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Conserved domains on  [gi|85541650|sp|Q15652|]
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RecName: Full=Probable JmjC domain-containing histone demethylation protein 2C; AltName: Full=Jumonji domain-containing protein 1C; AltName: Full=Thyroid receptor-interacting protein 8; Short=TR-interacting protein 8; Short=TRIP-8

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 2382-2481 2.07e-11

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


The actual alignment was detected with superfamily member pfam02373:

Pssm-ID: 477354  Cd Length: 114  Bit Score: 63.09  E-value: 2.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   2382 DSSEIPGALWHIYAGKDVDKIREFLQKISKEQGLEVLPEHDPIRDQSWYVNKKLRQRLLEEyGVRTCTLIQFLGDAIVLP 2461
Cdd:pfam02373   16 EDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGEQPDDLLHLNTIISPKQLREN-GIPVYRFVQKPGEFVFTF 94

                           90       100
                   ....*....|....*....|
gi 85541650   2462 AGALHQVQNFHSCIQVTEDF 2481
Cdd:pfam02373   95 PGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 2278-2350 1.31e-05

A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).


:

Pssm-ID: 214721  Cd Length: 58  Bit Score: 44.55  E-value: 1.31e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 85541650    2278 YEDLLKSLPLpeycnpegKFNLASHLPGFFVRPDLGPRLcsAYGVVaakdhdIGTTNLHIEVSDVVNILVYVG 2350
Cdd:smart00558    1 QLWNLAKLPF--------KLNLLSDLPEDIPGPDVGPYL--YMGMA------GSTTPWHIDDYDLVNYLHQGA 57
PTZ00121 super family cl31754
MAEBL; Provisional
 307-672 2.18e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   307 RSIRPNKRKGSDSSIPDEEKMKEEKydyISRGENPKGKNKHLmnkrrKPEEDEKKLNMKRLRTDNVSDFSESSDSENSNK 386
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEE---AKKAEEAKIKAEEL-----KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   387 RIIDNSSEQKPENELKNKNTskingEEGKPHNNEKAGEETLKNSQPPWDQIQEDKKHEEAEKRKSVDTQLQEDMIIHSSE 466
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAE-----EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   467 QSTVSDH----NSNDLLPQECNMDKTHTMELLPKEKFVSRPPTPKCVI-------DITNDTNLEKVAQENSSTFG--LQT 533
Cdd:PTZ00121 1734 EAKKEAEedkkKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIeeeldeeDEKRRMEVDKKIKDIFDNFAniIEG 1813

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   534 LQKMDPNVSDSKHSIANAkFLETAKKDSDQSWVSDVVKVDLTQSSVTNASSGNDHLNMEKEKYvsyisplsavsVMEDKL 613
Cdd:PTZ00121 1814 GKEGNLVINDSKEMEDSA-IKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKD-----------LKEDDE 1881

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 85541650   614 HkrspppETIKSKLNTSVDTHKIKSSPSPEVVKPKITHSPDSVKSKATYVNSQATGERR 672
Cdd:PTZ00121 1882 E------EIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETRE 1934
RX-CC_like super family cl36576
Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato ...
 127-175 4.06e-03

Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato virus X resistance protein (RX) confers resistance against potato virus X. It is a member of a family of resistance proteins with a domain architecture that includes an N-terminal coiled-coil domain (modeled here), a nucleotide-binding domain, and leucine-rich repeats (CC-NB-LRR). These intracellular resistance proteins recognize pathogen effector proteins and will subsequently trigger a response that may be as severe as localized cell death. The N-terminal coiled-coil domain of RX has been shown to interact with RanGAP2, which is a necessary co-factor in the resistance response.


The actual alignment was detected with superfamily member cd14798:

Pssm-ID: 453100 [Multi-domain]  Cd Length: 124  Bit Score: 39.53  E-value: 4.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650  127 AVEFLVDKQLDFLTEDSAF--------QPYQDDIDSLNPVLRD---NPQLHEEVKVWVKE 175
Cdd:cd14798    4 AVSFLLEKLGELLEQEADLlsgvkeeiESLKDELESMQAFLKDadaKQDEDEELKDWVKQ 63
 
Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 2382-2481 2.07e-11

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.


Pssm-ID: 396791  Cd Length: 114  Bit Score: 63.09  E-value: 2.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   2382 DSSEIPGALWHIYAGKDVDKIREFLQKISKEQGLEVLPEHDPIRDQSWYVNKKLRQRLLEEyGVRTCTLIQFLGDAIVLP 2461
Cdd:pfam02373   16 EDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGEQPDDLLHLNTIISPKQLREN-GIPVYRFVQKPGEFVFTF 94

                           90       100
                   ....*....|....*....|
gi 85541650   2462 AGALHQVQNFHSCIQVTEDF 2481
Cdd:pfam02373   95 PGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 2278-2350 1.31e-05

A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).


Pssm-ID: 214721  Cd Length: 58  Bit Score: 44.55  E-value: 1.31e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 85541650    2278 YEDLLKSLPLpeycnpegKFNLASHLPGFFVRPDLGPRLcsAYGVVaakdhdIGTTNLHIEVSDVVNILVYVG 2350
Cdd:smart00558    1 QLWNLAKLPF--------KLNLLSDLPEDIPGPDVGPYL--YMGMA------GSTTPWHIDDYDLVNYLHQGA 57
PTZ00121 PTZ00121
MAEBL; Provisional
 307-672 2.18e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   307 RSIRPNKRKGSDSSIPDEEKMKEEKydyISRGENPKGKNKHLmnkrrKPEEDEKKLNMKRLRTDNVSDFSESSDSENSNK 386
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEE---AKKAEEAKIKAEEL-----KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   387 RIIDNSSEQKPENELKNKNTskingEEGKPHNNEKAGEETLKNSQPPWDQIQEDKKHEEAEKRKSVDTQLQEDMIIHSSE 466
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAE-----EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   467 QSTVSDH----NSNDLLPQECNMDKTHTMELLPKEKFVSRPPTPKCVI-------DITNDTNLEKVAQENSSTFG--LQT 533
Cdd:PTZ00121 1734 EAKKEAEedkkKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIeeeldeeDEKRRMEVDKKIKDIFDNFAniIEG 1813

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   534 LQKMDPNVSDSKHSIANAkFLETAKKDSDQSWVSDVVKVDLTQSSVTNASSGNDHLNMEKEKYvsyisplsavsVMEDKL 613
Cdd:PTZ00121 1814 GKEGNLVINDSKEMEDSA-IKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKD-----------LKEDDE 1881

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 85541650   614 HkrspppETIKSKLNTSVDTHKIKSSPSPEVVKPKITHSPDSVKSKATYVNSQATGERR 672
Cdd:PTZ00121 1882 E------EIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETRE 1934
RX-CC_like cd14798
Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato ...
 127-175 4.06e-03

Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato virus X resistance protein (RX) confers resistance against potato virus X. It is a member of a family of resistance proteins with a domain architecture that includes an N-terminal coiled-coil domain (modeled here), a nucleotide-binding domain, and leucine-rich repeats (CC-NB-LRR). These intracellular resistance proteins recognize pathogen effector proteins and will subsequently trigger a response that may be as severe as localized cell death. The N-terminal coiled-coil domain of RX has been shown to interact with RanGAP2, which is a necessary co-factor in the resistance response.


Pssm-ID: 271353 [Multi-domain]  Cd Length: 124  Bit Score: 39.53  E-value: 4.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650  127 AVEFLVDKQLDFLTEDSAF--------QPYQDDIDSLNPVLRD---NPQLHEEVKVWVKE 175
Cdd:cd14798    4 AVSFLLEKLGELLEQEADLlsgvkeeiESLKDELESMQAFLKDadaKQDEDEELKDWVKQ 63
 
Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 2382-2481 2.07e-11

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.


Pssm-ID: 396791  Cd Length: 114  Bit Score: 63.09  E-value: 2.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   2382 DSSEIPGALWHIYAGKDVDKIREFLQKISKEQGLEVLPEHDPIRDQSWYVNKKLRQRLLEEyGVRTCTLIQFLGDAIVLP 2461
Cdd:pfam02373   16 EDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGEQPDDLLHLNTIISPKQLREN-GIPVYRFVQKPGEFVFTF 94

                           90       100
                   ....*....|....*....|
gi 85541650   2462 AGALHQVQNFHSCIQVTEDF 2481
Cdd:pfam02373   95 PGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 2278-2350 1.31e-05

A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).


Pssm-ID: 214721  Cd Length: 58  Bit Score: 44.55  E-value: 1.31e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 85541650    2278 YEDLLKSLPLpeycnpegKFNLASHLPGFFVRPDLGPRLcsAYGVVaakdhdIGTTNLHIEVSDVVNILVYVG 2350
Cdd:smart00558    1 QLWNLAKLPF--------KLNLLSDLPEDIPGPDVGPYL--YMGMA------GSTTPWHIDDYDLVNYLHQGA 57
PTZ00121 PTZ00121
MAEBL; Provisional
 307-672 2.18e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   307 RSIRPNKRKGSDSSIPDEEKMKEEKydyISRGENPKGKNKHLmnkrrKPEEDEKKLNMKRLRTDNVSDFSESSDSENSNK 386
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEE---AKKAEEAKIKAEEL-----KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   387 RIIDNSSEQKPENELKNKNTskingEEGKPHNNEKAGEETLKNSQPPWDQIQEDKKHEEAEKRKSVDTQLQEDMIIHSSE 466
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAE-----EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   467 QSTVSDH----NSNDLLPQECNMDKTHTMELLPKEKFVSRPPTPKCVI-------DITNDTNLEKVAQENSSTFG--LQT 533
Cdd:PTZ00121 1734 EAKKEAEedkkKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIeeeldeeDEKRRMEVDKKIKDIFDNFAniIEG 1813

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650   534 LQKMDPNVSDSKHSIANAkFLETAKKDSDQSWVSDVVKVDLTQSSVTNASSGNDHLNMEKEKYvsyisplsavsVMEDKL 613
Cdd:PTZ00121 1814 GKEGNLVINDSKEMEDSA-IKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKD-----------LKEDDE 1881

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 85541650   614 HkrspppETIKSKLNTSVDTHKIKSSPSPEVVKPKITHSPDSVKSKATYVNSQATGERR 672
Cdd:PTZ00121 1882 E------EIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETRE 1934
RX-CC_like cd14798
Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato ...
 127-175 4.06e-03

Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato virus X resistance protein (RX) confers resistance against potato virus X. It is a member of a family of resistance proteins with a domain architecture that includes an N-terminal coiled-coil domain (modeled here), a nucleotide-binding domain, and leucine-rich repeats (CC-NB-LRR). These intracellular resistance proteins recognize pathogen effector proteins and will subsequently trigger a response that may be as severe as localized cell death. The N-terminal coiled-coil domain of RX has been shown to interact with RanGAP2, which is a necessary co-factor in the resistance response.


Pssm-ID: 271353 [Multi-domain]  Cd Length: 124  Bit Score: 39.53  E-value: 4.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 85541650  127 AVEFLVDKQLDFLTEDSAF--------QPYQDDIDSLNPVLRD---NPQLHEEVKVWVKE 175
Cdd:cd14798    4 AVSFLLEKLGELLEQEADLlsgvkeeiESLKDELESMQAFLKDadaKQDEDEELKDWVKQ 63
 
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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