ID A0A0A2F279_9PORP Unreviewed; 1024 AA.
AC A0A0A2F279;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Sortilin N-terminal domain-containing protein {ECO:0000259|Pfam:PF15902};
GN ORFNames=HQ41_03560 {ECO:0000313|EMBL:KGN85123.1};
OS Porphyromonas sp. COT-290 OH860.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1515615 {ECO:0000313|EMBL:KGN85123.1, ECO:0000313|Proteomes:UP000030116};
RN [1] {ECO:0000313|EMBL:KGN85123.1, ECO:0000313|Proteomes:UP000030116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-290 OH860 {ECO:0000313|Proteomes:UP000030116};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas sp. strain:COT-290_OH860 Genome sequencing.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C25 family.
CC {ECO:0000256|ARBA:ARBA00006067}.
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:KGN85123.1}.
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DR EMBL; JRAR01000032; KGN85123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2F279; -.
DR eggNOG; COG3291; Bacteria.
DR eggNOG; COG4447; Bacteria.
DR Proteomes; UP000030116; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR031778; Sortilin_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR12106; SORTILIN RELATED; 1.
DR PANTHER; PTHR12106:SF27; VPS10 HOMOLOG 1-RELATED; 1.
DR Pfam; PF15902; Sortilin-Vps10; 1.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR SUPFAM; SSF49299; PKD domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030116};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 627..733
FT /note="Sortilin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15902"
FT REGION 915..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 114202 MW; 9B89977633543DF0 CRC64;
MLHSASLLSG QETQLYFDPY VPEPLPSGSP EWLREIELNP SGVNYFKMDS LFRDWCAKDI
DARVKTLERK PAVNFYRRWA KAYRDFVNAE GRIVLPQQED YAQKVELQNR QVRQHLRAIA
TEERRQPLWR NIGPNRTAEN NRGKLSEKDS QVCVFRLAVA PSNHNVVYSG TETGVVFRSD
NKGLEWQACD AAHNFGGSIY AIAVSPRDEN LVLVGAGTFL WKSTDGGKSW TRLTQINARV
NSIRFSPQNP RQITIATHAA EQGFGGFWRS DDAGASWLKT LDLLCHDHEL KPDDPNTVYL
LAQRAPKEPF FFYVSTDGGQ TFQQRQLPVE GVRSGRLAVS EAPTGTNYVY ALVNAQVTSH
SLQAMGDLRG LPHILKSTDA GLTWSDQTTR GSNLRFNTFS PFIDNDYGGQ GYFDMMIGVS
NKDPELVIYG LCNAYRSTTG GTGSVHTNAI GGYERQGNLH PDIQDIAIAG DDTYISTDGG
IKYSTDFFAT PGQIRHQGIY ASEYHGFDQG WNEDVMVGGR WHNGDAVHAA NYGEGNTLYV
GGVEQATGHV MVSDPYKVYF SDAGRMVMPR EMTGQIDLAN YGTYFSKKPY EVLQTNGTIA
FDPRYALRLV INPIDDTNAS WGGPSDKVYL STDEGRSFSM LYGLDGENIA NFAYARSNPD
YFYISGAYDI YRTIDGGKNW SLAKTRPFPE KTIPNGITQI AIHPRDEKKL WAVNPNEPHK
LVYSTDAGDT WTPDLSPVLR DQPLQFVIVV GDERNGIYVA TGGRGARVYY KDDSLEDWID
YSEGINPGSR IARILPYYKE GKLRMATDQG IWEAPLYRPD FVPVAQPMAT NVGSGDLTGK
ADMPIQLESY SIVNQSQASW RWSFFPKPKS VSNPTSRNPI VVFGYNASYD VTLTVTTPQG
SDTKTVKKMF VVRDGVEHPN PDEGYTPPEP SDPTGINPEA EVEQRIKLYP TVQTSGQTIR
VELTNLREDA KLTLHSAKGH ELRHVALPAG SSTYHLTTEG LTPGVYLYSL LSRSEKHYGR
IIIK
//
