ID A0A0M0KR91_9BACI Unreviewed; 722 AA.
AC A0A0M0KR91;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=2,' 3'-cyclic nucleotide 2'-phosphodiesterase {ECO:0000313|EMBL:KOO41117.1};
GN ORFNames=AMD01_19420 {ECO:0000313|EMBL:KOO41117.1};
OS Priestia koreensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=284581 {ECO:0000313|EMBL:KOO41117.1, ECO:0000313|Proteomes:UP000037558};
RN [1] {ECO:0000313|Proteomes:UP000037558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16467 {ECO:0000313|Proteomes:UP000037558};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14210 dsm16467.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
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:KOO41117.1}.
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DR EMBL; LILC01000030; KOO41117.1; -; Genomic_DNA.
DR RefSeq; WP_053403099.1; NZ_LILC01000030.1.
DR AlphaFoldDB; A0A0M0KR91; -.
DR STRING; 284581.AMD01_19420; -.
DR PATRIC; fig|284581.3.peg.4269; -.
DR OrthoDB; 9775118at2; -.
DR Proteomes; UP000037558; Unassembled WGS sequence.
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:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
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; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR11575:SF48; 5' NUCLEOTIDASE, ECTO-LIKE; 1.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF00395; SLH; 3.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
DR PROSITE; PS51272; SLH; 3.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Reference proteome {ECO:0000313|Proteomes:UP000037558};
KW Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 25..722
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5039741212"
FT DOMAIN 543..606
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 607..666
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 668..722
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
SQ SEQUENCE 722 AA; 78692 MW; EB05922250B70F51 CRC64;
MRKNVFKPIV SLSLASALSL GAFAAPFSND FAKAETQNIK VQLLGLNDFH GQMDYSDKLD
LDKDGVKETP IGGIAYTAAA IKQHQAENPN TLLVEAGDMV GGSPLVSSYF QDEPTIEILK
EMGFSVGTLG NHEFDEGVTE MLRMVNGGNH PDGKSIPGVD YTGTGFPVVA ANVVYKDTGK
LMLDPYTIKE VGGEKIGFIG VVTQETPYMI VQKGNENLAF TDEAEAINKY TKELKEKGIK
SIVVLAHNPT TNTTDNASFD ASKIAEKVDD EVDVIFAAHN HVGVNKVVDN KLIVQAYSYG
TAFSDVDLEI DPTTHDIVKK SADVVTVIQS KYTPDPKVQA IVDKYEEKVK PVKEQVVGES
AVELSGKYAQ KGPVGDNSLG NLIADGMKEN MKADFALMNG GGIRASVNAG PITWGELFSV
QPFGNTLAKV DVTGQDLEDI LNAQIDPVKG LDVSVGGFKY TWSSQTNKVV DIFLPDGSKI
DKKKTYSVVV NNYMYGNPTY RIAELGENME VGPSDLEATV EYVKSLKQPI SYKAEGRISE
VTLSLPFKDV ADNHWAHDYI NDLYFKNIIK GTSDTMFSPD KELSRSQFAS LLVRALNIKT
DKTTDFKDTA KLSEQVQKEV AAAVSSGIVV GRTAKTFAPY APITRAEMMT MLMRAYKVKN
GSVPAPTKDV FKDTSTLKPE MKDAIEVAYE LGYVDGFGDQ FKPFNTAKRA ESAKVLYMLL
KK
//