ID R8HIX8_BACCE Unreviewed; 465 AA.
AC R8HIX8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Aminopeptidase Y {ECO:0000313|EMBL:EOO72782.1};
GN ORFNames=IIC_04029 {ECO:0000313|EMBL:EOO72782.1};
OS Bacillus cereus VD021.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1053224 {ECO:0000313|EMBL:EOO72782.1, ECO:0000313|Proteomes:UP000014040};
RN [1] {ECO:0000313|EMBL:EOO72782.1, ECO:0000313|Proteomes:UP000014040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VD021 {ECO:0000313|EMBL:EOO72782.1,
RC ECO:0000313|Proteomes:UP000014040};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA Swiecicka I., Hansen B.M., Andrup L., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus cereus VD021.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOO72782.1}.
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DR EMBL; AHES01000035; EOO72782.1; -; Genomic_DNA.
DR RefSeq; WP_016102317.1; NZ_KB976281.1.
DR AlphaFoldDB; R8HIX8; -.
DR PATRIC; fig|1053224.3.peg.4078; -.
DR HOGENOM; CLU_024336_3_0_9; -.
DR Proteomes; UP000014040; Unassembled WGS sequence.
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; cd05661; M28_like_PA; 1.
DR CDD; cd00538; PA; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:EOO72782.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:EOO72782.1};
KW Protease {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:EOO72782.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..465
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004467331"
FT DOMAIN 130..219
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 246..445
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 465 AA; 50402 MW; DA7E58303775741F CRC64;
MRKSLKQKIV SSLLAVSLAV SLAPIGQAKA DSTSEITQTP PITKQVDANR AIDHIRFLSE
TIGPRPGGTK SEEWASRYVG MKLKSMGYEV EYQPFQVPDQ YVGFIESPLG TKRNWQAGAA
PNALISTEAV TAPLIFVQGG TKLDDIPNEV NGKIVLFERG ATVADYNKQV ENAVSKGAKG
VLLYSLIGGR GNYGQTFNPR LTKKQAIPVF GLAYAQGNAF KEEIAKKETT ILSLKARHES
NLTSLNVIAK KKPKNSTGNE KAVVVSSHYD SVVGAPGAND NASGTGLVLE LARAFQNVET
DKEIRFIAFG SEETGLLGSD YYVNSLSQKE RDRILGVFNA DMVATNYDKA KNLYAMTPDG
STNLVTDAAL HAGKQLNNDL VLQGKFGSSD HVPFAEVGIP SALFIWMGVD SWNPLIYHIE
KVYHTPQDNV FENISPERMK MALEVIGTGV YNSLQPTVKT GQKAA
//
