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Database: UniProt
Entry: A0A182Q5M1_9DIPT
LinkDB: A0A182Q5M1_9DIPT
Original site: A0A182Q5M1_9DIPT 
ID   A0A182Q5M1_9DIPT        Unreviewed;       749 AA.
AC   A0A182Q5M1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   08-NOV-2023, entry version 31.
DE   RecName: Full=Transglutaminase-like domain-containing protein {ECO:0000259|SMART:SM00460};
OS   Anopheles farauti.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF003526-PA, ECO:0000313|Proteomes:UP000075886};
RN   [1] {ECO:0000313|Proteomes:UP000075886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AFAF003526-PA}
RP   IDENTIFICATION.
RC   STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF003526-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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; AXCN02000839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A182Q5M1; -.
DR   STRING; 69004.A0A182Q5M1; -.
DR   EnsemblMetazoa; AFAF003526-RA; AFAF003526-PA; AFAF003526.
DR   VEuPathDB; VectorBase:AFAF003526; -.
DR   OrthoDB; 5344745at2759; -.
DR   Proteomes; UP000075886; 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; 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.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2}.
FT   DOMAIN          315..409
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        323
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        382
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   ACT_SITE        406
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT   BINDING         446
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         448
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         496
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT   BINDING         501
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ   SEQUENCE   749 AA;  82909 MW;  E6E1021626FF570F CRC64;
     MASKPKPKSY KIWPPRKASG NRSVKEPLCV ESVDLCFQEN GAAFHTASYE MMMKPRPTKR
     PRQLVVRRGA PFLVRLICNR HLEPTADTMV LVLSVLPFNS ETVCFGNGTE TYVLVHANDG
     GNGGPAEQPA DEWGAVLMGS QNKPKGKVEL TVSITTPSYS PIARWNMAVH CRLDTTDAKT
     EFMLKEPIYL LYNPWCKEDA VYMEDEASRK EYVLDDSTMI CKPSAQGPRM TSWFLGQYEA
     SVLDCVLYII SEVGNVQSAL SGNPVLVTRA LSGALNSASG FGVLQGNWSG NYENGTPPMS
     WSGSVKILQE FFETKETVQF GQCWVYSGLF ATVCRSIGIP ARVITNFESA GDHDASLSID
     YFLDDTDTVT SDMSVDSIWN YHVWIEGWMR RKDLQNSDFD GWQVLDATPQ QISDGMYKCG
     PCPVGAIRLG HVHVPYDGEF IYAEVNADVI YWSIGNDQNP PKPLQIKTDQ IGRDMSTKAV
     GSGQREDVTA QYKYPEGSPE ERDVMKTAMK FSCQRFCSAG LAKRLLGNMV SEVSADEDSI
     TLHLKSSEEL VLGSTFQIEL TVTNRSAVGE VEVTGNLILK DSDYTGRLTE TLKKLPFAMK
     LEAQETKSMV VPLDYKEYSQ TAKNKTNLKA TCMADVKGCN RTVFTMATFH LSPPAIELTP
     IEHSVAGPLA VQVDMRNPLP VPLTGGRFVV EGSRFTDPIE KLYDFIPVDG TVQFIYPINL
     SHKGKMVISA SFISNELKNV HGDVTLNIP
//
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