ID A0A2C5XGZ1_9PEZI Unreviewed; 1093 AA.
AC A0A2C5XGZ1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Putative zinc protease mug138 {ECO:0000313|EMBL:PHH55390.1};
GN Name=mug138 {ECO:0000313|EMBL:PHH55390.1};
GN ORFNames=CFIMG_000596RA {ECO:0000313|EMBL:PHH55390.1};
OS Ceratocystis fimbriata CBS 114723.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=1035309 {ECO:0000313|EMBL:PHH55390.1, ECO:0000313|Proteomes:UP000222788};
RN [1] {ECO:0000313|EMBL:PHH55390.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH55390.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=23931120; DOI=10.1016/j.funbio.2013.06.004;
RA Simpson M.C., Wilken P.M., Coetzee M.P., Wingfield M.J., Wingfield B.D.;
RT "Analysis of microsatellite markers in the genome of the plant pathogen
RT Ceratocystis fimbriata.";
RL Fungal Biol. 117:545-555(2013).
RN [2] {ECO:0000313|EMBL:PHH55390.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH55390.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=24563841; DOI=10.5598/imafungus.2013.04.02.14;
RA Wilken P.M., Steenkamp E.T., Wingfield M.J., de Beer Z.W., Wingfield B.D.;
RT "IMA Genome-F 1: Ceratocystis fimbriata: Draft nuclear genome sequence for
RT the plant pathogen, Ceratocystis fimbriata.";
RL IMA Fungus 4:357-358(2013).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHH55390.1}.
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DR EMBL; APWK03000011; PHH55390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5XGZ1; -.
DR STRING; 1035309.A0A2C5XGZ1; -.
DR OrthoDB; 129328at2759; -.
DR Proteomes; UP000222788; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:PHH55390.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000222788};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 53..202
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 229..408
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 415..703
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 709..889
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1071..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1093 AA; 124481 MW; D1D46A56DB48ADE6 CRC64;
MGVEIKQSTA TATTAATSAE TLPKATFITE QIEKPDVDDR KYRVIRLAND LEVLLAHDPN
TDKASAALDV NVGAFSDEDD MPGMAHAVEH LLFMGTEKYP AENHYHQYLS SNSGSSNAYT
ASTSTNYFFD VAAKPANDGE PTEENPSPFH DALDIFAQFF ICPLFLSETL DRELKAVDSE
NKKNLQSDVW RLHQLDKALA NPNHPYCHFS TGNFEVLKTI PESKGINVRE KFMEFHDKYY
SANLMKLVIL GREPLDILEK WAIEIFTPIP NKNLQRNRWT DEVPLRKSEL QKICYAKPVY
DKRELCLSFP IMDEDLQYRS QPSRYVSHLI GHESPGSLMA YLKAKGWVNN LSVGAMSICP
GSPGILECEM RLTEAGLKHY TEITKAFFQY VSLLRETKPQ KWIFDEQRLM GDVTFKFRQK
TTESRFTSKM SASMQRPFPR EWILSGTSKY REFNTKLIEQ VIGSITPDNF RMTIVSKTYP
GDWDQREKWY KTEYKQVDMT DDFVKELWVA TKSNASNRPN ELHLPAKNRF IPTNLVVKMK
EVKDPAVAPT LIRNDSKART WWKKDDTFGV PKASIIVQVR QPLAYSTCQS AIQAKLYGDL
VRDALEEHSY DAELAGLSYN VGVGSHGYNI EVSGYNDKLA ALLEEVLLKV RDLKITDERF
NIIKERSQRN LRNWKLQSAY NQVSFITQCL IAEKEYPVEN LLEHLGPTTA DDVRYFHKLL
ISQAHFEVLV HGNLCKEDAL NITTLVETTL PARELPEFEW PVSRYLILPP GSNQVLSKTL
EDPENVNNCI EYWLYIGSCD DMKLRATLLL FEQIINEPAF DQLRTKEQLG YIVFSATRIW
DSMMAFRILI QSEKYPQYLH SRIEAFLDMQ QKQFAAMSDA DFETHKRSLI VRRLKKHDNL
SSETSRFHSQ ITSGYYRFDI AQKDADYIKD LTKQDVVEFF NTYIANGSPS KAKLIVELYA
RGETEIENIV TKALEAVPSA NFETESALRA AIVEAVLRGS KEGLAKVLSA RVRLAPNVVE
AIVEAAGDSV EEVANKRSGD KEKEMAFTLP EPVYGEGASV ITDVPKWKSS LQASSAPTPA
KDLREFEQLG PKL
//
