ID A0A0G0ZYU1_9BACT Unreviewed; 1165 AA.
AC A0A0G0ZYU1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Parallel beta-helix repeat protein {ECO:0000313|EMBL:KKS27166.1};
GN ORFNames=UU84_C0009G0002 {ECO:0000313|EMBL:KKS27166.1};
OS Candidatus Yanofskybacteria bacterium GW2011_GWC2_41_9.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1619029 {ECO:0000313|EMBL:KKS27166.1, ECO:0000313|Proteomes:UP000033859};
RN [1] {ECO:0000313|EMBL:KKS27166.1, ECO:0000313|Proteomes:UP000033859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKS27166.1}.
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DR EMBL; LCCE01000009; KKS27166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0ZYU1; -.
DR PATRIC; fig|1619029.3.peg.190; -.
DR Proteomes; UP000033859; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 1.10.575.10; P1 Nuclease; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR008947; PLipase_C/P1_nuclease_dom_sf.
DR PANTHER; PTHR41339; LIPL48; 1.
DR PANTHER; PTHR41339:SF1; LIPOPROTEIN; 1.
DR Pfam; PF13229; Beta_helix; 1.
DR Pfam; PF00932; LTD; 1.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF74853; Lamin A/C globular tail domain; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF48537; Phospholipase C/P1 nuclease; 1.
DR PROSITE; PS51841; LTD; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 528..656
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT REGION 420..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1165 AA; 125532 MW; 1DABA68C84B44F78 CRC64;
MENNRFIKLF SFFGIFLAFP LFIFAYSEKT THPALTDEIV DLFNLYYPKL KLSEEEKELL
KKGSIEEDWL YRPIYHFYDP VYNRGLEGTT ISSKEWAMDT VAQASVFRPL AGAITGLFGA
PSDYSWERAI YDYVWKDKER GLVALGHILH LIEDASVPDH TRNDPHPPNL DTSPYEFWAK
KFTPENLEGL ATMIYHSGHS HPVFNSLNEH FDSLATYSNN KFFSKDRIFY KDYDKPIVNY
YSNGFGFYDK EEKYLLIRKI SKFDGTVEYS LIDNKNRILT DYWSHLSKQA VLHGVEVVRL
FFEEAEKERK NWELFAKNKN LMDRVEGNVL NSWGLGLGEA PPKIAEIPPE AFEPVPPPAS
PVIEVELQSE PVAIVPESAT SDDAQVDVKP LLVRQAGPKF DNEENVKHSV LNTLIPIPAG
AGGGGAPAEE EEKSPAPPAD TTGPAVSLSV SECSNSLSAE GCLLASSTLA LSWSSSDSDL
DHYIIECEVA GAACSGFDFA STAATSTNYT LPTDDSAYTF KAEGVDKSGN TGSQVTKTVD
YYTRPVVINE IAWAGTATSS FDEWIELYNR TSKTVSLTNW ALYAEDGVPY VNLSSTIAAG
GYYLIERGAN DTVSDIAADL VTPFSGTGSG SGLSNSGEVL ILSQASTTID QTPSSSACSG
WCAGLVAGFL TMERIDPDTS GTASSNWGSH NGTVKNGQDA GGAALAGTAR ARNSLNYLIT
AGTNLTVSKT LKKSKSPYII KDGVTVNSGV TLTIEPGVVI KFYDADSYLT SQGAIKANGA
SADKIVFTSF KDDEYGGDLN ADAASTTPAA LDWRTIEIQG PGTEFDYAVI RYGGKWYSGI
TFGRTNLKVI NTSVSIKKST IEEAGIYGLW LDGASGTVEG NTFKNNKNDN AAAGIYLIGG
SATITSNTFD TNKVGLKIEP DGSNNPNASS AVNNTFTSNQ NEAINLVRSY PTFSGNSASS
NGINGIVAEG NQNQDYTFVA NLPYVINVSY TVNSGKTLTI NSGTVVKFKD NQSSLAVDGK
ILANGTSASK IVFTSLKDDV HGGDTNNDGS TSSPQAGDWV SVQFNSGAAT STLDNVTMRY
GGGFFNASGA VRISGSSHEI KNSLFELNNF NAIWSSGTGT TTVSNTAFRN NQTGIKVESP
HVFVNGGGII FENNTTNTSP VELVP
//
