ID A0A0V0V7C6_9BILA Unreviewed; 1163 AA.
AC A0A0V0V7C6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cytosolic purine 5'-nucleotidase {ECO:0000313|EMBL:KRX59404.1};
DE Flags: Fragment;
GN ORFNames=T09_10516 {ECO:0000313|EMBL:KRX59404.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX59404.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX59404.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX59404.1};
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:KRX59404.1}.
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DR EMBL; JYDN01000073; KRX59404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0V7C6; -.
DR Proteomes; UP000054681; 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; 2.
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; 2.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
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:UP000054681};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 714..773
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 774..832
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX59404.1"
SQ SEQUENCE 1163 AA; 131158 MW; BC5FD8872F1A97DF 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 LMPHENRGRN VTISESMEGL
SVGEPMTTVH HHHPHHHHLQ SCAVMNDSES KRFTRAETPT ESTYVHEEEE REEDSCVNNG
NFSLVHDATQ QSAAAAAAAT TTTTMQSQRM CKHALLVVVA AWEKLHAPID FHFWNKRRKE
KQLAAANNKQ WRLRKSMIIK PLSKEAFVLL RYSTLFSLLF ITKQQLTALF AFSWDAFLSP
HSVHSVEGTN SPMFGSFKRA KHVRIDFNDS MTNSNSDSIQ NDLARYGINN VSNEECEACK
KSIVGQVAIA LGKMWHEEHF VCAHCGERLA HRNFYERSGS IYCEHDYHRL FSPRCAYCNT
PIKEKCITAL DQTWHPEHFY CAKCGRPIGE EIFHEKDGRA FCHKDYFTNF TPTCHGCKRP
ITGHYITALN LIPRETRKFL KIGHETKVIC QGFTGKQATF HCRQMLDYGT KIVGGVSPTK
AGTKHLNLPV FGSVEEAVKE TEADATILYV PAQASADAIH EAIDAKVPLI VVITEGIPQL
DMVKVKQKLL KQSDCRLVGP NCPGLIRPNE CKIGIMPGHI HQPGCVGIVS RSGTLTYEAV
QQTTDVGLGQ TLCIGIGGDP FNGTNFVDCL DLFLQDPETR GIILIGEIGG NAEERAAEYL
KINNTGANAK PVVSFIAGVT APPGRRMGHA GAIISGGKGT AAHKIEALKE AGVTVVMSPA
QMGISLARHF DLAHSNELND IYF
//
