ID A0A509AS83_PLABA Unreviewed; 1993 AA.
AC A0A509AS83;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific, putative {ECO:0000313|EMBL:VUC58423.1};
GN ORFNames=PBANKA_1436200 {ECO:0000313|EMBL:VUC58423.1};
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823 {ECO:0000313|EMBL:VUC58423.1, ECO:0000313|Proteomes:UP000074855};
RN [1] {ECO:0000313|EMBL:VUC58423.1, ECO:0000313|Proteomes:UP000074855}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ANKA {ECO:0000313|EMBL:VUC58423.1,
RC ECO:0000313|Proteomes:UP000074855};
RX PubMed=25359557; DOI=10.1186/preaccept-1233682211145405;
RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA Janse C.J.;
RT "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT expression.";
RL BMC Biol. 12:86-86(2014).
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DR EMBL; LK023129; VUC58423.1; -; Genomic_DNA.
DR STRING; 5823.A0A509AS83; -.
DR VEuPathDB; PlasmoDB:PBANKA_1436200; -.
DR InParanoid; A0A509AS83; -.
DR OMA; FIHAPFF; -.
DR OrthoDB; 207178at2759; -.
DR Proteomes; UP000074855; Chromosome 14.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd15489; PHD_SF; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001646; 5peptide_repeat.
DR InterPro; IPR046341; SET_dom_sf.
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 InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00805; Pentapeptide; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF141571; Pentapeptide repeat-like; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000074855};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1128..1181
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1131..1178
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 482..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1958..1993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1962..1976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1993 AA; 233792 MW; D78ED9A13F27A73C CRC64;
MSFSAIKYES KILESLASML NLNEKTDNEI LDEIKDENPN ITFEIDDDIK KLIDINKINC
TCNASKKKID EYKGKKFEYF YNIETYGVDF FLDICNALCR SNYKPFLTEE GKNEIINGLR
IRRNSNLYKY VSFFLSKERL NKERLSDKKS PEHIYHCFKC LKSVLHIYND DQNNNETKNM
YLNQNKYITE EIEEKIENDI LNSNDTFKSQ QQNHQDGVIS VFKYKSELSS ITRKSNQKIV
QTIFEHTKNF NTKEHKLAFI KDTKLKGSNM QNTVNTDSTT NSIPSNEFYI NNSIMSNSNF
NNSIMSNSNF NNSIMSNSNF NNSIMSNSNF TNTYSMENNN PENSIQEGNE KYIPNTNEFK
TKRFSLRSRQ FSGKKECSNK YKNLNKKVKL NSQNKSLTRN SYRNDCNSIT NYCNNRQIRK
RRTFSNNRKN RNSTNSFMPD YLYLENTREQ IDSIYFSNSI FKSIDKSIEK IDMIVNENKF
FDNDDEESQS KFKESQTKEN EVQENIENEN YKGKSEKNEP EEYNPYLESE NGNVLGEINN
EKKSLDNLSS IIINQNELNN LSNNENFIDI INENEDANKL IDTKIKSLHE QTNERDLEEQ
LNKQNIILDE SKEKNVSEYG IYEKHTLSKN FCNYEEYEGN QSDDTSYSTN GSNYSKYLKR
KKKLEEQGKI VIDLNLLHRN TIKPNMKQYR DEKMAEKLRI EKLKKILEEK KMLLCRVEDI
AKKRNRIHVK TQILSEDSKI KRIYFSHKMK KVYNYKFGYF GSGWSNNKTE WTPFIHAPFF
DNQHNTIYKN RNKKLYEEIY DTILHGRIHP HIKVVELKDH MHPIRLCTPS NEDCYSVIYT
GEKIKSTDER VIFGEYTGFV ANNKELPQEK HQYIFALTFN KKVFNDRKNV VFINEIDSYD
NESDEKENSV EGNISEMKYT NMKNGNNYKG NQFNLDEDKH KEEINTETEK MNDAGKGEKN
KSLGNNNKNK ENDDIIDKSK KKKENKNSNI NDKSKELNNL IILPDNYTYA VDSSYMFNEM
SLVNHYKTCS IFNNYDFRIN AEWQIVYLDG WPHIILTSIP GVEIETGEEI FADFGFEWFD
RVNDICLNDF IKNNYEHRLN EIGIKNIKEK NFNGLDDIVD KYNLLKNYTT CNICIHSVNT
DCSNYIICSG CNHVYHLKCV NRLNFQINEN YDWFCSSCIQ FSMNIISQKE FLEYIKKENN
KRLINYFIEH NKHIDQGKTK SSEKLLMLEN NNENNLDSYN CEKNHEIQLD DENYINSFEN
IKKLLQCKEN IDDLLNNQQI INAFLENVDN NINILQGEEG QNDNIILKNP ELKNLIENSY
ELHLLIEYKN KIDDLLLCRE NINFLLNNEQ AKQTFQMRIK TINYLMQNKK CIENLVESIE
KKNRGEITKN NNATFKTTND QLQLLMTDNA QNGNTGNLSS LDLFKYENGE QNFVALREEN
ETTQSTIISA HGKYPYSKDG CYFTSVYENV LYKKTNHIIK NLKDLKNKNR KSRFKNNSIK
NEVNDENNNG SDGAGLNAYY NYMMKLSKKL LGLPLIREFE KGINTHQPSL PLNANLKKLE
VCSNCYKKHG NLAKAVICRV TKLHFETNYN DGLGEEELHK MSSECIQYVI KELANTIKEY
RKQELNSAFI QYTKKKKQSG LVNNKEHDIK IGNRFSDIIT SSDIINSTFN KTDIENKDFY
HSLSKSLYKD TYETDDNIAI QRSHLSYIDK NRSVNNSFEN QQDGNSTLQT NTYTIFGKKH
ENNDDGDGNG KSRHQVNISS DTIDEKNASD QENFKNDKYI SYNDENISTH NNDINNVYFR
SENGDSNNND YKNQKTNNFK NDDELLTTNE ILLDDKKKED KSISNNNLNI NNFIPLFGIE
LGKTKFQREF TNGTYVGTVT KQIKDDNDNH FFVVTYEDGD VEWITPFFLF QELLKQGTNN
IEYPLATPFK DLMNPNFKKD IKLNNYFLEL KVEKKKKKGT GEYNSNNNSA TKRQKHNQEG
TSSKTKKRYS AKQ
//
