ID A0A0M9VMP5_9BASI Unreviewed; 1078 AA.
AC A0A0M9VMP5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Zn2+-dependent endopeptidase {ECO:0000313|EMBL:KOS12449.1};
GN ORFNames=Malapachy_2754 {ECO:0000313|EMBL:KOS12449.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS12449.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS12449.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS12449.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOS12449.1}.
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DR EMBL; LGAV01000013; KOS12449.1; -; Genomic_DNA.
DR RefSeq; XP_017990081.1; XM_018137242.1.
DR AlphaFoldDB; A0A0M9VMP5; -.
DR STRING; 77020.A0A0M9VMP5; -.
DR GeneID; 28729117; -.
DR VEuPathDB; FungiDB:Malapachy_2754; -.
DR OrthoDB; 227593at2759; -.
DR Proteomes; UP000037751; 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:UP000037751}.
FT DOMAIN 64..145
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 202..410
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1050..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1078 AA; 118767 MW; 164C1F37AEDB0634 CRC64;
MTSDATQHIG AFRRLAQERL PYAPEMVVEK WRSTKSGLTV LWANFESPML NAYITVASEI
FADSGVPHTL EHLVFLGSQQ YPYKGVLDSL ANRAFAQGTN AWTANDHTAY TLTTAGADGF
LRMLPVYCDH VFFPTLTDAG FVTEVYHING KLEDAGVVYS EMQGRENSCA DLMELKTQRM
LYPRTSAYRS ETGGLMSALR VLTIDDIRLY HKTYYTPHNA ALVLCGPLDR TALFETLQAI
DQCFLEQGAA HGEYGPPGWR RPFVETPSAV PPVIDGRQLH CEGVDDADPP MDPRRRRVFI
DFPEKDESVG EVQISWVGPP LDATLDLHAL DVLGTYLTDS PVSPMQHTFV EKDEPLCTDI
YFGNNERAGA SVLSASLASV PTAHLDDLDR QLDTLLRDVA KQGLDMSRMH TILRRERERL
LSQLEMRPAD CFSDVLIHEF LYGEREGREL GQALDDMKRF DTLDTYTSDD WVRVLTTYLI
DNPRLVVVGR PSASLVMQLK QETEARVQKR REACGEAGAQ AYEAALQAAR KENDAPIPPA
ILDAFAVPRS DTIQWISVAT AATGPTTDAE PAIPSSPADQ QLQAHIDRDG PATPFSIQFD
HVPSKFVLLS VVISTAHVPR PLRSYLTLYL SMLFSLPIHR VDGTSLSYED VVKHLDEDVL
EYDATIGIGS SFAESIALEF KAPADKYEKA VQWVYDLLWQ SDLALERVKI AAAKLAQSLP
EQKRDGRVIS WALLRSLLYS TTDSTCAANT VLTQAEHVPA LVDALQSRPD EVLAHLQEVR
HALLHPAHMR ISVAGDVHAL AHPVAPWRNV LPTTPCASLT PLPWASDVLN TLGHAPQREG
QLCIVPAIES SYAVFTSKGL RGYTDDDYAP LVVTLTLLNA MESFLWRYIR GAGLAYGASI
RNDAEAQHLH FILYRAPDAA KAFVEARKVI QALAHGTPLD DESVPTFDET MLETAKSSLH
FSVADAESTV GAAALESFVD IRLKRVGRGR GQRLLQRASQ VTLQDVQRCV TQYLLPLFAS
ETSVCAIASA PSTAESIRAQ LMALGYEMTD VDMPGGHASD SSSSSGSDSD SSSESDRE
//
