ID A0A0V0TWN2_9BILA Unreviewed; 1504 AA.
AC A0A0V0TWN2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Putative phosphoribosylformylglycinamidine synthase, chloroplastic/mitochondrial {ECO:0000313|EMBL:KRX43377.1};
DE Flags: Fragment;
GN ORFNames=T05_14411 {ECO:0000313|EMBL:KRX43377.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX43377.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX43377.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX43377.1};
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 -!- 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:KRX43377.1}.
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DR EMBL; JYDJ01000121; KRX43377.1; -; Genomic_DNA.
DR STRING; 144512.A0A0V0TWN2; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
DR CDD; cd02204; PurL_repeat2; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR036604; PurS-like_sf.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR SUPFAM; SSF82697; PurS-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048}.
FT DOMAIN 175..288
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 529..673
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 925..1025
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1206
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1338
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1504
FT /evidence="ECO:0000313|EMBL:KRX43377.1"
SQ SEQUENCE 1504 AA; 168190 MW; 5EE41EE4EAD69496 CRC64;
MIVVRLQELF VQCSSSKAGW HEKPKEENPF KLPIEWKNVV NAVSKNISNR KQSKNHPIKH
PLLAHSKKHA APVRRLPSQE IVILISATAQ KCSFDDCEKS SFSVIFLVST AYSTVVINIT
SITVIKMPNE TVFRFYYWQI NEQLGNEILK KLLNDMLEGE NLSVESVRCE FTFCVVSTRS
SITNEEIAKL KWLIERPFNM ETLAAESAFA YTRPENRVII EIGTRPYLVT PFNINAVVAC
KLAGLNFVSR LEKTRRYCIH YNRGKLSLPI RRKILTALHD RMTECEYTSD VVDFGTRRER
QKVQEVEIMI DDKVDLTIED EDIKYMLDLF KYKLKRNPTD VEIYDLTQSN SVIRGLNVLQ
MRPVDPTEAS EFQIFPVLSH IVLAAETNNF QAEFDADLGI CPSTGAASGT GGRIRNIHAT
GRGAYVVAGI FGLAFGNLNV PGHRLPWERC NHAESCTFAS PLQICVQASD GSSEYGNKFG
EPVICGFTRS FDQYVNELAC RYAYLKPVMF SGGVGRIDEM NIQKLKPAPG MLIVKLGGPA
YRVSLGGGTS STIEIHGNGC LQYEAVHRGD PGMGQKLNRT IRTCSELGRN NPIISIYDQA
AGGNGNVIRK LIEPYGASIE SDNFSLGDSS LSIQELWSSE YQESDAILMN PKNVPLIEKI
CQRERCLYNV VGSLLVKNFH DAADSFELPK SFILSKPVRS ATQTFRKFSL DAPIETALKR
VLLLPSVGSK NFITNKVDRS VTGLVAQQQC VGPFHTPVAD VAVTALSYFE TVGAAVAVGE
QPIKMLIHPE VGARLTVGES LTNLDVKCNA NWMWPATSPE ERYRMLEACD AMCKIMNKLG
IAVDGGNESL FLEAEINEEV VKAPGTLVIT SYALCTDITK TVTPDLKCTT EDGCLILVRF
ASLFDSWRLG GCAIAQGYGR TGCDSPDLDN VEQFKSAFRI TQSLISDRMI SAGHDISDGG
LIVCLLEMAF SGGRSIVIDL PFTEKPINLL FSEELGIVIE VSQSNFDKVL NDFHAANVPV
AYIGKSKSLT DEEPMIEIKI NGDVVLAGSV QSYRCTWQQT SCRLEKLQCN PICVEEEVFR
LKLKLPKYEM QSLMEIPAVS QHATVKDAST PCVAILREEG TTGDREMAAA FMCAGFRVWD
LSMQDLFDNN ISLNNFQGIV FPGGFSYSDV LGASKAWACS ILYHPKVKYQ IEQFLQRRDT
FSLGVCNGCQ LMATLGWIGS NEAIGRSVQS VSLEQNISGR FESRFATVRI ERSRSIMLRG
MENSVLGIWI AHGEGRFQFR DDLAYAAVEF NHLIALRYVD WENEIALAYP YNPNGSPGGI
AAICSANGRH LAMMPHPERS FMTWQWPYWP YEHAPVSPWY HMFRNAYEWF LAFLLRGFNG
QWIEPVKCLD YISSSICSGI LKVYGEDRCR IDFLFGRYQC CWTCAATLGI PIDSLGRFND
QQGFYFYHPG CPNNVRDAID ALGSSSTQWC MHWKEKNNGM NCYEPLFQYK CYKTCRVKCG
AFSD
//
