ID A0A452HPF5_9SAUR Unreviewed; 523 AA.
AC A0A452HPF5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Cytosol aminopeptidase domain-containing protein {ECO:0000259|PROSITE:PS00631};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000016880.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000016880.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR AlphaFoldDB; A0A452HPF5; -.
DR STRING; 38772.ENSGAGP00000016880; -.
DR Ensembl; ENSGAGT00000019268.1; ENSGAGP00000016880.1; ENSGAGG00000012605.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR Gene3D; 3.40.50.10590; Zn-dependent exopeptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR041417; NPEPL1_N.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963:SF4; AMINOPEPTIDASE NPEPL1-RELATED; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF18295; Pdase_M17_N2; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020}.
FT DOMAIN 340..347
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT REGION 502..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 56035 MW; F6ABEC7544705DB3 CRC64;
MANVQLEFQA SAGEADPQSR PLLVLGQLHN LHRLPWAQLR GKLQPRVSEE IWQAALSTLN
PNPTDNCPLY LNYATVAALP SRVSRHNSPS AAHFITRLVR NCLPGGINRC IVMVCERSEV
FASACALARA FPLFTHRSSA SRRTEKKTVI VEFFLVGQNN GPIEVATLNC LASATEGVRL
AARIVDTPCN EMNTNCFLEE IKKVGKDLGI VPTIIRDEEL NEKGFGGIYG VGKAAVHPPA
LAVLSHTPDG ATQTIAWVGK GIVYDTGGLS IKGKTTMPGM KRDCGGAAAV LGAFKATVKQ
GFKDNLHAVF CLAENSVGPN ATRPDDIHVL YSGKTVEINN TDAEGRLVLA DGVAYACKDL
GADIILDMAT LTGAQGIATG KYHAAVLTNN EDWEKACVIA GRNCGDLVHP LVYCPELHFS
EFTSAVADMK NSVADRDNTP SSCAGLFIAS HIGFDWSGVW VHIDIAAPVH AGERATGYGV
ALLLSLFGRA SEDPLLNMVS PLGCNGDSPD EEMERDSKRR RLV
//
