ID E0VU28_PEDHC Unreviewed; 760 AA. AC E0VU28; DT 02-NOV-2010, integrated into UniProtKB/TrEMBL. DT 02-NOV-2010, sequence version 1. DT 24-JAN-2024, entry version 69. DE SubName: Full=Hemocyte protein-glutamine gamma-glutamyltransferase, putative {ECO:0000313|EMBL:EEB16884.1}; DE EC=2.3.2.13 {ECO:0000313|EMBL:EEB16884.1}; GN Name=8230915 {ECO:0000313|EnsemblMetazoa:PHUM442960-PA}; GN ORFNames=Phum_PHUM442960 {ECO:0000313|EMBL:EEB16884.1}; OS Pediculus humanus subsp. corporis (Body louse). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae; OC Pediculus. OX NCBI_TaxID=121224; RN [1] {ECO:0000313|EMBL:EEB16884.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=USDA {ECO:0000313|EMBL:EEB16884.1}; RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S., RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K., RA Amedeo P., Strausberg R.; RT "Annotation of Pediculus humanus corporis strain USDA."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EEB16884.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=USDA {ECO:0000313|EMBL:EEB16884.1}; RG The Human Body Louse Genome Consortium; RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.; RT "The genome of the human body louse."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EnsemblMetazoa:PHUM442960-PA} RP IDENTIFICATION. RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM442960-PA}; RG EnsemblMetazoa; RL Submitted (FEB-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAZO01005406; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DS235778; EEB16884.1; -; Genomic_DNA. DR RefSeq; XP_002429622.1; XM_002429577.1. DR AlphaFoldDB; E0VU28; -. DR STRING; 121224.E0VU28; -. DR EnsemblMetazoa; PHUM442960-RA; PHUM442960-PA; PHUM442960. DR GeneID; 8230915; -. DR KEGG; phu:Phum_PHUM442960; -. DR CTD; 8230915; -. DR VEuPathDB; VectorBase:PHUM442960; -. DR eggNOG; ENOG502QQ46; Eukaryota. DR HOGENOM; CLU_013435_0_2_1; -. DR InParanoid; E0VU28; -. DR OMA; LEITHEY; -. DR OrthoDB; 5344745at2759; -. DR Proteomes; UP000009046; 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:UniProtKB-EC. 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:SF52; 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. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000313|EMBL:EEB16884.1}; KW Calcium {ECO:0000256|PIRSR:PIRSR000459-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000009046}; KW Transferase {ECO:0000313|EMBL:EEB16884.1}. FT DOMAIN 328..425 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 COMPBIAS 7..22 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 336 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT ACT_SITE 399 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT ACT_SITE 422 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT BINDING 462 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 464 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 521 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 526 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" SQ SEQUENCE 760 AA; 86586 MW; 5C1F17C3A53A0FBF CRC64; MSLRNDMGFY NGRSNNQNRN PEITNYMSNL MKKFNKDYER RRKQDENFSH HFMGSPEFNI LTTMDVEFYA IENSKTHHTD KFELVQQDPK IPILRRGQHF FIAVKFNRKI NFENDVIRLI FIFGPKPSVN KGTRAIVQVV KKDELNEDKW DAAVHEINGD IVSIKVNIPV VSPVGLWNLN IQTSSTDVTS SFKNYKCKKD IYVLFNPWCK DDEVYLEDEN ERNEYVLNDT GKIWMGSYLK PKGRRWFYGQ FDDVVLPAVV HLLEKSKLKH GERGNVIQMA RAISAVVNSE DEDGLIEGKW VGDFAGGTSP FAWTGSVAIM ENYLKSNGKS VKYGQCWVFS GAAVTICRAL GIPARPVTNY ASAHDTNSSL TLDKYFTRDG TEIEGGPDGD CYDSCWNFHV WVDVWMKRPD LPPSFSGWQI IDSTPQELSD NAYKCGPAPI EAVRRGEIGY LYDTPFAFAA VNADILHFQE DDESPWGFSR LNFDDCHVGK KLVTKKVGVD DDDEDSVNDM EDVTNLYKNP EGSTSERLAV LTAIRKSRKA RIQYDIALPH EEDVVFRLDE IDTIDYGQSF RVIVRIENNS EEPRTIQATM AANSVFYTGV SAYDLKKASG TMHLKGRTTE IMHITITPEE YLDKLVDHSL VKIFSIATVK ETKQNWSKED YFSFTKPSID ITVSGHLKVG YPVTAYFTFK NPIYRRLTDC TVSFEGPGLQ RPKLVNFADV EPNDDVHFTE TFVPKKSGPR KIMALFNSKL LNNVTAPVIK //