NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2024415346|ref|XP_040558294|]
View 

probable JmjC domain-containing histone demethylation protein 2C isoform X3 [Gallus gallus]

Protein Classification

lysine-specific demethylase( domain architecture ID 16112604)

lysine-specific demethylase is a jumonji C domain-containing (JMJD) family histone demethylase demethylates specific residues of histone, similar to human lysine-specific demethylases 3A and 3B that specifically demethylate 'Lys-9' of histone H3, thereby playing a central role in the histone code

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
2166-2265 1.60e-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: 1.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415346 2166 DSSELPGALWHIYAGKDADKIREFLQKIAKEQGLEVLPEHDPIRDQSWYVNKKLRQRLLEEyGVKTCTVIQFLGDAIILP 2245
Cdd:pfam02373   16 EDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGEQPDDLLHLNTIISPKQLREN-GIPVYRFVQKPGEFVFTF 94
                           90       100
                   ....*....|....*....|
gi 2024415346 2246 AGALHQVQNFHSCVQVTEDF 2265
Cdd:pfam02373   95 PGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
2062-2134 1.22e-06

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: 47.63  E-value: 1.22e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024415346  2062 YEDLLKSLPLpeycspegKLNLASHLPGFFVRPDLGPRLcsAYGVAATkdhdigTTNLHIEVSDVVNILVYVG 2134
Cdd:smart00558    1 QLWNLAKLPF--------KLNLLSDLPEDIPGPDVGPYL--YMGMAGS------TTPWHIDDYDLVNYLHQGA 57
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
847-1093 4.08e-04

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.84  E-value: 4.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415346  847 VKYDKDAERSVSELYKMKHSVPQSLPQSNYFttlsnsvvnePPRSYPSKEASSAYVD--KQTNCPSTAASPQSLPSYISS 924
Cdd:PTZ00449   489 IKKSKKKLAPIEEEDSDKHDEPPEGPEASGL----------PPKAPGDKEGEEGEHEdsKESDEPKEGGKPGETKEGEVG 558
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415346  925 lSKPPPLIKHQPESEGSVSKVPEQLSQSVQSHSVGSFRNdSRSPTQLSVSSSNTLRSMPALHRAPvfhppvhQNLEKKES 1004
Cdd:PTZ00449   559 -KKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKK-PKRPRSAQRPTRPKSPKLPELLDIP-------KSPKRPES 629
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415346 1005 SYSSLSPPTLT-PVQPVNAGGGKIQELQKPPT--LVP-EPKEAQTVYkgssDQNLSEAWKSNNTAANEKVDWHGERASGK 1080
Cdd:PTZ00449   630 PKSPKRPPPPQrPSSPERPEGPKIIKSPKPPKspKPPfDPKFKEKFY----DDYLDAAAKSKETKTTVVLDESFESILKE 705
                          250
                   ....*....|...
gi 2024415346 1081 AQSATASVIVRPP 1093
Cdd:PTZ00449   706 TLPETPGTPFTTP 718
 
Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
2166-2265 1.60e-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: 1.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415346 2166 DSSELPGALWHIYAGKDADKIREFLQKIAKEQGLEVLPEHDPIRDQSWYVNKKLRQRLLEEyGVKTCTVIQFLGDAIILP 2245
Cdd:pfam02373   16 EDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGEQPDDLLHLNTIISPKQLREN-GIPVYRFVQKPGEFVFTF 94
                           90       100
                   ....*....|....*....|
gi 2024415346 2246 AGALHQVQNFHSCVQVTEDF 2265
Cdd:pfam02373   95 PGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
2062-2134 1.22e-06

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: 47.63  E-value: 1.22e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024415346  2062 YEDLLKSLPLpeycspegKLNLASHLPGFFVRPDLGPRLcsAYGVAATkdhdigTTNLHIEVSDVVNILVYVG 2134
Cdd:smart00558    1 QLWNLAKLPF--------KLNLLSDLPEDIPGPDVGPYL--YMGMAGS------TTPWHIDDYDLVNYLHQGA 57
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
847-1093 4.08e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.84  E-value: 4.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415346  847 VKYDKDAERSVSELYKMKHSVPQSLPQSNYFttlsnsvvnePPRSYPSKEASSAYVD--KQTNCPSTAASPQSLPSYISS 924
Cdd:PTZ00449   489 IKKSKKKLAPIEEEDSDKHDEPPEGPEASGL----------PPKAPGDKEGEEGEHEdsKESDEPKEGGKPGETKEGEVG 558
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415346  925 lSKPPPLIKHQPESEGSVSKVPEQLSQSVQSHSVGSFRNdSRSPTQLSVSSSNTLRSMPALHRAPvfhppvhQNLEKKES 1004
Cdd:PTZ00449   559 -KKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKK-PKRPRSAQRPTRPKSPKLPELLDIP-------KSPKRPES 629
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415346 1005 SYSSLSPPTLT-PVQPVNAGGGKIQELQKPPT--LVP-EPKEAQTVYkgssDQNLSEAWKSNNTAANEKVDWHGERASGK 1080
Cdd:PTZ00449   630 PKSPKRPPPPQrPSSPERPEGPKIIKSPKPPKspKPPfDPKFKEKFY----DDYLDAAAKSKETKTTVVLDESFESILKE 705
                          250
                   ....*....|...
gi 2024415346 1081 AQSATASVIVRPP 1093
Cdd:PTZ00449   706 TLPETPGTPFTTP 718
KLF4_N cd21582
N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as ...
905-1041 3.56e-03

N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as Krueppel-like factor 4 or gut-enriched Kruppel-like factor/GKLF) is a protein that, in humans, is encoded by the KLF4 gene. Evidence also suggests that KLF4 is a tumor suppressor in certain cancers, including colorectal cancer, gastric cancer, esophageal squamous cell carcinoma, intestinal cancer, prostate cancer, bladder cancer and lung cancer. It may act as a tumor promoter where increased KLF4 expression has been reported, such as in oral squamous cell carcinoma and in primary breast ductal carcinoma. KLF4 is one of four key factors that are essential for inducing pluripotent stem cells. KLF4 is highly expressed in non-dividing cells and its overexpression induces cell cycle arrest. KLF proteins KLF1, KLF2, KLF4, KLF5, KLF6, and KLF7 are transcriptional activators. KLF4 belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF4, which is related to the N-terminal domains of KLF1 and KLF2.


Pssm-ID: 409228 [Multi-domain]  Cd Length: 335  Bit Score: 41.99  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415346  905 QTNCPSTAASPQSLPSYISSLSKPPPLIKHQPESEGSVSKVPEQLSQSVQSHS------------VGSFRNDSRSPTQLS 972
Cdd:cd21582    182 SINVSKSAPMTKSSVAPSSSLPFMCPRIKQENPSTCTISRPMDGHLGGNSQHGfsqraplpsrttPSGGPGGGNSSTAES 261
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024415346  973 VSSSNTLRSMPALHRAPV-----FHPPvhqnlekkeSSYSSLSPPTLTPVQPvnagggkiQELQKPPTLVP-EPK 1041
Cdd:cd21582    262 LMSRDHHPSSQVLSHPPLplpqgYHPS---------PGYPPFPPPPSQPQQY--------QELMSPGSCLPeEPK 319
 
Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
2166-2265 1.60e-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: 1.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415346 2166 DSSELPGALWHIYAGKDADKIREFLQKIAKEQGLEVLPEHDPIRDQSWYVNKKLRQRLLEEyGVKTCTVIQFLGDAIILP 2245
Cdd:pfam02373   16 EDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFGGEQPDDLLHLNTIISPKQLREN-GIPVYRFVQKPGEFVFTF 94
                           90       100
                   ....*....|....*....|
gi 2024415346 2246 AGALHQVQNFHSCVQVTEDF 2265
Cdd:pfam02373   95 PGWYHQVFNLGFNIAEAVNF 114
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
2062-2134 1.22e-06

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: 47.63  E-value: 1.22e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024415346  2062 YEDLLKSLPLpeycspegKLNLASHLPGFFVRPDLGPRLcsAYGVAATkdhdigTTNLHIEVSDVVNILVYVG 2134
Cdd:smart00558    1 QLWNLAKLPF--------KLNLLSDLPEDIPGPDVGPYL--YMGMAGS------TTPWHIDDYDLVNYLHQGA 57
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
847-1093 4.08e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.84  E-value: 4.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415346  847 VKYDKDAERSVSELYKMKHSVPQSLPQSNYFttlsnsvvnePPRSYPSKEASSAYVD--KQTNCPSTAASPQSLPSYISS 924
Cdd:PTZ00449   489 IKKSKKKLAPIEEEDSDKHDEPPEGPEASGL----------PPKAPGDKEGEEGEHEdsKESDEPKEGGKPGETKEGEVG 558
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415346  925 lSKPPPLIKHQPESEGSVSKVPEQLSQSVQSHSVGSFRNdSRSPTQLSVSSSNTLRSMPALHRAPvfhppvhQNLEKKES 1004
Cdd:PTZ00449   559 -KKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKK-PKRPRSAQRPTRPKSPKLPELLDIP-------KSPKRPES 629
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415346 1005 SYSSLSPPTLT-PVQPVNAGGGKIQELQKPPT--LVP-EPKEAQTVYkgssDQNLSEAWKSNNTAANEKVDWHGERASGK 1080
Cdd:PTZ00449   630 PKSPKRPPPPQrPSSPERPEGPKIIKSPKPPKspKPPfDPKFKEKFY----DDYLDAAAKSKETKTTVVLDESFESILKE 705
                          250
                   ....*....|...
gi 2024415346 1081 AQSATASVIVRPP 1093
Cdd:PTZ00449   706 TLPETPGTPFTTP 718
KLF4_N cd21582
N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as ...
905-1041 3.56e-03

N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as Krueppel-like factor 4 or gut-enriched Kruppel-like factor/GKLF) is a protein that, in humans, is encoded by the KLF4 gene. Evidence also suggests that KLF4 is a tumor suppressor in certain cancers, including colorectal cancer, gastric cancer, esophageal squamous cell carcinoma, intestinal cancer, prostate cancer, bladder cancer and lung cancer. It may act as a tumor promoter where increased KLF4 expression has been reported, such as in oral squamous cell carcinoma and in primary breast ductal carcinoma. KLF4 is one of four key factors that are essential for inducing pluripotent stem cells. KLF4 is highly expressed in non-dividing cells and its overexpression induces cell cycle arrest. KLF proteins KLF1, KLF2, KLF4, KLF5, KLF6, and KLF7 are transcriptional activators. KLF4 belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF4, which is related to the N-terminal domains of KLF1 and KLF2.


Pssm-ID: 409228 [Multi-domain]  Cd Length: 335  Bit Score: 41.99  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024415346  905 QTNCPSTAASPQSLPSYISSLSKPPPLIKHQPESEGSVSKVPEQLSQSVQSHS------------VGSFRNDSRSPTQLS 972
Cdd:cd21582    182 SINVSKSAPMTKSSVAPSSSLPFMCPRIKQENPSTCTISRPMDGHLGGNSQHGfsqraplpsrttPSGGPGGGNSSTAES 261
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024415346  973 VSSSNTLRSMPALHRAPV-----FHPPvhqnlekkeSSYSSLSPPTLTPVQPvnagggkiQELQKPPTLVP-EPK 1041
Cdd:cd21582    262 LMSRDHHPSSQVLSHPPLplpqgYHPS---------PGYPPFPPPPSQPQQY--------QELMSPGSCLPeEPK 319
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH