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Database: UniProt
Entry: A0A2V0NV63_9CHLO
LinkDB: A0A2V0NV63_9CHLO
Original site: A0A2V0NV63_9CHLO 
ID   A0A2V0NV63_9CHLO        Unreviewed;       562 AA.
AC   A0A2V0NV63;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:GBF91229.1};
GN   ORFNames=Rsub_03549 {ECO:0000313|EMBL:GBF91229.1};
OS   Raphidocelis subcapitata.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX   NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF91229.1, ECO:0000313|Proteomes:UP000247498};
RN   [1] {ECO:0000313|EMBL:GBF91229.1, ECO:0000313|Proteomes:UP000247498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-35 {ECO:0000313|EMBL:GBF91229.1,
RC   ECO:0000313|Proteomes:UP000247498};
RX   PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA   Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT   "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT   insight into genome evolution and environmental adaptations in the
RT   Sphaeropleales.";
RL   Sci. Rep. 8:8058-8058(2018).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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:GBF91229.1}.
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DR   EMBL; BDRX01000023; GBF91229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V0NV63; -.
DR   STRING; 307507.A0A2V0NV63; -.
DR   InParanoid; A0A2V0NV63; -.
DR   Proteomes; UP000247498; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361153};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247498};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..562
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016068736"
FT   DOMAIN          180..356
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   REGION          404..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..435
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..466
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   562 AA;  61027 MW;  4050B7A10950517F CRC64;
     MAPRRRDRAA SLALVLIALQ CAAQISQAAP HCKKLSYASP PRGRPAPPVK LVGDQFVDST
     TGKPVQMHGV NWFGFNNGVT MLNGLWVGAK SANSDFATIA YQMQLLGFNA IRLPFIFKDL
     KSQASQIGGY CQGASTAEEI ARRTVDPAFK GPITKKPPAP VVPLPTIDAP GKCNSYIPGG
     QTIDRYLWVV QWLVANGWYV LIDYHPMGAE TTSYNAAEFI DNWKWVWNRV ACLPNFQSDL
     AGRVMVDILN EPDSQRQGWQ AMDGKAGMTE LYLGVMDALW SITPGAPLFF VEGGGQGNFK
     GINWGNGFVT DPSIIRSNSI SDANPFFRTL MGKPYLNNVV ISPHVYGPSV STRRDGVAVA
     PTLWEALDGS FGYLNQKGYC LPKSGANATA AEPDSHAVEL MSADGAASDA RAAASDAPGR
     KGERKAGRGK PGKADRGKPS LTPAPARRPT PTPAPAPAPA PAPAPVQAPR GACHTFPIAI
     GEFGSRFTDK DDLDHLRDFT MWLRNEGAGN TGKHKPINNY FYWCYNANSG DTGGLVNDSW
     MDWEWKKLTY LQSRFGLKPW YM
//
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