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Conserved domains on  [gi|511005418|gb|EPB86760|]
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hypothetical protein HMPREF1544_06458 [Mucor circinelloides f. circinelloides 1006PhL]

Protein Classification

ADP-ribosylglycohydrolase family protein( domain architecture ID 10003641)

ADP-ribosylglycohydrolase family protein similar to vertebrate [protein ADP-ribosylarginine] hydrolase, which catalyzes the reverse reaction of mono-ADP-ribosylation, and Tripedalia cystophora major lens protein crystallin J1

CATH:  1.10.4080.10

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DraG COG1397
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
15-397 3.53e-32

ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441007  Cd Length: 256  Bit Score: 121.89  E-value: 3.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418  15 IVDKVKGLIFGAILGDSLGLATEGLSRSEIQAIYGdgPIRfGMDEDGvpfhrdeyrsKFEENDFGDDAEQVLLVMESLFE 94
Cdd:COG1397    1 LLDRARGALLGLAIGDALGAPVEFYSREEIRARYG--PIT-DYVGGG----------NLPPGEWTDDTQMALALAESLLE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418  95 NGGhFLPKDFASRLYSYGEHGiknlhkLPTGMNATNQAVLANptYKTSpqqaaiEVWKTRNNLRGaNGALVRAPLLGALK 174
Cdd:COG1397   68 AGG-FDPEDLARRFLRWLRTG------PGRDIGPTTRRALRN--LRRG------GAGESGEGSAG-NGAAMRIAPLGLAY 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418 175 FWDGTTVIENTTECCRVTHPDPRCMISCVIASTLIARLLRGQDLEiEInhsptpsidqqhqpsfnYFIDTLPvndrlqal 254
Cdd:COG1397  132 AGDPEEAAELARASAALTHGHPRAIAGAVAYAAAVAAALRGADLE-EG-----------------YVVETLP-------- 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418 255 vrnvvetnkpmliapqtdplfitpetdmnqmqkyyhqlvdycvpsslgdlalddsadcrdtfkclsAALYCLTRevplqs 334
Cdd:COG1397  186 ------------------------------------------------------------------AALWALLR------ 193
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511005418 335 eTEYFKKMLMDVVMQGGEADTNATAAGAMLGARFGYSQLPTEWVVGMKRWEWLEDKVDEFCSL 397
Cdd:COG1397  194 -ADDFEEALLLAVNLGGDTDTTAAIAGALAGALYGLEAIPERWLEPLERRDRLEELAERLAAL 255
 
Name Accession Description Interval E-value
DraG COG1397
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
15-397 3.53e-32

ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441007  Cd Length: 256  Bit Score: 121.89  E-value: 3.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418  15 IVDKVKGLIFGAILGDSLGLATEGLSRSEIQAIYGdgPIRfGMDEDGvpfhrdeyrsKFEENDFGDDAEQVLLVMESLFE 94
Cdd:COG1397    1 LLDRARGALLGLAIGDALGAPVEFYSREEIRARYG--PIT-DYVGGG----------NLPPGEWTDDTQMALALAESLLE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418  95 NGGhFLPKDFASRLYSYGEHGiknlhkLPTGMNATNQAVLANptYKTSpqqaaiEVWKTRNNLRGaNGALVRAPLLGALK 174
Cdd:COG1397   68 AGG-FDPEDLARRFLRWLRTG------PGRDIGPTTRRALRN--LRRG------GAGESGEGSAG-NGAAMRIAPLGLAY 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418 175 FWDGTTVIENTTECCRVTHPDPRCMISCVIASTLIARLLRGQDLEiEInhsptpsidqqhqpsfnYFIDTLPvndrlqal 254
Cdd:COG1397  132 AGDPEEAAELARASAALTHGHPRAIAGAVAYAAAVAAALRGADLE-EG-----------------YVVETLP-------- 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418 255 vrnvvetnkpmliapqtdplfitpetdmnqmqkyyhqlvdycvpsslgdlalddsadcrdtfkclsAALYCLTRevplqs 334
Cdd:COG1397  186 ------------------------------------------------------------------AALWALLR------ 193
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511005418 335 eTEYFKKMLMDVVMQGGEADTNATAAGAMLGARFGYSQLPTEWVVGMKRWEWLEDKVDEFCSL 397
Cdd:COG1397  194 -ADDFEEALLLAVNLGGDTDTTAAIAGALAGALYGLEAIPERWLEPLERRDRLEELAERLAAL 255
ADP_ribosyl_GH pfam03747
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ...
21-376 9.97e-30

ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ADP-ribosylarginine hydrolase EC:3.2.2.19 cleaves ADP-ribose-L-arginine. The family also includes dinitrogenase reductase activating glycohydrolase. Most surprisingly the family also includes jellyfish crystallins, these proteins appear to have lost the presumed active site residues.


Pssm-ID: 461037 [Multi-domain]  Cd Length: 200  Bit Score: 113.82  E-value: 9.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418   21 GLIFGAILGDSLGLATEGLSRSEIQAIYGdgpirfgmdeDGVPFHRDEYRSKFEENDFGDDAEQVLLVMESLFENGGhFL 100
Cdd:pfam03747   1 GALLGLAVGDALGAPVEFWSYDEIRREYG----------GIGTPMPGGGHLGLPPGEWTDDTQMALALLESLLEAGG-FD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418  101 PKDFASRLYsygehgiknlhklptgMnatnqavlanptyktspqqaaievwktrnnlrgangalvRAPLLGALKFWDGTT 180
Cdd:pfam03747  70 PEDLARRLA----------------M---------------------------------------RIAPLGLLYPGDPEE 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418  181 VIENTTECCRVTHPDPRCMISCVIASTLIARLLRGQDLEIEINHSPTPSidqqhqpsfnYFIDTLPvndrlqalvrnvve 260
Cdd:pfam03747  95 AAELARESARLTHGHPRAVAGAVAYAAAIAAALRGADLEEALEAIGGGG----------YVVEALP-------------- 150
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418  261 tnkpmliapqtdplfitpetdmnqmqkyyhqlvdycvpsslgdlalddsadcrdtfkclsAALYCLTRevplqsETEYFK 340
Cdd:pfam03747 151 ------------------------------------------------------------AALYALLR------AGDDFE 164
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 511005418  341 KMLMDVVMQGGEADTNATAAGAMLGARFGYSQLPTE 376
Cdd:pfam03747 165 EALLAAVNLGGDTDTTAAIAGALLGAYYGLEAIPEE 200
 
Name Accession Description Interval E-value
DraG COG1397
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
15-397 3.53e-32

ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441007  Cd Length: 256  Bit Score: 121.89  E-value: 3.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418  15 IVDKVKGLIFGAILGDSLGLATEGLSRSEIQAIYGdgPIRfGMDEDGvpfhrdeyrsKFEENDFGDDAEQVLLVMESLFE 94
Cdd:COG1397    1 LLDRARGALLGLAIGDALGAPVEFYSREEIRARYG--PIT-DYVGGG----------NLPPGEWTDDTQMALALAESLLE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418  95 NGGhFLPKDFASRLYSYGEHGiknlhkLPTGMNATNQAVLANptYKTSpqqaaiEVWKTRNNLRGaNGALVRAPLLGALK 174
Cdd:COG1397   68 AGG-FDPEDLARRFLRWLRTG------PGRDIGPTTRRALRN--LRRG------GAGESGEGSAG-NGAAMRIAPLGLAY 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418 175 FWDGTTVIENTTECCRVTHPDPRCMISCVIASTLIARLLRGQDLEiEInhsptpsidqqhqpsfnYFIDTLPvndrlqal 254
Cdd:COG1397  132 AGDPEEAAELARASAALTHGHPRAIAGAVAYAAAVAAALRGADLE-EG-----------------YVVETLP-------- 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418 255 vrnvvetnkpmliapqtdplfitpetdmnqmqkyyhqlvdycvpsslgdlalddsadcrdtfkclsAALYCLTRevplqs 334
Cdd:COG1397  186 ------------------------------------------------------------------AALWALLR------ 193
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511005418 335 eTEYFKKMLMDVVMQGGEADTNATAAGAMLGARFGYSQLPTEWVVGMKRWEWLEDKVDEFCSL 397
Cdd:COG1397  194 -ADDFEEALLLAVNLGGDTDTTAAIAGALAGALYGLEAIPERWLEPLERRDRLEELAERLAAL 255
ADP_ribosyl_GH pfam03747
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ...
21-376 9.97e-30

ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ADP-ribosylarginine hydrolase EC:3.2.2.19 cleaves ADP-ribose-L-arginine. The family also includes dinitrogenase reductase activating glycohydrolase. Most surprisingly the family also includes jellyfish crystallins, these proteins appear to have lost the presumed active site residues.


Pssm-ID: 461037 [Multi-domain]  Cd Length: 200  Bit Score: 113.82  E-value: 9.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418   21 GLIFGAILGDSLGLATEGLSRSEIQAIYGdgpirfgmdeDGVPFHRDEYRSKFEENDFGDDAEQVLLVMESLFENGGhFL 100
Cdd:pfam03747   1 GALLGLAVGDALGAPVEFWSYDEIRREYG----------GIGTPMPGGGHLGLPPGEWTDDTQMALALLESLLEAGG-FD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418  101 PKDFASRLYsygehgiknlhklptgMnatnqavlanptyktspqqaaievwktrnnlrgangalvRAPLLGALKFWDGTT 180
Cdd:pfam03747  70 PEDLARRLA----------------M---------------------------------------RIAPLGLLYPGDPEE 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418  181 VIENTTECCRVTHPDPRCMISCVIASTLIARLLRGQDLEIEINHSPTPSidqqhqpsfnYFIDTLPvndrlqalvrnvve 260
Cdd:pfam03747  95 AAELARESARLTHGHPRAVAGAVAYAAAIAAALRGADLEEALEAIGGGG----------YVVEALP-------------- 150
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511005418  261 tnkpmliapqtdplfitpetdmnqmqkyyhqlvdycvpsslgdlalddsadcrdtfkclsAALYCLTRevplqsETEYFK 340
Cdd:pfam03747 151 ------------------------------------------------------------AALYALLR------AGDDFE 164
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 511005418  341 KMLMDVVMQGGEADTNATAAGAMLGARFGYSQLPTE 376
Cdd:pfam03747 165 EALLAAVNLGGDTDTTAAIAGALLGAYYGLEAIPEE 200
 
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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