ID   H2AMJ5_KAZAF            Unreviewed;      1222 AA.
AC   H2AMJ5;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=K Homology domain-containing protein {ECO:0000259|SMART:SM00322};
GN   Name=KAFR0A01570 {ECO:0000313|EMBL:CCF55595.1};
GN   ORFNames=KAFR_0A01570 {ECO:0000313|EMBL:CCF55595.1};
OS   Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS   1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF55595.1, ECO:0000313|Proteomes:UP000005220};
RN   [1] {ECO:0000313|EMBL:CCF55595.1, ECO:0000313|Proteomes:UP000005220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC   NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR   EMBL; HE650821; CCF55595.1; -; Genomic_DNA.
DR   RefSeq; XP_003954730.1; XM_003954681.1.
DR   AlphaFoldDB; H2AMJ5; -.
DR   STRING; 1071382.H2AMJ5; -.
DR   GeneID; 13882323; -.
DR   KEGG; kaf:KAFR_0A01570; -.
DR   eggNOG; KOG2208; Eukaryota.
DR   HOGENOM; CLU_003293_1_0_1; -.
DR   InParanoid; H2AMJ5; -.
DR   OrthoDB; 5489311at2759; -.
DR   Proteomes; UP000005220; Chromosome 1.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd22452; KH-I_ScSCP160_rpt7; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 7.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   PANTHER; PTHR10288; KH DOMAIN CONTAINING RNA BINDING PROTEIN; 1.
DR   PANTHER; PTHR10288:SF171; P-ELEMENT SOMATIC INHIBITOR, ISOFORM C; 1.
DR   Pfam; PF00013; KH_1; 7.
DR   SMART; SM00322; KH; 7.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 6.
DR   PROSITE; PS50084; KH_TYPE_1; 7.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00117}.
FT   DOMAIN          178..256
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          634..706
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          710..775
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          780..855
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          859..933
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          937..1004
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          1151..1221
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1222 AA;  135328 MW;  215B727524F14CDD CRC64;
     MSNALEESNT PATSVDTTID SVPEATTPTT SQSVAPQDNE SAADSTTVEE QKKTPLPSLK
     DLPSLVSKDA FTKTPVSWGP NMKPVAATLM SQTFTSSSST PGPRRMRSTN IQESFTLDLQ
     SQLSITKPEL SRIVLSIKQS LDVSIESTLS KNSRTFLISG VADNVHSAKR ELIKKLTKPI
     NDRIQIPTRC KAAVIGSGGK TIREISNKFE VKVNVGKEEI EGSYDEDLDD TATDVSFFGD
     FESVNLAKAK IMQIVKEETK NATIKVSVTD SLLLPFVQIN SIDSIPGTIK CQFFKDTGDI
     VISGLRDDAK QAKITIQKYL DALANTLTEQ KVKIPTKFQF LIDANELKEK FNVTVTFPTA
     HKDDFVSFAG EEKKVKEAIS FARASSKAYV VDSLDIARAH SKNIEHAKNL VLYFMKYNAL
     KTVLDQSPEI QISLPSVEEL VLAENDVNIN ISAKSEDVAK IKAARKDIIG VVNGITPEDT
     LTVTDLDYDL FHKNIKQILS GLNEKIAFIQ LGDYIKGNDS VILMAITSDE DFKPTSEEIK
     ETLQRANGLL NPLREKLNSM STKVYDLDSA KQEELLSKSS VTLPLIMEDI SNEDGNVQFK
     LHTPENDKLT VRGDEKAVKL VNKAINLIIE SPSKKSKITV EVPSNTVSRL IGNKGSNLQN
     IKDKFDVNVD VPPQESNSKD KQVEITLTGL EYNLNHAKKF VLAEAKKWAD IVTKQLVVPA
     KYYRNLMGPR GSYRTRLQEK YSVFINFPTN GDIVTVRGPS RGVKQAYEEL NSLLDFEMEN
     GHKATMQVPA EHVPRVIGKN GDIINDIRAE FGVEMDFLQK NDDEKVKETG LMDLEIVGSR
     QAIKEAQAKV QQIVSEASDY TNEVLTVDRK YHRTIVGPGG RTLREIISKA GGDEIRNKNV
     DIPNVNSESD VITVQGPKSF VSKVVKEINK IVEEGENSIT RELDIPKERQ GALVGPGGVV
     RRQLETEFNV VVQVPNKDKT GPVTLTGLPE NIEKAENKII NEILKDNFDV ELEVPAAAHE
     FVSERGALIQ KLRIDESINI KHGNSTKRAT KLNRAKLVIP LDRVYPATEE EKSEKVKVTI
     EELSESAKLE EGNIPWRLTY EPIDISYILA DDEETEAKEP KKNTIDEAKK KQALETATKI
     IEDRVSKAPA AKFVGYVWVS DVKRFNKIIG PGGSNIKQIR EATGALINVP RKSDAPNDVV
     YIRGTKEGVE KAAEMVVKSL KN
//