ID F4W518_ACREC Unreviewed; 1043 AA.
AC F4W518;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Pyroglutamyl-peptidase 1 {ECO:0000313|EMBL:EGI70714.1};
GN ORFNames=G5I_00507 {ECO:0000313|EMBL:EGI70714.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI70714.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) 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; GL887596; EGI70714.1; -; Genomic_DNA.
DR AlphaFoldDB; F4W518; -.
DR STRING; 103372.F4W518; -.
DR EnsemblMetazoa; XM_011054516.1; XP_011052818.1; LOC105145132.
DR eggNOG; KOG4755; Eukaryota.
DR InParanoid; F4W518; -.
DR Proteomes; UP000007755; 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:UP000007755};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT REGION 477..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 114770 MW; E7360B1BD488143A CRC64;
MDVNAKCTIL VTGFGPFSIH TVNASWEAVK ELQELWKNSV EFSDVKLITE KIPVSYDYVS
DHIPQLWKKH NPSIVLHVGV SREAKSLTIE QHAYSNGYNK FDIYNKCPNE TDVECKVLKT
EIDVRELCNN VNENFERSGC KVCLSDNAGR YLCEYIFYQS LCIEPTKTLF VHVPDFNKYP
SKQTANDLNL SIRIHKKRLM PCNTIAASLI VDDNMNPEGN DGNSQGKAEV RLDVGLKNDN
QSVDQDTRTS KVQLENGAEE QLRLNNNSGE SNIKLVLPSK TSVVFSNGTN SIQTPVSDSA
NFLEQNVCQD ANISSIFTNA TANIKSQTVN TNTVNCQLKH KTVMNASSLN LPKSQMHLNL
SSTQANIHHN HNLGPAVLNS TATTSAMLHS SVSTLNVSVI PPNLSTIKSN DDMDMKNNVD
YASAIEKCPS KVSCSSDSSP EADCCWTSKS YGSKRVLNNI GGSIGSTSQG TCSFLRPNIN
GSREVAGPSG LQRTSQREQI ERMDSSSGNE GDMSDGEDYC FYTYKGNNDV IPSDQQEELN
QNHAANQEAE GQNHSGRSSP EMDYLEMDFD PGPSCEQDTG DSDLASINED IQNIALDNVE
QDPVLNDLSS GKVVSRQGLV SMPQTSKQTT QHVNHTTFQQ CTSNQCTVEQ NAKSTYSAPW
MPSTSAGTGR WDSATLYRNT GCPVRESYGY HNTSGDLISP GDNRDSDSEL WVESSTASLP
DNSNLNARKV NLISTLYHRI MAKKLMLNKH AAFNQSGDSN LENELCNERL DGLPPVEKVM
LWSEQEATMK QVTQIGTSAC GATSAINALL ALNVSFSLEV LVKGVNTKLR ELGVPLPRYL
VSRSVAGATH KDIARGITLS THGAVVTKFF AFYPERKVSL SHWLHYWISR GAAPIATLNL
QHCGEGCDIP DAWHHQMIFG VGQAGIYLTN PLECLPEQLV WHQLVSPSIL LIRKTDVLAH
WNENTDLTPL ATMDQKWRKL NVLGQVVNMV RESMSQRQQP NSTTTGATHI RIPASYQAGI
TLVMCADSAA ATELLHAEQL PLL
//