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Conserved domains on  [gi|1958756377|ref|XP_006256422|]
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probable JmjC domain-containing histone demethylation protein 2C isoform X2 [Rattus norvegicus]

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 ...
2300-2399 1.28e-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: 63.47  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756377 2300 DSSEIPGALWHIYAGKDVDKIREFLQKVSKEQGLEVLPEHDPVRDQGWYVNRRLRQRLLEEyGVRACTLVQFLGDAIVLP 2379
Cdd:pfam02373   16 EDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGEQPDDLLHLNTIISPKQLREN-GIPVYRFVQKPGEFVFTF 94
                           90       100
                   ....*....|....*....|
gi 1958756377 2380 AGTLHQVQNFHSCIQVTEDF 2399
Cdd:pfam02373   95 PGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
2196-2268 1.78e-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: 44.17  E-value: 1.78e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958756377  2196 YEDFLRSLPLpeycnpegKFNLASHLPGFFVRPDLGPRLcsAYGVAaakdhdIGTTNLHIEASDVVNVLVYVG 2268
Cdd:smart00558    1 QLWNLAKLPF--------KLNLLSDLPEDIPGPDVGPYL--YMGMA------GSTTPWHIDDYDLVNYLHQGA 57
RX-CC_like super family cl36576
Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato ...
126-174 6.93e-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: 38.76  E-value: 6.93e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756377  126 AVEFLIDKQVDFLTEESAFQLY-QDDIDSLKPEL-------RD---NPQLHAEVKVWVKE 174
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 ...
2300-2399 1.28e-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: 63.47  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756377 2300 DSSEIPGALWHIYAGKDVDKIREFLQKVSKEQGLEVLPEHDPVRDQGWYVNRRLRQRLLEEyGVRACTLVQFLGDAIVLP 2379
Cdd:pfam02373   16 EDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGEQPDDLLHLNTIISPKQLREN-GIPVYRFVQKPGEFVFTF 94
                           90       100
                   ....*....|....*....|
gi 1958756377 2380 AGTLHQVQNFHSCIQVTEDF 2399
Cdd:pfam02373   95 PGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
2196-2268 1.78e-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: 44.17  E-value: 1.78e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958756377  2196 YEDFLRSLPLpeycnpegKFNLASHLPGFFVRPDLGPRLcsAYGVAaakdhdIGTTNLHIEASDVVNVLVYVG 2268
Cdd:smart00558    1 QLWNLAKLPF--------KLNLLSDLPEDIPGPDVGPYL--YMGMA------GSTTPWHIDDYDLVNYLHQGA 57
RX-CC_like cd14798
Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato ...
126-174 6.93e-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: 38.76  E-value: 6.93e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756377  126 AVEFLIDKQVDFLTEESAFQLY-QDDIDSLKPEL-------RD---NPQLHAEVKVWVKE 174
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 ...
2300-2399 1.28e-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: 63.47  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756377 2300 DSSEIPGALWHIYAGKDVDKIREFLQKVSKEQGLEVLPEHDPVRDQGWYVNRRLRQRLLEEyGVRACTLVQFLGDAIVLP 2379
Cdd:pfam02373   16 EDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGEQPDDLLHLNTIISPKQLREN-GIPVYRFVQKPGEFVFTF 94
                           90       100
                   ....*....|....*....|
gi 1958756377 2380 AGTLHQVQNFHSCIQVTEDF 2399
Cdd:pfam02373   95 PGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
2196-2268 1.78e-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: 44.17  E-value: 1.78e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958756377  2196 YEDFLRSLPLpeycnpegKFNLASHLPGFFVRPDLGPRLcsAYGVAaakdhdIGTTNLHIEASDVVNVLVYVG 2268
Cdd:smart00558    1 QLWNLAKLPF--------KLNLLSDLPEDIPGPDVGPYL--YMGMA------GSTTPWHIDDYDLVNYLHQGA 57
RX-CC_like cd14798
Coiled-coil domain of the potato virux X resistance protein and similar proteins; The potato ...
126-174 6.93e-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: 38.76  E-value: 6.93e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756377  126 AVEFLIDKQVDFLTEESAFQLY-QDDIDSLKPEL-------RD---NPQLHAEVKVWVKE 174
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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