ID A0A1Y5K874_9BACL Unreviewed; 1434 AA.
AC A0A1Y5K874;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Polysaccharide lyase {ECO:0000313|EMBL:OUS73388.1};
GN ORFNames=B1748_23245 {ECO:0000313|EMBL:OUS73388.1};
OS Paenibacillus sp. MY03.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=302980 {ECO:0000313|EMBL:OUS73388.1, ECO:0000313|Proteomes:UP000195591};
RN [1] {ECO:0000313|EMBL:OUS73388.1, ECO:0000313|Proteomes:UP000195591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MY03 {ECO:0000313|EMBL:OUS73388.1,
RC ECO:0000313|Proteomes:UP000195591};
RA Liu H., Cheng Y., Gu J.Y., Han W.J.;
RT "Draft genome of a polysaccharide-degrading bacterium Paenibacillus sp.
RT MY03.";
RL Submitted (MAR-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:OUS73388.1}.
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DR EMBL; MXQD01000033; OUS73388.1; -; Genomic_DNA.
DR OrthoDB; 6636047at2; -.
DR Proteomes; UP000195591; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd01083; GAG_Lyase; 1.
DR CDD; cd08547; Type_II_cohesin; 1.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR Gene3D; 2.60.220.10; Polysaccharide lyase family 8-like, C-terminal; 1.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR002102; Cohesin_dom.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
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 InterPro; IPR001119; SLH_dom.
DR NCBIfam; NF033679; DNRLRE_dom; 1.
DR PANTHER; PTHR38481; HYALURONATE LYASE; 1.
DR PANTHER; PTHR38481:SF1; HYALURONATE LYASE; 1.
DR Pfam; PF00963; Cohesin; 1.
DR Pfam; PF02278; Lyase_8; 1.
DR Pfam; PF02884; Lyase_8_C; 1.
DR Pfam; PF08124; Lyase_8_N; 1.
DR Pfam; PF00395; SLH; 3.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49863; Hyaluronate lyase-like, C-terminal domain; 1.
DR PROSITE; PS51272; SLH; 3.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:OUS73388.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195591};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1434
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012938333"
FT DOMAIN 1256..1319
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1320..1379
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1381..1434
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 1184..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1434 AA; 155793 MW; 8415E56ED52554EA CRC64;
MKSGKLRTGL IITTILSLVF TLLQPTPAAA AQQSEKLGEL RLKWFDFLTG GTDIDLQDED
IKRAAQANAA KVTNESGTGA WDTMNKQEGR SSLWADYNST TNSSHITNSY NRLKDMAIAF
ATPGTELHKD TGLRDDILAG IDWMYQNRYN VTRASYNNWW DWEIGAPLAL ADIVTLMYDD
LSEEQITAYT STIDRFVPNP DKRLIGAPGL TETGANLMDK ALAVVLRGIL GSNEAKIAQS
RDALDSVFPY VSGGDGFYKD GSFIQHNNIA YTGSYGSVLL GNMGKLLTLL ADSDWPVDSP
GFENVWNWVT DSFEPVIYNG HIMEMVSGRA VSRYNNNTRG AVWTILRLSQ FAPEEEAQRY
KEMVKEWLLA DQSVANPYEG VPIRDIVALK KLLNDDSIER RGGLARNYAL TAMDRIVHSR
EAFTFGISMS STRIANYEGS TNGEHTKGWY TGDGMTYLYN QDAGYYRDGF WPTIDPLRLA
GVTSDGKQRT ATRTTSSTWV GGSSLDKAYG AAGMDLSPPG SDLRGKKSWF MFDDEIVALG
ADLTTGTPRT DGKQVETIVE NRMIASADEN ALTVDGEMMP AQSDWSEKLS QVQWAHIAGT
LPGADVGYYF PGGSDVSALR ETRSEAWSSI NPSGPTTPLT RNYLSLAVEH GAKATAAEYA
YVLLPGKNTG DTNMYSENPD IRILSNTAAM QAVQETKLGV TGINFWRAGE TEQVRAYQPA
SVMVKEEGDE WTVVVSDPTQ AQAKVRVELA AVALEQLEAD STVTVLRSSP SVLLEVATAG
TKGASHTVKL KVDPDADTDL PVEEGVSPDP EAVIRVDVTA DAYVNGGANA AVNYGNTGYL
NIRNGTGLYD RRTYLKYDLS TLSSEVERAY LYVYGRVNDS AGGTANIGAY AVEDDSWTET
GLNYNNRPAE GARMDDVTFN ATNEWRSFDV TSFMNQELLS NETATVMLRQ FDGDKSSEIR
SRENESGTYR SYLELLMKDE VAPTTTVRFE TDAESAGLDG QPVTLLVDAR DNEGGWGVWR
TQYRINGGGW MTVDAGRIVL QGDGSYRVEY RSTDKAGNVE QTKQLAVITI STPTAELVGP
EQAVAGESIE IMYRMNTGLN HLYASEFVVE YDSEKLIFDS AEAAQQHIIV AGLANEPGRL
GVIVAGLGQP LGGNENLVKL VFKAASVEET ATTRLEVVEA QAADRTGKEL TLRPTSIAVT
VKAQTEEPGT GEPGTGEPGT GGPGTSDPGT SEPGTGGPGT GEPGSEEPGT DEPGTDEPRE
WSDVQGHWSE SVIKEAAKLN WLNGYPDGTF RPDKAMTRAE FAVLVVRALG LNKANTLAFA
DTEQLPEWAR DAIAIGVTNG FIAGYEDNTF RANRPITRLE MAVMIARVLE LTRSKQTEHV
FADAGDIPAW GRDSVAAVFE NGLFQGKGGN RFVPNAGATR AEAVTVLLRA LNRK
//
