ID S1QZZ6_9ENTE Unreviewed; 1279 AA.
AC S1QZZ6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESK60855.1};
GN ORFNames=OMO_01810 {ECO:0000313|EMBL:ESK60855.1};
OS Enterococcus cecorum DSM 20682 = ATCC 43198.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1121864 {ECO:0000313|EMBL:ESK60855.1, ECO:0000313|Proteomes:UP000017415};
RN [1] {ECO:0000313|EMBL:ESK60855.1, ECO:0000313|Proteomes:UP000017415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43198 {ECO:0000313|EMBL:ESK60855.1,
RC ECO:0000313|Proteomes:UP000017415};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus cecorum DSM 20682 (= ATCC 43198)
RT (Illumina assembly).";
RL Submitted (OCT-2013) 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:ESK60855.1}.
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DR EMBL; AHYS01000008; ESK60855.1; -; Genomic_DNA.
DR RefSeq; WP_016250463.1; NZ_KI535313.1.
DR AlphaFoldDB; S1QZZ6; -.
DR STRING; 44008.GCA_001318175_01278; -.
DR GeneID; 60870520; -.
DR PATRIC; fig|1121864.4.peg.252; -.
DR eggNOG; COG5492; Bacteria.
DR HOGENOM; CLU_004172_0_0_9; -.
DR OrthoDB; 6636047at2; -.
DR Proteomes; UP000017415; 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:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd01083; GAG_Lyase; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.220.10; Polysaccharide lyase family 8-like, C-terminal; 1.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR048734; HL_N-beta.
DR InterPro; IPR023295; Hyaluronate_lyase_beta_dom_sf.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR019931; LPXTG_anchor.
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; IPR005877; YSIRK_signal_dom.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
DR PANTHER; PTHR38481; HYALURONATE LYASE; 1.
DR PANTHER; PTHR38481:SF1; HYALURONATE LYASE; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF21461; HL_N-beta; 1.
DR Pfam; PF02278; Lyase_8; 1.
DR Pfam; PF02884; Lyase_8_C; 1.
DR Pfam; PF08124; Lyase_8_N; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49863; Hyaluronate lyase-like, C-terminal domain; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Reference proteome {ECO:0000313|Proteomes:UP000017415};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT REGION 56..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1279 AA; 141823 MW; A8299E6857DD4762 CRC64;
MKYPFETRGR FSIRKLSIGV CSVCLGFAIL NAVHSHQTVL AQEGTTDAQP AVTSEFSTYD
KPVNEANSPE SSTLTSTTTS EGVETTHANL EVATSTAPTS TTSELSSNSQ PSETSHLTAN
EGSANQTQPI SESATSNETT EVANTPTTSA SSSEPANTSA TEAPTSETEK QNTPVAENLV
KNGDFTQTKA KTGTWTAEAA TSWNNPWIPS NITASSKSKA QLAVVDGRLM ISAPETFRTS
IAQVLEVDAS KKYEVSYDVE TQNVEGAGVR VRFLPVDEKG ATLKTPEGKT VDAPTTSYVN
KTNTKTITQQ VTFDPIVSRV KLEIFFETGT GTAYFDNITF KEYIKPQEET KDAPKAETED
IQLGLNKYYL PNLSDATYTV ENPEIAEVRN QIITPKQTGS TKVTITKEGQ TLGSFTLNVE
NHDATIYDQI LNSWENVSLG NENYQSDNPY MQEFLAKIES GVEESLAHWD DDVANRESIF
DDVTDFTKSA NITKTYRRLE QFAQVLDNKS SKYYQNYDLA VKLKQGMEYL YKHVYNEQKE
IVGNWWDYEI GTPRAVVDVL AYANAYFTQE EINRYIKPID KFVADPTVIR STTTIPVPAV
GGNQTDLSKV TILSGALKQD SARIQEGVDG LLTVLEFVKE GQGFYRDGSF IDHTDVAYTG
AYGNVLMDGF SQILPMIANT SFALPAEKTA ILYEWIDRAY FPIILNGELM DMTRGRSISR
ASAESHAAAI EALRGVVRIA QASDEAQKMH LLSAVKGRIG EDTFYVPYQN LKSYTDISLF
EKLLNDDTIP AVKPETFLHS FHNMDKFVYN NAENHFAIAL SMYSDRTQNY EDMNNENRHG
WYTSDGMVYL YNNDLTHYSE GYWPTVDPYK MPGTTELVTA REDGSGQVNL PSRFVGASKF
DEKNAAVAMD FTNYNEELSA RKAWFIFGDK IVMLTTNIQN KSSDASVTTI ENRKLVPDKN
TKIYVNGEEM TADKVTNSTV DTFYLETADP NQRIGYAFLT PLSLDIEKQA RTHSWSEINY
GQPSDPVTNT FVTVTHTTQQ NGENLAYVLM PNQDQEALNA AKDTVKVVVQ KNDLQVVYDE
TSQTYGVIKY TDTPYELTDK VTLSQSGIYM IKKTSDGFDL SFAHPRDDAK FSMLEGSADE
VSFKVLKTAD EVDRTTKLHL ILPTETTDSS TQTDNPSMSD SGTQTDNPST SDSGTQIELP
KEEEKQSNKD NVKEQPKKEL GSQAKRNKKV KEQSSVQSDA ASVKRLPKTG NQADQALLLS
GFASIGLSAG IFFKRKKEQ
//
