ID A0A3B3ZZV5_9GOBI Unreviewed; 438 AA.
AC A0A3B3ZZV5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein K {ECO:0000256|ARBA:ARBA00018447};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000010065.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000010065.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
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DR AlphaFoldDB; A0A3B3ZZV5; -.
DR STRING; 409849.ENSPMGP00000010065; -.
DR Ensembl; ENSPMGT00000010741.1; ENSPMGP00000010065.1; ENSPMGG00000008349.1.
DR Proteomes; UP000261520; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd22432; KH-I_HNRNPK_rpt1; 1.
DR CDD; cd22433; KH-I_HNRNPK_rpt2; 1.
DR CDD; cd22434; KH-I_HNRNPK_rpt3; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 3.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012987; ROK_N.
DR PANTHER; PTHR10288:SF339; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN K; 1.
DR PANTHER; PTHR10288; KH DOMAIN CONTAINING RNA BINDING PROTEIN; 1.
DR Pfam; PF00013; KH_1; 3.
DR Pfam; PF08067; ROKNT; 1.
DR SMART; SM00322; KH; 3.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022728};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00022728};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728}.
FT DOMAIN 41..106
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 119..190
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 350..420
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 438 AA; 48302 MW; 63DFAAB2D0B560A6 CRC64;
METEIEQQEE STFSNTESNG KRPAEDADEQ KSFKRSRNSD EMVELRVLLQ SKNAGAVIGK
GGKNIKALRS DFNASVSVPD SSGPERILSI SADIETVGEI LLKTIPTLEE YQQYNGMDFD
CELRLLIHQS LAGSIIGVKG AKIKELRENT KTSIKLFQEC CPQSTDRVVL VGGKTERVVD
CIKTILDLIS EAPIKGRAQP YDPNFYDETY DYGGFTMMFD ERGGGRRLMG GFPMRGGRSG
GGGDRGFDRM SSSRGARGPM PPSRRDYDEM SPRRGPPPPH PRSISRGSNR SRNMPMSPCS
THSYGPLLHS DRRGRPDRYS DNMPSLCFHR LTLPRVLSGG RGSYSDMGGP VITTQVTIPK
DLAGSIIGKG GQRIKQIRHE SGASIKIDEP LEGSEDRIIT ITGTQDQIQN AQYLLQNRQV
PTRPLSPWWS NGDGCEGV
//