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Database: UniProt
Entry: A0A1V4M8X5_9FIRM
LinkDB: A0A1V4M8X5_9FIRM
Original site: A0A1V4M8X5_9FIRM 
ID   A0A1V4M8X5_9FIRM        Unreviewed;       890 AA.
AC   A0A1V4M8X5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=CBS domain-containing protein {ECO:0000259|PROSITE:PS51371};
GN   ORFNames=AVO34_03210 {ECO:0000313|EMBL:OPL11115.1};
OS   Firmicutes bacterium ML8_F2.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1775675 {ECO:0000313|EMBL:OPL11115.1, ECO:0000313|Proteomes:UP000189969};
RN   [1] {ECO:0000313|EMBL:OPL11115.1, ECO:0000313|Proteomes:UP000189969}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ML8_F2 {ECO:0000313|EMBL:OPL11115.1};
RA   Hamilton T.L., Pearson A., Macalady J.;
RT   "Carbon and sulfur cycling below the chemocline in a meromictic lake.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. {ECO:0000256|ARBA:ARBA00007265,
CC       ECO:0000256|RuleBase:RU003953}.
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:OPL11115.1}.
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DR   EMBL; LQBG01000067; OPL11115.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4M8X5; -.
DR   Proteomes; UP000189969; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR   CDD; cd04595; CBS_pair_DHH_polyA_Pol_assoc; 1.
DR   CDD; cd05398; NT_ClassII-CCAase; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 2.
DR   Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR   Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR001667; DDH_dom.
DR   InterPro; IPR038763; DHH_sf.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002646; PolA_pol_head_dom.
DR   InterPro; IPR032828; PolyA_RNA-bd.
DR   PANTHER; PTHR47788:SF1; A-ADDING TRNA NUCLEOTIDYLTRANSFERASE; 1.
DR   PANTHER; PTHR47788; POLYA POLYMERASE; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF01368; DHH; 1.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU003953};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          312..370
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          374..434
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   890 AA;  101557 MW;  CE68D9C063881C69 CRC64;
     MDLIITHENS DFDALAAVVA AAKLYPGSYV LLPEQLQPNV RSFVNLHRDL LPLIDPREIV
     DDNIDLLLII DTNRRERLGK WEYMVDRAAH VYIYDHHPGD EDIDAEKSSI EAIGATTTIL
     LEKLRKKKIK ITEFEATLFA LGIYEDTGCL TYEITTSRDA RAVSYLWDAD LSVSLLQEYL
     RSPLNDTQKR LLEKLIHSSE LHELNRRRVL ISSTSLNEYV VGASVLLQLL DEIEDAGMTI
     VIIRMTDSIY MAARSRDEDL NLLELLAPFD VRGYPAAVST HFKGTNTEVV KEQVLAYLEE
     NLPFSLTAGE VASRPVFSLD SDTSLDVADG LLVEHNFKGC PVMEKGRLVG IISRRDLQKG
     MRNELGHAPV KGFMTRQVIT ASPQDSLTEL RRLMMEHNIG RVPIVDEMDK LGGIITRSDI
     LRHLNYFDRH GHSLKKRSSI DGSYERVDGE EKLTGGDELN LLELVESGLS TEIKSLLRTI
     SRLAERKNME VYMVGGIIRD LLLRYPPEKD LDFVVIGDAI AFTYALQKIS NGTVRHFDQF
     GTASLYMKDG TRLDFVTARR EYYESPAALP RVESSGLKND LFRRDFTINA MACSLDSENY
     GRLYDYFNGR KDLRNRLIRV LYELSFVDDP LRILRAVRFE QRYNFTIDEE TLKLIEKAID
     KKVLVKVSRQ RINHELRIVF REPSPVRILK RFEQLGLIDL LYPGAKTDSE TWLRLSSLEK
     LLRRAEEKGW QNKPDREMVY LSSLLYGLES AKRSAIIKKL NLSREKADAV KVACLEAPSV
     VEKLADEEHK PSTIVSLLQH LPAETIFLAY TLAGLKTIRS RLKLYLDQLQ LVKPHLNGSD
     LKRIGLKPGP FYRRVMADLQ KAVLDGELKT EEEEVAFVEK YMKEMKTGED
//
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