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Database: UniProt
Entry: A0A239L8Y9_9ACTN
LinkDB: A0A239L8Y9_9ACTN
Original site: A0A239L8Y9_9ACTN 
ID   A0A239L8Y9_9ACTN        Unreviewed;       508 AA.
AC   A0A239L8Y9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Aminopeptidase S {ECO:0000313|EMBL:SNT26452.1};
GN   ORFNames=SAMN05421812_104100 {ECO:0000313|EMBL:SNT26452.1};
OS   Asanoa hainanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Asanoa.
OX   NCBI_TaxID=560556 {ECO:0000313|EMBL:SNT26452.1, ECO:0000313|Proteomes:UP000198362};
RN   [1] {ECO:0000313|EMBL:SNT26452.1, ECO:0000313|Proteomes:UP000198362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5593 {ECO:0000313|EMBL:SNT26452.1,
RC   ECO:0000313|Proteomes:UP000198362};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC       {ECO:0000256|ARBA:ARBA00005957}.
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DR   EMBL; FZPH01000004; SNT26452.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239L8Y9; -.
DR   OrthoDB; 345880at2; -.
DR   Proteomes; UP000198362; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd03876; M28_SGAP_like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR041756; M28_SGAP-like.
DR   InterPro; IPR000998; MAM_dom.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS50060; MAM_2; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:SNT26452.1};
KW   Hydrolase {ECO:0000313|EMBL:SNT26452.1};
KW   Protease {ECO:0000313|EMBL:SNT26452.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198362};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..508
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013303323"
FT   DOMAIN          333..508
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
SQ   SEQUENCE   508 AA;  51469 MW;  0A1B39455C8AA456 CRC64;
     MRIPRIIPIL LTAVVTAALT ATTGAGPAVA AVPGPNIPLA NVKAHLTQLQ SIATANGGNR
     AHGQPGYLAS VNYVRGRLDA AGYTTAVQSF SYGGATGYNL IADWPGGDTT NTVIVGAHLD
     SVAAGPGIND NGSGSAAILE VALEVARQGI TPTRHLRFAW WGAEERGLIG SDFYVDSLSA
     AARANIEAYY NFDMVGSPNP GYFLYDGDNS DGTGAGPGPA GSALLEAVLA EYFTSIGVPT
     EGTDFDGRSD YGPFIAAGIP AGGTFTGAEG RKTAAQATKW GGSSGVAYDV CYHRSCDTTT
     NINDTALDRN ADAIAYAVWN VAVSPPAPPA TVYSDTFETA TGWTANPAGT DTATLGQWVR
     GDPAATTSSG AKQLGTTVSG TNDLVTGAAA GTSAGDFDVD GGTTTIQSPA ITLPATGPLN
     LSFSWYLAHG SNSSSADSFS AAVVHSGGTT TLFTQAGAAS NRNGAWATRT ASLTAYAGQS
     VRILFRAVDA STASLVEAGV DDVRITRG
//
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