ID A0A1E5AD81_9RHOB Unreviewed; 955 AA.
AC A0A1E5AD81;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=P/Homo B domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AB838_15380 {ECO:0000313|EMBL:OED47973.1};
OS Rhodobacteraceae bacterium (ex Bugula neritina AB1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1868286 {ECO:0000313|EMBL:OED47973.1, ECO:0000313|Proteomes:UP000094333};
RN [1] {ECO:0000313|EMBL:OED47973.1, ECO:0000313|Proteomes:UP000094333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB1-7 {ECO:0000313|EMBL:OED47973.1};
RX PubMed=27681823; DOI=10.1038/srep34362;
RA Miller I.J., Weyna T.R., Vanee N., Fong S., Lim-Fong G.E.;
RT "Single sample resolution of rare microbial dark matter in a marine
RT invertebrate metagenome.";
RL Sci. Rep. 6:34362-34362(2016).
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:OED47973.1}.
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DR EMBL; MDLF01000074; OED47973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5AD81; -.
DR STRING; 1868286.AB838_15380; -.
DR Proteomes; UP000094333; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011635; CARDB.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF07705; CARDB; 2.
DR Pfam; PF00353; HemolysinCabind; 3.
DR Pfam; PF01483; P_proprotein; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 4.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 53..127
FT /note="P/Homo B"
FT /evidence="ECO:0000259|Pfam:PF01483"
FT DOMAIN 145..232
FT /note="CARDB"
FT /evidence="ECO:0000259|Pfam:PF07705"
FT DOMAIN 254..362
FT /note="CARDB"
FT /evidence="ECO:0000259|Pfam:PF07705"
FT REGION 777..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 101420 MW; 0CFB4395E1753C91 CRC64;
MGQAVYSSGT DRNIGQGTYN FYFNPTGDTL FATVTNVAYK FKIDYNGGAK VDLGKVDIYL
YSPNGERHTI YYNFDHFGND TDAGKDSDSA YDHDIYYDGS GGESTFSRGF DGNQVNGNWR
LRVDNDTGKT LTMYYVDTRV DFLTAPDMIV EDIEITGDRA LGEKVRIEAT LKNIGESDYF
GIGKNFDVEY LVNGKVVGTD SVTYGLNAGQ SNKESLTYTV ETAGQQNVEV RVSGISGEGV
TSNNSKPAGF FAAAPDLVVQ DIQVFGELKT GEEIKLKATL ANIGGADYGG LLAGGFELEY
FVETTSGGDR YIGKDSVSFG LTAGQTNTET IRYTLQSGDT GTFKVKIVDT ANESDTTNNT
RTELVGEMHD EKQSVAESLE HVELGTLFAR SVYGERNIGS DYRGSADNGL GDRYDNYFDT
LGWQVLTDTE LGNHFVPNED ARFNGGGLFE GKAEALVPGW DAQSLLALGE TAGGSKTLVL
TFRGTDGSFA AFANGQAFSG DGLFHHYNAH KPLVEAALAY ANDPANGIDK LIVSGHSLGG
SMADIFAAID AQRLDEAVEL TVVSLAPAGI DKTLYSHTEA FDGFENQHDP NVVDVEGGSV
DLIEPSYYIG LSHNKDAVTF AETVDLDSID GYVGNNILRN NKNFDDAITS LFMPNLDNSE
TDSGGFWFPK GFGAHHNIGV YWANISALAA DTLAKLYDNS QKISFGLTDY SQVKDIDGNA
LPVFPAFTGS DMSAYDNDAG ANTLRGGATA DYILGLSGDD NILGGLGDDL LSGGDGRDAV
SGGSGQDALS GGKNADRLSG NGGNDQLFGD AGRDNLRGGS GQDQLTGGSG NDKLRGGAGA
DQLIGGKGKD TMTGGGGNDH FIFKSVPEIR ADKIRDFKTG DKVDLSRIDA SGTDAGNQAF
SFVGDTDFSG TAGELRYETL SDRLLLQGDV DGDGLADFSI AMMGLTDMQA SDLIL
//