ID A0A1X0RW98_RHIZD Unreviewed; 1127 AA.
AC A0A1X0RW98;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=A-pheromone processing metallopeptidase Ste23 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BCV71DRAFT_19532 {ECO:0000313|EMBL:ORE16325.1};
OS Rhizopus microsporus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=58291 {ECO:0000313|EMBL:ORE16325.1, ECO:0000313|Proteomes:UP000242381};
RN [1] {ECO:0000313|EMBL:ORE16325.1, ECO:0000313|Proteomes:UP000242381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11559 {ECO:0000313|EMBL:ORE16325.1,
RC ECO:0000313|Proteomes:UP000242381};
RX PubMed=27956601; DOI=10.1073/pnas.1615148113;
RA Lastovetsky O.A., Gaspar M.L., Mondo S.J., LaButti K.M., Sandor L.,
RA Grigoriev I.V., Henry S.A., Pawlowska T.E.;
RT "Lipid metabolic changes in an early divergent fungus govern the
RT establishment of a mutualistic symbiosis with endobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:15102-15107(2016).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; KV921389; ORE16325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0RW98; -.
DR VEuPathDB; FungiDB:BCV72DRAFT_203143; -.
DR OMA; WIFDEMK; -.
DR Proteomes; UP000242381; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000242381};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 82..218
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 245..422
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 429..714
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 718..897
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1074..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1016..1051
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1082..1097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 129869 MW; DB066B158B4CDA59 CRC64;
MFRLFTLSCL HSIRPYPLHN SRSRLLFRSA SEMITTKEIP SSSTSDWELV GSYWLYKKPL
EKSDNDDRDY RLIKLASNEL QVLLVHDKST DKASAALDVH VGHISDPPTL QGLAHFCEHL
LFMGTEKYPK ENDYNQYLSE HSGFSNAFTS VEDTNYYFEV AHSHLEGALD RFAQFFISPL
FSDSCTEREL KAVDSEHKKN KQQDSWRIFQ LEKSLCNPSH PYCNFGTGNL ETLYENPKAN
GQDIRQELLK FHDTYYSANI MKLCILGRES LDQLTEWAVE KFKDVRNKNI EPPSFPDNPL
TKKELMKQIF IKPVKDVRIL EMTFPFPDQR PLYAVQPGRY LSHLIGHEGH GSILSLLKKN
GWANYLQVAT SHGGIGFEFM RISIDLTEEG LNRYKDVVVI VFKYIDLLKK KGIQSRIFEE
VQSLASLAFR FKEKQRPSQY TSRVAGLMQH GYPSQYILSG PSLIRHYDPD LIKENLNWLR
PDNFRILLAC QNPPGGVQFT QKERWYQSEY TVIDFDNDFI NSLENLEPEN ALVLPGKNAF
IPTNFEMNKK EVETPATKPD IVENSPLLRL WHKKDDTFWV PRANVWILLR SPLAYATPSN
CVKTRLYADL LKDSLNEYAY DAEVAGLAYT IENQLEGMLL AIGGYNDKLP VLLEKVVQKM
RNFEVDIERF KLLKEQLLRI YKNFALEPPY QHALYYHSYL TQDTMWTNAE KLKELEMITA
EDVQSFYPSL ISRLHIEALV HGNFSREDAQ KMLHDTIDIL KPKALQPSEL IGNRSLTLPH
GSKWVYQRDV EDPNNVNSGI EYVIQVGNIT ETSLRAKLTL LAQIAQEPCF DQLRTKEQLG
YLVFSGVRKQ VGSMGLRFIL QSERDTIYLE NRIEDFLDKL RALVEKMTPE EYDAQVQSVI
TKKLEKDKNL AQEGSKYWSH IHSGFYEFDQ AEKDIKELKE IKKEDLLAFM SEYIDPCSSK
FRKLSVHIQS QKAQTAQPKK FKVNIESLHT CLVSQGVTRL SIEDIRSAVE KGDAGEASIE
ANLRELLTDE TKAEEEEIEA LMAKLVTAMR ETESVDGSLV NVKSQKTARR LSMVSRQLNN
NDSDQDQKER DHTKLPEGNK IVTNVREFKN SLELSPAPCP LIDFQVI
//
