ID A0A1M6I911_9CLOT Unreviewed; 1420 AA.
AC A0A1M6I911;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=2',3'-cyclic-nucleotide 2'-phosphodiesterase / 3'-nucleotidase {ECO:0000313|EMBL:SHJ30950.1};
GN ORFNames=SAMN02745163_01734 {ECO:0000313|EMBL:SHJ30950.1};
OS Clostridium cavendishii DSM 21758.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121302 {ECO:0000313|EMBL:SHJ30950.1, ECO:0000313|Proteomes:UP000184310};
RN [1] {ECO:0000313|EMBL:SHJ30950.1, ECO:0000313|Proteomes:UP000184310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21758 {ECO:0000313|EMBL:SHJ30950.1,
RC ECO:0000313|Proteomes:UP000184310};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FQZB01000007; SHJ30950.1; -; Genomic_DNA.
DR RefSeq; WP_072986269.1; NZ_FQZB01000007.1.
DR STRING; 1121302.SAMN02745163_01734; -.
DR Proteomes; UP000184310; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008252; F:nucleotidase activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR CDD; cd00845; MPP_UshA_N_like; 1.
DR Gene3D; 3.60.21.10; -; 2.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 2.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR019079; Capsule_synth_CapA.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR11575:SF48; 5' NUCLEOTIDASE, ECTO-LIKE; 1.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR Pfam; PF02872; 5_nucleotid_C; 2.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF09587; PGA_cap; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 2.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 2.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Reference proteome {ECO:0000313|Proteomes:UP000184310};
KW Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1420
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009918340"
FT TRANSMEM 1398..1416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1389..1420
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT REGION 1154..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1420 AA; 155382 MW; 267415F68862CB3A CRC64;
MRKMCKMKRV TGALLTVMMT AYTVTPGFST LVRADELQKG DKVIDLVGIT DFHGQLTYVK
GDKVTQTAAI LSKAVKDVQK SNPEGTLVIG GGDLYQGTPE SNILKGVPVQ KVMSGLGMEV
TALGNHEFDW GLETIKDETM KDAKYEILCA NMYKKGTNER PYKPYKVIKK NGVKIAVVGA
ISTDTPGIVL KSRVENYEFK DEATEINKAV EEVKDAEKPD AVILTIHEGE RDDPKEIPLT
KVVNKLKGVD AVFGGHSHWQ KDMIVKDADG KERPVVIASS NGKGYVDMKM TVKADNTLSF
SAPKTNYNNL LKAKEEDPEA RAIVDEAVAQ VAPKFAVEIG STTKGLNRSF KGDYGDSQLG
NWACEVTKKA TKADVAIQNN GGIRADIPAG KITVGTMFNI MPFDNELVTL ELTGAQFKTL
LEQSVADTEK GKASGVQIAG AKFEYDMSRP SGNRITKVTK DDGSAIKADQ KLVLATSDFL
STGTASNLTV FGDKTIQESI NKTHRLLRDV FADAVKETGV IDSAVDGRIK VGKVVENADK
NVQILATSDL HNRMVAWDYA TDSANPKGSF AKVATKVKAL RETNENTILV DAGDAVQDNS
AALFLDMTKY PVHPMIQGMN KLGYDIWTLG NHEFNYGIPT LKNFIKTSNA KVLCANLYDT
DGKTRIAAPY EIVERDGVKI GFIGITTPNI NKWDSVNLKD YKVTGAVEEV QAAIKELTGK
VDTMVGVFHM GEQDEYDIPE TGVISVASKC PELSTIIAAH MHITIDKHYA YKGKAYGSIT
DKTGKITYVA LDKDINSTNV TKEEYDEAVK NGVMIVENGK FAENLGKLNL TFANKDGKYQ
LTNKTFGLEN LANVEEDKEF VELFKQYDEI AKQDAKIVIG QLKGGDLVPQ DVVKGIPESQ
VAPTAMIDLI NKVQMYYGEK ISGKKIDVAA AAAFRGDANI KEGNITKSGT SLIYKYDNTL
YVVEVTGKQL KEYMEWSSSY YNTYKDGDLT VSFNPKMPGY NYDMFTGVKY QIDISKNVGN
RILNLTKMDG TKITDDMKLT LAVNDYRGKS QLMGAKTIFS DKSEAKLICK SEDKMGDDGR
IRDLLRSYIV DVKSGVITPE CDNNWSIVGN NWDPAQRAAL IKAVNEGKLQ PKASEDGKTS
NAIALTWADV QAVGGSVDPS NPVDPSNPVD PNKPVDPTNP VDPGKPVNPT KPENKEQAKV
ESKLENNKVV VNKIANKDAE NVIEAKDLDS KNVTEIEIGN AEEMRDGKGS IKVNIKDAVI
NLPFSAIDKE LLVPGSTVVL RSKVIDNADI VKNLKGVKKV YSFDLIVKNG DKETQIHNFK
DGKAEITITL SDDELKGLNK DKLAVFYYNE QTKKFEIMET KVDGNKVTFL TPHFSQYVIA
EKQDGDSSLP KTGSDVNTTN VALLALGLIG LGVVVIRRKK
//
