ID   A0A1K1QH16_9FLAO        Unreviewed;      1115 AA.
AC   A0A1K1QH16;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Por secretion system C-terminal sorting domain-containing protein {ECO:0000313|EMBL:SFW59215.1};
GN   ORFNames=SAMN02927921_02560 {ECO:0000313|EMBL:SFW59215.1};
OS   Sinomicrobium oceani.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Sinomicrobium.
OX   NCBI_TaxID=1150368 {ECO:0000313|EMBL:SFW59215.1, ECO:0000313|Proteomes:UP000182248};
RN   [1] {ECO:0000313|EMBL:SFW59215.1, ECO:0000313|Proteomes:UP000182248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12145 {ECO:0000313|EMBL:SFW59215.1,
RC   ECO:0000313|Proteomes:UP000182248};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC       {ECO:0000256|ARBA:ARBA00006699}.
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DR   EMBL; FPJE01000013; SFW59215.1; -; Genomic_DNA.
DR   RefSeq; WP_072317776.1; NZ_FPJE01000013.1.
DR   AlphaFoldDB; A0A1K1QH16; -.
DR   STRING; 1150368.SAMN02927921_02560; -.
DR   OrthoDB; 6394136at2; -.
DR   Proteomes; UP000182248; 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   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
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; IPR000421; FA58C.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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; IPR026444; Secre_tail.
DR   NCBIfam; NF033679; DNRLRE_dom; 1.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   PANTHER; PTHR38481; HYALURONATE LYASE; 1.
DR   PANTHER; PTHR38481:SF1; HYALURONATE LYASE; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF02278; Lyase_8; 1.
DR   Pfam; PF02884; Lyase_8_C; 1.
DR   Pfam; PF08124; Lyase_8_N; 1.
DR   Pfam; PF18962; Por_Secre_tail; 1.
DR   SMART; SM00231; FA58C; 1.
DR   SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49863; Hyaluronate lyase-like, C-terminal domain; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182248};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          708..845
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
SQ   SEQUENCE   1115 AA;  121385 MW;  54F81513B1EF8378 CRC64;
     MRKTITLKVF FTFLLWYGIH EEAFSQAVYD SISGRIRSEL LLTGAVSSLD ATVSDYLNTV
     QADGSWTDID YQSDARTMWP ANVHLVRLKD MARAYTIPAS SHYGSGTLHT AIVNALDFWD
     TTDPQSDNWW YNQISSPQGL GQILLLLRAG STPVPSALEA GLIAQMNRGN PASWTGANKL
     DIAIHYLYRA CLLEDDDIMQ VAIDEAFYPI VLTTGEGLQH DNSYMQHGAQ LMISSYGSVF
     LDGEYRIADW VRDTPYALSP QKKQLLSGYY KDTYLRTIRG SYIDFSTEGR GISRPNILRK
     SGEKGRLERA KKVDPANNAA WNAAIARTSG AAAPGYMVVP WHKHFYRGDY TVHQRPGYLF
     NVRTVSSRTI RTESGNEENL KGVFLPDGAT NIQRRGGEYY NIMPVWEWDK IPGTTSAAYT
     EVPPTATWGE AGSTAFAGGV TDSVYGITAY HLNFKNTTAR KAWFFLDDAV VCLGAGINGS
     GTADITTTIN QCWLSGDVLV SGTGGSPGVQ TSQTEVFYTD PQWILHDSIG YFIPEGGNVR
     VSNREQSGSW YGINHSYPDD MVSGDVFKMW VDHGTAPSDA TYAYIVVPGM ASGADMQSYD
     LSRIRIVENT PAVQAVKYED ADMMQVVFYQ AGTLSDGDVS LTVDRPCTVM LKGLEEEEVK
     VYIADPAQQQ STVTLFADVP GIPGTRQLEC PLPAAPHSGA TAYVVIDENT PEAGEILTGL
     PIIQVTASAD DGNVPANTID DNLGTRWSAE GDGQWIRFDL GTVHTITGLG VGWYLGDQRS
     SSFDVEVSAD GTGWTDIYSG TSAGNTTAQE NYDLPDTSGR YVRIIGHGNS SNDWNSITEV
     DIFGYMDMAT ATYGAVGDAF VRDGSYADTN YGGNTSLILK KDGTGYSREV YLQFDLDSAQ
     LPVSNAVLRL YCSYGNTTAE SSQWQLSLVP DNSWTESGIT WNNKPAGTTV LDTRPGTATP
     GYTDWDITTA VNSLSSGGLL SLVLVSTVGG QTTDAGFVSS EALSAAQHPE IICTYESLPD
     TSARVSMLPE VQELQTTEEN TVLFPNPLSF GKGTISSDVI IRSVKVYSKD GRLVQQTDRL
     NTTGYELDLT GFAPGFYFVV ISGDTTEVTK KVVKP
//