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Conserved domains on  [gi|307103051|gb|EFN51316|]
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hypothetical protein CHLNCDRAFT_141287 [Chlorella variabilis]

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];
1-320 1.59e-29

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


:

Pssm-ID: 441007  Cd Length: 256  Bit Score: 113.42  E-value: 1.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051   1 MEHALGALLGAAT---VGAFLEFFPRRPREAGVEQALALPGGGclNVGPGQFTDDTELALAGTEpGVPRQRGRTAVRLV- 76
Cdd:COG1397    2 LDRARGALLGLAIgdaLGAPVEFYSREEIRARYGPITDYVGGG--NLPPGEWTDDTQMALALAE-SLLEAGGFDPEDLAr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051  77 -----VQASQPFDMGNATHNAFgmrgwegiadcaAQALQNVHNEYSAASKANGALMRATPLAVWAHRlGTDAIAACAKAD 151
Cdd:COG1397   79 rflrwLRTGPGRDIGPTTRRAL------------RNLRRGGAGESGEGSAGNGAAMRIAPLGLAYAG-DPEEAAELARAS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051 152 AQLSHPNQACQDANAAYvmacaslirwpgdagaaltaaeeraaanacrevqewlaeardnGAMAAYNAHGASM--GFVKH 229
Cdd:COG1397  146 AALTHGHPRAIAGAVAY-------------------------------------------AAAVAAALRGADLeeGYVVE 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051 230 AFCLAFYHLRRHSGFVEGLRHTLLCGGDTDTNACIVGGVLGARYGAAGIPPELRGEVEGYsfdgsgrghrrpqqllgSQL 309
Cdd:COG1397  183 TLPAALWALLRADDFEEALLLAVNLGGDTDTTAAIAGALAGALYGLEAIPERWLEPLERR-----------------DRL 245
                        330
                 ....*....|.
gi 307103051 310 APLAERLYQEA 320
Cdd:COG1397  246 EELAERLAALA 256
 
Name Accession Description Interval E-value
DraG COG1397
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
1-320 1.59e-29

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


Pssm-ID: 441007  Cd Length: 256  Bit Score: 113.42  E-value: 1.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051   1 MEHALGALLGAAT---VGAFLEFFPRRPREAGVEQALALPGGGclNVGPGQFTDDTELALAGTEpGVPRQRGRTAVRLV- 76
Cdd:COG1397    2 LDRARGALLGLAIgdaLGAPVEFYSREEIRARYGPITDYVGGG--NLPPGEWTDDTQMALALAE-SLLEAGGFDPEDLAr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051  77 -----VQASQPFDMGNATHNAFgmrgwegiadcaAQALQNVHNEYSAASKANGALMRATPLAVWAHRlGTDAIAACAKAD 151
Cdd:COG1397   79 rflrwLRTGPGRDIGPTTRRAL------------RNLRRGGAGESGEGSAGNGAAMRIAPLGLAYAG-DPEEAAELARAS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051 152 AQLSHPNQACQDANAAYvmacaslirwpgdagaaltaaeeraaanacrevqewlaeardnGAMAAYNAHGASM--GFVKH 229
Cdd:COG1397  146 AALTHGHPRAIAGAVAY-------------------------------------------AAAVAAALRGADLeeGYVVE 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051 230 AFCLAFYHLRRHSGFVEGLRHTLLCGGDTDTNACIVGGVLGARYGAAGIPPELRGEVEGYsfdgsgrghrrpqqllgSQL 309
Cdd:COG1397  183 TLPAALWALLRADDFEEALLLAVNLGGDTDTTAAIAGALAGALYGLEAIPERWLEPLERR-----------------DRL 245
                        330
                 ....*....|.
gi 307103051 310 APLAERLYQEA 320
Cdd:COG1397  246 EELAERLAALA 256
ADP_ribosyl_GH pfam03747
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ...
6-281 3.80e-21

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: 89.17  E-value: 3.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051    6 GALLGAA---TVGAFLEFFPR-RPREAGVEQALALPGGGCLNVGPGQFTDDTELALagtepgvprqrgrtavrlvvqasq 81
Cdd:pfam03747   1 GALLGLAvgdALGAPVEFWSYdEIRREYGGIGTPMPGGGHLGLPPGEWTDDTQMAL------------------------ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051   82 pfdmgnathnafgmrgwegiadCAAQALQNvHNEYSAASKANGALMRATPLAVWAHRlGTDAIAACAKADAQLSHPNQAC 161
Cdd:pfam03747  57 ----------------------ALLESLLE-AGGFDPEDLARRLAMRIAPLGLLYPG-DPEEAAELARESARLTHGHPRA 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051  162 QDANAAYVMACASLIRwpgdagaaltaaeeraaanaCREVQEWLAEardngamaaynahGASMGFVKHAFCLAFYHLRRH 241
Cdd:pfam03747 113 VAGAVAYAAAIAAALR--------------------GADLEEALEA-------------IGGGGYVVEALPAALYALLRA 159
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 307103051  242 SG-FVEGLRHTLLCGGDTDTNACIVGGVLGARYGAAGIPPE 281
Cdd:pfam03747 160 GDdFEEALLAAVNLGGDTDTTAAIAGALLGAYYGLEAIPEE 200
dinitro_DRAG TIGR02662
ADP-ribosyl-[dinitrogen reductase] hydrolase; Members of this family are the enzyme ...
2-280 1.23e-09

ADP-ribosyl-[dinitrogen reductase] hydrolase; Members of this family are the enzyme ADP-ribosyl-[dinitrogen reductase] hydrolase (EC 3.2.2.24), better known as Dinitrogenase Reductase Activating Glycohydrolase, DRAG. This enzyme reverses a regulatory inactivation of dinitrogen reductase caused by the action of NAD(+)--dinitrogen-reductase ADP-D-ribosyltransferase (EC 2.4.2.37) (DRAT). This enzyme is restricted to nitrogen-fixing bacteria and belongs to the larger family of ADP-ribosylglycohydrolases described by pfam03747. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 131710  Cd Length: 287  Bit Score: 58.27  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051    2 EHALGALLGAA---TVGAFLEFFPRRP--REAGVEQALAlpGGGCLNVGPGQFTDDTELALAGTEPGVprQRGRTAVRLV 76
Cdd:TIGR02662   3 SRALGAYLGLAvgdALGATVEFMTKGEiaAQYGVHRHIT--GGGWLRLKPGQVTDDTEMSLALGRAIL--AAGEWDVTRI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051   77 VQA------SQPFDMGNATHNA---FGMRGwegiadcaaqALQNVHNEYSAaskANGALMRATPLAVWAhrLGTDAI-AA 146
Cdd:TIGR02662  79 AEEfavwlkSKPVDVGNTCRRGirrFMLHG----------TLSAPESEWDA---GNGAAMRNLPAALAT--LGDDAAfER 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051  147 CAKADAQLSHpNQACQDAnaayvmACASLirwpgdaGAALTAAEERAAANACREVQEWLAEARDNGAMAAYnaHGASMGF 226
Cdd:TIGR02662 144 WSVEQAHITH-NHPLSDA------ATLTL-------GRMVHRLVLGGSVRDVRREANRLIAKHRTFKFEPY--RGLSTAY 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 307103051  227 VKHAFCLAFYHLRRHSGFVEGLRHTLLCGGDTDTNACIVGGVLGARYGAAGIPP 280
Cdd:TIGR02662 208 IVDTMQTVLHYYFQTDSFESCLIETVNQGGDADTTGAIAGMLAGATYGVEGIPP 261
 
Name Accession Description Interval E-value
DraG COG1397
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
1-320 1.59e-29

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


Pssm-ID: 441007  Cd Length: 256  Bit Score: 113.42  E-value: 1.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051   1 MEHALGALLGAAT---VGAFLEFFPRRPREAGVEQALALPGGGclNVGPGQFTDDTELALAGTEpGVPRQRGRTAVRLV- 76
Cdd:COG1397    2 LDRARGALLGLAIgdaLGAPVEFYSREEIRARYGPITDYVGGG--NLPPGEWTDDTQMALALAE-SLLEAGGFDPEDLAr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051  77 -----VQASQPFDMGNATHNAFgmrgwegiadcaAQALQNVHNEYSAASKANGALMRATPLAVWAHRlGTDAIAACAKAD 151
Cdd:COG1397   79 rflrwLRTGPGRDIGPTTRRAL------------RNLRRGGAGESGEGSAGNGAAMRIAPLGLAYAG-DPEEAAELARAS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051 152 AQLSHPNQACQDANAAYvmacaslirwpgdagaaltaaeeraaanacrevqewlaeardnGAMAAYNAHGASM--GFVKH 229
Cdd:COG1397  146 AALTHGHPRAIAGAVAY-------------------------------------------AAAVAAALRGADLeeGYVVE 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051 230 AFCLAFYHLRRHSGFVEGLRHTLLCGGDTDTNACIVGGVLGARYGAAGIPPELRGEVEGYsfdgsgrghrrpqqllgSQL 309
Cdd:COG1397  183 TLPAALWALLRADDFEEALLLAVNLGGDTDTTAAIAGALAGALYGLEAIPERWLEPLERR-----------------DRL 245
                        330
                 ....*....|.
gi 307103051 310 APLAERLYQEA 320
Cdd:COG1397  246 EELAERLAALA 256
ADP_ribosyl_GH pfam03747
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ...
6-281 3.80e-21

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: 89.17  E-value: 3.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051    6 GALLGAA---TVGAFLEFFPR-RPREAGVEQALALPGGGCLNVGPGQFTDDTELALagtepgvprqrgrtavrlvvqasq 81
Cdd:pfam03747   1 GALLGLAvgdALGAPVEFWSYdEIRREYGGIGTPMPGGGHLGLPPGEWTDDTQMAL------------------------ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051   82 pfdmgnathnafgmrgwegiadCAAQALQNvHNEYSAASKANGALMRATPLAVWAHRlGTDAIAACAKADAQLSHPNQAC 161
Cdd:pfam03747  57 ----------------------ALLESLLE-AGGFDPEDLARRLAMRIAPLGLLYPG-DPEEAAELARESARLTHGHPRA 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051  162 QDANAAYVMACASLIRwpgdagaaltaaeeraaanaCREVQEWLAEardngamaaynahGASMGFVKHAFCLAFYHLRRH 241
Cdd:pfam03747 113 VAGAVAYAAAIAAALR--------------------GADLEEALEA-------------IGGGGYVVEALPAALYALLRA 159
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 307103051  242 SG-FVEGLRHTLLCGGDTDTNACIVGGVLGARYGAAGIPPE 281
Cdd:pfam03747 160 GDdFEEALLAAVNLGGDTDTTAAIAGALLGAYYGLEAIPEE 200
dinitro_DRAG TIGR02662
ADP-ribosyl-[dinitrogen reductase] hydrolase; Members of this family are the enzyme ...
2-280 1.23e-09

ADP-ribosyl-[dinitrogen reductase] hydrolase; Members of this family are the enzyme ADP-ribosyl-[dinitrogen reductase] hydrolase (EC 3.2.2.24), better known as Dinitrogenase Reductase Activating Glycohydrolase, DRAG. This enzyme reverses a regulatory inactivation of dinitrogen reductase caused by the action of NAD(+)--dinitrogen-reductase ADP-D-ribosyltransferase (EC 2.4.2.37) (DRAT). This enzyme is restricted to nitrogen-fixing bacteria and belongs to the larger family of ADP-ribosylglycohydrolases described by pfam03747. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 131710  Cd Length: 287  Bit Score: 58.27  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051    2 EHALGALLGAA---TVGAFLEFFPRRP--REAGVEQALAlpGGGCLNVGPGQFTDDTELALAGTEPGVprQRGRTAVRLV 76
Cdd:TIGR02662   3 SRALGAYLGLAvgdALGATVEFMTKGEiaAQYGVHRHIT--GGGWLRLKPGQVTDDTEMSLALGRAIL--AAGEWDVTRI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051   77 VQA------SQPFDMGNATHNA---FGMRGwegiadcaaqALQNVHNEYSAaskANGALMRATPLAVWAhrLGTDAI-AA 146
Cdd:TIGR02662  79 AEEfavwlkSKPVDVGNTCRRGirrFMLHG----------TLSAPESEWDA---GNGAAMRNLPAALAT--LGDDAAfER 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307103051  147 CAKADAQLSHpNQACQDAnaayvmACASLirwpgdaGAALTAAEERAAANACREVQEWLAEARDNGAMAAYnaHGASMGF 226
Cdd:TIGR02662 144 WSVEQAHITH-NHPLSDA------ATLTL-------GRMVHRLVLGGSVRDVRREANRLIAKHRTFKFEPY--RGLSTAY 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 307103051  227 VKHAFCLAFYHLRRHSGFVEGLRHTLLCGGDTDTNACIVGGVLGARYGAAGIPP 280
Cdd:TIGR02662 208 IVDTMQTVLHYYFQTDSFESCLIETVNQGGDADTTGAIAGMLAGATYGVEGIPP 261
 
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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