ID   A0A1V2L4W8_CYBFA        Unreviewed;       961 AA.
AC   A0A1V2L4W8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=A-factor-processing enzyme {ECO:0000313|EMBL:ONH66952.1};
GN   ORFNames=BON22_2966 {ECO:0000313|EMBL:ONH66952.1};
OS   Cyberlindnera fabianii (Yeast) (Hansenula fabianii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=36022 {ECO:0000313|EMBL:ONH66952.1, ECO:0000313|Proteomes:UP000189513};
RN   [1] {ECO:0000313|Proteomes:UP000189513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=65 {ECO:0000313|Proteomes:UP000189513};
RX   PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA   van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT   "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT   and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT   Zimbabwe.";
RL   Genome Announc. 5:E00064-E00064(2017).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:ONH66952.1}.
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DR   EMBL; MPUK01000005; ONH66952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V2L4W8; -.
DR   STRING; 36022.A0A1V2L4W8; -.
DR   VEuPathDB; FungiDB:BON22_2966; -.
DR   OMA; WIFDEMK; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000189513; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; IPR001431; Pept_M16_Zn_BS.
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.
DR   PROSITE; PS00143; INSULINASE; 1.
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:UP000189513};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          31..166
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          192..370
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          377..658
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          661..844
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   961 AA;  109579 MW;  9B508F8EB316D9D7 CRC64;
     MTFHKSNNIE KPDLDNREYK FVKLPNDLTA LLISDPKTDK SAAALDVNVG AFSDYEHLPG
     LAHFCEHLLF MGTKKYPSEN EYSSFLSNHG GHSNAYTAAE DTNYYFEVNH QYLEGALDRF
     AQFFISPLFD PSCKDREIRA VDSENKKNLQ NDTWRLYQLD KALSNPVHPY HKFSTGNLQT
     LGEIPTSQGI DTREELLKFY KDYYSSNLMK LAVIGREDLE TLEKWVLEKF SDVANYNRPK
     PTFEGAVFTD KQLKKLIKAK PVMTKNKLSI AFVAPDHDLH WDVQSSHYYS HLLGHEGNGS
     ILAYLKEKGW ANGLSAGGYT ISKGNGTFGV DIDLTEDGIS HYEEILVVLF QYLNLLKREG
     AHQWIYNELQ EVSEMNFKFK QKSSPSSTVS KLAKDMQQAQ IPPEFLLSKT VMRKFDADLI
     KEYGEYLSLD NLRVSLISQS VETDKKEKWY GTDYAIDDLS PELCAKLANA GTNSSLYLPT
     KNDFIPTSFE VEKTDVAEPS KKPVLLKDTE QFRFWHKKDD QFWVPKAIVE LFLNLPSVTA
     TPYSTVMTSL YVDLVQDKLI DVSYNAEIAG LNFWMHTGKE GIILNIDGYN EKIDVLLKEV
     LKSLVSFEPK KERIDVIKEK TIRNLKNAGY KVPYQQITSV FLNLVNERTY DNEERLAALQ
     NITFNDLQHF IPSIFKQAHV EGLIHGNIRT EEANQIAKVV EETLVDSKTL FGDQLSKPRT
     YLLPEGKTFR YDKFLPDEKN TNTCVQYFIQ LAQVTDISAF ALGDMVAQLI REPAFDTLRT
     KEQLGYIVFS GLVETRTTFG LRVLIQSERN AAYLESRIVN FLNQYKNILD EMTDEEFEKN
     KEALINKKLE SLKNLGQENS RFTRAITCGY YDFLHNDVIA DHLRKLTKSQ VQKFYTEKVV
     HGSAKLIVNL HARASTDTEE VAGFPTGIAV ESAGALKSQL YLTPAPMPAE EITPKNFGPK
     L
//