NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|16307225|gb|AAH09701|]
View 

PADI2 protein [Homo sapiens]

Protein Classification

phenolic acid decarboxylase( domain architecture ID 10553848)

phenolic acid decarboxylase catalyzes the decarboxylation and detoxification of phenolic derivatives, including ferulic, p-coumaric and caffeic acids

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PAD_M pfam08527
Protein-arginine deiminase (PAD) middle domain; This family represents the central ...
 116-274 1.45e-102

Protein-arginine deiminase (PAD) middle domain; This family represents the central non-catalytic domain of protein-arginine deiminase. This domain has an immunoglobulin-like fold.


:

Pssm-ID: 462510  Cd Length: 159  Bit Score: 301.73  E-value: 1.45e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16307225   116 IEISLDVDADRDGVVEKNNPKKASWTWGPEGQGAILLVNCDRETPWLPKEDCRDEKVYSKEDLKDMSQMILRTKGPDRLP 195
Cdd:pfam08527   1 VEISLDVDADRDGVVEKNNPDKGSWTWGPNGQGAILLVNCDRDNPGSQKPDCEDSKVFSLEDLKDMSLMVLRTQGPSKLF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16307225   196 AGYEIVLYISMSDSDKVGVFYVENPFFGQRYIHILGRRKLYHVVKYTGGSAELLFFVEGLCFPDEGFSGLVSIHVSLLE 274
Cdd:pfam08527  81 DGYKLVLHVSKSDADKVRVFHAQGGDSGSRYKLVLGPGKLSYVVEYLGGQAEITFYVEGLAFPDADFSGLVSISVSLLE 159
PAD super family cl09549
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
 284-436 1.70e-87

Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence of calcium ions, PAD enzymes EC:3.5.3.15 catalyze the post-translational modification reaction responsible for the formation of citrulline residues: Protein L-arginine + H2O <=> Protein L-citrulline + NH3. Several types are recognized (and included in the family) on the basis of molecular mass, substrate specificity, and tissue localization. The expression of type I PAD is known to be under the control of oestrogen.


The actual alignment was detected with superfamily member pfam03068:

Pssm-ID: 460794  Cd Length: 393  Bit Score: 271.79  E-value: 1.70e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16307225   284 PIFTDTVIFRIAPWIMTPNILPPVSVFVCCMKDN--YLFLKEVKNLVEKTNCELKVCFQYLNRGDRWIQDEIEFGYIEAP 361
Cdd:pfam03068   1 PIFSDTVVFRVAPWIMTPNTQPPEEVYVCRGKENsqQGFVKELTDLVKKAGIQLPVCPFNENRGDRWMQDEMEFGYTQAP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16307225   362 HKGFPVVLDSPRDGNLKDFPVKELLGPDFGYVTREPLFESVTSLDSFGNLEVSPPVTVNGKTYPLGRILIGSSFP 436
Cdd:pfam03068  81 GKGLPVVLDSPRGRGLEDFPFKQLLGPDFGYVTRETDGFGVSELDSFGNLEVSPPVTVGGKEYPLGRILIGSSSY 155
PAD_N pfam08526
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal ...
 1-114 1.87e-45

Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal non-catalytic domain of protein-arginine deiminase. This domain has a cupredoxin-like fold.


:

Pssm-ID: 462509  Cd Length: 113  Bit Score: 153.10  E-value: 1.87e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16307225     1 MLRERTVRLQYGSRVEAVYVLGTYLWTDVYSAAPAGAQTFSLKHSEHVWVEVVRDGEAEEVATnGKQRWLLSPSTTLRVT 80
Cdd:pfam08526   1 MAFQRTVRLSLDSPTHAVCVLGTETLVDVYRSAPKGCKSFSVKGSPGVLVDIAPSVPRTTEPS-GTSRWPLDPNTDVLVS 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 16307225    81 MSQASTEASSDKVTVNYYDEEGSIPIDQAGLFLT 114
Cdd:pfam08526  80 MDSASSEVNDDKVSVSYYGPDEEAPLGTAVLYLT 113
 
Name Accession Description Interval E-value
PAD_M pfam08527
Protein-arginine deiminase (PAD) middle domain; This family represents the central ...
 116-274 1.45e-102

Protein-arginine deiminase (PAD) middle domain; This family represents the central non-catalytic domain of protein-arginine deiminase. This domain has an immunoglobulin-like fold.


Pssm-ID: 462510  Cd Length: 159  Bit Score: 301.73  E-value: 1.45e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16307225   116 IEISLDVDADRDGVVEKNNPKKASWTWGPEGQGAILLVNCDRETPWLPKEDCRDEKVYSKEDLKDMSQMILRTKGPDRLP 195
Cdd:pfam08527   1 VEISLDVDADRDGVVEKNNPDKGSWTWGPNGQGAILLVNCDRDNPGSQKPDCEDSKVFSLEDLKDMSLMVLRTQGPSKLF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16307225   196 AGYEIVLYISMSDSDKVGVFYVENPFFGQRYIHILGRRKLYHVVKYTGGSAELLFFVEGLCFPDEGFSGLVSIHVSLLE 274
Cdd:pfam08527  81 DGYKLVLHVSKSDADKVRVFHAQGGDSGSRYKLVLGPGKLSYVVEYLGGQAEITFYVEGLAFPDADFSGLVSISVSLLE 159
PAD pfam03068
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
 284-436 1.70e-87

Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence of calcium ions, PAD enzymes EC:3.5.3.15 catalyze the post-translational modification reaction responsible for the formation of citrulline residues: Protein L-arginine + H2O <=> Protein L-citrulline + NH3. Several types are recognized (and included in the family) on the basis of molecular mass, substrate specificity, and tissue localization. The expression of type I PAD is known to be under the control of oestrogen.


Pssm-ID: 460794  Cd Length: 393  Bit Score: 271.79  E-value: 1.70e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16307225   284 PIFTDTVIFRIAPWIMTPNILPPVSVFVCCMKDN--YLFLKEVKNLVEKTNCELKVCFQYLNRGDRWIQDEIEFGYIEAP 361
Cdd:pfam03068   1 PIFSDTVVFRVAPWIMTPNTQPPEEVYVCRGKENsqQGFVKELTDLVKKAGIQLPVCPFNENRGDRWMQDEMEFGYTQAP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16307225   362 HKGFPVVLDSPRDGNLKDFPVKELLGPDFGYVTREPLFESVTSLDSFGNLEVSPPVTVNGKTYPLGRILIGSSFP 436
Cdd:pfam03068  81 GKGLPVVLDSPRGRGLEDFPFKQLLGPDFGYVTRETDGFGVSELDSFGNLEVSPPVTVGGKEYPLGRILIGSSSY 155
PAD_N pfam08526
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal ...
 1-114 1.87e-45

Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal non-catalytic domain of protein-arginine deiminase. This domain has a cupredoxin-like fold.


Pssm-ID: 462509  Cd Length: 113  Bit Score: 153.10  E-value: 1.87e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16307225     1 MLRERTVRLQYGSRVEAVYVLGTYLWTDVYSAAPAGAQTFSLKHSEHVWVEVVRDGEAEEVATnGKQRWLLSPSTTLRVT 80
Cdd:pfam08526   1 MAFQRTVRLSLDSPTHAVCVLGTETLVDVYRSAPKGCKSFSVKGSPGVLVDIAPSVPRTTEPS-GTSRWPLDPNTDVLVS 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 16307225    81 MSQASTEASSDKVTVNYYDEEGSIPIDQAGLFLT 114
Cdd:pfam08526  80 MDSASSEVNDDKVSVSYYGPDEEAPLGTAVLYLT 113
PAD_N cd04214
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic ...
 7-115 6.24e-40

N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic domain of protein-arginine deiminase has a cupredoxin-like fold, but lacks the Cu binding site. PAD (protein-arginine deiminase) and protein L-arginine iminohydrolase catalyze the conversion of protein arginine residues to citrulline residues post-translationally in a process called citrullination. The modification plays crucial regulatory roles in development and cell differentiation.


Pssm-ID: 259876  Cd Length: 108  Bit Score: 138.66  E-value: 6.24e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16307225   7 VRLQYGSRVEAVYVLGTYLWTDVYSAAPAGAQTFSLKHSEHVWVEVVRDGEAEEVATnGKQRWLLSPSTTLRVTMSQAST 86
Cdd:cd04214   1 LRLDTGSRTHAVCVLGTETTLDIYGSAPAGATSFSVKASPGVVVDVAHSPPAKKEPT-GLWPWPLDTDVEVTMTMKAASK 79

                        90       100
                ....*....|....*....|....*....
gi 16307225  87 EASSDKVTVNYYDEEGSIPIDQAGLFLTA 115
Cdd:cd04214  80 EVNDSKVRVSYYGPKEDAPLGKAVLYLTG 108
 
Name Accession Description Interval E-value
PAD_M pfam08527
Protein-arginine deiminase (PAD) middle domain; This family represents the central ...
 116-274 1.45e-102

Protein-arginine deiminase (PAD) middle domain; This family represents the central non-catalytic domain of protein-arginine deiminase. This domain has an immunoglobulin-like fold.


Pssm-ID: 462510  Cd Length: 159  Bit Score: 301.73  E-value: 1.45e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16307225   116 IEISLDVDADRDGVVEKNNPKKASWTWGPEGQGAILLVNCDRETPWLPKEDCRDEKVYSKEDLKDMSQMILRTKGPDRLP 195
Cdd:pfam08527   1 VEISLDVDADRDGVVEKNNPDKGSWTWGPNGQGAILLVNCDRDNPGSQKPDCEDSKVFSLEDLKDMSLMVLRTQGPSKLF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16307225   196 AGYEIVLYISMSDSDKVGVFYVENPFFGQRYIHILGRRKLYHVVKYTGGSAELLFFVEGLCFPDEGFSGLVSIHVSLLE 274
Cdd:pfam08527  81 DGYKLVLHVSKSDADKVRVFHAQGGDSGSRYKLVLGPGKLSYVVEYLGGQAEITFYVEGLAFPDADFSGLVSISVSLLE 159
PAD pfam03068
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
 284-436 1.70e-87

Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence of calcium ions, PAD enzymes EC:3.5.3.15 catalyze the post-translational modification reaction responsible for the formation of citrulline residues: Protein L-arginine + H2O <=> Protein L-citrulline + NH3. Several types are recognized (and included in the family) on the basis of molecular mass, substrate specificity, and tissue localization. The expression of type I PAD is known to be under the control of oestrogen.


Pssm-ID: 460794  Cd Length: 393  Bit Score: 271.79  E-value: 1.70e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16307225   284 PIFTDTVIFRIAPWIMTPNILPPVSVFVCCMKDN--YLFLKEVKNLVEKTNCELKVCFQYLNRGDRWIQDEIEFGYIEAP 361
Cdd:pfam03068   1 PIFSDTVVFRVAPWIMTPNTQPPEEVYVCRGKENsqQGFVKELTDLVKKAGIQLPVCPFNENRGDRWMQDEMEFGYTQAP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16307225   362 HKGFPVVLDSPRDGNLKDFPVKELLGPDFGYVTREPLFESVTSLDSFGNLEVSPPVTVNGKTYPLGRILIGSSFP 436
Cdd:pfam03068  81 GKGLPVVLDSPRGRGLEDFPFKQLLGPDFGYVTRETDGFGVSELDSFGNLEVSPPVTVGGKEYPLGRILIGSSSY 155
PAD_N pfam08526
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal ...
 1-114 1.87e-45

Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal non-catalytic domain of protein-arginine deiminase. This domain has a cupredoxin-like fold.


Pssm-ID: 462509  Cd Length: 113  Bit Score: 153.10  E-value: 1.87e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16307225     1 MLRERTVRLQYGSRVEAVYVLGTYLWTDVYSAAPAGAQTFSLKHSEHVWVEVVRDGEAEEVATnGKQRWLLSPSTTLRVT 80
Cdd:pfam08526   1 MAFQRTVRLSLDSPTHAVCVLGTETLVDVYRSAPKGCKSFSVKGSPGVLVDIAPSVPRTTEPS-GTSRWPLDPNTDVLVS 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 16307225    81 MSQASTEASSDKVTVNYYDEEGSIPIDQAGLFLT 114
Cdd:pfam08526  80 MDSASSEVNDDKVSVSYYGPDEEAPLGTAVLYLT 113
PAD_N cd04214
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic ...
 7-115 6.24e-40

N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic domain of protein-arginine deiminase has a cupredoxin-like fold, but lacks the Cu binding site. PAD (protein-arginine deiminase) and protein L-arginine iminohydrolase catalyze the conversion of protein arginine residues to citrulline residues post-translationally in a process called citrullination. The modification plays crucial regulatory roles in development and cell differentiation.


Pssm-ID: 259876  Cd Length: 108  Bit Score: 138.66  E-value: 6.24e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16307225   7 VRLQYGSRVEAVYVLGTYLWTDVYSAAPAGAQTFSLKHSEHVWVEVVRDGEAEEVATnGKQRWLLSPSTTLRVTMSQAST 86
Cdd:cd04214   1 LRLDTGSRTHAVCVLGTETTLDIYGSAPAGATSFSVKASPGVVVDVAHSPPAKKEPT-GLWPWPLDTDVEVTMTMKAASK 79

                        90       100
                ....*....|....*....|....*....
gi 16307225  87 EASSDKVTVNYYDEEGSIPIDQAGLFLTA 115
Cdd:cd04214  80 EVNDSKVRVSYYGPKEDAPLGKAVLYLTG 108
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH