ID A0A1M4S0Q8_9ACTO Unreviewed; 759 AA.
AC A0A1M4S0Q8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=5'-nucleotidase/apyrase {ECO:0000313|EMBL:SHE25749.1};
GN ORFNames=ACGLYG10_1985 {ECO:0000313|EMBL:SHE25749.1};
OS Actinomyces glycerinitolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=1892869 {ECO:0000313|EMBL:SHE25749.1, ECO:0000313|Proteomes:UP000184291};
RN [1] {ECO:0000313|Proteomes:UP000184291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Strepis N.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQTT01000011; SHE25749.1; -; Genomic_DNA.
DR RefSeq; WP_073331106.1; NZ_FQTT01000011.1.
DR AlphaFoldDB; A0A1M4S0Q8; -.
DR STRING; 1892869.ACGLYG10_1985; -.
DR OrthoDB; 1016457at2; -.
DR Proteomes; UP000184291; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
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 PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Reference proteome {ECO:0000313|Proteomes:UP000184291};
KW Signal {ECO:0000256|RuleBase:RU362119};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 31..759
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5039745754"
FT TRANSMEM 737..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..250
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 352..533
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 759 AA; 77391 MW; EE142C05E1C66247 CRC64;
MPHLYRRLVA FTAALALGAF APAITAPATA AEAADTTTLS ILGITDLHGH IETTGDEPGA
VTLACEVAAA RERNPSTLFV SNGDNVGGSA YISSILDDQP TIDVLNAIGL DVTSAGNHEF
DKGITDLADR LLPAFNAPIL SANVTGNAAL GAEGSGNGTW ITEVDGVTVG FIGVVTEELP
SLVSKSALEG LTVSDATATA NARATALKDG DAANGEADVV VVLAHEDAAI YGNQFNGAVD
AVVAGHTHVP FADVVKSTDG TDIAVVQPDH YGLKLGEISL TVTTAADGTK DVTAATARNL
DLAESDCTTD AYGVADIVAK AKTDSEAAGN EVLTTLGSNF YRGTDTGTDY GANRSTESTA
SNLIATSFAS WLAEDIQPSS DYAIGLMNPG GVRADYLAGE LTAGEAYTVQ PFGNEMAYAT
YTGAQVKQVL AEQFQPTTTR AALMLGTSDN VEVYLDQDAA DQLEDYFTQI STAASEAERS
ALVESLADDI ADARSRVIDA VYIDGELLDD AATVTVASNT FLLAGGDNFD TLGEKTMINT
GILDRTVTSE YLVRISPATA SYDKHQVGTS LAVDGDTVTA RFTGLSYSAT AEQGVRDAAT
SIAATVDMAD GTTRTLTTSD IDQSVTPGLP ETGQATLTFT LPDGVATQDC TVDGVSTTCA
TVSFTITRAD ESTETLAVTA QVVRAVSPET PAPSTPSAAV GPATGAPTTA GVVPVVAGTP
ATGHGSRGAL ARTGAPIALG LLALGLMGGG TLLTARRRD
//
