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Database: UniProt
Entry: A0A2H3KPM7_9CHLR
LinkDB: A0A2H3KPM7_9CHLR
Original site: A0A2H3KPM7_9CHLR 
ID   A0A2H3KPM7_9CHLR        Unreviewed;      1830 AA.
AC   A0A2H3KPM7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=LamG-like jellyroll fold domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A9Q02_10970 {ECO:0000313|EMBL:PDW00116.1};
OS   Candidatus Chloroploca asiatica.
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Oscillochloridaceae; Candidatus Chloroploca.
OX   NCBI_TaxID=1506545 {ECO:0000313|EMBL:PDW00116.1, ECO:0000313|Proteomes:UP000220922};
RN   [1] {ECO:0000313|EMBL:PDW00116.1, ECO:0000313|Proteomes:UP000220922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7-9 {ECO:0000313|EMBL:PDW00116.1,
RC   ECO:0000313|Proteomes:UP000220922};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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:PDW00116.1}.
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DR   EMBL; LYXE01000059; PDW00116.1; -; Genomic_DNA.
DR   OrthoDB; 135806at2; -.
DR   Proteomes; UP000220922; Unassembled WGS sequence.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.200; -; 3.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   InterPro; IPR006558; LamG-like.
DR   InterPro; IPR001791; Laminin_G.
DR   PANTHER; PTHR35279; -; 1.
DR   PANTHER; PTHR35279:SF1; ARABINANASE_LEVANSUCRASE_INVERTASE; 1.
DR   Pfam; PF13385; Laminin_G_3; 3.
DR   SMART; SM00282; LamG; 3.
DR   SMART; SM00560; LamGL; 3.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 3.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000220922};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          1129..1255
FT                   /note="LamG-like jellyroll fold"
FT                   /evidence="ECO:0000259|SMART:SM00560"
FT   DOMAIN          1129..1245
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|SMART:SM00282"
FT   DOMAIN          1386..1512
FT                   /note="LamG-like jellyroll fold"
FT                   /evidence="ECO:0000259|SMART:SM00560"
FT   DOMAIN          1386..1502
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|SMART:SM00282"
FT   DOMAIN          1643..1769
FT                   /note="LamG-like jellyroll fold"
FT                   /evidence="ECO:0000259|SMART:SM00560"
FT   DOMAIN          1643..1759
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|SMART:SM00282"
FT   REGION          519..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1074..1093
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1304..1360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1564..1609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..581
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1075..1093
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1304..1329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1330..1356
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1564..1592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1593..1609
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1830 AA;  189214 MW;  5C5907A546C94E92 CRC64;
     MRRIVSSPFF FGGLFLGLLL VLSSFAASLV SATVPNRQPW VHVAGTCDPA VQGAVFTSAN
     ENCGGPGQGF DANEIYASVI LQDTATSIAP CPGIAEGETC YRMWYTGVAT SGLRRIGYAI
     SPDGRTWTRV PGLAGLGSVL GAGPTGRFDS AEVSFPTVVR TATGFTMWYV GGNGSLFSLG
     MATSTDGLNW TRVEGPLTGG SVLRPSGLDG TFDQDIVAAP RVIVDQASTL APCENGRTSG
     ACYRMWYQGV DVSPVYTYLI GHAVSPDGLN WTRLAGAGYG GAVIDRGPAG TFDAANAAVP
     AVIKDGALYR MWYDARSTGG QATIGHVVST DGVNWVRPVP NDPVWRGSDD PGTLSPDDLW
     APAVVKDGAT YRIWYNHTIR PNARRLSYAT MTPGTSFADL QLTNTATTYT LTFTSQAIPA
     GGSVLVTLPA SVPFAQVTPG NVTGFGATAT LVAEADAITD AASGNLARGA LLVRLPDGAP
     AGAKTIAFTL AVQPSADSAV LVQTFDAREV LQYGNATVVG SGLPTPTPLP TSTPVPTLTS
     TPLPTNTPGP TSTPGPTSTP TTPPTNTPLP TSTPLPTPGP AANNQPWQSV PGTCPESLNG
     AIFGLAGDNC GGNGTSFDVT EIFPPQVLRD DARVGAPCEN GRTSGLCYRM WYVGTGPAPL
     QERRIGYAIS PDGITWTRVP GNGTGGSVFE ASGQNGTFDA AGVSTMNIIR FGATYRMYYT
     GFRDASSIDG IGLAESQDGI TWTRVPGNLA GGALLRASGV PGQFDGTYIV APAVLIDQAS
     TTAPCENGRT TGTCHRMWFE GVSTSPAYTF RIGYAVSPDG VIWTRIATNP DGSIIAPGTF
     GTFDDNNIGV PAVMKDGVFY RMWYEAAGYT AGYTTGYIVS TDGINWVRPS PNQPVWTGAN
     DAIIAGSPDE VWAVRMLKEG SRYRLYYTTS TRPNSRRFAL AEMQPGAPLT DVSLTSAGND
     HTIFFTTPSL PVGGSVLVTL PPTVDIATVT VTGLGGFGEG ATFVAEPGAV TDAYAAGTAR
     GALLVRLPNG APAGQKGLSF SLTGPVPGEG TTLIQAFNTR EVVGYAEVDL PSIPLPSPTI
     GPSPTPTNTP IPTNTPIPTN TPVPGSNFAL AFDGVNDDLR GDAIAGLNGT QTVEFWLRPN
     VAGQNGVILA TTNDASGWSL ELESGRITWW IYTAAGQWQG VTHPVALPAG TWSHVAATYN
     AGVAQIFVNG TGGTATTVGT ITAGPRVRVG GLTPYGFVNA QIDEVRFSNN VRYAANFTVP
     AAAFMPDANT LALFSFDEAN GQTTTDRSGN GYVLTLGAST NAANDDPTWV ASSAPTEGSG
     AVPTPTNTAT PAPTSTPGPS PTPTNTPIPT NTPIPTNTPV PGSNFALAFD GVNDDLRGDA
     IAGLNGTQTV EFWLRPNTAG QNGVILATTN DASGWSLELD GGRITWWIYT AAGQWQGLTH
     PVALPAGTWS HVAATYNAGV AQLFVNGTGG TATTVGTITA GPRVRVGGLA PYGFVNAQID
     ELRFSNSVRY ATNFTVPTAA FLPDANTLAL FSFDEANGQT TTDRSGNGYV LTLGASANAA
     NDDPTWVASS APTEGSGAVP TPTNTATPAS TSTPGPSPTP TNTPLPTNTP IPTSTPVPGT
     NFALAFDGAN DDLRGIAIAG LNGTQTVEFW LRPNTAGQNG VILATTDDAS GWSLELDGGR
     ITWWIYTAAG QWQGLTHPVA LTAGTWSHVA ATYNAGVAQI FVNGTGGTAT TVGTITAGPR
     LRVGGLLPYG FVNAQLDELR FSNNVRYAAN FGVPTAPFAP DANTLALFNF NEGAGQTVAD
     AQSPYTLTLG ATANAENDDP TWVASTVPFN
//
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