M28P2_UNCRE
ID M28P2_UNCRE Reviewed; 503 AA.
AC C4JHZ6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Probable zinc metalloprotease UREG_01421;
DE EC=3.4.-.-;
DE Flags: Precursor;
GN ORFNames=UREG_01421;
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
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DR EMBL; CH476615; EEP76572.1; -; Genomic_DNA.
DR RefSeq; XP_002541905.1; XM_002541859.1.
DR AlphaFoldDB; C4JHZ6; -.
DR SMR; C4JHZ6; -.
DR PRIDE; C4JHZ6; -.
DR EnsemblFungi; EEP76572; EEP76572; UREG_01421.
DR GeneID; 8440675; -.
DR KEGG; ure:UREG_01421; -.
DR VEuPathDB; FungiDB:UREG_01421; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_047420_0_0_1; -.
DR InParanoid; C4JHZ6; -.
DR OrthoDB; 607736at2759; -.
DR Proteomes; UP000002058; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..503
FT /note="Probable zinc metalloprotease UREG_01421"
FT /id="PRO_0000411764"
FT DOMAIN 416..503
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 503 AA; 55305 MW; 93BDEB1781A97276 CRC64;
MHSLSSALAG STFVLLFLCL LASAQPLTTP NPARALPDAL TGGSSIFSCP AASWPPTRIG
SPNRPQRPSR ELRSILSQIS HKRIEASILK LVSFGTRHTL STQTNATHGI GAARDWIASE
FKRYADASDG RLSVDVIGYE QQPDGNRIPF PVRISDVVAT LKGTEEPERI YLISGHYDSR
VTDVNDYTSF APGANDDASG VAVSLELARV MSQPHFPRPR ATLVFAAVAG EEQGLYGSRF
LAETYRNKSA NIEGMFTNDI VGSSTADDGT RDPHVVRLFG QGLPPLTVED QKQRETRLTI
GGENDTPARQ LSRFVKETAE NEHTDMRVSV IYRLDRYLRG GDHRPFLEAG YPAARFTEPH
ENFAHQHQDV RVETDPKTGR KKQYGDLPEF CDFRYIARVG KVNAAALWSL ANSPGMPRNV
RVSTRDLSND SKFFWDPPVG GNEGVGGYEI VWRSTVAPFW THVLDVGMAR EATVDLSKDN
VIFGIRARGK NGERGVAVLP FPA
