ID A0A2U1B464_9BACT Unreviewed; 881 AA.
AC A0A2U1B464;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Alginate lyase {ECO:0000313|EMBL:PVY43484.1};
GN ORFNames=C8D82_1089 {ECO:0000313|EMBL:PVY43484.1};
OS Victivallis vadensis.
OC Bacteria; Lentisphaerota; Lentisphaeria; Victivallales; Victivallaceae;
OC Victivallis.
OX NCBI_TaxID=172901 {ECO:0000313|EMBL:PVY43484.1, ECO:0000313|Proteomes:UP000245959};
RN [1] {ECO:0000313|EMBL:PVY43484.1, ECO:0000313|Proteomes:UP000245959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14823 {ECO:0000313|EMBL:PVY43484.1,
RC ECO:0000313|Proteomes:UP000245959};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:PVY43484.1}.
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DR EMBL; QEKH01000008; PVY43484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1B464; -.
DR Proteomes; UP000245959; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.70.98.70; -; 1.
DR Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR012480; Hepar_II_III.
DR InterPro; IPR032518; HepII_N.
DR PANTHER; PTHR15532; -; 1.
DR PANTHER; PTHR15532:SF5; DERMATAN SULFATE EPIMERASE-LIKE PROTEIN; 1.
DR Pfam; PF16332; DUF4962; 1.
DR Pfam; PF07940; Hepar_II_III; 1.
DR SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lyase {ECO:0000313|EMBL:PVY43484.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000245959};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..881
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015403008"
FT DOMAIN 294..475
FT /note="Heparinase II N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16332"
SQ SEQUENCE 881 AA; 96945 MW; 10ABEBD1FE7CCF2E CRC64;
MKKLMMMFAA GAALTAAAAL PEVRDTASKP LVPKTEFDFS AEVTSPQLWI ETADGGRRTV
AQAQSGGVLR LAPGETLVMD AALLPPSGTL SVRVRTSAGG GGPLLKFPFG KMMLTTGREA
RRPVWLTGIP GAETADGRLN GRGEAPDGHW TLLSVGYSPD KVQFHFDGQF AGEGKARLGA
PAGTVRIGGK LPLEVRDIAC YDVLFDFNDV LKAVSRSPEA LAENAKRLGR TPATFRSAAR
PRLLASAQDQ AELRSAVKQD PAMAALLARY VTRYEAEIAG GVPKEEKVGE IKREDGNRLA
MLAILYGATG DKRYVKTASE YIDRIVDYRI WDGDRPYWTN SDLVTGHLLL GLALAYDWMY
DELAPELKTR MREVVRFRAG DFARRILYKR WTWANQAMNN HGCVTCTGLM AAAVAFHGDL
PETAVWADAA RGWMKNFLAN QPADGGDYEG IGYSQYTLGH LLIYADLVRA EFGDDCYRDC
GWLAKTMDFR IQSSIPRKHW VIQKMPGGRQ RLDHSLISFG DTRQRDFFIP TGPARKLAAE
YRRGDYLAFA DKVDAIDNFC RAHEYLSLLY LHQARKSGVK PSSAPLPAFA YYPQVGKVLM
RSGWDGNEAV MIFRCGTPAG TEALKNFSTA QGDGHVHPDV GAVSLFAAGE LMLINSDYCY
KLTSQENTLT VNGVGQRGDD RQWLDTTDFY KHKLKPEILR AESHDAYDYT VGDATAAYRP
ESGLTRFRRH ILFLKPDCFV IADELAADRP STFETRYHSL LPGKASGKSA MFGGRRGELQ
IRALQPRDGE LTYEIADVRL IDRATAPRKT GVVTQRNTVP AKSTLFVTVL YAAPKGGTAD
FSARIADDVI TVRNGRKVRK VKLIRKGGVR LEVAEPGNGA E
//
