ID L0G0H9_ECHVK Unreviewed; 448 AA.
AC L0G0H9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative aminopeptidase {ECO:0000313|EMBL:AGA78813.1};
GN OrderedLocusNames=Echvi_2571 {ECO:0000313|EMBL:AGA78813.1};
OS Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Echinicola.
OX NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA78813.1, ECO:0000313|Proteomes:UP000010796};
RN [1] {ECO:0000313|Proteomes:UP000010796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC {ECO:0000313|Proteomes:UP000010796};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Echinicola vietnamensis DSM 17526.";
RL Submitted (FEB-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; CP003346; AGA78813.1; -; Genomic_DNA.
DR RefSeq; WP_015266366.1; NC_019904.1.
DR AlphaFoldDB; L0G0H9; -.
DR STRING; 926556.Echvi_2571; -.
DR KEGG; evi:Echvi_2571; -.
DR PATRIC; fig|926556.3.peg.2712; -.
DR eggNOG; COG2234; Bacteria.
DR HOGENOM; CLU_047420_0_0_10; -.
DR OrthoDB; 9787436at2; -.
DR Proteomes; UP000010796; 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.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:AGA78813.1};
KW Hydrolase {ECO:0000313|EMBL:AGA78813.1};
KW Protease {ECO:0000313|EMBL:AGA78813.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010796}.
FT DOMAIN 363..448
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 448 AA; 50023 MW; 695545C2DBFA4E45 CRC64;
MKKILLIILI MVPFSVFSQV QIMHQNTEIA DMVQEISPSK LEEYIQGLVS FGTRHSLSVD
QEGRGIEAAR QYVLSTFESF EEASGGRLSA KIDYFTVEKD GRRIPEDVRM GNVMATLKGT
DPADDRIFIV SGHLDSRVSD IMNAESDAPG ANDDGSGVAA LMEMARIMSK RSFSATIIFV
AVSGEEQGLK GAAHLARKAK EEGWNLAAMI NNDMIGNSAS SGTQLRDNTR VRVFSEGVPL
HETEEMAKLR QYTNGENDSK SRQLARYIKE IGERYVAQLE VKLVYRNDRF LRGGDHTPFS
KEGFTAVRIC EYNENYTQQH QDLRTADKVQ YGDLPEHIDY EYLRKNSGVN LAVLASLASA
PSVPQEVGID VSELTNSTTL RWEEPENGKA KGYYVLMRET SSPVWEKKFF TDALSMTLPY
SKDNYFFAVQ AVGEGMVESR AVFPAPVR
//
