ID F0WX44_9STRA Unreviewed; 584 AA.
AC F0WX44;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Serine protease family S10 putative {ECO:0000313|EMBL:CCA26034.1};
GN Name=AlNc14C342G10802 {ECO:0000313|EMBL:CCA26034.1};
GN ORFNames=ALNC14_121780 {ECO:0000313|EMBL:CCA26034.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA26034.1};
RN [1] {ECO:0000313|EMBL:CCA26034.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA26034.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431}.
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DR EMBL; FR824387; CCA26034.1; -; Genomic_DNA.
DR AlphaFoldDB; F0WX44; -.
DR ESTHER; 9stra-f0wx44; Carboxypeptidase_S10.
DR MEROPS; S10.A68; -.
DR EnsemblProtists; CCA26034; CCA26034; ALNC14_121780.
DR HOGENOM; CLU_008523_11_3_1; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR PANTHER; PTHR11802:SF190; PHEROMONE-PROCESSING CARBOXYPEPTIDASE KEX1; 1.
DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CCA26034.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:CCA26034.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..584
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003259635"
FT TRANSMEM 520..541
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 584 AA; 65551 MW; 1EFF6885120310D3 CRC64;
MRLWQVFASV SIITIHAARI TPPSNKHFLS QNHPSEPTEL STEISKATSD RIETLPGLNE
DIVVDHHAGL ITLDSGVNDR LFYWHFNAYK SPEKAPLIIW LNGGPGCSSM EGLFYGISPF
YLDKGEGIRT NPHSWLNTAN MLFLDQPVGT GMSSTHKNEH RVDEETLAKD FREFLIKFLK
LHPEYLSLSS DKPAISRPIY IFGESHAGRY IPQFSQHILE QNLDTKDIHI SLHGVGIGNG
WVHPIIQYDY SEFAHGIGLI TLGQVRELKA IYAKCIADLN ISFYSRTCLD NIDTIIDSVS
NSRVNRLNQY DVRMFMESSQ EYPAGLNHMT EYLNRLDVRK ALHANTDQSF RYNQCSSRVH
TSLLKFDGVS SLKNVDFLLE NGVQVLFYNG QWDMVCNPYN TEKLLLFLEW KGSQEFHGSE
KFTWMVKGQQ EPAGYAQHGG NLTYLVVAGA GHMVTYNVPA VALDMVDRFI HGKGFADQKQ
SVASIYTNSS HLASYQCPSV EDLQAVSALF HSGKSFATAL WIWIVILMTL LSAAISSIAT
ASCMRSRISQ GLEHCVLLDQ DENELLKDQT VEVGAMAGDT KEPM
//
