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KEX1_ASPFU
ID   KEX1_ASPFU              Reviewed;         632 AA.
AC   Q4WTK9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=AFUA_1G08940;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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}.
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DR   EMBL; AAHF01000004; EAL90223.1; -; Genomic_DNA.
DR   RefSeq; XP_752261.1; XM_747168.1.
DR   AlphaFoldDB; Q4WTK9; -.
DR   SMR; Q4WTK9; -.
DR   STRING; 746128.CADAFUBP00000820; -.
DR   ESTHER; aspfu-kex1; Carboxypeptidase_S10.
DR   MEROPS; S10.007; -.
DR   EnsemblFungi; EAL90223; EAL90223; AFUA_1G08940.
DR   GeneID; 3510479; -.
DR   KEGG; afm:AFUA_1G08940; -.
DR   VEuPathDB; FungiDB:Afu1g08940; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_11_0_1; -.
DR   InParanoid; Q4WTK9; -.
DR   OMA; EMADQFV; -.
DR   OrthoDB; 607679at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
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..38
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..632
FT                   /note="Pheromone-processing carboxypeptidase kex1"
FT                   /id="PRO_0000411904"
FT   TOPO_DOM        39..523
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        524..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        545..632
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          480..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..632
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        390
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        452
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   632 AA;  70499 MW;  AFF7584F825F78C1 CRC64;
     MLLTTPSSRG SRAQSGIANV SWLALSLLLL FSPTLGSAKS AADYYVRSLP GAPEGPLLKM
     HAGHIEVDAQ NNGNLFFWHY QNRHIANRQR TVIWLNGGPG CSSMDGALME IGPYRLKDNH
     TLEYNNGSWD EFANLLFVDQ PVGTGFSYVN TNSYIHELDE MSAQFITFLE KWFQLFPEYE
     GDDIYIAGES YAGQHIPYIA KAIQERNNKI QNDQSIRWNL RGIVIGNGWI SPAQQYPSYL
     TFAYEEGLVT KGSSLAKDLE VYQSVCESKI SASPNAINIR DCEEILQQIL ARTKDTNKQC
     YNMYDVRLRD TYPSCGMNWP TDLVDVKPYL QRPDVVQALN INPEKKSGWE ECSGAVSSTF
     NAANSLPSVQ LLPELLESGI PILLFSGDKD LICNHVGTEQ LINNMKWNGG TGFETSPGVW
     APRHDWTFEG EPAGIYQYAR NLTYVLFYNA SHMVPYDLPR QSRDMLDRFM KVDIANIGGK
     PADSRIDGEK LPQTSVGGHP NSTAAEQQAK EKIKETEWKA YAKSGEAALI VVIIGVTVWG
     FFIWRSRRRN RGYQGVYQRD IGSGSILERF HNKRSGPADV EAGDFDESEL DNLHSPGLEQ
     EHYAVGDDSD EESPNHQPAA PPSSTKPGGA QP
 
 
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