ID A0A016UAW9_9BILA Unreviewed; 1325 AA.
AC A0A016UAW9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=SET domain protein {ECO:0008006|Google:ProtNLM};
GN Name=Acey_s0048.g1545 {ECO:0000313|EMBL:EYC11977.1};
GN Synonyms=Acey-lin-59 {ECO:0000313|EMBL:EYC11977.1};
GN ORFNames=Y032_0048g1545 {ECO:0000313|EMBL:EYC11977.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC11977.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:EYC11977.1}.
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DR EMBL; JARK01001384; EYC11977.1; -; Genomic_DNA.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46147; HISTONE-LYSINE N-METHYLTRANSFERASE ASH1; 1.
DR PANTHER; PTHR46147:SF3; HISTONE-LYSINE N-METHYLTRANSFERASE ASH1; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 640..685
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 683..803
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 808..824
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 1137..1264
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 34..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1325 AA; 148160 MW; 915F26FBD1E74506 CRC64;
MSYEAVPCMF RSSAQNGNGE TQYLGLLIRP SANQQAPNGA PAGAVVGRSN TGQPVTALPP
GATPVKPPQP LLVQGVYPQG APIVVQGETP KVLVPAKVQV RLQQGGDASV AISPTALPST
TLPMATSTMA WPQAAPVKAA FPAPVHNALS SPCNSQPRSL SVCSASPQLD SSPMSPLPNI
IQYHNHTTPS TTRPGLQADP RSVRVPPGQW TAPVSDSSTT PDSGIQSVPG SPPSSHPLTP
PTMQLEGCDS VCEERYDNDE DFADMPRLIP ADQEEEPQCS NSCVSVREDV ASAHGSECET
APTPSISITT TMDTKEIVEQ LIMLDPQKAN VIANLIKRRQ SSNKRRSTSK QENSSKRGRP
GSAASEDAKK SEEEPNPASR VTTRSTSRAS SLKDGRTSTS SMTKLEVSPV CVDETKDVAS
QEVSPVPCVQ NPTESPSSEE RRSDAKPSTD EMEVRKMYRE AVKRMLREKV SLLLESTIVD
LQGLHIGLRE RHDRKSSKER KNTWAVNWDH VKKRRRKDED RKRTSERSGK KKEVVSKRQD
KGQAKQEHRE AKQEHREEKA DDAASHPLEK TSEKRGRKRR NDSVEKEKEK EKEEPRTRSA
HSIPAKRTSC CETPSQPKKE KEYEEIPRSV AVGSLPEWES PMLSCGCTRG ACTSDSECVN
RALCVQCPPG CAAPLCANKK FWKDDALKSL IVGGAKTRKI LRTKQTRRAG DFLGEFAGEV
VRYQDAKKRW ETYSKTDTSP VILCLTSRLF VDATVRGNVT RYVRHSCKPN ARLEVWSVNG
NYRGGLFALG DIASGAEITI DMNGLLPTSR SCHCGAIDCR KRVIMARNAH IASAGDLSIN
EERVVRKHQV FLVRNRQHCI ARAIASGLHG SFEPSTSQLD GLRKILKGIV YRVRRIDGRL
PLKATAGYHR VRRVLQNVER RRSQLNKAEI AAAFDTEMTR WLDELADDDF DRAYAALRGR
YLFESGKSEK EEKPKRDRRR DARLVNQDTN LEYIDSSFRV GGYDPDAVWP EGKANEKDDA
VRCVCGSLEE DGEMTLCDTC NFWLHSECLQ DVDQDDEYKC QFCRGSIDGS RPCSDVVLAK
QPEIRLHGCS YYKALVNNRS IQVRLNETVH VKRTAGDDHK KILKKLMDAN EKKKKNEKEE
KFDDIPPANN EPLPHETFHR KDLRVFRVER LFTAPGGHRF VFGFYYARPH ETFCDSQRIF
HRNEVFATPL YDTLPLDAVV GRCAVLDPSV WCIGRPTVPE FKEADVYLCE YQIDRNQRSF
EKIPSKNRYP INTQPYVFRK FEEPITIKRD FTPFIVDPTC SPSKSLTKLD KEAHDAAYLK
RFVSF
//
