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Database: UniProt
Entry: A0A0A1TFK7_9HYPO
LinkDB: A0A0A1TFK7_9HYPO
Original site: A0A0A1TFK7_9HYPO 
ID   A0A0A1TFK7_9HYPO        Unreviewed;       733 AA.
AC   A0A0A1TFK7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   13-SEP-2023, entry version 33.
DE   RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN   ORFNames=VHEMI09144 {ECO:0000313|EMBL:CEJ93564.1};
OS   [Torrubiella] hemipterigena.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX   NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ93564.1, ECO:0000313|Proteomes:UP000039046};
RN   [1] {ECO:0000313|EMBL:CEJ93564.1, ECO:0000313|Proteomes:UP000039046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA   Hertweck C., Linde J.;
RT   "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT   Verticillium hemipterigenum.";
RL   Genome Announc. 3:e01439-e01414(2015).
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; CDHN01000005; CEJ93564.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1TFK7; -.
DR   HOGENOM; CLU_001805_1_2_1; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000039046; 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:UP000039046};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          239..726
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   733 AA;  83566 MW;  742124FB1B26D6F5 CRC64;
     MATYTNSANC GRRCPQPLPR ILSTEEIVPT MERIISQYEA ARNSVLNNVT VETASFASVL
     QPIVDVEQET NGEIGVIWML QYGAPEIATQ EAVHKARQLF VAAEGCWNSD DSMYKLLVAA
     RDNSDKDANP DVASKLLLDH TLLRYKLAGC GAKANRNNET QESFSKESLD LSNALSTTLS
     NIAQENDGMW FAVEELEDLP SDELSRIKQK RQLEIVPHEQ GKEMIFVPFS NGGTIAVLTF
     SGNQQVRKRM YLADQRKLQK NIPILQDIVV KRQRLAKRLG YESHAHMRME DRLLAGPEQV
     HELLESLTDG LIRRGREELD VIQRARLKDM RQRQNVSSNG HSVAKSAFPP WDLKYYQNIV
     NIDRNIDQSK IAEYFSMEYA IPAMLQIFNT TLGLQFDPIP DDQMQRNEKW DDSVTAFAVW
     DTRSSSDEAT FVGYLYFDVL WRPNKFRGAH NVTMEYGFER SNGDRKYPST IVMSAFPTAS
     GDSRLVLLKH HQLLTVFHEL GHAIHSLVSR TKYSRFHGTS LPPDFVEIPS LMLENWCWMP
     EVLKSMSTHY SYLCPEYLAK WKAENPGKEQ PPKEIPDAIV DALVKYRYAS RGLYHLYQLS
     ISLFDMAIHS PSSAVEATAV NVQKLWYDIR ERIEGLDFTE VRDIGSELVA FNHLLGGFDV
     AYYSYLCCSS FAQDLFQNLF VEEPMNPEAW DRYRRIILQP GGEHLALYKL VEEALGHSPD
     LTALIKPLRN AVL
//
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