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Database: UniProt
Entry: A0A0A7CN57_9STRA
LinkDB: A0A0A7CN57_9STRA
Original site: A0A0A7CN57_9STRA 
ID   A0A0A7CN57_9STRA        Unreviewed;       953 AA.
AC   A0A0A7CN57;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Carbohydrate-binding protein {ECO:0000313|EMBL:OQR94062.1};
DE   SubName: Full=Secreted protein {ECO:0000313|EMBL:AIG55859.1};
GN   ORFNames=ACHHYP_01876 {ECO:0000313|EMBL:OQR94062.1};
OS   Achlya hypogyna.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Achlya.
OX   NCBI_TaxID=1202772 {ECO:0000313|EMBL:AIG55859.1};
RN   [1] {ECO:0000313|EMBL:AIG55859.1, ECO:0000313|Proteomes:UP000243579}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 48635 {ECO:0000313|EMBL:AIG55859.1,
RC   ECO:0000313|Proteomes:UP000243579};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
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DR   EMBL; KM038398; AIG55859.1; -; Genomic_DNA.
DR   EMBL; JNBR01000378; OQR94062.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A7CN57; -.
DR   STRING; 1202772.A0A0A7CN57; -.
DR   OrthoDB; 52988at2759; -.
DR   Proteomes; UP000243579; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd01100; APPLE_Factor_XI_like; 5.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 5.
DR   InterPro; IPR000177; Apple.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   InterPro; IPR003609; Pan_app.
DR   PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR47190:SF5; PX DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   Pfam; PF14295; PAN_4; 5.
DR   SMART; SM00223; APPLE; 5.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000243579};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..953
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002038118"
FT   DOMAIN          279..293
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   REGION          624..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..737
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   953 AA;  99538 MW;  2F8D8CCAF538D5F7 CRC64;
     MGNHISHSIA TVAILTCTVV GDTYDVIVIG SGPGGLVASE FLSRNASLSV LVLEAGGPSL
     QASGGTDVPG YAAVQGLTRF DIPGEYSNVA FQSDNKYRMN TDWIASPANL WLGKVVGGSS
     SLNGMLYFQT PDSYVTEASW PYNAASVAAG YTAIEQTFSY TNNPSPDGQR YLQEAYTIVG
     SALAAGGYKE SAALNSDRNA KSKSFGHPPF AIKDGLRNSP AKTFLGAAKG RSNFKLITGA
     TVQYIVQSKG QASGVVYQQN GNTITVNLSA RGAVVVAGSA VMTPKILMQS GVGPKSQLQL
     LANTGAFPGV SKDASTWAVN ENVGNSLFDT HQLLMTFSRS DMKTFLHSQS PSAAIQQYMT
     SGHSGPWASP DPVLMAYENY NINGRDYQFQ VTTFCHGFNG GTQNDLGVAV YVNNPVSRDA
     ARFTPDGKYH LDTSRSMYND QRDTTAMANF VDKLRSMLSK QGVREVGPSA TLSSLNLVQS
     RVEGANHYGG SCYTSGDGSD SSRCADETFR VVGTKNIFVG DGSLMKTGTV NPYGFIMYAG
     YQTGVNVAKA VGSYSSVTPP PATCTAYEND VDYYGNDVGS TQRASADFCC SDCVAQSGCT
     VYVWNSHNGG TCWLKSKRGT KSALPGAKSA SVGSATPTPP PAPGSCSAFE NDVDYYGNDV
     GSTQRSSADS CCADCAAKPG CTLYVWNSHN GGTCWLKSKR GAKSTLLGAR SGSLGTTTPT
     STPVTPSPTP SPTTSPTPAP GSCSSFENDV DYYGNDVGST QRANAKFCCA DCAAKPGCTL
     YVWNSHNGGT CWLKSKRGTK STLPGAKSGA IAATNPICGI PEPATDFTGQ DVANVPGSSP
     GDCCTACQNN KACNAWSLWN NVCWLKSGHN GRKAAPGTIA GIVNKCSILE VGVDYVGNDI
     AQAAAVVADD CCAICRNTNG CGAFSWYQGM CYMKSSKGAT KANGGVISAS VVQ
//
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