ID A0A0V0S0J7_9BILA Unreviewed; 1774 AA.
AC A0A0V0S0J7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Lysine-specific demethylase 8 {ECO:0000313|EMBL:KRX20256.1};
GN Name=Kdm8 {ECO:0000313|EMBL:KRX20256.1};
GN ORFNames=T07_4647 {ECO:0000313|EMBL:KRX20256.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX20256.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX20256.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX20256.1};
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:KRX20256.1}.
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DR EMBL; JYDL01000051; KRX20256.1; -; Genomic_DNA.
DR Proteomes; UP000054630; 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:KRX20256.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Transferase {ECO:0000313|EMBL:KRX20256.1}.
FT DOMAIN 493..644
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1310..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1726..1774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 943..1052
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1095..1136
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1310..1329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1774 AA; 201588 MW; 8C0023178C133D34 CRC64;
MILLVRIGLA LLQCCFGYTW SILECFFKKP KSVTDKVIVI TGAARGIGKG LALLLAHLHA
KIVLVDLDES TNKQTAEELR QETSACVYAY TADVTDPESM RQVANAIVTN PELGCPDVLV
CSAGVLIPKL LEDHSDVEIY RTMNTIRAFY PYILKRGQGH IVAVSSYGGH FGNSYSCCYS
ASKFAVRGLM ESLEWEIYDH GFGGEIKTTT IYPFFTRTDL LSSCNVTSDL IPVLTAEETS
QGILKAILYE QTEAFIPFYG SLICYFFKGR TFKAIELEDF EAAVEICKFM LNFIWERLNT
GHWSEVNISW RILYTMVSLL LSIAHIANGR LKDALCSCDK GLLLGCPISG NVLARLASLL
HCKMIDTYPL EDMLINDKFD QALASMNDVC EHFEHCVPRV ECPSLETFQR DFLIPQNPVV
IEGALESWQA MEKWNIAYLM SKCAYRTVPI EIGSKYTNDE WSQKLLTITD FVHEYFNPDA
REKAYLAQHQ LFEQITELKD DIAVPDYCCL QCAPEDVDIN AWFGPANTVS PLHTDPRDNL
FAQVFGKKYL RLCHPTATKN LYPITDGLMS NTSQIDMEKI DYEKFPLVKN VKFYETIVKP
GDLLFIPKAT GIACDVMSSA GSAAVQSSLA SGLLPSPSNL YYQSLGHITG GEGISRNGSR
TPVSQRRVGH FTRARHHSSC DVHSLCDGVT FERCFDSQLP PADPQIHAGG LKGGFPFSAR
SSSNSYRQPT LSSHLSHGNL GYLQSDCDWS ADLDPLVKNG RGSNEAPVCG SGSKIVNGRM
TTTNCCPADC DALREDLRVA MEKLNATMGS IKSFWSPELK RERALRKEET AKMNMLQEQL
KLSLVNNQKQ SVLIEQLQNE LRFQCNSGRS RRFPDDGPLI GHEDYRTVCQ ERDMYRRDWL
ISSDAVKELQ YQLESQRQLL LSKDESVKRL LEALHSKGVP ASVAQSCAEM ELAQNRIVEL
EEKCSRLQAH CDDLESHLQQ SHDGLSNLRK DAVIESLQDE VASYEAELKR LRSGGAIHER
EFTDKMVTDK EYQELKLKAD KLELELGQKT VEIQALYTRL STAEESASDF KKHLELMKES
NASKDQQATL LQSDIDALRG KLESKNEMID QKAQQITELQ ADKNRLLSEL NLLNEQHRIS
EVGLSTKDRK IDLLEETIRE RDCELNLIRT RLNSSPGVIQ EKKLQDEINR LVQERDLWRK
RFNEEHECLA IERKRDGEAH EKENKDLRIA IASLQKEISD RQVFIESQNE KINDMVRQTE
ALTKENSLYK ELNKTNGVDL LKAEIERLNQ AVDESRSEVD RLLKIIHNSE KEKNEGRESG
NDSKRFHSNT ENADYQSVLM HKDRRIEELE EALKESVSIT AEREMAVAQQ KLNSQRAEQR
IAALKDELKT LQEQYDELSI QLKQLRQEKV QSDATIKTMQ EERKRYVDEV MQLKGEVLLA
AIEEKDAHIA FLENFHGRKS SEEIDNVKKQ KEELLQRLKE ENARRVKLHN DPTLNFTDHF
PKVSGIDLVR HWWPAMGIAW YNRVYLYSDP EKSDRQDVLL DSLQTALDNM DAKQAGFFSL
TSETFFSTTT TNAKPVHLFQ SSEFPETTFV LVGDTLGSAS TFLFAEKSIT QMIRNLDGAY
CTKPISKVEC RGNKYVISDF TVRTSVATIA SNFKGILVEI EYRPCVAMQL CGDLMKEFCT
ALLGSAASAP PTFVGLTKPN QRYVPIDTIF QYHCYFMHFR KMSVQTAGPN EQQSQAQPQP
QQQQQQQQPQ QQQQQQQQQQ QQQQQQQQQQ QQQQ
//
