ID A0A151XEN1_9HYME Unreviewed; 1045 AA.
AC A0A151XEN1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE SubName: Full=Pyroglutamyl-peptidase 1 {ECO:0000313|EMBL:KYQ58728.1};
GN ORFNames=ALC60_02376 {ECO:0000313|EMBL:KYQ58728.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ58728.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ58728.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ58728.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ58728.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C15 family.
CC {ECO:0000256|ARBA:ARBA00006641}.
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DR EMBL; KQ982254; KYQ58728.1; -; Genomic_DNA.
DR RefSeq; XP_018317483.1; XM_018461981.1.
DR AlphaFoldDB; A0A151XEN1; -.
DR STRING; 64791.A0A151XEN1; -.
DR GeneID; 108731594; -.
DR OrthoDB; 2896846at2759; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00501; Peptidase_C15; 1.
DR Gene3D; 3.40.630.20; Peptidase C15, pyroglutamyl peptidase I-like; 1.
DR InterPro; IPR000816; Peptidase_C15.
DR InterPro; IPR016125; Peptidase_C15-like.
DR InterPro; IPR036440; Peptidase_C15-like_sf.
DR PANTHER; PTHR23402; PROTEASE FAMILY C15 PYROGLUTAMYL-PEPTIDASE I-RELATED; 1.
DR PANTHER; PTHR23402:SF1; RE07960P; 1.
DR Pfam; PF01470; Peptidase_C15; 1.
DR PRINTS; PR00706; PYROGLUPTASE.
DR SUPFAM; SSF53182; Pyrrolidone carboxyl peptidase (pyroglutamate aminopeptidase); 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT REGION 485..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1045 AA; 114719 MW; 12F11B17573B8790 CRC64;
MDANAKCTIL VTGFGPFSIH TVNASWEAVK ELQELWKNSV EFSDVKLVVE KIPVSYDYVS
DHISQLWKKH NPSIVLHVGV SHEAKSLTIE QHAHSNGYDR FDIYNKCPDE TDVECKVLKT
EIDVKELCNN VNERSGCKVC LSDNAGRYLC EYIFYQSLCI EPTKTLFVHV PDFDKYPSKQ
TANDLNLSIR IHNKKSTVYS KMPCNTIAAS LVVDDNMNPE GNDGNSQGKA EVRLDVGLKN
DNQSVDQDAR TSKVQLENGA EEQLRLNNNS GESNIKLVLP SKTSVVLSNG TNSIQTPVSD
SANFLEQNVC QDANISSIFT NATANIKSQT VNTNIVNCQL KHKTVMNASS LNLPKSQMHL
NLSSTQANIH HNHNLGSAVL NSTATTSAML HSSVSTLNVS VIPPNLSTIK SNDDMDMKNN
VDYASAIEKC PSKVSCSSDS SPEADCSWTS KSYGSKRVLN NIGGSIGSTS QGTCCFLRPN
INGSREVAGP SGLQRTSQRE QIERMDSSSG NEGDMSDGED YCFYTYKGNN DMIPLDQQEE
LNQDHAANQE AEGQNHSGRS SPEMDYLEMD FDPGPSCEQD TGDSDLASIN EDIQNIALDN
VEQDPVLNDL SSGKVVSRQG LVSIPQTSKQ TAQHVNHTTF QQCTSNQCTV EQSAKSTYSA
PWMPNTSAGT GRWDSATLYR NTGCPVRESY GYHNTSGDLI SPGDNRDSDS ELWVESSTAS
LPDNSNLNAR KVNLISTLYH RIMAKKLMLN KHAAFNQSGD SNLENELCNE RLDGLPPVEK
VMLWSEQEAT MKQVTQIGTS ACGATSAINA LLALNVSFSL EVLVKGVNTK LRELGVPLPR
YLVSRSVAGA TYKDIARGIS LSTNGAAITK FFAFYPERKV SLSHWLHYWI SRGAAPIATL
NLQHCGEGCD IPDAWHHQMI FGVGQAGIYL TNPLECLPEQ LVWHQLVSPS ILLIRKTDIL
AHWNENTDLT PLATMDQKWR KLNVLGQVVN MVRESMSQRQ QPNNTTTGAT HIRIPASHQA
GITLVMCADS AAATELLHAE QLPLL
//
