ID A6QSG5_AJECN Unreviewed; 1158 AA.
AC A6QSG5;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=A-pheromone processing metallopeptidase Ste23 {ECO:0008006|Google:ProtNLM};
GN ORFNames=HCAG_00321 {ECO:0000313|EMBL:EDN02457.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN02457.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; CH476655; EDN02457.1; -; Genomic_DNA.
DR AlphaFoldDB; A6QSG5; -.
DR STRING; 339724.A6QSG5; -.
DR VEuPathDB; FungiDB:HCAG_00321; -.
DR HOGENOM; CLU_004639_1_2_1; -.
DR OMA; WIFDEMK; -.
DR OrthoDB; 129328at2759; -.
DR Proteomes; UP000009297; 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:UP000009297};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 33..114
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 167..221
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 247..426
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 432..720
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 725..906
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 119..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1158 AA; 130603 MW; 2509578C362E5BB0 CRC64;
MAIVERLTED LEKPSVDDRS YRVIRLPNKL EALLVHDPDT DKASASVNVN VGNFSDDDDL
PGIAHAVEHA LFMGTKKYPK ENAYNQYLAA HSGHSNAYTG ATETNYFFEV AATATSVSKS
TQSSTPATPI PAEVEPLTDG LSRPTIPLTA TAADSAVSSS SDLVPPLYGA LDRFAQFFIA
PLFLEATLDR ELRAVDSENK KNLQNDDWRL MQLNKSLSNP KHPYHHFSTG NLQTLRDGPQ
SRGVNVRDEF IRFYETNYSA NRMKLVVLGR ESLDELEGWV AELFADVKNK NLPQNRWDDV
QPYTPADLQK ICFAKPVMDT RSLDIFFTYQ DEENLYDSKP ARYISHLIGH EGPGSILAHI
KAKGWAYGLS AGPIPICPGS AFFTISIRLT EDGVNNYQEV IKTIFQYISI LKSRVPEEWI
FEEMKTLAEV DFKFRQKSPA SGFTSSLSSV MQKPFPREWL LSGPYLLRKF DGQAIQRALD
CFRIDSFNIE LVSQTYPGNW DSKEKWYGTE YRVEKLPTDL LSEIGRILEA PSYNPMPELH
LPHKNEFLPT RFDVEKKEVA QPAKRPTLIR NDDRVRAWFK KDDTFYVPKA SVEIILRNPL
AYATPGNNVL TKLACGLIRD DLQEYSYDAE LGGLDYSLSP SVFGLEVSVS GYNDKMAVLL
EKVLHSMRDF RVKPDRFKIV KQRMADGFSN SEYQQPYHQV GNVTRYLTAE KTWITEQLAA
ELEHIEPGDV AAFFPQLLRQ THIELLGHGN LYREDVLKMG NMVESAFHAR PLPRSQWNVR
RNIIIPPGSN YIYEKTLKDP ANINHCIEYY LFVGDITDPQ LRAKLLLFGQ LTNEPAFDQL
RTQEQLGYVV WSGIRYGATT LGYRVIIQSE KPNQYLESRI DAFLIRFARA LDSMTDEEFE
DHKRSLINKR LEKLKNLNSE MSRFWSHITS EYFDFTQHET DAEKVAGLTK DDIVEFYQQY
IDPQSRTRAK LSVHLNAQSS ATDDERKKKV VEKLSNLVSS SSTEFDSEKF KASFANVNFM
TTDVMTNKDA IVSILRGFLE TELKLDSEKV TSIVEPATHV LNEILQGLEI KAIPSPPSTT
GGAAVPATEK VNVTVNGAIN GTTNGAANGH AVIPAPSSKP GQPAYITNVS EYKARLAVSA
GPSPIVDLSE FEEIDPKL
//
