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Conserved domains on  [gi|767903526|ref|XP_011539455|]
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protein-arginine deiminase type-4 isoform X4 [Homo sapiens]

Protein Classification

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 ...
 113-273 1.58e-94

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: 279.77  E-value: 1.58e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903526  113 VEISLCADITRTGKVKptRAVKDQRTWTWGPCGQGAILLVNCDRDNLESSAMDCEDDEVLDSEDLQDMSLMTLSTKTPKD 192
Cdd:pfam08527   1 VEISLDVDADRDGVVE--KNNPDKGSWTWGPNGQGAILLVNCDRDNPGSQKPDCEDSKVFSLEDLKDMSLMVLRTQGPSK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903526  193 FFTNHTLVLHVARSEMDKVRVFQATRGKLSSKCSVVLGPKWPSHYLMVPGGKHNMDFYVEALAFPDTDFPGLITLTISLL 272
Cdd:pfam08527  79 LFDGYKLVLHVSKSDADKVRVFHAQGGDSGSRYKLVLGPGKLSYVVEYLGGQAEITFYVEGLAFPDADFSGLVSISVSLL 158


                  .
gi 767903526  273 D 273
Cdd:pfam08527 159 E 159
PAD super family cl09549
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
 283-396 2.18e-53

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: 182.04  E-value: 2.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903526  283 VVFQDSVVFRVAPWIMTPNTQPPQEVYACSIFEN--EDFLKSVTTLAMKAKCKLTICPEEENMDDQWMQDEMEIGYIQAP 360
Cdd:pfam03068   1 PIFSDTVVFRVAPWIMTPNTQPPEEVYVCRGKENsqQGFVKELTDLVKKAGIQLPVCPFNENRGDRWMQDEMEFGYTQAP 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767903526  361 HKTLPVVFDSPRNRGLKEFPIKRVMILSIGPFYRRR 396
Cdd:pfam03068  81 GKGLPVVLDSPRGRGLEDFPFKQLLGPDFGYVTRET 116
PAD_N cd04214
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic ...
 7-112 5.45e-53

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: 171.79  E-value: 5.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903526   7 IRVTPEQPTHAVCVLGTLTQLDICSSAPEDCTSFSINASPGVVVDIAHGPPAKKKSTGSSTWPLDPGVEVTLTMKVASGS 86
Cdd:cd04214    1 LRLDTGSRTHAVCVLGTETTLDIYGSAPAGATSFSVKASPGVVVDVAHSPPAKKEPTGLWPWPLDTDVEVTMTMKAASKE 80

                         90       100
                 ....*....|....*....|....*...
gi 767903526  87 TGDQKVQISYYGPKT--PPVKALLYLTG 112
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 ...
 113-273 1.58e-94

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: 279.77  E-value: 1.58e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903526  113 VEISLCADITRTGKVKptRAVKDQRTWTWGPCGQGAILLVNCDRDNLESSAMDCEDDEVLDSEDLQDMSLMTLSTKTPKD 192
Cdd:pfam08527   1 VEISLDVDADRDGVVE--KNNPDKGSWTWGPNGQGAILLVNCDRDNPGSQKPDCEDSKVFSLEDLKDMSLMVLRTQGPSK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903526  193 FFTNHTLVLHVARSEMDKVRVFQATRGKLSSKCSVVLGPKWPSHYLMVPGGKHNMDFYVEALAFPDTDFPGLITLTISLL 272
Cdd:pfam08527  79 LFDGYKLVLHVSKSDADKVRVFHAQGGDSGSRYKLVLGPGKLSYVVEYLGGQAEITFYVEGLAFPDADFSGLVSISVSLL 158


                  .
gi 767903526  273 D 273
Cdd:pfam08527 159 E 159
PAD pfam03068
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
 283-396 2.18e-53

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: 182.04  E-value: 2.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903526  283 VVFQDSVVFRVAPWIMTPNTQPPQEVYACSIFEN--EDFLKSVTTLAMKAKCKLTICPEEENMDDQWMQDEMEIGYIQAP 360
Cdd:pfam03068   1 PIFSDTVVFRVAPWIMTPNTQPPEEVYVCRGKENsqQGFVKELTDLVKKAGIQLPVCPFNENRGDRWMQDEMEFGYTQAP 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767903526  361 HKTLPVVFDSPRNRGLKEFPIKRVMILSIGPFYRRR 396
Cdd:pfam03068  81 GKGLPVVLDSPRGRGLEDFPFKQLLGPDFGYVTRET 116
PAD_N cd04214
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic ...
 7-112 5.45e-53

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: 171.79  E-value: 5.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903526   7 IRVTPEQPTHAVCVLGTLTQLDICSSAPEDCTSFSINASPGVVVDIAHGPPAKKKSTGSSTWPLDPGVEVTLTMKVASGS 86
Cdd:cd04214    1 LRLDTGSRTHAVCVLGTETTLDIYGSAPAGATSFSVKASPGVVVDVAHSPPAKKEPTGLWPWPLDTDVEVTMTMKAASKE 80

                         90       100
                 ....*....|....*....|....*...
gi 767903526  87 TGDQKVQISYYGPKT--PPVKALLYLTG 112
Cdd:cd04214   81 VNDSKVRVSYYGPKEdaPLGKAVLYLTG 108
PAD_N pfam08526
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal ...
 1-111 1.07e-52

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: 171.21  E-value: 1.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903526    1 MAQGTLIRVTPEQPTHAVCVLGTLTQLDICSSAPEDCTSFSINASPGVVVDIAHGPPAKKKSTGSSTWPLDPGVEVTLTM 80
Cdd:pfam08526   1 MAFQRTVRLSLDSPTHAVCVLGTETLVDVYRSAPKGCKSFSVKGSPGVLVDIAPSVPRTTEPSGTSRWPLDPNTDVLVSM 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767903526   81 KVASGSTGDQKVQISYYGPKTPP--VKALLYLT 111
Cdd:pfam08526  81 DSASSEVNDDKVSVSYYGPDEEAplGTAVLYLT 113
 
Name Accession Description Interval E-value
PAD_M pfam08527
Protein-arginine deiminase (PAD) middle domain; This family represents the central ...
 113-273 1.58e-94

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: 279.77  E-value: 1.58e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903526  113 VEISLCADITRTGKVKptRAVKDQRTWTWGPCGQGAILLVNCDRDNLESSAMDCEDDEVLDSEDLQDMSLMTLSTKTPKD 192
Cdd:pfam08527   1 VEISLDVDADRDGVVE--KNNPDKGSWTWGPNGQGAILLVNCDRDNPGSQKPDCEDSKVFSLEDLKDMSLMVLRTQGPSK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903526  193 FFTNHTLVLHVARSEMDKVRVFQATRGKLSSKCSVVLGPKWPSHYLMVPGGKHNMDFYVEALAFPDTDFPGLITLTISLL 272
Cdd:pfam08527  79 LFDGYKLVLHVSKSDADKVRVFHAQGGDSGSRYKLVLGPGKLSYVVEYLGGQAEITFYVEGLAFPDADFSGLVSISVSLL 158


                  .
gi 767903526  273 D 273
Cdd:pfam08527 159 E 159
PAD pfam03068
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
 283-396 2.18e-53

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: 182.04  E-value: 2.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903526  283 VVFQDSVVFRVAPWIMTPNTQPPQEVYACSIFEN--EDFLKSVTTLAMKAKCKLTICPEEENMDDQWMQDEMEIGYIQAP 360
Cdd:pfam03068   1 PIFSDTVVFRVAPWIMTPNTQPPEEVYVCRGKENsqQGFVKELTDLVKKAGIQLPVCPFNENRGDRWMQDEMEFGYTQAP 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767903526  361 HKTLPVVFDSPRNRGLKEFPIKRVMILSIGPFYRRR 396
Cdd:pfam03068  81 GKGLPVVLDSPRGRGLEDFPFKQLLGPDFGYVTRET 116
PAD_N cd04214
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic ...
 7-112 5.45e-53

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: 171.79  E-value: 5.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903526   7 IRVTPEQPTHAVCVLGTLTQLDICSSAPEDCTSFSINASPGVVVDIAHGPPAKKKSTGSSTWPLDPGVEVTLTMKVASGS 86
Cdd:cd04214    1 LRLDTGSRTHAVCVLGTETTLDIYGSAPAGATSFSVKASPGVVVDVAHSPPAKKEPTGLWPWPLDTDVEVTMTMKAASKE 80

                         90       100
                 ....*....|....*....|....*...
gi 767903526  87 TGDQKVQISYYGPKT--PPVKALLYLTG 112
Cdd:cd04214   81 VNDSKVRVSYYGPKEdaPLGKAVLYLTG 108
PAD_N pfam08526
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal ...
 1-111 1.07e-52

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: 171.21  E-value: 1.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903526    1 MAQGTLIRVTPEQPTHAVCVLGTLTQLDICSSAPEDCTSFSINASPGVVVDIAHGPPAKKKSTGSSTWPLDPGVEVTLTM 80
Cdd:pfam08526   1 MAFQRTVRLSLDSPTHAVCVLGTETLVDVYRSAPKGCKSFSVKGSPGVLVDIAPSVPRTTEPSGTSRWPLDPNTDVLVSM 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767903526   81 KVASGSTGDQKVQISYYGPKTPP--VKALLYLT 111
Cdd:pfam08526  81 DSASSEVNDDKVSVSYYGPDEEAplGTAVLYLT 113
 
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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