ID A0A0D2C3N8_9EURO Unreviewed; 1068 AA.
AC A0A0D2C3N8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=Zinc metalloprotease {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV07_08983 {ECO:0000313|EMBL:KIW25843.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW25843.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW25843.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW25843.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847044; KIW25843.1; -; Genomic_DNA.
DR RefSeq; XP_016246059.1; XM_016396203.1.
DR AlphaFoldDB; A0A0D2C3N8; -.
DR MEROPS; M16.A04; -.
DR GeneID; 27348177; -.
DR VEuPathDB; FungiDB:PV07_08983; -.
DR HOGENOM; CLU_006065_0_0_1; -.
DR OrthoDB; 227593at2759; -.
DR Proteomes; UP000054466; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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 PANTHER; PTHR43016:SF16; METALLOPROTEASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07610)-RELATED; 1.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT DOMAIN 58..141
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 198..375
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1016..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1049
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1068 AA; 120360 MW; 6512ED5763D0EA28 CRC64;
MVSIRAKPRF RQRQRIDPDY CPCTITQYES ERTGMRVVVV DQEGPKLHGF FVLATEIHDD
SGAPHTLEHL CFMGSKSYKY KGFLDKLATR AYAGTNAWTA TDHTAYTLET AGWAGFAQIL
PVYLEHVILP TLTDAGCTTE VHHVDGSGND AGVVYSEMQG VQNMASELIE LQSKKILYPE
GVGYRYETGG MLEQLRVLTA DRIREFHREM YQPKNLCVAI FGEANHDELL AILDEFETSI
LPDIPSPDAP FKRPWIESKL APALNQTTLL RVEFPEEDES FGEVDIRFLG PNCADALELG
ALNVALNYLA GSSAAVLDHV LVEKEQLASS VYYQLDSRPR TEIQFSLSSV ETKRLEEVEK
RFFEVLKEAM EQPLNMDFMK DCIDRVVRTT KYNAEGSATA FADFIISDYL YGKRDGSTLE
IVKSLKHYTQ ALASWTEDQW KAYIKKYISD APHVSILGVP SARLSEKLKT DEANRIEEQK
ARLGPEGLKR MQEKLDAAKA ENDREIPRDL LGKFKVPLTD SIHFVTIPGA RAGRALDLGR
RDNRFQKIID EDAKDVPLFI NFEHIPTNFT RVHLIISTET LPDDLRPLLA IYMEAFWSLP
IKRGDEIIDF RQVVTELERD TVGYSIDAAN NLGNVEGIRI SFQVERERYG VAVKWLTELL
YNSIFDVERL RAVNTRLLAD VPDAKRSGDD MMMTVHFMTH LAPKSITRAR TILVKALYLK
RIRHLLKVDP ERVVSQLERL RNLLCRFENY RILVITDLEK TQKPVSTWQP FLEKLEPTKE
LNPIGRRIDR LSDAGKNPGK LAYVVPMPTI DSSFAFAVAR GPTSYDDPQL PAIMVALAYM
NAVEGPLWVA VRGTGLAYGT NMGFDIESGF IHIDVYRSPD AYKAFEASRK IISDYMTGAV
DFDPLMLEGA ISSIVVMFAN EQATLAGAAA MSFIRSIMQR LPDDHMQRML KRVREVSVQD
IKDALEKVVF NVFVPEKADI VVTCAPGLKE GIAGGLKDAG FSPEIRDLNY FQDDYGLKPI
DGEDEEDDDD DDDEEEDGDE DEDGREDTEG SDDIGGSEGY EIIEGNED
//
