ID K2MYH5_TRYCR Unreviewed; 1834 AA.
AC K2MYH5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Glutamine-dependent carbamoyl-phosphate synthetase, putative {ECO:0000313|EMBL:EKF27406.1};
GN ORFNames=MOQ_008873 {ECO:0000313|EMBL:EKF27406.1};
OS Trypanosoma cruzi marinkellei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF27406.1, ECO:0000313|Proteomes:UP000007350};
RN [1] {ECO:0000313|EMBL:EKF27406.1, ECO:0000313|Proteomes:UP000007350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:EKF27406.1,
RC ECO:0000313|Proteomes:UP000007350};
RX PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA Andersson B.;
RT "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT with the bat-restricted subspecies T. cruzi marinkellei.";
RL BMC Genomics 13:531-531(2012).
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:EKF27406.1}.
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DR EMBL; AHKC01018306; EKF27406.1; -; Genomic_DNA.
DR EnsemblProtists; EKF27406; EKF27406; MOQ_008873.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000007350; Unassembled WGS sequence.
DR GO; GO:0004055; F:argininosuccinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR CDD; cd00532; MGS-like; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.1260.10; Argininosuccinate synthetase, chain A, domain 2; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR048268; Arginosuc_syn_C.
DR InterPro; IPR024074; AS_cat/multimer_dom_body.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF20979; Arginosuc_syn_C; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF69864; Argininosuccinate synthetase, C-terminal domain; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000007350};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 499..691
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1043..1235
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT ACT_SITE 254
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 341
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1834 AA; 206159 MW; CCBE25B71C2B2D76 CRC64;
MFEEKVKASL VLHGGECFEG YSFGYEESVA GEVVFATGMV GYPEALTDPS YQGQILVLTS
PMIGNYGIPP VETDHFGLTK YFESMGGKIH VSAVVVSEYC DEPAHWQMWE TLGQWLRRNN
IPGIMMVDTR HIVLKLREMG TALGKVVVDD KDVPFVDPNM RHLVAEVSTK TRSTYGHGTL
VILVIDMGVK LNSLRCLLKY DVTLIVVPHD WDITKETYDG LFISNGPGNP QMCTKTIEHV
RWAITQDKPI FGICMGNQVL ALAAGGTTYK MKYGHRGQNQ PSTCRADGHV FITTQNHGFA
VDFKSVSKDE WEECFYNPND DSNEGLRHRT KPFFSVQFHP EGRCGPQDTE YLFGEFITRV
KESKVKEASK YKPRKVLVLG AGGIVIAQAG EFDYSGSQCL KALSEEGIET VLVNPNIATV
QTDDEMADQI YFVPVTAEAV ERVIEKERPD GIMLAWGGQT ALNCGLEMDR LGILKKYNVQ
VLGTPISTIT VTEDRDLFRN ALLQINEQVA KSLAVTSIEE AVGASNVIGF PLMLRAAYCL
GGQGSGIVYN EEELRHKVGV ALAVSPQVLL EESVAGWKEV EYEVVRDIYD NCITVCNMEN
FDPMGIHTGE SIVVAPSQTL TNDEYHMLRS ASIKIIRHLG IVGECNIQYG LDPKSHRYVV
IEVNARLSRS SALASKATGY PLALVAAKIA LGKGLFEIAN GVTKTTMACF EPSLDYIVVK
VPRWDLNKFN MVSQNIGSMM KSVGEVMAIG RTFEEALQKA LRMVDPSHTG FDVPPRLEAR
KNWDHMQDLK IPTPDRIFAI CRALHEGVSV EVIHEMTRIN LFFIKKLHKL ILLQNHMLEK
YKGKIRTMPR EYLLKMKANG FSDAQIAKYV SCTTDDVRER RMELKVTPKV KQIDTVAGEI
PAAQCGFLYT SYNAYHDDVE FTERMYAVLG CGVYRIGNSV EFDYGGVLVA RELRRLGKKV
ILINYNPETV STDYDECDRL YFEEVSEESV LDILLKERIQ GVVISLGGQI VQNMALRLKQ
HGLPILGTDP VNVDKAENRH KFSKMCDELG VLQPEWILST SVEQVHEFCK QVGFPTLVRP
SYVLSGSAMA VIASAADINR YLEEATLVSG EHPVVVSKYY EGAMEYDVDI VAHHGRVLCY
AICEHVENAG VHSGDATMFL PPQNTEKEVM KRIYNTTALI AEELDVVGPM NIQFLLTKDK
QLRVIEANIR SSRSVPFVSK TLGISFPAVM VSAFLSQRDS NLVPIKRARM THIGCKASVF
SFNRLAGADP ILGVEMASTG EVGVFGRDKK EVFLKAMLCQ NFRYPKRGVF ISCDVDAMAE
DLCPCFERIA HRFPVFTTKQ TSRVLADYGI PHTVLTQRHE ESDPTFDMAV AVKEKFDLVI
QLRDKRQDFM LRRCTQENAT PDYWIRRLAV DYNHSLLTEP NVVRMFCETL DVDVKEIEIE
PFRHYVPRVY NKMENDNYTM LHRHKVGLCI TSTNDSKVLA ICLREEKIAL TCFHACLGGI
KNNSEEIAEQ FRSIGVPVEI IDLRTEMAEL GFDMVMAIVD DDTNNWHLQK LSLHVMGLYL
LQAMRMRHMT VVAQSSSRGK KDLNFERYVR TFFPQMGVYN PWRDPSLLDQ FPSEAHKVAF
LRMHGVEARI AQVESHSSVC GITYTFSDTR SMPTPQMVRP LRDCLSVPEF CSLTFRSARC
TNINRTEVTP LQALQMANEI AGRNGIGLVR TREGVMYETP GMTMLSKALR FLYDVCFDRG
AADMFRLYSS HLASQLASQG LMERHTQSAL EAIRYLTREV DGVVEVELNQ GEVIFLKVSH
VRKPAKKRAV KLITEEELED VFQPGNGSFS DVQW
//