Reviewed, UniProtKB/Swiss-Prot Q5AW75 (JHD1_EMENI)

Names and origin

Protein names

Recommended name:
    JmjC domain-containing histone demethylation protein 1
    EC=1.14.11.27
Alternative name(s):
    [Histone-H3]-lysine-36 demethylase 1

Gene names

Name:	jhd1
ORF Names:	AN7455

Organism

Emericella nidulans (Aspergillus nidulans)

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	1407 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code By similarity.
Catalytic activity	Protein N(6),N(6)-dimethyl-L-lysine + 2-oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO(2). Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O(2) = protein L-lysine + succinate + formaldehyde + CO(2).
Cofactor	Binds 1 Fe(2+) ion per subunit By similarity.
Subcellular location	NucleusBy similarity.
Domain	The JmjC domain mediates the demethylation activity By similarity.
Sequence similarities	Belongs to the JHDM1 histone demethylase family. Contains 1 JmjC domain. Contains 1 PHD-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	Iron Metal-binding Zinc
Molecular function	Chromatin regulator Dioxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	histone demethylase activity (H3-K36 specific) Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1407	1407	JmjC domain-containing histone demethylation protein 1		PRO_0000226797
Regions
	Domain	577 – 735	159	JmjC
	Zinc finger	323 – 382	60	PHD-type
Sites
	Metal binding	631	1	Iron; catalytic By similarity
	Metal binding	633	1	Iron; catalytic By similarity
	Metal binding	703	1	Iron; catalytic By similarity
	Binding site	628	1	Substrate By similarity
	Binding site	648	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5AW75-1 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: CE85B1C78A76A2D0	FASTA	1,407	156,107
	10 20 30 40 50 60 MISATSFVTA IGSRPPRYRT PSPPRRAVEP ISPCSTADYR TYRASREISA SATSDHVRST 70 80 90 100 110 120 PTDKRPSPAD VPASHRSGHG RSSSTIDTLA TIALATSPTF TPLTHRPPSD KSNTTLSMFP 130 140 150 160 170 180 PETEPVERPA KRPRSERDES SYTQHRSNAF SIARPPAISD SMKTDAELLL NFARPTNLYP 190 200 210 220 230 240 PIPSSKRANT DDSYHNHTFH TQAQIKERNA STYWVTNHEN VIFNHSAMHN IPPSRMRSQS 250 260 270 280 290 300 DGSAAISRPV IEGLRPNTSS STLPPLAFQE EADSGDRHWD MERKPVLEES QVDFCKPDET 310 320 330 340 350 360 VPILSQSQPL KKELDADSNG SSQASCATCN LVRIPVDNED QDVTWISCDG CKRWFHIVCA 370 380 390 400 410 420 GFKNDRETRT VDKFICKTCR PIHGQTTFVR KSSRVRTSID YAGLNQGLVK SATDSLEHHY 430 440 450 460 470 480 IEPIKQNKIR FLPENFPRMR PELVTAEYFE KGNGMTEPIV IPAEFNTHAT IPPTNPEFDA 490 500 510 520 530 540 LVQDAPSQEM FDELLDHLPN VDHETVIDCG QNQLDMVIPQ GLTVRTVSEL YGPEERVEVI 550 560 570 580 590 600 DVKSQHGEDK RWTMQKWADY YESTGDKVVR NVISLEVSQS KLGRLIRRPK IVRDLDLQDA 610 620 630 640 650 660 VWPEELKAVG NFPKVQFYCL MSVADCYTDF HIDFGGSSVY YHILKGKKTF FFIPPKDKHL 670 680 690 700 710 720 KKYEEWCNSP AQDYTFLGDQ TKECYRVDLS EGDTMLIPSG WIHAVWTPEN SLVIGGNFLT 730 740 750 760 770 780 RLNYGMQIKI AKIEKETKVP MKFRYPFFQK IQWYAVLKYL EEDPVPQSVL AAFSQDENYR 790 800 810 820 830 840 FHRKYPIYYE FGERANTEPK GSPYHNSRFY SQAELEGLPD LAKYLLRTAL IAGSYLVEGV 850 860 870 880 890 900 TADTRNAVKR SIPAMPGEPI DVIRTFGVWI AWKRGNEKAA HWTRPGVVES NAKLSLAEKR 910 920 930 940 950 960 PAGRPSRRSE RNADNQRTYA ERQAVQRLSE RPAVDIQKDS APGDESVAPL ANNSPPAATS 970 980 990 1000 1010 1020 GIPVPVMNED TSQKHKTASR GSGLGPKRVA CDACRKRRIR CHHKEENNGA SGSQMTVSTS 1030 1040 1050 1060 1070 1080 SLGHHTPTAQ DAASALNSLA AIASGAGFQN GLHSIKGMDR MDASANFATS ISATPHGVTL 1090 1100 1110 1120 1130 1140 KVGDGSPDGL NSAKKGRSKA CDDCRKSKRR CIHDEYGRID PIKAQERSKP RATSLAKRPR 1150 1160 1170 1180 1190 1200 VHEEAAPSSA NKRLKQESTS PVAQPVHSSH MDTETPTRAQ DSVENGVLDQ YPRKSNTQHA 1210 1220 1230 1240 1250 1260 DGLPAEKALL PDQSSYASPP AFQADAVATK ELPATVSKPA AVLVSPPTSL ADEMDIHDQV 1270 1280 1290 1300 1310 1320 DAGGEHVSVI YTPSSGSRQS SRQPRQVERY MPEVHFAKTA KSTTTTPQTT RRSSFGSSGR 1330 1340 1350 1360 1370 1380 KTTPGLSSGS KKSGSRPSSS HGKKSLSPSV EKKAERHAIS SAPFGQHGRG SKSEHGTSDV 1390 1400 DPDAESLRLI REIQEQEFGL RRRAGRA

References

[1]

"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AACD01000129 Genomic DNA. Translation: EAA62035.1.
RefSeq	XP_680724.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2869726.
KEGG	ani:AN7455.2.
Family and domain databases
InterPro	IPR013129. TF_JmjC. IPR003347. TF_JmjC_AAH. IPR001965. Znf_PHD. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Gene3D	G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.
Pfam	PF02373. JmjC. 1 hit. PF00628. PHD. 1 hit. [Graphical view]
SMART	SM00558. JmjC. 1 hit. SM00249. PHD. 1 hit. [Graphical view]
PROSITE	PS51184. JMJC. 1 hit. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

JHD1_EMENI

Accession

Primary (citable) accession number: Q5AW75

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	April 26, 2005
Last modified:	November 25, 2008
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)