ID A0A1S3MJP9_SALSA Unreviewed; 906 AA.
AC A0A1S3MJP9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Lysine-specific demethylase 7B-like {ECO:0000313|RefSeq:XP_014003458.1};
GN Name=LOC106573199 {ECO:0000313|RefSeq:XP_014003458.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014003458.1};
RN [1] {ECO:0000313|RefSeq:XP_014003458.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014003458.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. JHDM1D
CC subfamily. {ECO:0000256|ARBA:ARBA00006942}.
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DR RefSeq; XP_014003458.1; XM_014147983.1.
DR AlphaFoldDB; A0A1S3MJP9; -.
DR STRING; 8030.ENSSSAP00000080534; -.
DR PaxDb; 8030-ENSSSAP00000080534; -.
DR GeneID; 106573199; -.
DR KEGG; sasa:106573199; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000087266; Chromosome ssa16.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1360; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR PANTHER; PTHR23123:SF15; LYSINE-SPECIFIC DEMETHYLASE 7A; 1.
DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 5..56
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 198..354
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 444..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..493
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 102722 MW; E1FF99BD92D8BD63 CRC64;
MAAAPLYCVC RQSYDVSRFM IECDICNDWF HGSCVQVEEH HAVDIDVYHC PKCDVQHGPS
LMKNRNNWHR HDYTEPDDGS RPVQAGTSVF VRELQNRTFP SADEIMVQMQ GHQVTQKYLE
KQGFRYPITV PKLDGLGLKL PPSSFSVRDV EEYVGGDKIV DVIDVARQAD SKMKLREFVK
YYYKPHRPKV LNVISLEFSD TKMAELVVVP DIAQKMSWVE NYWPDDSFFP KPFVQKYCLM
GVKDSYTDFH IDFGGTSVWY HVLWGEKIFY LIKPTQANLA LYEAWSSSPN QSEVFFGDKV
DKCYKCVVSQ GTTVLIPTGW IHAVLTSQDC MAFGGNFLHN LNIGMQLRCY EMERRLKTPD
LFKFPYFEAI CWYVAKNLLE TLKELREDNC QPPAYLTEGV KALITALKNW LKREVTEPAS
EVPDHIRPNR LIKELTKEIR YLEEEQQSGA GGSKPMKSQG SGACPLTRST LDRASHHARR
TARRLRHHHH HAPKTPSNLE ILELHTRQVL KRLEVGPFEE DVPFSSTVTA KFNKASVASA
AAVERSLDNN LRLVMCHGRI IRDERCHTRV KNSPVQEGER TGGHQLGEVL VKTEINDTMQ
EQHRDPERGE IQSPLSSESN WSSHRLSING LEFFERVNSD LRKGTAVYSD ISDSESEECC
STQKRDSSGK DSGSSDEEYK ELCRTERGTG SVTDLHQASQ ALSQHHKPLK GEHPTSPTTE
EEAVEGMLSM AGLLYPQRPE ESSTAQEPWW SSPAHRSPDR GEREPASGEE SQDSDSNSTL
SLQDERRAQQ HVRKECRAEL SQRIQENKNF MDSQSSGSNS SEAWGDQSPS RAASTPLCLD
PSPGTDYQYC ETTLSPPLHP SKRSAPNTPP ISNQATKGKR PKKGMATTKQ RLGKILKLSR
NNHFLL
//
