ID A0A0S7X423_9BACT Unreviewed; 1584 AA.
AC A0A0S7X423;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Sortilin N-terminal domain-containing protein {ECO:0000259|Pfam:PF15902};
GN ORFNames=AMJ49_01075 {ECO:0000313|EMBL:KPJ57189.1};
OS Parcubacteria bacterium DG_74_2.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1703766 {ECO:0000313|EMBL:KPJ57189.1, ECO:0000313|Proteomes:UP000051668};
RN [1] {ECO:0000313|EMBL:KPJ57189.1, ECO:0000313|Proteomes:UP000051668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_74_2 {ECO:0000313|EMBL:KPJ57189.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC {ECO:0000256|ARBA:ARBA00037986}.
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:KPJ57189.1}.
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DR EMBL; LJNF01000003; KPJ57189.1; -; Genomic_DNA.
DR PATRIC; fig|1703766.3.peg.910; -.
DR Proteomes; UP000051668; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd15482; Sialidase_non-viral; 3.
DR Gene3D; 2.120.10.10; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 8.
DR InterPro; IPR036278; Sialidase_sf.
DR InterPro; IPR031778; Sortilin_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR Pfam; PF15902; Sortilin-Vps10; 2.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 5.
DR SUPFAM; SSF50939; Sialidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 5..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 383..485
FT /note="Sortilin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15902"
FT DOMAIN 614..722
FT /note="Sortilin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15902"
SQ SEQUENCE 1584 AA; 178191 MW; 0A9D7106C25F2FE5 CRC64;
MKKKILIGLI ISILIVVGII FIIRSFTKPA EINWVQTSGP QGGRIFRLFQ NPYKHNELYA
VTEMGVYKSE NKGENWEIMK YSTFSQPPIS IAFTEDKVFA CGGFGIFYYD NRGSVRPNLL
NINNIIRGGG ECNDLKISNN KLFATFSTPS PKDSKKIIYT DLNSGFFIWK DWKDISPSES
ELKDLILPPE DAPFGRVIRI PHILVTDNRI LANIIAESFG SGEFTNGNLY ISEDLGQTWS
KVDLDTPKDI IISNIIQDQN DREHIILAFK HILHDSYHPL SEFLRESYDG GLTWAPLTDI
TFDNNAVGDV DITESSYYIT LQKGNFIIKL DKLDTSKYEL IEMPRAEGYD KDIPFTLAEL
LFDFDNQNIV YGRTNEMWAF GLVKSEDNMK TWKKIDRDII RSSPTIVVVH PTNPDIIFTS
GNTAHEAYFT KDGGQTWEPF SKFTFGDELK FDPHDPNHLI FIDENTKIME SYDLGKTWKQ
INSGFGGEEE KSNFTSAKIF DFEVAGDKIY VSNTGVGISE YNPKDNSWHY LLHSPDYVYD
FEIDPEDNNI LYASYSPKIF ENYSSVWKYS PSQEENLGWS EILRVEDSKG ITSLRFDPQN
PNRIYAGVTG REGEIYVSND KGKTWSKLND ELTFTTIMRH SQLQVDPKNK NTVYAGTWGG
GTYKSTDGGK NWVKLEGAPE SPTCLAIYEK DPNIIYACDR TKPVIHKSED GGHTWQEYYK
FDRSNVLTSA IAINPNDSDT IYAATFGLPF CVEAGELVKI KNGVVVADLN KNLPGIKEGI
PEAAVEIEID PNNPNTIYVS KHGYGVFKSI DDGETWKRLD DREGGLPRLG YYDIDVDYSN
SNTLYAAGLC ELLPEYIIGP TGLPQNIEQG ACGAYKSTDG GKNWTRMLET DHATMAVEVD
PQNPNLLYVA TGAQGIFVSS DGGKSWKQEN KGLPSFGTAA VIAKDGYVYA GVGGSGVYAG
IINDDYSITW DKSRSNKPKA YVSKIQIEID PKDSTRIYAS AYPGGMFRSD DKGKTWYERN
TSQPSIIVDD PVRQGYYSFA IDPNHPADIW QGVYGKGLFR SHEYMNVSMF ANGDKNEMLG
KHITAVVIDP RDSKTVYVGT QEGVFVTKDD GKSWSEMNEG LETLDILSLK IASVEYPPFE
DDFEDGNADG WERGGDWRVV QYNGNYVLQG IDHNWSTVGS ESWTDYTFES KVKLIKGSLH
INYRISQVGR YAIGVSEGGL YLMKTIFPDN HINLVNIGFP LEKNTWNKIK IIGKGNNTKV
YVNNVLKINY TDSEPLLNGR IGFESHPDSK VYVDDVQVTP ERVDSVLYAG TAGYGLYKFY
PATKKWQNLG RTLGIGWWSA WDRRMYQFTS ILFDPDIPGR VYLGHFPSGF FISEDNGHTW
KDSSLGLGND GMFSLTMHPT NHDVLFAGTY NGVSKSVDRG KTWVIKSNGM PPEQWPYTVA
IDDQDPNIMY VSTKNGKNKG FCDRNFDTFC GVVMKSTDGG ETWFEIMKGL NRKSEFYKLI
IYPLNHNILF LSTNRGVYLS KNAGESWKSI NNGLPGLCKT KASMCNQVRD NVADNLILTP
DNKYLILGLA MNGVWKADLS KLSP
//
