ID V3ZZF9_LOTGI Unreviewed; 743 AA.
AC V3ZZF9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Transglutaminase-like domain-containing protein {ECO:0000259|SMART:SM00460};
GN ORFNames=LOTGIDRAFT_231723 {ECO:0000313|EMBL:ESO96923.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO96923.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO96923.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
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; KB201362; ESO96923.1; -; Genomic_DNA.
DR RefSeq; XP_009052416.1; XM_009054168.1.
DR AlphaFoldDB; V3ZZF9; -.
DR STRING; 225164.V3ZZF9; -.
DR EnsemblMetazoa; LotgiT231723; LotgiP231723; LotgiG231723.
DR GeneID; 20248685; -.
DR KEGG; lgi:LOTGIDRAFT_231723; -.
DR CTD; 20248685; -.
DR HOGENOM; CLU_013435_0_2_1; -.
DR OMA; NHRTSRY; -.
DR OrthoDB; 2962236at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro.
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; 2.
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 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR000459-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746}.
FT DOMAIN 323..416
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 331
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 390
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 413
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 455
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 507
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ SEQUENCE 743 AA; 84613 MW; 1ABE0FF6579DEFC4 CRC64;
MGSGASKPRR PGSAGSITRE TYHNTHSALN PPTYRYRYVA SYGDKLSKDP KKKDNVLQVE
KVDYNIRQNT PRHNTDLFEI TQDDETPDPQ LVVRRGTPFD ITLTFNKPYD KNNDDLRLVF
ETGDKPLPNK KTHVEFVLSD EDKPKEWGGK VKRQDRNNLE ITIFTPPTCY VAKWDFKVDV
VKKSDTKSSI FRYTHKDPIY ILFNPFSKED TVYKETDLKE YILNENGRIY SGTYKNISPK
PWNFGQFQGK VLDCVMHLLD ISGLNWVCRG NPIQVVRKLT SMINAPDDGG VLVGNWSGDY
RGGKSPLTWT GSEAIFEEYY NTDRPVKFGQ CWVFSGVLTT ACRALGIPAR SVTNFASAHD
TDGSVSIDIH FDHLGEPDET KNSDSVWNFH VWNEVWMARN DLPTGYGGWQ AADATPQETS
DGVYCCGPAS LEAVKNGELA YAFDGPFIFA EVNADKIYWT TELDGTMINN HTEKKSVGRK
ISTKYPLRPE REDVTHLYKY AEGSEEERTA VLRANQTGSC RHDIYAMGPQ DVEFELEQQD
DVYVGQDFDV IFKIKNTSRN TERYITGRLS CRSMYYTGVG ADKIKTDTFE LFVPPGEVRE
QKLHIEADEY MNKLKDMCML KFSAMAKVQG TEQVFTTQED FRLCKPSLVV KVPNEIKKGK
SFDVEVSFTN PLGESMTECY LEVEGPGLLK RKQYPQRNVK PKQTFVTKFE LTPKKLGEKE
ILVMFNSKQL EDVTATTVVN VKN
//
