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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//