ID A0A0J8QMS6_COCIT Unreviewed; 718 AA.
AC A0A0J8QMS6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE SubName: Full=Thimet oligopeptidase {ECO:0000313|EMBL:KMU73771.1};
GN ORFNames=CISG_03821 {ECO:0000313|EMBL:KMU73771.1};
OS Coccidioides immitis RMSCC 3703.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU73771.1, ECO:0000313|Proteomes:UP000054559};
RN [1] {ECO:0000313|Proteomes:UP000054559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR EMBL; DS268131; KMU73771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8QMS6; -.
DR STRING; 454286.A0A0J8QMS6; -.
DR Proteomes; UP000054559; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06455; M3A_TOP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000054559};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 221..716
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 718 AA; 82108 MW; EA7D2A4CDF3C911D CRC64;
MAPSHLKSPP QAPPLFTGTP SSIVDDTKRL IEQSRKVQDA VAKNVSHEAA DFAKVLLPLA
HDENSMALES HILGFYQAVS TDSKLRDAST EAEKLMDDFA IESAMREDLF KLVDAVLKKG
EKLEPESQRL LEKEHKDYIR NGLGLPAGPK RDRFKEIKKR LSQIAIEFQK NLNEEKGGVW
LTREELHGVP EDVVSGLKKG EGENEGKLFL TFKYPDLFPL TKYATNADVR KRVMIANENK
CNQNVPLFKE AIILRDEAAR LLGYPNHATF RIEDKMAKTP ETVDKFLGDL RARLKDGGQK
EIEKLKELKA KDLKARTPSQ EADGHYFLWD HRFYDRMMLE KDYQLDHQLI AEFFPLQTTI
RGMLKIFEDL FGLVFVEIEG EERSKLSETG KGDDIVWHED VQVFSVWDDE GEGSGFVGYL
YLDLFPREGK YGHAANFNLQ PGFIDKDGKR RYPATALVCN FSKSTPKKPS LLKHDEVVTL
FHELGHGIHD LVSKTTYSRF HGTNTVRDFV EAPSQMLENW CWTPSQLKSL SKHFSYLSPE
YLEAWKEQAG DKPRPSEQIP DELIENLIKT KHVNDALFNL RQLHFGIFDM AVHEPVDHDA
IQKLDVSEKY NSLRKEITNF EGPEVLGLGY NWGHGQATFG HLIGGYDAGY YGYLSSQVYS
TDMFYSVFKD EPMNKKEGRR YRYTVLEKGG SQDEMETLKE FLGREPKPDA FYKELGLA
//