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Database: UniProt
Entry: A0A024GIK0_9STRA
LinkDB: A0A024GIK0_9STRA
Original site: A0A024GIK0_9STRA 
ID   A0A024GIK0_9STRA        Unreviewed;      1325 AA.
AC   A0A024GIK0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Glycoside hydrolase family 5 domain-containing protein {ECO:0000259|Pfam:PF00150};
GN   ORFNames=BN9_076730 {ECO:0000313|EMBL:CCI46718.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI46718.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI46718.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI46718.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
CC       {ECO:0000256|ARBA:ARBA00007528}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCI46718.1}.
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DR   EMBL; CAIX01000138; CCI46718.1; -; Genomic_DNA.
DR   STRING; 65357.A0A024GIK0; -.
DR   InParanoid; A0A024GIK0; -.
DR   OrthoDB; 52366at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0005840; C:ribosome; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR004886; Glucanosyltransferase.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR001684; Ribosomal_bL27.
DR   PANTHER; PTHR31468; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS1; 1.
DR   PANTHER; PTHR31468:SF2; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS1; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF03198; Glyco_hydro_72; 1.
DR   Pfam; PF01016; Ribosomal_L27; 1.
DR   PRINTS; PR00063; RIBOSOMALL27.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   SUPFAM; SSF110324; Ribosomal L27 protein-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1325
FT                   /note="Glycoside hydrolase family 5 domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025528849"
FT   DOMAIN          98..322
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   REGION          164..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          816..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1285..1314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1297..1314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1325 AA;  148666 MW;  27B09B5769B761C8 CRC64;
     MMRMTRFKFT SLVWTIFCFN CADVNGQHIQ EAIRRGSVAV KGVNLGGWLV AEYWMTYDSV
     IWKDVPEATR LQGEHATMTF LGHDRGDGRF EEHRSTWITE EDIKELSGRG LNCVRVPVGY
     WIKDSDVTPS IFAPGGLKYL DNLIFNWANK HNVAVLISFH AHRGSQNGRD HSATPVQGKA
     QWSDNPSNVE NSIEVATFLA DRYKNSPAFL GLGMMNEPEY PTKPDVVRSY FTRTLNMIRA
     SGNTCVLVTA PMLSEQRSPY YEDFMKNAPN VWHEWHPYYK WGYEGKTEGQ IIQAAANYEN
     AVRNWQGNPL TISEWSMGTH EQSAPFNDIS EYKNFGQTML QSFKTARGGV HQSMVKYTQL
     LALGASALTM HPAATSGDEN TTASSTNPLV VKGYRFFDSV SGDYFAFSGV NYYPRPNAGS
     LDINNFDFFT SNYSHMWQRD LPKFTALGAN SIRLYAVDPT QDHDTFMCAL QAEGIYVMVE
     LGSSCEGCEI TAKKAPDCYT ASYKERGERI IQAFAKYDNV VGFSGGNEIN HRVGSNGPEW
     NAPCQKKFIR DMRAYIKSCP TMRQIPVGVV MADTHRKENA QYYNCRTDPS DDLENVEWYG
     LNVYIQCDDI ADPKMATGFN NLAQDLSTLN YSVPLILTEF GCLSPAFPSV NGYEGQRTHH
     DARFMNMDPY TKVLNGGFVF EYNTEMANAR STSPYPFTKF GPQNYGLGYF SPANCDDINV
     PCVYNEMPNF EFLADAYKST DTSSEPNFDS FSIEANRQET SECPAAFPKL SAFTWASDGA
     ESIKCPATTR LQCPNAKPNQ KVTKVTKKRL VILKNSSTSE ASGSSESEAK DNSAENDLND
     VAVVKDENAE TSSDCGSGES CGENSVHDSE ARFVVNVSRN AIQECFAVAY GDSETIRIYA
     SSSAMLLHEF SIIHAHLHAM LYTSFADSIV TLESDNDSDD EIYLCVYHDW REKDLVRGYK
     LPLGVTLQAH PVPLSSLLAV CTVTGRIAVA MDSVINLWQC SHGFFHHILE LSVHFTNSET
     SPYIQDIAIH DKYIAVTSPV ELLILQIHFH DRQQPIQSVC DRISDDIKAQ SGEENESQSL
     NQVPPDDIQC VKIRSAEDLR HLTKITVTSR ARGRLDPITG LRKLKAGKRS PKERKINNRA
     SFTDRKIQNV IVMESETEEA SLLKGTIKPS DVRMNQTLSY YTTINDIETL LRRYFPRNHS
     VRNLQFLPET ITYEGVIAVK MQRYPRVLST TMETCFSLLS DQEARIKNGR DSESKRLGVK
     KFGGQAVNPG NIIIRQRGTK YHPARGVGIG KITPFSRSGK DRNTPQRLVP SMQQQSTLLC
     DNIQS
//
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