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Database: UniProt
Entry: A0A2G8KX74_STIJA
LinkDB: A0A2G8KX74_STIJA
Original site: A0A2G8KX74_STIJA 
ID   A0A2G8KX74_STIJA        Unreviewed;       733 AA.
AC   A0A2G8KX74;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Putative set1/Ash2 histone methyltransferase complex subunit ASH2-like {ECO:0000313|EMBL:PIK52591.1};
GN   ORFNames=BSL78_10533 {ECO:0000313|EMBL:PIK52591.1};
OS   Stichopus japonicus (Sea cucumber).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX   NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK52591.1, ECO:0000313|Proteomes:UP000230750};
RN   [1] {ECO:0000313|EMBL:PIK52591.1, ECO:0000313|Proteomes:UP000230750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shaxun {ECO:0000313|EMBL:PIK52591.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PIK52591.1};
RX   PubMed=29023486;
RA   Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA   Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA   Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA   Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT   "The sea cucumber genome provides insights into morphological evolution and
RT   visceral regeneration.";
RL   PLoS Biol. 15:E2003790-E2003790(2017).
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:PIK52591.1}.
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DR   EMBL; MRZV01000323; PIK52591.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8KX74; -.
DR   STRING; 307972.A0A2G8KX74; -.
DR   Proteomes; UP000230750; Unassembled WGS sequence.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd15583; PHD_ash2p_like; 1.
DR   CDD; cd12872; SPRY_Ash2; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.90.980.20; -; 1.
DR   InterPro; IPR037353; ASH2.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   PANTHER; PTHR10598; SET1/ASH2 HISTONE METHYLTRANSFERASE COMPLEX SUBUNIT ASH2; 1.
DR   PANTHER; PTHR10598:SF0; SET1_ASH2 HISTONE METHYLTRANSFERASE COMPLEX SUBUNIT ASH2; 1.
DR   Pfam; PF21198; ASH2L-like_WH; 1.
DR   Pfam; PF00622; SPRY; 2.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000313|EMBL:PIK52591.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW   Transferase {ECO:0000313|EMBL:PIK52591.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00146}.
FT   DOMAIN          198..253
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          461..649
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   REGION          1..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   733 AA;  81432 MW;  C60F93E9A4F2263B CRC64;
     MDEPTEKADS ELTSSLASDK KQEGTTTSTV HQQDQTLDTA GSETLIEKKP DSGKESPKEK
     VDQSNTEKPA SEMEIDEPSD SQDNAAEQAD TQVTFDPPGI AQTDLNQEES GGESLDSKET
     ETVEIGPTGE TASIEEDISM EITDGQEVEL MDTSGIETAS EETTTVTTET AVTEQRLGRE
     EAVTEQSSTV EASEKGGKPT CCYCGRGRNL DVVELQCSIC MKWFHKDCLS INLGNCIPFM
     MSYTFCCKRC NPNNVEMYSR KVPNFSVLCY VVLANLTAQS RKADPPKTMF SKDGDIIPFI
     DANWELLTPA QRRTTVTWHS TIVKAMMKDA EMFVFKEKPD NPDENDEEYP LFGLLDQDLS
     KIGPNYDPRG DATQKSGSLS SSLNGNSGLL MTNVGRGRGA RKRGLDSSQN LGANKKTKGE
     LSASLRVSQH GYPLEHPFNK DGYRYTLTEN DPHAPAALFD EDIWIGKPIP AHLYRKALST
     QVLLALHDRA PQLKISSDRL TVSGEKGYSM VRSTHGVRYG TWYFEVTINE MPENTATRIG
     WSQPLGNLQA PLGYDKFGYS WRSRKGTKFH QSRGTRYTDG YGEGDVLGCL ILLPENIDKS
     RILPDTYKNR TLIKFKSHLY FEEKDEPTET EKSLKVTPGS KISFYKNGKN QGTAFSDIHD
     GLYYPCVSLY KSCSATVNFG PKFKHPPTDV GDYKPISDLA EISQVEQTLS DAIFHVEHEK
     MYEDAARGIL VVF
//
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