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Conserved domains on  [gi|767904618|ref|XP_011539874|]
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protein-arginine deiminase type-3 isoform X3 [Homo sapiens]

Protein Classification

phenolic acid decarboxylase; protein-arginine deiminase domain-containing protein( domain architecture ID 10553848)

phenolic acid decarboxylase catalyzes the decarboxylation and detoxification of phenolic derivatives, including ferulic, p-coumaric and caffeic acids| protein-arginine deiminase (PAD) domain-containing protein may catalyze the conversion of protein-bound arginine residues to citrulline residues in a calcium ion-dependent manner

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAD_M pfam08527
Protein-arginine deiminase (PAD) middle domain; This family represents the central ...
 115-273 6.27e-91

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: 271.68  E-value: 6.27e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904618  115 VDISLDCDLNCEGRQDRNFVDKRQWVWGPSGYGGILLVNCDRDDPSCDVQDNCDQHVHCLQDLEDMSVMVLRTQGPAALF 194
Cdd:pfam08527   1 VEISLDVDADRDGVVEKNNPDKGSWTWGPNGQGAILLVNCDRDNPGSQKPDCEDSKVFSLEDLKDMSLMVLRTQGPSKLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904618  195 DDHKLVLHTSSYDAKRAQVFHICGPeDVCEAYRHVLGQDKVSYEVPRLHGDEER-FFVEGLSFPDAGFTGLISFHVTLLD 273
Cdd:pfam08527  81 DGYKLVLHVSKSDADKVRVFHAQGG-DSGSRYKLVLGPGKLSYVVEYLGGQAEItFYVEGLAFPDADFSGLVSISVSLLE 159
PAD_N pfam08526
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal ...
 1-113 2.05e-51

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: 168.51  E-value: 2.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904618    1 MSLQRIVRVSLEHPTSAVCVAGVETLVDIYGSVPEGTEMFEVYGTPGVDIYISPNMERGRERADTRRWRFDATLEIIVVM 80
Cdd:pfam08526   1 MAFQRTVRLSLDSPTHAVCVLGTETLVDVYRSAPKGCKSFSVKGSPGVLVDIAPSVPRTTEPSGTSRWPLDPNTDVLVSM 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767904618   81 NSPSNDLNDSHVQISYHSSHEPLPLAYAVLYLT 113
Cdd:pfam08526  81 DSASSEVNDDKVSVSYYGPDEEAPLGTAVLYLT 113
PAD super family cl09549
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
 283-385 2.78e-51

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: 177.03  E-value: 2.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904618  283 PIFTDTVVFRVAPWIMTPSTLPPLEVYVCRVRNN--TCFVDAVAELARKAGCKLTICPQAENRNDRWIQDEMELGYVQAP 360
Cdd:pfam03068   1 PIFSDTVVFRVAPWIMTPNTQPPEEVYVCRGKENsqQGFVKELTDLVKKAGIQLPVCPFNENRGDRWMQDEMEFGYTQAP 80

                          90       100
                  ....*....|....*....|....*
gi 767904618  361 HKTLPVVFDSPRNGELQDFPYKRIL 385
Cdd:pfam03068  81 GKGLPVVLDSPRGRGLEDFPFKQLL 105
 
Name Accession Description Interval E-value
PAD_M pfam08527
Protein-arginine deiminase (PAD) middle domain; This family represents the central ...
 115-273 6.27e-91

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: 271.68  E-value: 6.27e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904618  115 VDISLDCDLNCEGRQDRNFVDKRQWVWGPSGYGGILLVNCDRDDPSCDVQDNCDQHVHCLQDLEDMSVMVLRTQGPAALF 194
Cdd:pfam08527   1 VEISLDVDADRDGVVEKNNPDKGSWTWGPNGQGAILLVNCDRDNPGSQKPDCEDSKVFSLEDLKDMSLMVLRTQGPSKLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904618  195 DDHKLVLHTSSYDAKRAQVFHICGPeDVCEAYRHVLGQDKVSYEVPRLHGDEER-FFVEGLSFPDAGFTGLISFHVTLLD 273
Cdd:pfam08527  81 DGYKLVLHVSKSDADKVRVFHAQGG-DSGSRYKLVLGPGKLSYVVEYLGGQAEItFYVEGLAFPDADFSGLVSISVSLLE 159
PAD_N pfam08526
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal ...
 1-113 2.05e-51

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: 168.51  E-value: 2.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904618    1 MSLQRIVRVSLEHPTSAVCVAGVETLVDIYGSVPEGTEMFEVYGTPGVDIYISPNMERGRERADTRRWRFDATLEIIVVM 80
Cdd:pfam08526   1 MAFQRTVRLSLDSPTHAVCVLGTETLVDVYRSAPKGCKSFSVKGSPGVLVDIAPSVPRTTEPSGTSRWPLDPNTDVLVSM 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767904618   81 NSPSNDLNDSHVQISYHSSHEPLPLAYAVLYLT 113
Cdd:pfam08526  81 DSASSEVNDDKVSVSYYGPDEEAPLGTAVLYLT 113
PAD pfam03068
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
 283-385 2.78e-51

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: 177.03  E-value: 2.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904618  283 PIFTDTVVFRVAPWIMTPSTLPPLEVYVCRVRNN--TCFVDAVAELARKAGCKLTICPQAENRNDRWIQDEMELGYVQAP 360
Cdd:pfam03068   1 PIFSDTVVFRVAPWIMTPNTQPPEEVYVCRGKENsqQGFVKELTDLVKKAGIQLPVCPFNENRGDRWMQDEMEFGYTQAP 80

                          90       100
                  ....*....|....*....|....*
gi 767904618  361 HKTLPVVFDSPRNGELQDFPYKRIL 385
Cdd:pfam03068  81 GKGLPVVLDSPRGRGLEDFPFKQLL 105
PAD_N cd04214
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic ...
 7-114 1.53e-44

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: 150.22  E-value: 1.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904618   7 VRVSLEHPTSAVCVAGVETLVDIYGSVPEGTEMFEVYGTPGVDIYISPNMERGRERADTRRWRFDATLEIIVVMNSPSND 86
Cdd:cd04214    1 LRLDTGSRTHAVCVLGTETTLDIYGSAPAGATSFSVKASPGVVVDVAHSPPAKKEPTGLWPWPLDTDVEVTMTMKAASKE 80

                         90       100
                 ....*....|....*....|....*...
gi 767904618  87 LNDSHVQISYHSSHEPLPLAYAVLYLTC 114
Cdd:cd04214   81 VNDSKVRVSYYGPKEDAPLGKAVLYLTG 108
 
Name Accession Description Interval E-value
PAD_M pfam08527
Protein-arginine deiminase (PAD) middle domain; This family represents the central ...
 115-273 6.27e-91

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: 271.68  E-value: 6.27e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904618  115 VDISLDCDLNCEGRQDRNFVDKRQWVWGPSGYGGILLVNCDRDDPSCDVQDNCDQHVHCLQDLEDMSVMVLRTQGPAALF 194
Cdd:pfam08527   1 VEISLDVDADRDGVVEKNNPDKGSWTWGPNGQGAILLVNCDRDNPGSQKPDCEDSKVFSLEDLKDMSLMVLRTQGPSKLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904618  195 DDHKLVLHTSSYDAKRAQVFHICGPeDVCEAYRHVLGQDKVSYEVPRLHGDEER-FFVEGLSFPDAGFTGLISFHVTLLD 273
Cdd:pfam08527  81 DGYKLVLHVSKSDADKVRVFHAQGG-DSGSRYKLVLGPGKLSYVVEYLGGQAEItFYVEGLAFPDADFSGLVSISVSLLE 159
PAD_N pfam08526
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal ...
 1-113 2.05e-51

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: 168.51  E-value: 2.05e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904618    1 MSLQRIVRVSLEHPTSAVCVAGVETLVDIYGSVPEGTEMFEVYGTPGVDIYISPNMERGRERADTRRWRFDATLEIIVVM 80
Cdd:pfam08526   1 MAFQRTVRLSLDSPTHAVCVLGTETLVDVYRSAPKGCKSFSVKGSPGVLVDIAPSVPRTTEPSGTSRWPLDPNTDVLVSM 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767904618   81 NSPSNDLNDSHVQISYHSSHEPLPLAYAVLYLT 113
Cdd:pfam08526  81 DSASSEVNDDKVSVSYYGPDEEAPLGTAVLYLT 113
PAD pfam03068
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
 283-385 2.78e-51

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: 177.03  E-value: 2.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904618  283 PIFTDTVVFRVAPWIMTPSTLPPLEVYVCRVRNN--TCFVDAVAELARKAGCKLTICPQAENRNDRWIQDEMELGYVQAP 360
Cdd:pfam03068   1 PIFSDTVVFRVAPWIMTPNTQPPEEVYVCRGKENsqQGFVKELTDLVKKAGIQLPVCPFNENRGDRWMQDEMEFGYTQAP 80

                          90       100
                  ....*....|....*....|....*
gi 767904618  361 HKTLPVVFDSPRNGELQDFPYKRIL 385
Cdd:pfam03068  81 GKGLPVVLDSPRGRGLEDFPFKQLL 105
PAD_N cd04214
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic ...
 7-114 1.53e-44

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: 150.22  E-value: 1.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767904618   7 VRVSLEHPTSAVCVAGVETLVDIYGSVPEGTEMFEVYGTPGVDIYISPNMERGRERADTRRWRFDATLEIIVVMNSPSND 86
Cdd:cd04214    1 LRLDTGSRTHAVCVLGTETTLDIYGSAPAGATSFSVKASPGVVVDVAHSPPAKKEPTGLWPWPLDTDVEVTMTMKAASKE 80

                         90       100
                 ....*....|....*....|....*...
gi 767904618  87 LNDSHVQISYHSSHEPLPLAYAVLYLTC 114
Cdd:cd04214   81 VNDSKVRVSYYGPKEDAPLGKAVLYLTG 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.
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