ID V8PAI6_OPHHA Unreviewed; 1346 AA.
AC V8PAI6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Putative histone-lysine N-methyltransferase NSD2 {ECO:0000313|EMBL:ETE71559.1};
DE Flags: Fragment;
GN Name=WHSC1 {ECO:0000313|EMBL:ETE71559.1};
GN ORFNames=L345_02612 {ECO:0000313|EMBL:ETE71559.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE71559.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE71559.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE71559.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:ETE71559.1}.
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DR EMBL; AZIM01000343; ETE71559.1; -; Genomic_DNA.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd21991; HMG-box_NSD2; 1.
DR CDD; cd15654; PHD3_NSD2; 1.
DR CDD; cd15660; PHD5_NSD2; 1.
DR CDD; cd20162; PWWP_NSD2_rpt1; 1.
DR CDD; cd20165; PWWP_NSD2_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 4.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR041306; C5HCH.
DR InterPro; IPR047443; HMG-box_NSD2.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR047441; PHD3_NSD2.
DR InterPro; IPR047442; PHD5_NSD2.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR047434; PWWP_NSD2_rpt1.
DR InterPro; IPR047435; PWWP_NSD2_rpt2.
DR InterPro; IPR001214; SET_dom.
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 PANTHER; PTHR22884:SF293; HISTONE-LYSINE N-METHYLTRANSFERASE NSD2; 1.
DR PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF17982; C5HCH; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00855; PWWP; 2.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00249; PHD; 4.
DR SMART; SM00293; PWWP; 2.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50812; PWWP; 2.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ETE71559.1};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:ETE71559.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 253..317
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 476..525
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 687..733
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 747..793
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 861..905
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 910..972
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1041..1091
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 1093..1210
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DNA_BIND 476..525
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1346
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE71559.1"
SQ SEQUENCE 1346 AA; 152494 MW; 329E67FD1A5AAB2C CRC64;
MDFKKRYQPH QNEACPRDPG QPPRKAPRLR SEPGVFCLPG QEPPFRHTTG RCQAEIQRPR
RPALHPRGEA PGSHLPRLQR GVGDARRPXK PKYNGHDALP FIPVEKLQDL TSRVFNGESG
TPDAKLRFES QDLREAATPP NTTPAKNGSP EIKLKITKTY MNGKPLFESS ICGDSVLEVT
QAEPNPGSKE KRSRKRSIKY DSLLEQGFVE AALLSNLSGS SDEKISAEEE EDDEDSSLVP
GKEDKTQLLK YSVGDVVWSK VSGYPWWPCM ISSDPLLHSF TKLNGQKKSF RQYHVQFFGD
APERAWVFEK SLVAFKGEEQ FEQLCQESAK HSINKAEKIK LLKPVSGKLR PQWEMGVKQA
KDALSMSMEE RKAKYTFIYV RGRPVLNPQV AKEAGLVVKS LEEMDKIYSD EDLSQTLKSS
KEHDVPAKRG RRTKSLCPSE SEGFAPPERS LEERGGTGGP PFGRKKAIPY APRSRKSDGV
PQFLVFCQKH RDEVVAEHPE ASCDEIEELL ESQWNMLSEK QKTRYNTKFA IVTSPKCEED
TGKRNLYGNK RKPVKRTRKP TEDFEVQEAS RKRLRMDKKN YQKRERSNEK TAKRSSTKAA
ESPQKRRPGL SDACKPLKKR NRASGPDSSH LPYSKSSSPS ASLTENEISD GPGDERSESP
YESADEGLGE VSQLSKKADR GATARKEYVC QVCEKPGEVM LCEGRCLGAF HASCSGLSGR
PKGQFVCGEC TSGKSSSGRD RRCIHTCFVC KEKQSEIKRC IVSHCGKFYH EACVKKFPLT
IFENRGFRCP LHSCESCHVA NPSNPKVSKG KMIRCVRCPV AYHVGDNCVA AGCAMLSSSS
IVCTNHFTAT KGKSHHGHVN VSWCFVCSKG GSLLCCESCP AAFHPDCLNI EMPDGSWFCN
DCKAGKKIHF QDIIWVKLGN YRWWPAEVCH PKNVPPNIQK MKHEIGEFPV FFFGSKDYYW
THQARVFPYM EGDRGSRYQA IKGIGKVFKN ALQDAETRFR EIKFQREAKE TQENERKPPP
YKHIKVNKPF GRVQTYTADI SEIPKCNCKP SDENPCGLDS ECLNRMLMYE CHPQVCPAGE
RCQNQCFTKR QYPETKIIRT EGKGWGLVAK RDIKKGEFVN EYVGEVIDEG ECMARIKYAH
ENDITHFYML TIDKDRIIDA GPKGNYSRFM NHSCQPNCET LKWTVHGDTR VGLFANSSSN
ASEEKGKKGK RRAKRRKTKS EARKKTEDYC FRCGDGGQLV LCDRKFCTKA YHLSCLDLVK
RPFGKWECPW HHCDVCGKPS VSFCHFCPNS FCKDHQEEAM LECNWSGQLF CPDHNGENFA
EKKARRPPRK LSSAKCKRQR NKWKRT
//
