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Database: UniProt
Entry: A0A177CUZ2_9PLEO
LinkDB: A0A177CUZ2_9PLEO
Original site: A0A177CUZ2_9PLEO 
ID   A0A177CUZ2_9PLEO        Unreviewed;       976 AA.
AC   A0A177CUZ2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   13-FEB-2019, entry version 12.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAG10607.1};
GN   ORFNames=CC84DRAFT_1193992 {ECO:0000313|EMBL:OAG10607.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Massarineae;
OC   Didymosphaeriaceae; Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG10607.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG10607.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG10607.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L.,
RA   Chaput D.L., Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|SAAS:SAAS01116863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; KV441549; OAG10607.1; -; Genomic_DNA.
DR   RefSeq; XP_018040972.1; XM_018181334.1.
DR   EnsemblFungi; OAG10607; OAG10607; CC84DRAFT_1193992.
DR   GeneID; 28764820; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000077069; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.390.10; -; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000077069};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    976       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008058631.
FT   DOMAIN      378    553       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   976 AA;  106883 MW;  D07652BE2B8D2A89 CRC64;
     MEMICAVYHL SSVLAAVSAI DNGLQKDVTW DSGSLLVDGE RIIVMSGEFH YQRLPVPELW
     LDVFQKFKAN GMNAVSIYFF WSYHSASKGT YDFTTPGKDI QRLFDLAKEA GLYVIARPGP
     YCNAETNGGG LALWGSDGSM GSLRTSDETY HQAWSEWIAE VGAIIAKNQI TNGGPVILTQ
     VENELQETKY DPNNTLVKYM IQIEDAFKEA GLIVPTSHNE KGFRSKSWSS EYNNVGGAVD
     IYGLDSYPGG MSCTNPNSGF NLPYTYYQWF HDVSPSQPQY LPEFEGGYFQ PWGGYFYDTC
     QAEHSPEFAD VFYKGIVAQR ATLLNLYVAF GGTNWGHSGA PVVYTSYDYS APLRETREIQ
     DKFKQYKLLT LFTRVSEGLA NTVMETNGSA VATGNADLWT WVLKNKETSS RFYLAQHNVT
     NSRSITDFSI TVSTSGGNVT IPDLQLAGRQ SRWIVTDYSI GKVTLLYSSA EVLTYGTFDR
     PVVVFYLREG QTGQFAFKDA EKVTFKTYGA ESGIKATESG DGFTYTQAKG STAVLFSNGV
     LAYFVDIPTA WTFFAPSTTS SPTVKPDEQI FVFGPYLVRS ARLHGDTVNI VGDNANSTTI
     EVYAGKKANT ISWNGDKIKT TKTAYGSLTA SITGAEDRQI SLPALTDFRA ADSVPEVSPS
     YNDKNWIVAN KTTTLSPVKP LTLPVLFSSD YKFYTGAKVY RGYFSEKNVT GANITAQGGV
     AAGWNAWLNG QFVGYHPGNV SLQSTTGTFS FKGVNLTDNN VLTVVTDYTG HDQTSTGPAG
     VENPRGLLGA QLQGGTFSQW KIQGNAGGEK NIDPIRGPMN EGGLYGERLG WHLPGFDTSK
     WTKASPVTDG VKGVGIKWFT TTFTLDIDRD LDVPLGIEVG APSGTIARVL LFINGYQYGK
     FVPHIGPQTR FPIPPGIINT RGKNTLSVAL WAQTEAGAKL STLQLIQYGK YQSGFGFDKI
     DGKALQPSWK DRSQYA
//
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