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Database: UniProt
Entry: A0A2S9BV84_9MICO
LinkDB: A0A2S9BV84_9MICO
Original site: A0A2S9BV84_9MICO 
ID   A0A2S9BV84_9MICO        Unreviewed;      1508 AA.
AC   A0A2S9BV84;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=F5/8 type C domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CQ034_05890 {ECO:0000313|EMBL:PRB65617.1};
OS   Microbacterium sp. MYb45.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1827294 {ECO:0000313|EMBL:PRB65617.1, ECO:0000313|Proteomes:UP000238044};
RN   [1] {ECO:0000313|EMBL:PRB65617.1, ECO:0000313|Proteomes:UP000238044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MYb45 {ECO:0000313|EMBL:PRB65617.1,
RC   ECO:0000313|Proteomes:UP000238044};
RA   Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA   Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA   Kaleta C., Schulenburg H.;
RT   "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT   from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC       {ECO:0000256|ARBA:ARBA00006699}.
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:PRB65617.1}.
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DR   EMBL; PCPG01000001; PRB65617.1; -; Genomic_DNA.
DR   OrthoDB; 5480482at2; -.
DR   Proteomes; UP000238044; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR   Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.220.10; Polysaccharide lyase family 8-like, C-terminal; 1.
DR   InterPro; IPR008929; Chondroitin_lyas.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR038970; Lyase_8.
DR   InterPro; IPR011071; Lyase_8-like_C.
DR   InterPro; IPR012970; Lyase_8_alpha_N.
DR   InterPro; IPR004103; Lyase_8_C.
DR   InterPro; IPR003159; Lyase_8_central_dom.
DR   PANTHER; PTHR38481; HYALURONATE LYASE; 1.
DR   PANTHER; PTHR38481:SF1; HYALURONATE LYASE; 1.
DR   Pfam; PF00754; F5_F8_type_C; 3.
DR   Pfam; PF02278; Lyase_8; 1.
DR   Pfam; PF02884; Lyase_8_C; 1.
DR   Pfam; PF08124; Lyase_8_N; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR   SUPFAM; SSF49863; Hyaluronate lyase-like, C-terminal domain; 1.
DR   PROSITE; PS50022; FA58C_3; 3.
DR   PROSITE; PS50853; FN3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1508
FT                   /note="F5/8 type C domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015478614"
FT   TRANSMEM        1481..1500
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          709..824
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          829..973
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          977..1117
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          1275..1363
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          437..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          725..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1508 AA;  158534 MW;  80F19F12B558E088 CRC64;
     MRRITAFIAF TVALVIGSSA LTTVPASAAP EDDVATVIDR LEEYYLGQGD DIIIANGIYL
     AKTSEALDYV ASQQEDGSWA DVNYADRTSS ANGSVWSAYT ALYRMLAMTQ AYKDPKAAGH
     GDKRLVDAVQ RALLHWDRVN PGNTNWWETE IGESIAMGRI SMFLGSELSE DAFRVSLAHN
     TGKLDPVGAN GSWRTSNYIF EALSTGDIAK VKEGFATIVA TIAVDHSGTV KEAVQPDASF
     WAHGAQLYSE GYGMVLFTYA ALWSDVARGT GLAFTRAQLD SIAFYFIEGT RWLIRGEIGM
     LYLNYRPPKT VSDITSHASE FIEPLQRMVR TDALYSTAYQ AVLDGVLGKT ETNGVTGAKY
     FWRSEFASHQ RDDYGIFTRL NSSRTFGAEL RTSYRDDLGN PVFWNAMGST AIQVNNREYL
     DLGPTFDWWH YPGVTAPDEK RTERGFENRG RNGDGASFTG GTSDGEFGAS VLTLDAAGTG
     ARKSYFTFDE GMVALGAGIA STSGAAVHTT INQASAKENA TVGGKPVAGD ADDQSVGGAR
     WAYNDEVGYV FADGQDVRVS NRAQSGSWEG QEAVSRDAFT LYVDHGTKPT AGTYDYTVLP
     AATPAEVAAF ADAPAMRTLR NDTSVQAVRH DAAGITMATF YAAGTLDLGG GRALTVDQPS
     IVLLDERGET PVVSLSNPDR PGLSVGVSLT GGGQDQHARF ALGSGENMGR TVTSALAAGP
     LPATSAFSAS STADGSSAAA LGDDDRDTAW RSAGDGTQWA AVTLPRGSWV TKATIDWTDA
     PAGDFVVQTS QNGVDWTDRA HVTDGDGGVD EIPLDPTPAE HVRVLLLDGE GEGYGIRELS
     VASSVNLSID GATRASGYAG YNLVHALADG DPSTRWRGNN ANSAWAQVDL GESKPVSTVR
     LSWEAAYAKA YRIQLSDDGR NWRDAYVTPS AGSDGGVDVI TLNDQSARFV RMQTVTRALD
     YGPSLWEFEI FSDRLVAEAP AVPVGNANLA LGRPTTADSV HQNNATITGP KATDGSRSTK
     WSSARAAAEH WLQVDLESVR SVSRAVVAWE AGTSNDYRIE GSVDGTTWMP LARVQAAQPT
     LIHQHDFAAT DVRYVRLSGM PATQYGLNIW ELELYGGYTF ECAGPVSAGR DGAAVVAATV
     SPVNPADTFT AVVMDDSVAT VKGDARVSAD GRVEVDLATR EPGRTTVGIR HQGGSEIAWC
     TVTVIADTGR LQAQVDAANT LDSTAYTSAS WKPLLPALEA GKDVLAAPGS AQGQVDAAAD
     ALAAALAGLI RLDAAPSAPR DVVATASGDR VNVQWTVPEN VGGSPIIAYE VAVGDRVVQA
     EGAVLTAAVT GLAAGEYAVT VRAQNAGGWS VPSAAIVVVV DPEVVTPSVT VEGSPKVGGR
     IDVSGVGFQP GIEYTVQLRS TPADLGTVTA ETDGSFAFRG VVPEDVEAGA HTLVVMHDGA
     DIASTPVRII AAAGPGAPGG PGDGGTDGSG ALPATGGDLA WLPWTLAMAL LLLLSGAVAM
     KARRQPRD
//
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