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Database: UniProt/TrEMBL
Entry: A0A158NI49_ATTCE
LinkDB: A0A158NI49_ATTCE
Original site: A0A158NI49_ATTCE 
ID   A0A158NI49_ATTCE        Unreviewed;       758 AA.
AC   A0A158NI49;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   08-NOV-2023, entry version 30.
DE   RecName: Full=Transglutaminase-like domain-containing protein {ECO:0000259|SMART:SM00460};
GN   Name=105620315 {ECO:0000313|EnsemblMetazoa:XP_012057207.1};
OS   Atta cephalotes (Leafcutter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012057207.1, ECO:0000313|Proteomes:UP000005205};
RN   [1] {ECO:0000313|Proteomes:UP000005205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA   Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA   Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA   Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA   Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA   Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA   Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA   Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA   Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA   Weinstock G.M., Gerardo N.M., Currie C.R.;
RT   "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT   insights into its obligate symbiotic lifestyle.";
RL   PLoS Genet. 7:e1002007-e1002007(2011).
RN   [2] {ECO:0000313|EnsemblMetazoa:XP_012057207.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) 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; ADTU01016274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADTU01016275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012057207.1; XM_012201817.1.
DR   AlphaFoldDB; A0A158NI49; -.
DR   EnsemblMetazoa; XM_012201817.1; XP_012057207.1; LOC105620315.
DR   GeneID; 105620315; -.
DR   KEGG; acep:105620315; -.
DR   eggNOG; ENOG502QQ46; Eukaryota.
DR   InParanoid; A0A158NI49; -.
DR   OrthoDB; 5344745at2759; -.
DR   Proteomes; UP000005205; 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; IPR008958; Transglutaminase_C.
DR   InterPro; IPR036238; Transglutaminase_C_sf.
DR   InterPro; IPR001102; Transglutaminase_N.
DR   PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR   PANTHER; PTHR11590:SF69; RE08173P; 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.
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:UP000005205}.
FT   DOMAIN          325..418
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   ACT_SITE        333
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        392
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        415
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         455
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         457
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         505
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         510
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   758 AA;  87346 MW;  744A4E24F8B8209B CRC64;
     MYPAFRSYPQ PGHPVHPDRR GMFYRFYDRY RIFNDRRTRP FPFRFYWEDF GVPVLTIHNV
     DPCIEENGEN HRTSRYELMT RQDDRARLVV RRGQEFYLHL SLSRDYSSSI DGVSIVFTLD
     GVERPQYGHG TLVATALLHP GEISEAAWQT TIDARGPNFL RIKVVTSANA IIGRWKMDID
     TKNKESEGAV SYTMDQPFYL ICNPWCRDDI VYLDGEAERQ EYVLAEDGLI WRGSHNRLRP
     TVWKYAQFER DILDCALHLM NYVGKVRVSG RNDPVIITRC LSAAVNSPDD NGAVLGNWSD
     DYGGGTPPTR WMGSQKILQQ YYKTKKPVKY GQCWVFSGVL ATICRTLGIP CRVVTNYSSA
     HDTQGSLTVD YFVNAEGKIM EELNSDSIWN FHVWNEVWMK RLDLSPDCSG WQMIDATPQE
     LSEGAYRCGP ASVAAVKKGE VLRPYDNAFL FAEVNADKVY WRYNGPTQPL KLVRKDMYGI
     GQLISTKAVG RWIREDITHT YKYPEKSDEE RAAMLKALRQ SESLFSRYYL NEEFNDVMFT
     FELRDDIIIG QPFSVVLLIK NRHSTLEYRV IVILRVETVL YTGRVGDPVK RLHIDRLVRP
     GVLEEIRMDV SWEEYSPRLL DQCAFNISCL ATVKDTNFEY FAQDDFRVRK PDIKIMLHND
     AVVGQTLHAS AKFRNPLPIP LRKGRFLIEG PGLDEQLKLK LLEPVEVDAD AECSFSMMPK
     LEGQARIAAK FYSRELEDID GHSNNFIVKS AKIINNSE
//
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