ID A0A0V0TBU4_9BILA Unreviewed; 1090 AA.
AC A0A0V0TBU4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Cytosolic purine 5'-nucleotidase {ECO:0000313|EMBL:KRX36462.1};
DE Flags: Fragment;
GN Name=NT5C2 {ECO:0000313|EMBL:KRX36462.1};
GN ORFNames=T05_497 {ECO:0000313|EMBL:KRX36462.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX36462.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX36462.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX36462.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC {ECO:0000256|ARBA:ARBA00009589}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC family. {ECO:0000256|RuleBase:RU000677}.
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:KRX36462.1}.
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DR EMBL; JYDJ01000362; KRX36462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0TBU4; -.
DR STRING; 144512.A0A0V0TBU4; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd07522; HAD_cN-II; 1.
DR CDD; cd09337; LIM2_Paxillin_like; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 3.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR HAMAP; MF_01988; Succ_CoA_alpha; 1.
DR InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR005810; CoA_lig_alpha.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR InterPro; IPR001781; Znf_LIM.
DR NCBIfam; TIGR02244; HAD-IG-Ncltidse; 1.
DR NCBIfam; TIGR01019; sucCoAalpha; 1.
DR PANTHER; PTHR12103; 5'-NUCLEOTIDASE DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR12103:SF15; CYTOSOLIC PURINE 5'-NUCLEOTIDASE; 1.
DR Pfam; PF05761; 5_nucleotid; 1.
DR Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR Pfam; PF00412; LIM; 2.
DR PRINTS; PR01798; SCOASYNTHASE.
DR SMART; SM00881; CoA_binding; 1.
DR SMART; SM00132; LIM; 3.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 3.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|RuleBase:RU000677};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 610..669
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 670..728
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 534..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX36462.1"
SQ SEQUENCE 1090 AA; 122989 MW; 7CFC52D3A9DDC3AE CRC64;
LGIFKSVAME NTMVKKYHRD PGKRVFVNRS LELEKIKFFG FDMDYTLAVY KSPEYEILGF
RLVIERLISI GYSPELLQLK YDNTFPIRGL WFDNLYGNLL KVDAFGNILV GVHGFEQAIE
SLYPNKFIQL SEDRVYVLNT LFNVPETYLI ACLVNYMDNC PGSSREPSGV KLGDMYMSYK
SMYQDVRAAV DWVHYHGDMK RITLNNLEKY VHKDPRLPML LTRMRDNGAK TFLLTNSGYF
YTDKVMTYLL DSETKSWRSY FDFIVVDANK PLWFAEGTVF RQVDQGTGTL RIGSHLGPLR
PNQIYAGGSS EVFSKLVGAR GREVLYLGDH IFGDVLRSKK GRGWRTFLVV PELVQELHVW
TERRGLFTRL QNLDIQLGAA FKNMDSSSEI RPDIREIRES MRSVTHEMDM AYGMLGSLFR
SGSRQTFFAS QVERYADLYA HSCCNLLYYP FFYFFRAPSM LMPHESTVEH EETGPIDFSG
LTPIDRGRNV TISESMEGLS VGEPMTTVHH HHPHHHHLQS CAVMNDSESK RFTRAETPTE
STYVHEEEER EEDSCDMSQH SVEGTNSPMF GSFKRAKHVR IDFNDSMTNS NSDSIQNDLA
RYGINNVSNE ECEACKKSIV GQVAIALGKM WHEEHFVCAH CGERLAHRNF YERSGSIYCE
HDYHRLFSPR CAYCNTPIKE KCITALDQTW HPEHFYCAKC GRPIGEEIFH EKDGRAFCHK
DYFTNFTPTC HGCKRPITGH YITALNCEWH SDCFVQQIIM ASRLLFRRFL NGNQHRSKDF
HRFLYSETRK FLKIGHETKV ICQGFTGKQA TFHCRQMLDY GTKIVGGVSP TKAGTKHLNL
PVFGSVEEAV KETEADATIL YVPAQASADA IHEAIDAKVP LIVVITEGIP QLDMVKVKQK
LLKQSDCRLV GPNCPGLIRP NECKIGIMPG HIHQPGCVGI VSRSGTLTYE AVQQTTDVGL
GQTLCIGIGG DPFNGTNFVD CLDLFLQDPE TRGIILIGEI GGNAEERAAE YLKINNTGAN
AKPVVSFIAG VTAPPGRRMG HAGAIISGGK GTAAHKIEAL KEAGVTVVMS PAQMGISLAR
HVYHGQPGAH
//
