ID A0A074XCW5_AURPU Unreviewed; 1052 AA.
AC A0A074XCW5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Zinc metalloprotease {ECO:0008006|Google:ProtNLM};
GN ORFNames=M438DRAFT_337950 {ECO:0000313|EMBL:KEQ81559.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ81559.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ81559.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ81559.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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DR EMBL; KL584991; KEQ81559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074XCW5; -.
DR STRING; 1043002.A0A074XCW5; -.
DR MEROPS; M16.A04; -.
DR HOGENOM; CLU_006065_0_0_1; -.
DR OrthoDB; 227593at2759; -.
DR Proteomes; UP000030706; 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; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000030706}.
FT DOMAIN 59..134
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 198..376
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 791..883
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1004..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1038
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1052 AA; 118054 MW; A5FBE9A8219261D9 CRC64;
MPAAKTQTHF KPIQKFKLDY APIDIAQYES ERTGMRVVIV DQKGPKVYGY FTLATEIHDD
SGSPHTLEHL CFMGSKNYRY KGVLDKLATR AYSNTNAWTA TDHTAYTLET AGWEGFAQIL
PVYLEHVLVP TLTDAGCYTE VFHVDGTGHD AGVVYSEMQG VQNQQGELME LQARRLMYPE
GDGFRYETGG MMEQLRVLTA DRIREFHREM YQPKNLCLVL IGEIDQPELL QILDDFEGTI
MEDIPSPEAP FQRPWVESKR TPPLKKTIVD TVKFPEDDES MGEVLVGFLG PDCNDHLQAS
ALGIMLIYLC GSSVSVLENT LVEKEQLCSM IYYSTDVRPD IAFWFNLSAV ETEKLADAEK
RLFEVLKETA SKNLDMGYMK DCLSRYRRQL KFKCESTGDF FATPIIEDHL FGNRDGKDLR
ELETLKDLDI LEGWSDQQWR DYLSMWFADA HHVSILGVPS KELSKKLKVD EKARVKAQKE
RLGEKGLKEL AEKLDQAKAE NDKPIPDEVL SQFPVPGTSS IHFIPTTTAR AGRARQMGKL
DNDIQQIVDK DDSDIPLFIH FEHIPSNFVR TKLIMCTGSL PTELKPLLAV YLSNFFMTPI
ERDGKRIEFE DVVTELEKDT VDYDITSGPG NGELLQITFQ VEAEKYSAMI DWLRTTLFSS
ILDKERLQTA ITKMLADIPD EKRSGMDMAT AVDSMIHLTR DSSSRSRNTL VKSVYLKRLK
KHLAKDPESV ISRLQTCIDT LHKPSNFRVY VAANMHNLSN PVSSWKALLA NHDDNTPLQP
LDSRRSKLSE ISKKPGNTAY IIPLSTIDSS YALLTSRGPD SWSHPDLPAL MVAQSYLDAV
EGPLWAAVRG TGLAYGTGFS RSTDVGLMTL RIYRSPDTFK AFLAAKTEVS NYATGATPFD
KFALEGAVSS IIMGFADEQP TMGSAANLSF VNQVIRGIPK NWNDGMLEKV RKVTEDEIKD
VLKRIIMPIF NPKSTNLVVS CATIMEENLV KNFTDAGFKP EVKSLSDFED DYGLENIDGE
DEDDEDDDEE DGSEDGGEDG SEGGSSSGRG EE
//
