ID I3YZQ6_AEQSU Unreviewed; 443 AA.
AC I3YZQ6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative aminopeptidase {ECO:0000313|EMBL:AFL82474.1};
GN OrderedLocusNames=Aeqsu_3036 {ECO:0000313|EMBL:AFL82474.1};
OS Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / 9-3).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL82474.1, ECO:0000313|Proteomes:UP000006049};
RN [1] {ECO:0000313|EMBL:AFL82474.1, ECO:0000313|Proteomes:UP000006049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3
RC {ECO:0000313|Proteomes:UP000006049};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Aequorivita sublithincola DSM 14238.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; CP003280; AFL82474.1; -; Genomic_DNA.
DR RefSeq; WP_014783723.1; NC_018013.1.
DR AlphaFoldDB; I3YZQ6; -.
DR STRING; 746697.Aeqsu_3036; -.
DR KEGG; asl:Aeqsu_3036; -.
DR PATRIC; fig|746697.3.peg.3095; -.
DR eggNOG; COG2234; Bacteria.
DR HOGENOM; CLU_047420_0_0_10; -.
DR OrthoDB; 9787436at2; -.
DR Proteomes; UP000006049; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR045175; M28_fam.
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; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:AFL82474.1};
KW Hydrolase {ECO:0000313|EMBL:AFL82474.1};
KW Protease {ECO:0000313|EMBL:AFL82474.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..443
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003684389"
FT DOMAIN 109..317
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 443 AA; 49642 MW; 43580F015F062CE3 CRC64;
MKKLLFLSIL SISFSIFSQT DQKIYDIVSS VSSKRIKADV TTLVNFGTRN TFSDTVSNTR
GIGAARRWIK SEFENISKNC SNCLNVFYQK NLVKAEGNDR VPTDTWIVNV AAVQKGTKYP
NRYIIMSGDI DSRNSDGSDF TKDAPGANDN ASGMAGTIEA ARVLSKYKFE NNIIYLGLSG
EEQGLFGGKG FAEFAKDNNW EIIGVFNNDM IGNIKGVDGV ISNRDFRIFS EPVPPTETEQ
ERQMRRFYGG EVDGISRQLA RYVYKTTKTY MPEMNPMMVY RLDRFGRGGH HRPFNDLGWA
GIRIMESHED YNHQHQDLRT ENGIEYGDKI EFVNFDYAAK LTAVNAINLA SIASAPPEPK
NVAIGGVVEA SAKLKWEKVD GATGYKIYWR DTTSPTWDHR RYVGDVSEFT LEGIVIDNSF
FGVASVGKNG FESIVVFPNS VFR
//
