ID D4AX96_ARTBC Unreviewed; 1233 AA.
AC D4AX96;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=A-pheromone processing metallopeptidase Ste23 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ARB_00823 {ECO:0000313|EMBL:EFE32301.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE32301.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE32301.1}.
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DR EMBL; ABSU01000016; EFE32301.1; -; Genomic_DNA.
DR RefSeq; XP_003012941.1; XM_003012895.1.
DR AlphaFoldDB; D4AX96; -.
DR STRING; 663331.D4AX96; -.
DR GeneID; 9523019; -.
DR KEGG; abe:ARB_00823; -.
DR eggNOG; KOG0959; Eukaryota.
DR HOGENOM; CLU_004639_1_2_1; -.
DR OMA; WIFDEMK; -.
DR OrthoDB; 129328at2759; -.
DR Proteomes; UP000008866; 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; 2.
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:UP000008866};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 125..206
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 262..316
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 343..521
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 527..813
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 819..998
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 209..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1233 AA; 138908 MW; 2D7F01E39B974935 CRC64;
MPPRFLTRRL HIPASRRPPL FTAGPAALVR PSSTQPVVPS IPPPLLLLGQ PPARFPRSSL
AFLQRGASLY TTTATATPRY SESPEDKSSS PVMAQVERLA DSLEKPSVDN RTYRVIRLPN
QLEALLVHDP DTDKASASVN VNVGNFSDDD DMPGMAHAVE HLLFMGTEKY PKENDYNQYL
ASHSGHSNAY TAATETNYFF EVAATSHPRS KAPSATPSAV PSAPPSQAPT PGGILADKMS
HLTVEGAPNS ASSSISDLTP PLYGALDRFA QFFIAPLFLP STLDRELQAV DSENKKNLQS
DPWRMLQLNK SLANPKHPYS HFSTGNLKTL RDDPQARGLD VRSEFMKFHD KHYSANRMKL
VVLGREPLDE LEAWVAELFA DVKNKDLPQN RWDDIEVFEK ENLLKMVFAK PVMDSRTLDI
YFPYPDEEDL YESQPSRYIS HLIGHEGPGS ILAYIKSKGW ATELSAGATP LSPGSSLFNI
SIRLTEDGLQ HYQEVVKIIF QYISLIKERA PEQWIFDEMK NLSEVDFKFK QKSPASKFTS
SLSSVMQKPY PREWLLSGSS LLRKFEPELI TKGLSYLRAD NFNIEIVSQH FPGGWDKKEK
WYGTEYKVEK VPEDLLSEIR RSLETSTGRT SELHMPHKNE FVPTRLDVEK KEVDQPAKRP
SLIRRDDQVR TWFKKDDTFW VPKAALEITL RTPLVYATPG NNVMAKLYCS LVRDALTEYS
YDAELAGLDY DLSPSVFGLE VAIVGYNDKM AVLLEKVLTI MRDLEIKPDR FRIVKERMAR
GYKNADYQLP YYQVGSFTRY LTAEKAWINE QLAPELEHIQ LEDVAAFYPQ LLRQTHIEVL
AHGNLYKEDA LKLTDLIEST LKPRVLPQSQ WHVRRNMIIP PGSNYIYEET LKDPANINHC
IEYYLFVGAL TDAQLRAKCL LFGQMTNEPA FDQLRTKEQL GYVVWSGARY SSTTLGYRVI
IQSERDNQYL ESRIDSFLEG FGEALTSMSD EEFEGHRRSI INKRLEKLKN LSSETSRFWS
HIGSEYFDFT QHEIDAAVLE NLTKDDIIAF YRQYIDPNSP TRAKLSVHMK AQASASLVAS
AEQKSAVLAK IEQFLGSAGA LVDTEKFKEA FKDITISSNN LDGIISTVHN HLTSVLQMAE
DEATKLLEPA KGALPALLAQ AGIKTVTNSD NESKSKEDPT PTANGTSNSA DKPSSRKPIY
ITNVPEFKAR LSVSPATAPV VDLSEFEDFD PKL
//
