV-SGL 345
Cdd:cd05679   398 EV-LGLPTLWVPHSYPACSQHAPNEHILAPVMREALRVmAGL 438
 
Name Accession Description Interval E-value
PAX smart00351
Paired Box domain;
19-150 3.17e-86

Paired Box domain;


Pssm-ID: 128645 [Multi-domain]  Cd Length: 125  Bit Score: 260.33  E-value: 3.17e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025   19 GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGsyqkdliRYYETGSIKPGVIGGSKP 98
Cdd:smart00351   1 GHGGVNQLGGVFVNGRPLPDEERQRIVELAQNGVRPCDISRQLCVSHGCVSKILG-------RYYETGSIRPGAIGGSKP 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207114025   99 KVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIR 150
Cdd:smart00351  74 KVATPKVVKKIADYKQENPGIFAWEIRDRLLSEGVCDKDNVPSVSSINRILR 125
PAX cd00131
Paired Box domain
 19-152 1.03e-81

Paired Box domain


Pssm-ID: 238076  Cd Length: 128  Bit Score: 248.87  E-value: 1.03e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025  19 GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGsyqkdliRYYETGSIKPGVIGGSKP 98
Cdd:cd00131     1 GQGGVNQLGGVFVNGRPLPDSIRQRIVELAQSGIRPCDISRQLRVSHGCVSKILN-------RYYETGSIRPGAIGGSKP 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207114025  99 KVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIRTK 152
Cdd:cd00131    74 RVATPEVVKKIEIYKQENPGMFAWEIRDRLLQEGVCDKSNVPSVSSINRILRNK 127
PAX pfam00292
'Paired box' domain;
19-150 6.90e-81

'Paired box' domain;


Pssm-ID: 366005  Cd Length: 125  Bit Score: 246.71  E-value: 6.90e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025  19 GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGsyqkdliRYYETGSIKPGVIGGSKP 98
Cdd:pfam00292   1 GHGGVNQLGGVFVNGRPLPDHIRQKIVELAHSGVRPCDISRQLRVSHGCVSKILG-------RYYETGSIRPGVIGGSKP 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1207114025  99 KVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIR 150
Cdd:pfam00292  74 KVATPEVVTKIAEYKRENPSIFAWEIRDRLLKEGVCDNDTVPSVSSINRILR 125
Pax2_C pfam12403
Paired-box protein 2 C terminal; This domain family is found in eukaryotes, and is ...
 359-450 6.61e-47

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: 158.40  E-value: 6.61e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025 359 ASTPCYGAYAHHAPSYCQYTSQHIIAGREMASTTLPGYPPHVPPTGQGSYPTSTLAGMVPGSDFSGNPYSHPQYTTYNEA 438
Cdd:pfam12403   1 ASLASFSAFAHLGSSYGQFQSYSLVAGRDMASTTLPGYPPHVPPTGQGSYSTSTLAGMVPGSDYSGNPYSHPQYSSYNEA 80

                          90
                  ....*....|..
gi 1207114025 439 WRFSNPALLMPH 450
Cdd:pfam12403  81 WRFPNPSLLGSP 92
Csa3 COG3415
CRISPR-associated protein Csa3, CARF domain [Defense mechanisms]; CRISPR-associated protein ...
 41-162 1.61e-05

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: 46.77  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025  41 RQRIVELAHQGVRPCDISRQLRVSHGCVSKILGsyqkdliRYYETG--SIKPGVIGGSKPKVaTPKVVEKIAEY-KRQNP 117
Cdd:COG3415    28 RLRAVLLLAEGLSVREIAERLGVSRSTVYRWLK-------RYREGGlaGLKDRPRGGRPSKL-SDEQRERLLELlREKSP 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207114025 118 TMFA-W---EIRDRLLAE-GVcdndTVpSVSSINRI-----IRTKVQQPFHPSSD 162
Cdd:COG3415   100 DQGSrWtlaELAELLEEEfGV----EV-SPSTVRRLlkrlgLSYKKPRPRAPKQD 149
M20_dipept_like cd05679
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
 225-345 8.32e-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: 38.63  E-value: 8.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025 225 SDSQGSVESLRKHLRADAFTQQQLEALDRVFerpSYPDVFPTSEHIKPEQANEYSLPALNPGLdevKPSLSTSVSSDLGS 304
Cdd:cd05679   324 TDPDTFIPAVRAHLDANGFDGVEVTASQMVF---AATRLDPDSPWVGWALASLQKTTGKKPAL---LPNLGGSLPNDVFS 397

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1207114025 305 SVsQSYPVVTESHSSSMCVKQEPHEASLAPFTPSSLAV-SGL 345
Cdd:cd05679   398 EV-LGLPTLWVPHSYPACSQHAPNEHILAPVMREALRVmAGL 438
 
Name Accession Description Interval E-value
PAX smart00351
Paired Box domain;
19-150 3.17e-86

Paired Box domain;


Pssm-ID: 128645 [Multi-domain]  Cd Length: 125  Bit Score: 260.33  E-value: 3.17e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025   19 GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGsyqkdliRYYETGSIKPGVIGGSKP 98
Cdd:smart00351   1 GHGGVNQLGGVFVNGRPLPDEERQRIVELAQNGVRPCDISRQLCVSHGCVSKILG-------RYYETGSIRPGAIGGSKP 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1207114025   99 KVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIR 150
Cdd:smart00351  74 KVATPKVVKKIADYKQENPGIFAWEIRDRLLSEGVCDKDNVPSVSSINRILR 125
PAX cd00131
Paired Box domain
 19-152 1.03e-81

Paired Box domain


Pssm-ID: 238076  Cd Length: 128  Bit Score: 248.87  E-value: 1.03e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025  19 GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGsyqkdliRYYETGSIKPGVIGGSKP 98
Cdd:cd00131     1 GQGGVNQLGGVFVNGRPLPDSIRQRIVELAQSGIRPCDISRQLRVSHGCVSKILN-------RYYETGSIRPGAIGGSKP 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207114025  99 KVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIRTK 152
Cdd:cd00131    74 RVATPEVVKKIEIYKQENPGMFAWEIRDRLLQEGVCDKSNVPSVSSINRILRNK 127
PAX pfam00292
'Paired box' domain;
19-150 6.90e-81

'Paired box' domain;


Pssm-ID: 366005  Cd Length: 125  Bit Score: 246.71  E-value: 6.90e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025  19 GHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGsyqkdliRYYETGSIKPGVIGGSKP 98
Cdd:pfam00292   1 GHGGVNQLGGVFVNGRPLPDHIRQKIVELAHSGVRPCDISRQLRVSHGCVSKILG-------RYYETGSIRPGVIGGSKP 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1207114025  99 KVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIR 150
Cdd:pfam00292  74 KVATPEVVTKIAEYKRENPSIFAWEIRDRLLKEGVCDNDTVPSVSSINRILR 125
Pax2_C pfam12403
Paired-box protein 2 C terminal; This domain family is found in eukaryotes, and is ...
 359-450 6.61e-47

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: 158.40  E-value: 6.61e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025 359 ASTPCYGAYAHHAPSYCQYTSQHIIAGREMASTTLPGYPPHVPPTGQGSYPTSTLAGMVPGSDFSGNPYSHPQYTTYNEA 438
Cdd:pfam12403   1 ASLASFSAFAHLGSSYGQFQSYSLVAGRDMASTTLPGYPPHVPPTGQGSYSTSTLAGMVPGSDYSGNPYSHPQYSSYNEA 80

                          90
                  ....*....|..
gi 1207114025 439 WRFSNPALLMPH 450
Cdd:pfam12403  81 WRFPNPSLLGSP 92
Csa3 COG3415
CRISPR-associated protein Csa3, CARF domain [Defense mechanisms]; CRISPR-associated protein ...
 41-162 1.61e-05

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: 46.77  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025  41 RQRIVELAHQGVRPCDISRQLRVSHGCVSKILGsyqkdliRYYETG--SIKPGVIGGSKPKVaTPKVVEKIAEY-KRQNP 117
Cdd:COG3415    28 RLRAVLLLAEGLSVREIAERLGVSRSTVYRWLK-------RYREGGlaGLKDRPRGGRPSKL-SDEQRERLLELlREKSP 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207114025 118 TMFA-W---EIRDRLLAE-GVcdndTVpSVSSINRI-----IRTKVQQPFHPSSD 162
Cdd:COG3415   100 DQGSrWtlaELAELLEEEfGV----EV-SPSTVRRLlkrlgLSYKKPRPRAPKQD 149
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 33-86 7.02e-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: 35.35  E-value: 7.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207114025  33 GRPLPDVVRQRIVE-LAHQGVRPCDISRQLRVSHGCVSKILGS-YQKDLIRYYETG 86
Cdd:cd00090     1 LKALSDPTRLRILRlLLEGPLTVSELAERLGLSQSTVSRHLKKlEEAGLVESRREG 56
M20_dipept_like cd05679
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ...
 225-345 8.32e-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: 38.63  E-value: 8.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207114025 225 SDSQGSVESLRKHLRADAFTQQQLEALDRVFerpSYPDVFPTSEHIKPEQANEYSLPALNPGLdevKPSLSTSVSSDLGS 304
Cdd:cd05679   324 TDPDTFIPAVRAHLDANGFDGVEVTASQMVF---AATRLDPDSPWVGWALASLQKTTGKKPAL---LPNLGGSLPNDVFS 397

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1207114025 305 SVsQSYPVVTESHSSSMCVKQEPHEASLAPFTPSSLAV-SGL 345
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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