ID   A0A068S4R4_9FUNG        Unreviewed;      1140 AA.
AC   A0A068S4R4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=A-pheromone processing metallopeptidase ste23 {ECO:0000313|EMBL:CDH56832.1};
GN   ORFNames=LCOR_07838.1 {ECO:0000313|EMBL:CDH56832.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH56832.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH56832.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:CDH56832.1}.
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DR   EMBL; CBTN010000041; CDH56832.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068S4R4; -.
DR   MEROPS; M16.020; -.
DR   VEuPathDB; FungiDB:LCOR_07838.1; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000027586; 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:UP000027586};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          94..230
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          257..434
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          441..726
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          730..910
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1089..1116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1090..1116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1140 AA;  130149 MW;  81856B1D780C9C79 CRC64;
     MPTLAPRILS LLNRRCSSLN FTTTAHRQQP LTTKRFSFIR SVSTMPGPTT AESPSDWALS
     SNGKYWTFTR PLEQSDNDDR KYRLIKLASN DLQVLLIHDA DTDKSSAALD VHVGHLSDPD
     DLQGLAHFCE HLLFMGTEKY PKENDYNQYL AEHSGFSNAF TGVENTNYYF EIGHEYLGGA
     LDRFAQFFIS PLFSASCTER ELRAVDSEHK KNRQQDSWRM FQLEKSLSNP NHPYCHFGTG
     NLETLYDSPK AKGQDIRAEL LKFHDNYYSA NIMKLCILGR ESLDQLTEWA VDKFNDVRNK
     GIEPPKFPGH PLTEKELMKQ IFIKPVKDVR SLEMTFPFPD QRPLYAIQPG RYISHLIGHE
     GAGSILSLLK KNGWANYLQV GSIHGGIGFE FLRISIDLTE EGLRSYEDVV VCVFQYINML
     RQSGVQRSIF NEVQSLASLA FRFKEKYPPS QYTSRLAGLM QHGYPAPFIL SGPSLIREYN
     VDIINENLEY LRPDNFRIMV ASQQPPNGAQ FTMREKWYDT EYNVLEFSDQ LKKTLQNLQA
     NDALYLPGKN DFIPTNFETH KKEILQPAKK PELILNNPKT RLWYKKDDTF WVPRANVWIL
     FRSPLAYATP TNCVKTRLFT DLLKDSLNEY AYDAEVAGLA YNIENLLEGM LLAVGGYNDK
     LSVLLEKVVQ KMRDLQVDPE RFKLLKDQLR RSYKNFALEP PYQHALYYLS YFTQDKMWTN
     AEKLRELDAI TAEDIQAFYP TILSHLHLEA LVHGNVLQKD AEDMMNTVIN ILNPRELLPS
     QLIGHRSLIL PPGSKWVYNR QVEDPHNVNS GIEYLIQVGN VTQTSLRARL SLLAQIAQEP
     CFDQLRTKEQ LGYLVFSGVR KQAGSMGMRF IVQSERDTIY LENRIEEFLI KLRSIIVNMS
     DEEYQAQVQS LIFKKLEKDK NLGQEGGKYW THIHSGYYEF DQVDKDVKEL KMISKESLLE
     FFDHHIDPAS DNVRKIAVHI QSQKTPPAPK YKVDIESLHT CLVAQGVNRV SIDDLRTAVE
     KGEAGEASME AVLREMLIDE SKGNEEEIEE LMSKLVTAMG MTEAAAQGNG TINGTFVTVD
     NKKTARRLSA VDGDSSTDSG QQTPVRDHSS LPEGNTIITD PVAFKSRMEL SPAAVPLIDF
//