ID Q5AUI6_EMENI Unreviewed; 1100 AA.
AC Q5AUI6; C8V608;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 24-JAN-2024, entry version 103.
DE SubName: Full=A-pheromone processing metallopeptidase Ste23 (AFU_orthologue AFUA_5G02010) {ECO:0000313|EMBL:CBF73765.1};
GN ORFNames=ANIA_08044 {ECO:0000313|EMBL:CBF73765.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF73765.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; BN001302; CBF73765.1; -; Genomic_DNA.
DR RefSeq; XP_681313.1; XM_676221.1.
DR AlphaFoldDB; Q5AUI6; -.
DR STRING; 227321.Q5AUI6; -.
DR MEROPS; M16.008; -.
DR EnsemblFungi; CBF73765; CBF73765; ANIA_08044.
DR GeneID; 2869155; -.
DR KEGG; ani:AN8044.2; -.
DR eggNOG; KOG0959; Eukaryota.
DR HOGENOM; CLU_004639_1_2_1; -.
DR InParanoid; Q5AUI6; -.
DR OMA; WIFDEMK; -.
DR OrthoDB; 129328at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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; 1.
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:UP000000560};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 35..200
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 226..405
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 411..698
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 703..883
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 118..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1100 AA; 125137 MW; 2C812739FD181D4B CRC64;
MTMRSAERLT EGLEKPSLDD RSYRVIQLPN KLEALLVHDP ETDKAAAAMD VHVGSFSDPA
DLQGLAHGLE HMLFMGTEKY PVENAYNQYL ASHSGSSNAY TAGTETNYFF EVSATGATGE
SSGQVTPNGT TNGTSAESKS NGPSPLYGAL DRFAQFFISP LFLENTLDRE MQAVDSENKK
NLQSDLWRLM QLNKSLSNPD HPYNHFSTGN LQTLKEEPQK RGVEIRNEFM KFYEKHYSAN
RMKLVVLGRE SLDELEKWVS ELFAGVSNKD LPQNRWDGIP IWLPNDMCKQ IFAKPVMDTR
SVDIYFPFLD EEKLYESQPS RYISHLIGHE GPGSILAYIK AKGWANGLSA GVMPVCPGAA
FFTVSVRLTQ EGLQQYQQVV KVIFEYIAMI KEREPEAWIF EEMKNLAEVE FKFKQKSPAS
RFTSRLSSVM QKPLPREWLL SGSLLRKFDP EAIKKALSYL REDNFKLIVV AQDYPGDWDT
KEKWYGTEYK VEDVPKDFMS GIRAALDTTP ETRLKELHMP HKNEFVPTRL SVEKKEVSEP
QKTPKLIRHD DHVRLWFKKD DRFWVPKATV FVTLRNPLVW ATPANLVKSK LYCELVRDAL
VEYSYDAELA GLDYHLSASI FGLDISVGGY NDKMAVLLEK VFTSMRDLEI NPDRFRIIKE
RLTRSYKNAE YQQPYYQVGD YTRYLTAERG WLNEQYAAEL DHIEAEDIKC FFPQILRQNH
IEVLAHGNIY KEDALRMTDT VESILNSRTL PQSQWYVRRN VIIPPGSDYI YERPLKDPAN
VNHCIEYYLF IGSIADEVLR AKLLLFAQMT DEPAFDQLRS KEQLGYVVWS GARYSATTIG
YRVIIQSERT AQYLESRIDS FLSNFGKTLE TMTEDEFEGH KRSVINKRLE KLKNLSSETS
RFWSHIGSED YDFQQNETDA ARVRALTKSD ILDFYKQMID PASPTRGKLS IHLKAQAGAH
AVELKEQKAR LLSFVTKQLE AAGFAADSDS LGIALEGVSP GDKEQVLSVL KTFLTSTLNL
SEQQVGPALE TIGQNFGLMS KQLGVESKQG SEGSSLTNRT KAARPTYITN VADFKARLAV
STGPNPITNL TEFEDFEAKL
//
