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Database: UniProt
Entry: A0A2V1AU92_9ASCO
LinkDB: A0A2V1AU92_9ASCO
Original site: A0A2V1AU92_9ASCO 
ID   A0A2V1AU92_9ASCO        Unreviewed;      1057 AA.
AC   A0A2V1AU92;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=A-factor-processing enzyme {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CXQ85_000633 {ECO:0000313|EMBL:PVH21650.1};
OS   [Candida] haemuloni.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH21650.1, ECO:0000313|Proteomes:UP000244309};
RN   [1] {ECO:0000313|EMBL:PVH21650.1, ECO:0000313|Proteomes:UP000244309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B11899 {ECO:0000313|EMBL:PVH21650.1,
RC   ECO:0000313|Proteomes:UP000244309};
RA   Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA   Litvintseva A.P.;
RT   "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT   Patient with Chronic Leg Ulcers in Israel.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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:PVH21650.1}.
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DR   EMBL; PKFO01000005; PVH21650.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1AU92; -.
DR   STRING; 45357.A0A2V1AU92; -.
DR   EnsemblFungi; CXQ85_000633-t46_1; CXQ85_000633-t46_1-p1; CXQ85_000633.
DR   VEuPathDB; FungiDB:CXQ85_000633; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000244309; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244309};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          36..174
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          200..377
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          386..671
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          675..869
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1057 AA;  121869 MW;  026E279883A597E7 CRC64;
     MRSAYTILAD DSAIEKPLLD DRSYRFIKLD SNDLHVLLIS DPSTDRSAAS LDVHVGSFAD
     KEYNVSGLAH FCEHLLFMGT SKYPEENEYS SYLSKHSGHS NAYTAAEHTN YFFEVSSDYL
     EGALDRFAQF FIDPLFSKSC KDREIRAVDS ENKKNLQNDM WRFYQLDKST SNPKHPYNGF
     STGNYKTLHE EPVSRGVNVR DVLLDFYKDH YSSNIMSLVV LGKDSLDDLN YWAITKFSDV
     PNANLSRPSY QGQLIYTPEN MGKLLKAKPI MDSNKLELTF MIPDDQEHNW DRRPGSYYSH
     LIGHESKGSI LYYLQKKNWV NELSAGNMKV CDGCSLFSME LDLTPSGLEN WQEIVVHVFE
     YLKMIQSQDP PEWLWKELSD MSKINFRFKQ KERTSNTVSK LSSSLFKFKE DYYIPPERLL
     NCTVLRDFDA EEIKKYGRHL NPSNLRISLS SQHLDDLPNT EKWYGTEYAY EDIPSELMDA
     LKSATVNPEL HLPAPNKFIP EDFTVKGEKS EKALAHPWLI TDTPKFEVWF KQDDRFRIPK
     GSISLVVHAP PLGETIESSV LGLLLGELME DEFNEMNYFA ELVGLNFSLS QFRDSFSIKA
     SGYNDKLPAF LVEVLNKFVN FEPKSDRFES IKYKITQDLK NSGYDIPYAQ IGTHFLQLLN
     ENTYPDPEKV KVLEKVTFDD LLKFTKEQLW TKGVFVQALI HGNFEYSTAK KVSQDLEDAF
     NNREQIAETK AAVDDIVRFQ SVKLDVGENV RYELPLQDPS NVNSCLEYFI QVGKVEKDNA
     RLRVLTDLLA TMLHEPCFNQ LRTKEQLGYV VFSGYRSTRS YFGLRVLVQS ERPCDYLQYR
     VERFLEMFKE QKLGSALTDE VFTKYKQSLK NMKLAKLKNL GEETSLYWNA INNGFYDFQQ
     KTNDVEILET ITQQELVDFF NDYFDVSGSS KSAHLTVCLN SRKTPVFDDK KNFITAVHNF
     IYETRSSVPT ESIDKIVEEK GIDINAVAEA VCGTQGDKSK FVKEIEERTK NPTPTSYPKG
     KLEEDTYHFK ESHPRGGAPT PVLPLSKYYY PHEEAHL
//
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