KEX1_EMENI
ID KEX1_EMENI Reviewed; 631 AA.
AC Q5BDJ6; C8VRU1; Q7SI81;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Pheromone-processing carboxypeptidase kex1;
DE EC=3.4.16.6;
DE AltName: Full=Carboxypeptidase D;
DE Flags: Precursor;
GN Name=kex1; ORFNames=AN1384;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=12949156; DOI=10.1099/mic.0.c0119-0;
RA Dyer P.S., Paoletti M., Archer D.B.;
RT "Genomics reveals sexual secrets of Aspergillus.";
RL Microbiology 149:2301-2303(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
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., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., 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.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., 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 [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
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 -!- FUNCTION: Protease with a carboxypeptidase B-like function involved in
CC the C-terminal processing of the lysine and arginine residues from
CC protein precursors. Promotes cell fusion and is involved in the
CC programmed cell death (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential release of a C-terminal arginine or lysine
CC residue.; EC=3.4.16.6;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA65214.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BK001295; DAA01786.1; -; Genomic_DNA.
DR EMBL; AACD01000019; EAA65214.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001308; CBF87602.1; -; Genomic_DNA.
DR RefSeq; XP_658988.1; XM_653896.1.
DR AlphaFoldDB; Q5BDJ6; -.
DR SMR; Q5BDJ6; -.
DR STRING; 162425.CADANIAP00001223; -.
DR ESTHER; emeni-q7si81; Carboxypeptidase_S10.
DR MEROPS; C98.001; -.
DR EnsemblFungi; CBF87602; CBF87602; ANIA_10184.
DR EnsemblFungi; EAA65214; EAA65214; AN1384.2.
DR GeneID; 2877162; -.
DR KEGG; ani:AN1384.2; -.
DR VEuPathDB; FungiDB:AN10184; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_0_1; -.
DR InParanoid; Q5BDJ6; -.
DR OMA; EMADQFV; -.
DR OrthoDB; 607679at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus; Hydrolase;
KW Membrane; Protease; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..631
FT /note="Pheromone-processing carboxypeptidase kex1"
FT /id="PRO_0000411920"
FT TOPO_DOM 36..520
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..631
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 477..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 449
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 631 AA; 70870 MW; B457AC0F569D3442 CRC64;
MGLLSFRQPS WRISRSQFYP IWALSQLLLN PIAVLAQSAA DYYVESLPGA PEGPLLKMHA
GHIEVDPEHN GHLFFWHYQN RHIANRQRTI IWLNGGPGCS SMDGALMEIG PYRLKDNETL
EYNEGSWDEF ANLLFVDQPV GTGFSFANTN SYLHELDEMA AQFITFLEKW FAVFPEYERD
DIYIAGESYA GQYIPYIAKA IQDRNKDIHE KQSSSARWNL RGLLIGNGWI SPAEQYPAYL
SFAYEEGLVE EGSKLGKELE TLLSICKSKM ETGPKISITD CEAVLNKLLD KTVDSNNQCI
NMYDIRLRDG SCGTTWPPDL VDVKPYLHTY EVIQALNISP EKESGWDECD GNVGAAFRPQ
KSEPSVKLLP GLLESGIEIL LFSGDKDLIC NHVGTEQLIS NMKWAGGTGF ETSPGVWAPR
HDWTFEDEPA GYYQYARNLT YVLLYNASHM APFDLPRRTR DMVDRFMHVD IASIGGAPAD
SRIDGEPLPQ TSVGGQPNST VHQEEEQQKI KETEWNAYAK SGEAVLVVVI IGVLVWGFLI
WRSRRRHNGY SGIAIKSPSR TSIMGRFHNN HSNGADVEAG DFDEAELDDL HSPGLDRENY
AVGEDSDDEA HRQDLPRAQE SSSKSENNLV T
