ID A0A0V1ASM0_TRISP Unreviewed; 1684 AA.
AC A0A0V1ASM0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Lysine-specific demethylase 6A {ECO:0000313|EMBL:KRY27766.1};
DE Flags: Fragment;
GN Name=KDM6A {ECO:0000313|EMBL:KRY27766.1};
GN ORFNames=T01_11476 {ECO:0000313|EMBL:KRY27766.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY27766.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY27766.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY27766.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000256|ARBA:ARBA00034483}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY27766.1}.
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DR EMBL; JYDH01000236; KRY27766.1; -; Genomic_DNA.
DR STRING; 6334.A0A0V1ASM0; -.
DR eggNOG; KOG1124; Eukaryota.
DR eggNOG; KOG1246; Eukaryota.
DR InParanoid; A0A0V1ASM0; -.
DR Proteomes; UP000054776; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032452; F:histone demethylase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1370; -; 1.
DR Gene3D; 2.10.110.20; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR046941; KDM6_GATAL_sf.
DR InterPro; IPR048562; KDM6A_B-like_C-hel.
DR InterPro; IPR048560; KDM6A_B-like_GATAL.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14017:SF1; LD02225P; 1.
DR PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF21322; KDM6_C-hel; 1.
DR Pfam; PF21326; KDM6_GATAL; 1.
DR Pfam; PF13432; TPR_16; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00473; PAN_AP; 3.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50005; TPR; 2.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KRY27766.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054776};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000313|EMBL:KRY27766.1}.
FT REPEAT 157..190
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 380..413
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 857..1020
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 534..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY27766.1"
SQ SEQUENCE 1684 AA; 191823 MW; C2EDE6B1E044FA95 CRC64;
LIRTNLLISH CGPACASADL GISIQYGQHK PFMCIICSAL LLKIRIICEM DDSNCCQTVF
THEEARRLET MDSTEFGCLN LVHPEKIFER RLALKFYEQR LEEIQRSTDA AVETDNRFLC
EVLLKLGHLN LLIHDFVKAL SAYQRFYECK AEYWKDAPFL YGLGLVYFHF NIHKSATEVF
QRLLYLFPNF CKAAEVNIRL GLAFKALHSF DLAIKNLRLA FVDPNPTIFS KAEIRFHIAH
CIELKGDLKK AHSEYQSLLQ SSQVVSPVLR ASLLRQLGWL FFREESFGDK AHRISVAINC
LQQSLKADPT SGRSHYYLGR CFSAAGRAHE AFLSYRHSID KNESNADIWC SIGVLYQQQQ
QPFDALQAFV CAIQLDDSLS PAWIDLGLLY EQYFQLNDAL KCYKNALKLK SKINQALFDR
IEFLETQLKG RTKVSVDGEN SKSAPLLPNI EDVSRLPIPA QLLDRQNGYQ RQRIDMYLKG
SLIGIGLNES EDGALPSLNS QQIQMMHILS QNQALLNPHQ MLTLRQLQET HALTQHFQQQ
REQQRDEEDN VSRSQETVNV DPITSTEIGM RTSPLSDLPQ VTQEDLQAFL GFTDQEDLTN
SCLEPDNRNK ARIDKNDPII PTNVLFSTPV TIQDSVNSDR PAFLAEPPPS CLSLTAPLNV
PCSISSNEIF QICKQRNLGR CKSVYEENVL PPQPPTCNRN LPKDKLLLTT PCTVVDTKKD
ASSLELQRFC YQQPIVVIRG LTSALKMDLS LFSTKTIVAE AANQQVELRT QYLQASDVNV
DSQGNVTWQC GSQPSYTTVG KYAAYQLQSF QNALKDDKEK MKREGDVECN SSKRKKDVAL
KKVVKFGTNV DLSDERKWHL QLKELNKLPS FCRVYSSCNL LSHLGHVVLG MNTVQLYMKV
PGARTPGHQE NNNFAGVNIN IGPGECEWFA VPYEYWDAVK TICENNKCDF LRGSWWPSLE
DLYENNIPLY RFTQKAGDVV WIGEGTVHWV HSTGWCNNIA WNVGPLTASQ YQLAIERYEF
NKLNSYKSLV PLIHLSWQLA RNIRFSDKTL FEMVRKTLIQ SIAYCQMVLD YVCERLRKEL
KHHPRIEGEN SHYCCVCEVE VFNILFVLPH EDKYIVYCLN CALKHEMDLK SFYVLNQYNM
DELAAVLDQF TLVGILFCLF NNLLSPYLEE NWNDMLKFQI SDFCLNQKPH PNCSCSFSVT
WPQYSPFSKA VPSGKVILDE IDPTSRCLLA AWSTQAKRYT DDTFVLLHLK LMSLGRGSAN
SGYYHCAAIL LFFTALFFAA NAQKSVSIKS LKSGVLPDGV KVNRLRVGGI GEVVNRCFLR
CRNCVVTNVV AVERQLFLSE AACLHRCLQA KYASGERCTA VLYMRYFSVC DLYTPTGLTP
STAKRVRFIG YNYYELDPDC GVNDQMPLLR LSQKLFQDAS VLPSIDGRCP NTTRVIFERF
DATQSKASHY ISQSCSSEEE CLTHCQNFRA IDDSLIFCYS ADFVPEAKLC RLNLGPGIDV
VRHSQNHVMH RNSSVIHFRS ICIQDRAASY CREGAAIDRA SNKILVLDPH LRQVPEQASS
FENCLERCLI SKEIADFTCL SAMYIPLDLE FNCILNEGSH FTHPEHFYDS STLPSEYASF
DDCLASTWGN RLGYNHANME VGNRLSRSTF NCMRDDENDD GLDEDKLNGY MVDVFLKHYK
KKKR
//
