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Database: UniProt/TrEMBL
Entry: C4P259_STRPU
LinkDB: C4P259_STRPU
Original site: C4P259_STRPU 
ID   C4P259_STRPU            Unreviewed;       751 AA.
AC   C4P259;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   SubName: Full=Nuclear transglutaminase {ECO:0000313|EMBL:ACQ66512.1};
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668 {ECO:0000313|EMBL:ACQ66512.1};
RN   [1] {ECO:0000313|EMBL:ACQ66512.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19403662; DOI=10.1242/dev.030775;
RA   Wong J.L., Wessel G.M.;
RT   "Extracellular matrix modifications at fertilization: regulation of
RT   dityrosine crosslinking by transamidation.";
RL   Development 0:0-0(2009).
RN   [2] {ECO:0000313|Proteomes:UP000007110}
RP   NUCLEOTIDE SEQUENCE.
RA   Murali S., Liu Y., Vee V., English A., Wang M., Skinner E., Han Y.,
RA   Muzny D.M., Worley K.C., Gibbs R.A.;
RT   "Genome sequencing for Strongylocentrotus purpuratus.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:NP_001154911}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JAN-2021) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000459-2};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR000459-2};
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000256|ARBA:ARBA00005968}.
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DR   EMBL; FJ829471; ACQ66512.1; -; mRNA.
DR   RefSeq; NP_001154911.1; NM_001161439.1.
DR   AlphaFoldDB; C4P259; -.
DR   STRING; 7668.C4P259; -.
DR   EnsemblMetazoa; NM_001161439; NP_001154911; LOC592303.
DR   GeneID; 592303; -.
DR   KEGG; spu:592303; -.
DR   eggNOG; ENOG502QQ46; Eukaryota.
DR   HOGENOM; CLU_326622_0_0_1; -.
DR   InParanoid; C4P259; -.
DR   OMA; REREICQ; -.
DR   OrthoDB; 5344745at2759; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   InterPro; IPR036985; Transglutaminase-like_sf.
DR   InterPro; IPR023608; Transglutaminase_animal.
DR   InterPro; IPR013808; Transglutaminase_AS.
DR   InterPro; IPR008958; Transglutaminase_C.
DR   InterPro; IPR036238; Transglutaminase_C_sf.
DR   InterPro; IPR001102; Transglutaminase_N.
DR   PANTHER; PTHR11590:SF40; HEMOCYTE PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE-LIKE PROTEIN; 1.
DR   PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR   Pfam; PF00927; Transglut_C; 1.
DR   Pfam; PF01841; Transglut_core; 1.
DR   Pfam; PF00868; Transglut_N; 1.
DR   PIRSF; PIRSF000459; TGM_EBP42; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007110}.
FT   DOMAIN          321..415
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        329
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        389
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        412
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         452
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         454
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         514
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         519
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   751 AA;  83918 MW;  42074B51E03F7EE0 CRC64;
     MSTLMETADE TGAGITSPPS PGRSVNVADA ERAYLGEGRD DDTDSPSNPN QLSVKNFDYE
     LVRNRERHHT SEYEIKNLFV RRGQAFDLDV TFNKVPKTEV FMLELTVRGA VVSSINRGTV
     IRMPFHRSQA DTPGGWGIRV GSTEGAKYSL VINCPSDAIV SRYNVAVVIK DTEEAEPRYF
     RQDDPIYVLF NAWCREDSVH MAGDIEKGEY VLNDNGYVFI GSARPGSQHP RPWVFGQFED
     SATEVVFDLL EKWVRVNARS DPVVVSRKFT HLINYMPEYG VPETKVGLLV GNWSGDYEGG
     ESPSKWTGST KIYETFAESG GKPVNYGQCW VFSGVLCTAM RCLGIPCRSV TNFASAHDTD
     VSMTIDTVID SETNEEIEYL SNDSVWNFHV WNEVYYSRSD TIPGMGGWQV VDATPQESSE
     GVFQCGPAPV TAIKQGLTYI NYDTKFAFAE VNADRINWVA TKKDRGPPDM KTVSINTNAV
     GKYISTKKLP LVPGGYISRW NARNDITLEY KYAEGSVEER NAVERAISYG TRPNTYREDV
     KTDDIEMAIV LDEKISVGSD FELKVAVNNK SSVSRVISLT MNAHMCYYTG VLAKKITSLR
     KELTVPAGKS EHVIEMIRAE IYSSCLVDQA CIKFYVYGKV KETSQQTVSQ DTVYLTPPEM
     KTEFKVVGHE VEAVVEFVNP LPITLTNCTI TFEGARLLRS MTLYANDVPS KGNFKQKVKF
     SPREKGKRTL VIDFDSKQIG NITDVVEIEI P
//
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