ID A0A0V0WXJ8_9BILA Unreviewed; 1739 AA.
AC A0A0V0WXJ8;
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 8 {ECO:0000313|EMBL:KRX80464.1};
GN Name=Kdm8 {ECO:0000313|EMBL:KRX80464.1};
GN ORFNames=T06_116 {ECO:0000313|EMBL:KRX80464.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX80464.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX80464.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX80464.1};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 20 family.
CC {ECO:0000256|ARBA:ARBA00010743}.
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:KRX80464.1}.
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DR EMBL; JYDK01000041; KRX80464.1; -; Genomic_DNA.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR019323; ELKS/CAST.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR013921; Mediator_Med20.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR12461:SF97; BIFUNCTIONAL PEPTIDASE AND (3S)-LYSYL HYDROXYLASE JMJD7-RELATED; 1.
DR PANTHER; PTHR12461; HYPOXIA-INDUCIBLE FACTOR 1 ALPHA INHIBITOR-RELATED; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF10174; Cast; 2.
DR Pfam; PF13621; Cupin_8; 1.
DR Pfam; PF08612; Med20; 1.
DR PRINTS; PR00081; GDHRDH.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000313|EMBL:KRX80464.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Transferase {ECO:0000313|EMBL:KRX80464.1}.
FT DOMAIN 486..637
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1303..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1706..1739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 936..1045
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1088..1129
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1356..1489
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1739 AA; 197003 MW; 2255DDA926265D0A CRC64;
MILLVRIGLA LLQCCFGYTW SILECFFKKP KSVTDKVIVI TGAARGIGKG LALLLAHLHA
KIVLVDLDES TNKQTAEELR QETSACVYAY TADVTDPESM RQVANAIVTN PELGCPDVLV
CSAGVLIPKL LEDHSDVEIY RTMNTIRAFY PYILKRGQGH IVAVSSYGGH FGNSYSCCYS
ASKFAVRGLM ESLEWEIYDH GFGGEIKTTT IYPFFTRTDL LSSCNVTSDV IPVLTPEETS
QGILKAILYE QTEAFIPFYG SLICYFFKGR TFKAIELEDF EAAVEICNFM LNTGHWSEVN
ISWRLLYSMV SLLLSIAHIA NGRLKDALCS CDKGLLLGCP ISGNILAKLA SLLHCKMIDT
YPLEDVLIND KFDQALASMN DVCEHFEHSV PRVECPSLET FQRDFLIPQN PVVIEGALES
WQAMEKWNIA YLMSKCAYRT VPIEIGSKYT NDEWSQKLLT VTDFVHEYFN PDAREKAYLA
QHQLFEQITE LKDDIAVPDY CCLQCAPEDV DINAWFGPAN TVSPLHTDPR DNLFAQVFGQ
KYLRLCHPTA TKNLYPITDG LMSNTSQIDM EKIDYEKFPL VKNVKFYETI VKPGDLLFIP
KATGIACDVM SSAGSAAVQS SLASGLLPSP SNLYYQSLGH ITGGEGISRN GSRTPVSQRR
VGHFTRARHH SSCDVHSLCD GVTFERCFDS QLPPADPQIH AGGFKSGFPF SARSSSNSYR
QPTLSSHLSH GNLGYLQSDC DWSADLDPLV KNGRGSNEAP GCGSVSKIVN GRMTTTNCCP
ADCDALREDL RVAMEKLNAT MGSIKSFWSP ELKRERALRK EETAKMNMLQ EQLKLSLVNN
QKQSVLIEQL QNELRFQCNS GRSRRFPDDG PLIGHEDYRT VCQERDMYRR DWLISSDAVK
ELQYQLESQR QLLLSKDESV KRLLEALHSK GVPASVAQSC AEMELAQNRI VELEEKCSRL
QAHCDDLESH LQQSHDGLSS LRKDAVIESL QDEVASYEAE LKRLRSGGAI HEREFTDKMV
TDKEYQELKL KADKLELELG QKTVEIQALY TRLSTAEESA SDFKKHLELM KESNASKDQQ
ATLLQSDIDA LRGKLESKNE MIDQKAQQIT ELQADKNRLL SELNLLNEQH RISEVGLSTK
DRKIDLLEET IRERDCELNL IRTRLNSSPG VIQEKKLQDE INRLVQERDL WRKRFNEEHE
CLAIERKRDG EAHEKENKDL RIAIASLQKE ISDRQVFIES QNEKINDMVR QTEALTKENS
LYKELNKTNG VDLLKAEIER LNQAVDESRS EVDRLLKIIH NSEKEKNEGR ESGNDSKRFH
SNTENADYQV RCEISVLMHK DRRIEELEEA LKESVSITAE REMAVAQQKL NSQRAEQRIA
ALKDELKTMQ EQYDELSIQL KQLRQEKVQS DATIKTMQEE RKRYVDEVMQ LKGEVLLAAI
EEKDAHIAFL ENFHGRKSSE EIDNVKKQKE ELLQRLKEEN ARRVKLHNDP TLNFTDHFPK
RHWWPAMGIA WYDLVYLYSD PEKSDRQDVL LDSLQTALDN MDAKQAGFFS LTSETFFSTT
TTNAKPVHLF QSSEFPETTF VLVGDTLGSA STFLFAEKSI TQMIRNLDGA YCTKPISKVE
CRGNKYVISD FTVRTSVATI ASNFKGILVE IEYRPCVAMQ LCGDLMKEFC TALLGSAASA
PPTFVGLTKP NQRYVPIDTI FQKMSVQTAG PNEQQSQAQP QPQQQQQQQP QQQQQQQQQ
//
