ID R9LV83_9FIRM Unreviewed; 1453 AA.
AC R9LV83;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Competence/damage-inducible protein CinA domain {ECO:0000313|EMBL:EOS62714.1};
GN ORFNames=C814_01108 {ECO:0000313|EMBL:EOS62714.1};
OS Anaerotruncus sp. G3(2012).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=1235835 {ECO:0000313|EMBL:EOS62714.1, ECO:0000313|Proteomes:UP000014129};
RN [1] {ECO:0000313|EMBL:EOS62714.1, ECO:0000313|Proteomes:UP000014129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G3(2012) {ECO:0000313|Proteomes:UP000014129};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anaerotruncus bacterium G3.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EOS62714.1}.
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DR EMBL; ASTA01000020; EOS62714.1; -; Genomic_DNA.
DR RefSeq; WP_016315801.1; NZ_KE159668.1.
DR STRING; 1235835.C814_01108; -.
DR PATRIC; fig|1235835.3.peg.1170; -.
DR eggNOG; COG1058; Bacteria.
DR eggNOG; COG1546; Bacteria.
DR eggNOG; COG2385; Bacteria.
DR eggNOG; COG4509; Bacteria.
DR HOGENOM; CLU_260753_0_0_9; -.
DR Proteomes; UP000014129; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:InterPro.
DR CDD; cd05826; Sortase_B; 1.
DR Gene3D; 3.30.70.2860; -; 1.
DR Gene3D; 3.90.950.20; CinA-like; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR Gene3D; 2.40.260.10; Sortase; 1.
DR InterPro; IPR036653; CinA-like_C.
DR InterPro; IPR008136; CinA_C.
DR InterPro; IPR041424; CinA_KH.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR005754; Sortase.
DR InterPro; IPR023365; Sortase_dom-sf.
DR InterPro; IPR013486; SpoIID/LytB.
DR InterPro; IPR013693; SpoIID/LytB_N.
DR InterPro; IPR009835; SrtB.
DR NCBIfam; TIGR02669; SpoIID_LytB; 1.
DR PANTHER; PTHR13939; NICOTINAMIDE-NUCLEOTIDE AMIDOHYDROLASE PNCC; 1.
DR PANTHER; PTHR13939:SF0; NICOTINAMIDE-NUCLEOTIDE AMIDOHYDROLASE PNCC; 1.
DR Pfam; PF02464; CinA; 1.
DR Pfam; PF18146; CinA_KH; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF04203; Sortase; 1.
DR Pfam; PF08486; SpoIID; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF142433; CinA-like; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR SUPFAM; SSF63817; Sortase; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000014129}.
FT DOMAIN 4..171
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
FT REGION 741..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 807..857
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 744..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1197
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 610
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR605754-1"
FT ACT_SITE 714
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR605754-1"
SQ SEQUENCE 1453 AA; 155225 MW; B4176EA7D751BE50 CRC64;
MIAEIIGVGQ ALLDGQTLDT VADLIAEQLE GCGVQTEDVC AAGSDPVRLR GAIGRAIGRS
DIVVLVGGLG MTPADISKET VCAGLGRRLV LHEESQRRIR EAYLHAGRQM PQQAVKLAMM
PEQSIVFPGV KGVTPGCAIS AGRQFLLMIP DNPDEFLPMF HKSIVPYLSR FSPAAVFTRT
LSLFGIEEAE LRTLLEGYLD SENPKVELFP SNGEFLVRIT ANAENKEEAA ELLNPVLFEI
RAVLGGSVYG VDVQGGLPAA TAALLQERGI QVNVGESGTN GLLADLLTGQ SDGRVVAYSV
SAYASHVKKD ALGIPDKVLK RYSPVSEQIA VHMAHGALQQ ENAAFGVAVT CNTALRGEDP
KKNGLLYAAV CDGKQVWVRR VLLPQDSSGD YVRHMAAMHT LNLLRLCAGT SGCPGGIPVD
EALDPKFALP KQENAFVSAR KWESGSKPAP VLPSQNRAWY AAVFPVKGDT PGAVFRKLLL
LAALVVFLGS AAFLIHYYLS GRSNAALYDE LRQVYLTGAD DQQAEEAVAR GKFPAGYQSK
FLNLYQTNED LVGWLSVGKN LFSYPVVQAD DNERYLNTNF QNKSSRYGTP MLDAGNSLAS
ESDNYLIYGH NMSDGQMFAG LTRYKPAEGG LDFLNANPTI SFADVYEDNE YEIVSVFITN
VTDKYGDVFY YNDYQDLSDP ARFIEFTEEV TARSFYTSDI AIQPGDRFLT LSTCSYEYGP
KSRDADVRTV VVARRLRDGE SPSASYALNP SPRMPSGFTD HQGGQSAPQD ADSIPSSGNA
ADVIDALAPV VDPDSLDDHE YSAYAAYESI KQALVDAEQA AKATRQAAQK AASAADEASA
QSEAEKAALE MKKAEDAYWR IADHVGVLND LREERSTEYI ESICERAQAA LVQAEAYRDA
SSQSAAQAGQ TGGGAPVASM EVASSAPSAG SSAPAPSSTP APSSSAPALS SSAPAPGSSV
PAPSSSAPAP SSSVPVSSSS APAPSSSAPA PSSSAPAPSS SAPAPSSSTP APSSSRPVPS
SSVPVKPVVS SSSREDVAAR NKEALEKTEE YQQTLDDVVS DAREVREIAR DASDEAYDAK
TAKAVRTAAD RIEDALEEIR SLCGEVEDTS DGLKTLYQRT NLQQTREAVQ DAADILEVLE
EYESEVEELW VDADNKAYKL ENEPSSSASS SSSGSSSGSS SKGDEDDEDD EDDEDGRPNS
AGELTISISG KKTTGSASEI VQQVVMAEMG SSFNDEAIKA QAVAAYSYIL HQNRGGTIPA
LGVKTPNDRM KKLVDSVIGE AVYYNGSLAF TPFYATSAGI TVSSEDTWGG SYPYLVSVDS
SVDEQAGGYE RTVTMSTSKV AERIKKILKE DIYDYSDDPE DWIEILSYSK GGKYVRKVRI
GKDEVSGRYM RENVFGLRSA AFEVVCDGDS FQFTTYGYGH GVGMSQTGAN LYAAKGWDYV
DILTHYYPGT TVK
//