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Conserved domains on  [gi|489212956|ref|WP_003121701|]
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MULTISPECIES: agmatine deiminase [Pseudomonas]

Protein Classification

agmatine deiminase( domain architecture ID 10014279)

agmatine deiminase catalyzes the hydrolysis of agmatine to form carbamoylputrescine and ammonia in the arginine decarboxylase pathway of putrescine biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13551 PRK13551
agmatine deiminase; Provisional
5-366 0e+00

agmatine deiminase; Provisional


:

Pssm-ID: 184135  Cd Length: 362  Bit Score: 733.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956   5 TSTPRADGFRMPAEWEPHEQTWMVWPERPDNWRNGGKPAQAAFAAVAKAIARFEPVTVCASAGQYENARARLDDgNIRVV 84
Cdd:PRK13551   2 NSTPKQDGFRMPAEWEPHDAVWMIWPERPDNWRLGGKPAQAAFAKVAEAIARFEPVTMGVSAAQYANARARLPD-NVRVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  85 EISSDDAWVRDTGPTFVIDDKGDVRGVDWGFNAWGGFEGGLYFPWQRDDQVARKILEIERRARYRTDDFVLEGGSIHVDG 164
Cdd:PRK13551  81 EMSSDDAWVRDTGPTFVINDKGEVRGVDWGFNAWGGLVGGLYFPWDKDDQVAQKVLEIEGRDRYRAKPFVLEGGSIHVDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956 165 EGTLITTEECLLNHNRNPHLSQVEIERTLRDYLAVDSIIWLPNGLYNDETDGHVDNFCCYVRPGEVLLAWTDDQDDPNYL 244
Cdd:PRK13551 161 EGTLLTTEECLLNPNRNPHLTKEQIEQLLRDYLGVEKVIWLPDGIYNDETDGHVDNVCCFVRPGEVALAWTDDENDPQYA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956 245 RCQAALRVLEESRDAKGRKLVVHKMPIPGPLYATQEECDGVDIVEGSQPRDPSIRLAGSYVNFLIVNGGIVAPSFDDPKD 324
Cdd:PRK13551 241 RSKAALEVLENTTDAKGRKLKVHKLPIPGPLYATEEESAGVDAVEGTVPREAGERLAASYVNFLIANGGIIFPLFDDPND 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 489212956 325 AEARAILQRVFPEHEVVMVPGREILLGGGNIHCITQQQPAPR 366
Cdd:PRK13551 321 ALALEILQQMFPDRKVVGVPAREILLGGGNIHCITQQIPAAK 362
 
Name Accession Description Interval E-value
PRK13551 PRK13551
agmatine deiminase; Provisional
5-366 0e+00

agmatine deiminase; Provisional


Pssm-ID: 184135  Cd Length: 362  Bit Score: 733.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956   5 TSTPRADGFRMPAEWEPHEQTWMVWPERPDNWRNGGKPAQAAFAAVAKAIARFEPVTVCASAGQYENARARLDDgNIRVV 84
Cdd:PRK13551   2 NSTPKQDGFRMPAEWEPHDAVWMIWPERPDNWRLGGKPAQAAFAKVAEAIARFEPVTMGVSAAQYANARARLPD-NVRVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  85 EISSDDAWVRDTGPTFVIDDKGDVRGVDWGFNAWGGFEGGLYFPWQRDDQVARKILEIERRARYRTDDFVLEGGSIHVDG 164
Cdd:PRK13551  81 EMSSDDAWVRDTGPTFVINDKGEVRGVDWGFNAWGGLVGGLYFPWDKDDQVAQKVLEIEGRDRYRAKPFVLEGGSIHVDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956 165 EGTLITTEECLLNHNRNPHLSQVEIERTLRDYLAVDSIIWLPNGLYNDETDGHVDNFCCYVRPGEVLLAWTDDQDDPNYL 244
Cdd:PRK13551 161 EGTLLTTEECLLNPNRNPHLTKEQIEQLLRDYLGVEKVIWLPDGIYNDETDGHVDNVCCFVRPGEVALAWTDDENDPQYA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956 245 RCQAALRVLEESRDAKGRKLVVHKMPIPGPLYATQEECDGVDIVEGSQPRDPSIRLAGSYVNFLIVNGGIVAPSFDDPKD 324
Cdd:PRK13551 241 RSKAALEVLENTTDAKGRKLKVHKLPIPGPLYATEEESAGVDAVEGTVPREAGERLAASYVNFLIANGGIIFPLFDDPND 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 489212956 325 AEARAILQRVFPEHEVVMVPGREILLGGGNIHCITQQQPAPR 366
Cdd:PRK13551 321 ALALEILQQMFPDRKVVGVPAREILLGGGNIHCITQQIPAAK 362
agmatine_aguA TIGR03380
agmatine deiminase; Members of this family are agmatine deiminase (3.5.3.12), as characterized ...
6-364 0e+00

agmatine deiminase; Members of this family are agmatine deiminase (3.5.3.12), as characterized in Pseudomonas aeruginosa and plants. Related deiminases include the peptidyl-arginine deiminase (3.5.3.15) as found in Porphyromonas gingivalis. [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 132423  Cd Length: 357  Bit Score: 682.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956    6 STPRADGFRMPAEWEPHEQTWMVWPERPDNWRNGGKPAQAAFAAVAKAIARFEPVTVCASAGQYENARARLDDgNIRVVE 85
Cdd:TIGR03380   1 TTPKQDGFRMPAEFEPQAQCWMIWPERPDNWRNGAKPAQKAFAEVAEAIAEFEPVTMLVSPAQYENARAQLPS-NIRVVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956   86 ISSDDAWVRDTGPTFVIDDKGDVRGVDWGFNAWGGFEGGLYFPWQRDDQVARKILEIERRARYRTDdFVLEGGSIHVDGE 165
Cdd:TIGR03380  80 MSSNDAWMRDTGPTFVVNDKGEIRGVDWEFNAWGGLVDGLYFPWDKDDLVARKVCELEGIDRYRAD-FVLEGGSIHVDGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  166 GTLITTEECLLNHNRNPHLSQVEIERTLRDYLAVDSIIWLPNGLYNDETDGHVDNFCCYVRPGEVLLAWTDDQDDPNYLR 245
Cdd:TIGR03380 159 GTLLTTEECLLSEGRNPHLTKEQIEEKLKDYLGVEKVIWLPDGLYNDETNGHVDNLCCFVRPGEVALSWTDDESDPQYEI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  246 CQAALRVLEESRDAKGRKLVVHKMPIPGPLYATQEECDGVDIVEGSQPRDPSIRLAGSYVNFLIVNGGIVAPSFDDPKDA 325
Cdd:TIGR03380 239 SKEAYDVLSNTTDAKGRKLKVHKLPIPGPLYITEEEAAGVDPVEGTLPREAGERLAASYVNFYIANGGIILPLFDDPNDK 318
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 489212956  326 EARAILQRVFPEHEVVMVPGREILLGGGNIHCITQQQPA 364
Cdd:TIGR03380 319 LAQQQLQELFPDRKVVGVPAREILLGGGNIHCITQQQPA 357
AguA COG2957
Agmatine/peptidylarginine deiminase [Amino acid transport and metabolism];
16-364 0e+00

Agmatine/peptidylarginine deiminase [Amino acid transport and metabolism];


Pssm-ID: 442197  Cd Length: 328  Bit Score: 509.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  16 PAEWEPHEQTWMVWPERPDNWRNGGKPAQAAFAAVAKAIARFEPVTVCASAGQYENARARL--DDGNIRVVEISSDDAWV 93
Cdd:COG2957    1 PAEWEPQEATWLAWPHREDDWGGGLEPVRAAFAAIARAIARFEPVTILVPDEDAEEARALLgeDLANVRLVEAPTNDAWA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  94 RDTGPTFVIDDKGDVRGVDWGFNAWGGfeggLYFPWQRDDQVARKILEIERRARYRTDdFVLEGGSIHVDGEGTLITTEE 173
Cdd:COG2957   81 RDTGPIFVVNDDGELAAVDWRFNGWGG----KYPPWDLDNQVARKVAELLGLPLYRSD-LVLEGGSIEVDGEGTLLTTES 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956 174 CLLNHNRNPHLSQVEIERTLRDYLAVDSIIWLPNGLYNDETDGHVDNFCCYVRPGEVLLAWTDDQDDPNYLRCQAALRVL 253
Cdd:COG2957  156 CLLNPNRNPGLTRAEIEAELKRYLGVEKVIWLPGGLAGDDTDGHIDTLARFVAPGTVVLVVCDDPDDPNYAVLQANLEEL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956 254 EESRDAKGRKLVVHKMPIPGPLYATQEecdgvdivegsqprdpsiRLAGSYVNFLIVNGGIVAPSFDDPKDAEARAILQR 333
Cdd:COG2957  236 KAATDADGRPLEIVPLPMPGPLYEDGE------------------RLPASYANFLIANGAVLVPTYGDPADAAALAILQE 297
                        330       340       350
                 ....*....|....*....|....*....|.
gi 489212956 334 VFPEHEVVMVPGREILLGGGNIHCITQQQPA 364
Cdd:COG2957  298 LFPGREVVGIDARALIWGGGSIHCITQQQPA 328
PAD_porph pfam04371
Porphyromonas-type peptidyl-arginine deiminase; Peptidyl-arginine deiminase (PAD) enzymes ...
15-362 1.27e-175

Porphyromonas-type peptidyl-arginine deiminase; Peptidyl-arginine deiminase (PAD) enzymes catalyze the deimination of the guanidino group from carboxy-terminal arginine residues of various peptides to produce ammonia. PAD from Porphyromonas gingivalis (PPAD) appears to be evolutionarily unrelated to mammalian PAD (pfam03068), which is a metalloenzyme. PPAD is thought to belong to the same superfamily as aminotransferase and arginine deiminase, and to form an alpha/beta propeller structure. This family has previously been named PPADH (Porphyromonas peptidyl-arginine deiminase homologs). The predicted catalytic residues in PPAD are Asp130, Asp187, His236, Asp238 and Cys351. These are absolutely conserved with the exception of Asp187 which is absent in two family members. PPAD is also able to catalyze the deimination of free L-arginine, but has primarily peptidyl-arginine specificity. It may have a FMN cofactor.


Pssm-ID: 461280  Cd Length: 324  Bit Score: 490.81  E-value: 1.27e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956   15 MPAEWEPHEQTWMVWPERPDN-WRNGGKPAQAAFAAVAKAIARFEPVTVCASAGQYENARARLDDG-NIRVVEISSDDAW 92
Cdd:pfam04371   1 MPAEWEPHSATWLAWPHRADTdWPEGLDEAQAAFAEIARAIARFEPVTLLVPDEQEEEARALLSELaNVRLVEAPTNDAW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956   93 VRDTGPTFVIDDkgDVRGVDWGFNAWGGfegglYFPWQRDDQVARKILEIERRARYRTDdFVLEGGSIHVDGEGTLITTE 172
Cdd:pfam04371  81 ARDTGPIFVVNG--GLAAVDFRFNGWGG-----KYPWDLDNLVARKLAELLGLPRYRSD-LVLEGGSIEVDGEGTLLTTE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  173 ECLLNHNRNPHLSQVEIERTLRDYLAVDSIIWLPNGLYNDETDGHVDNFCCYVRPGEVLLAWTDDQDDPNYLRCQAALRV 252
Cdd:pfam04371 153 SCLLNPNRNPGLSKAEIEAELKEYLGVEKVIWLPHGLAGDDTDGHIDNLARFVAPGTVVLAWCDDPDDPNYEVLQENLEI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  253 LEESRDAKGRKLVVHKMPIPGPlyatqeecdgvdivegsqPRDPSIRLAGSYVNFLIVNGGIVAPSFDDPKDAEARAILQ 332
Cdd:pfam04371 233 LKAATDAKGRPLEIVELPMPGP------------------IRDEGERLPASYANFLIVNGAVIVPTFGDPNDEAALEILQ 294
                         330       340       350
                  ....*....|....*....|....*....|
gi 489212956  333 RVFPEHEVVMVPGREILLGGGNIHCITQQQ 362
Cdd:pfam04371 295 ELFPDREVVGVDARALILGGGSIHCITQQQ 324
 
Name Accession Description Interval E-value
PRK13551 PRK13551
agmatine deiminase; Provisional
5-366 0e+00

agmatine deiminase; Provisional


Pssm-ID: 184135  Cd Length: 362  Bit Score: 733.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956   5 TSTPRADGFRMPAEWEPHEQTWMVWPERPDNWRNGGKPAQAAFAAVAKAIARFEPVTVCASAGQYENARARLDDgNIRVV 84
Cdd:PRK13551   2 NSTPKQDGFRMPAEWEPHDAVWMIWPERPDNWRLGGKPAQAAFAKVAEAIARFEPVTMGVSAAQYANARARLPD-NVRVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  85 EISSDDAWVRDTGPTFVIDDKGDVRGVDWGFNAWGGFEGGLYFPWQRDDQVARKILEIERRARYRTDDFVLEGGSIHVDG 164
Cdd:PRK13551  81 EMSSDDAWVRDTGPTFVINDKGEVRGVDWGFNAWGGLVGGLYFPWDKDDQVAQKVLEIEGRDRYRAKPFVLEGGSIHVDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956 165 EGTLITTEECLLNHNRNPHLSQVEIERTLRDYLAVDSIIWLPNGLYNDETDGHVDNFCCYVRPGEVLLAWTDDQDDPNYL 244
Cdd:PRK13551 161 EGTLLTTEECLLNPNRNPHLTKEQIEQLLRDYLGVEKVIWLPDGIYNDETDGHVDNVCCFVRPGEVALAWTDDENDPQYA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956 245 RCQAALRVLEESRDAKGRKLVVHKMPIPGPLYATQEECDGVDIVEGSQPRDPSIRLAGSYVNFLIVNGGIVAPSFDDPKD 324
Cdd:PRK13551 241 RSKAALEVLENTTDAKGRKLKVHKLPIPGPLYATEEESAGVDAVEGTVPREAGERLAASYVNFLIANGGIIFPLFDDPND 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 489212956 325 AEARAILQRVFPEHEVVMVPGREILLGGGNIHCITQQQPAPR 366
Cdd:PRK13551 321 ALALEILQQMFPDRKVVGVPAREILLGGGNIHCITQQIPAAK 362
agmatine_aguA TIGR03380
agmatine deiminase; Members of this family are agmatine deiminase (3.5.3.12), as characterized ...
6-364 0e+00

agmatine deiminase; Members of this family are agmatine deiminase (3.5.3.12), as characterized in Pseudomonas aeruginosa and plants. Related deiminases include the peptidyl-arginine deiminase (3.5.3.15) as found in Porphyromonas gingivalis. [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 132423  Cd Length: 357  Bit Score: 682.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956    6 STPRADGFRMPAEWEPHEQTWMVWPERPDNWRNGGKPAQAAFAAVAKAIARFEPVTVCASAGQYENARARLDDgNIRVVE 85
Cdd:TIGR03380   1 TTPKQDGFRMPAEFEPQAQCWMIWPERPDNWRNGAKPAQKAFAEVAEAIAEFEPVTMLVSPAQYENARAQLPS-NIRVVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956   86 ISSDDAWVRDTGPTFVIDDKGDVRGVDWGFNAWGGFEGGLYFPWQRDDQVARKILEIERRARYRTDdFVLEGGSIHVDGE 165
Cdd:TIGR03380  80 MSSNDAWMRDTGPTFVVNDKGEIRGVDWEFNAWGGLVDGLYFPWDKDDLVARKVCELEGIDRYRAD-FVLEGGSIHVDGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  166 GTLITTEECLLNHNRNPHLSQVEIERTLRDYLAVDSIIWLPNGLYNDETDGHVDNFCCYVRPGEVLLAWTDDQDDPNYLR 245
Cdd:TIGR03380 159 GTLLTTEECLLSEGRNPHLTKEQIEEKLKDYLGVEKVIWLPDGLYNDETNGHVDNLCCFVRPGEVALSWTDDESDPQYEI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  246 CQAALRVLEESRDAKGRKLVVHKMPIPGPLYATQEECDGVDIVEGSQPRDPSIRLAGSYVNFLIVNGGIVAPSFDDPKDA 325
Cdd:TIGR03380 239 SKEAYDVLSNTTDAKGRKLKVHKLPIPGPLYITEEEAAGVDPVEGTLPREAGERLAASYVNFYIANGGIILPLFDDPNDK 318
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 489212956  326 EARAILQRVFPEHEVVMVPGREILLGGGNIHCITQQQPA 364
Cdd:TIGR03380 319 LAQQQLQELFPDRKVVGVPAREILLGGGNIHCITQQQPA 357
PLN02690 PLN02690
Agmatine deiminase
7-366 0e+00

Agmatine deiminase


Pssm-ID: 178293  Cd Length: 374  Bit Score: 518.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956   7 TPRADGFRMPAEWEPHEQTWMVWPERPDNWRNGGKPAQAAFAAVAKAIARFEPVTVCASAGQYENARARL-DDGNIRVVE 85
Cdd:PLN02690   4 TPKELGYRMPAEWEPHAGCWMGWPERPDNWRDNAKPAQQQFAAVAKAISKFEPVTVCASPAQWENAREQLpGVSNVRVVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  86 ISSDDAWVRDTGPTFVIDDKGD--------VRGVDWGFNAWGGFEGGLYFPWQRDDQVARKILEIERRARYRTDdFVLEG 157
Cdd:PLN02690  84 MSMNDSWFRDTGPTFVVRDVPVdsssgereVAGIDWDFNAWGGALKGCYPDWSLDLLVARKILEAERLPRFPHS-MILEG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956 158 GSIHVDGEGTLITTEECLLNHNRNPHLSQVEIERTLRDYLAVDSIIWLPNGLYNDE-TDGHVDNFCCYVRPGEVLLAWTD 236
Cdd:PLN02690 163 GSIHVDGEGTCLTTEECLLNPNRNPHLTKEEIEEELKEYLGVEKVIWLPRGLYGDDdTNGHVDNMCCFARPGVVLLSWTD 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956 237 DQDDPNYLRCQAALRVLEESRDAKGRKLVVHKMPIPGPLYATQEECDGVDIVEGSQPRDPSIRLAGSYVNFLIVNGGIVA 316
Cdd:PLN02690 243 DEDDPQYERSVEALSILSNTTDARGRKLQVIKLHVPGPLYMTFEEASGVAQDGAAKPRLAGERLAASYVNFYIANGGIVA 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489212956 317 PSFDDPK-DAEARAILQRVFPEHEVVMVPG-REILLGGGNIHCITQQQPAPR 366
Cdd:PLN02690 323 PQFGDAKwDKEAIEVLSEAFPNHKVVGVESaREIVLGGGNIHCITQQQPAEL 374
AguA COG2957
Agmatine/peptidylarginine deiminase [Amino acid transport and metabolism];
16-364 0e+00

Agmatine/peptidylarginine deiminase [Amino acid transport and metabolism];


Pssm-ID: 442197  Cd Length: 328  Bit Score: 509.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  16 PAEWEPHEQTWMVWPERPDNWRNGGKPAQAAFAAVAKAIARFEPVTVCASAGQYENARARL--DDGNIRVVEISSDDAWV 93
Cdd:COG2957    1 PAEWEPQEATWLAWPHREDDWGGGLEPVRAAFAAIARAIARFEPVTILVPDEDAEEARALLgeDLANVRLVEAPTNDAWA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  94 RDTGPTFVIDDKGDVRGVDWGFNAWGGfeggLYFPWQRDDQVARKILEIERRARYRTDdFVLEGGSIHVDGEGTLITTEE 173
Cdd:COG2957   81 RDTGPIFVVNDDGELAAVDWRFNGWGG----KYPPWDLDNQVARKVAELLGLPLYRSD-LVLEGGSIEVDGEGTLLTTES 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956 174 CLLNHNRNPHLSQVEIERTLRDYLAVDSIIWLPNGLYNDETDGHVDNFCCYVRPGEVLLAWTDDQDDPNYLRCQAALRVL 253
Cdd:COG2957  156 CLLNPNRNPGLTRAEIEAELKRYLGVEKVIWLPGGLAGDDTDGHIDTLARFVAPGTVVLVVCDDPDDPNYAVLQANLEEL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956 254 EESRDAKGRKLVVHKMPIPGPLYATQEecdgvdivegsqprdpsiRLAGSYVNFLIVNGGIVAPSFDDPKDAEARAILQR 333
Cdd:COG2957  236 KAATDADGRPLEIVPLPMPGPLYEDGE------------------RLPASYANFLIANGAVLVPTYGDPADAAALAILQE 297
                        330       340       350
                 ....*....|....*....|....*....|.
gi 489212956 334 VFPEHEVVMVPGREILLGGGNIHCITQQQPA 364
Cdd:COG2957  298 LFPGREVVGIDARALIWGGGSIHCITQQQPA 328
PAD_porph pfam04371
Porphyromonas-type peptidyl-arginine deiminase; Peptidyl-arginine deiminase (PAD) enzymes ...
15-362 1.27e-175

Porphyromonas-type peptidyl-arginine deiminase; Peptidyl-arginine deiminase (PAD) enzymes catalyze the deimination of the guanidino group from carboxy-terminal arginine residues of various peptides to produce ammonia. PAD from Porphyromonas gingivalis (PPAD) appears to be evolutionarily unrelated to mammalian PAD (pfam03068), which is a metalloenzyme. PPAD is thought to belong to the same superfamily as aminotransferase and arginine deiminase, and to form an alpha/beta propeller structure. This family has previously been named PPADH (Porphyromonas peptidyl-arginine deiminase homologs). The predicted catalytic residues in PPAD are Asp130, Asp187, His236, Asp238 and Cys351. These are absolutely conserved with the exception of Asp187 which is absent in two family members. PPAD is also able to catalyze the deimination of free L-arginine, but has primarily peptidyl-arginine specificity. It may have a FMN cofactor.


Pssm-ID: 461280  Cd Length: 324  Bit Score: 490.81  E-value: 1.27e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956   15 MPAEWEPHEQTWMVWPERPDN-WRNGGKPAQAAFAAVAKAIARFEPVTVCASAGQYENARARLDDG-NIRVVEISSDDAW 92
Cdd:pfam04371   1 MPAEWEPHSATWLAWPHRADTdWPEGLDEAQAAFAEIARAIARFEPVTLLVPDEQEEEARALLSELaNVRLVEAPTNDAW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956   93 VRDTGPTFVIDDkgDVRGVDWGFNAWGGfegglYFPWQRDDQVARKILEIERRARYRTDdFVLEGGSIHVDGEGTLITTE 172
Cdd:pfam04371  81 ARDTGPIFVVNG--GLAAVDFRFNGWGG-----KYPWDLDNLVARKLAELLGLPRYRSD-LVLEGGSIEVDGEGTLLTTE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  173 ECLLNHNRNPHLSQVEIERTLRDYLAVDSIIWLPNGLYNDETDGHVDNFCCYVRPGEVLLAWTDDQDDPNYLRCQAALRV 252
Cdd:pfam04371 153 SCLLNPNRNPGLSKAEIEAELKEYLGVEKVIWLPHGLAGDDTDGHIDNLARFVAPGTVVLAWCDDPDDPNYEVLQENLEI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212956  253 LEESRDAKGRKLVVHKMPIPGPlyatqeecdgvdivegsqPRDPSIRLAGSYVNFLIVNGGIVAPSFDDPKDAEARAILQ 332
Cdd:pfam04371 233 LKAATDAKGRPLEIVELPMPGP------------------IRDEGERLPASYANFLIVNGAVIVPTFGDPNDEAALEILQ 294
                         330       340       350
                  ....*....|....*....|....*....|
gi 489212956  333 RVFPEHEVVMVPGREILLGGGNIHCITQQQ 362
Cdd:pfam04371 295 ELFPDREVVGVDARALILGGGSIHCITQQQ 324
 
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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