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Database: UniProt
Entry: K2MYH5_TRYCR
LinkDB: K2MYH5_TRYCR
Original site: K2MYH5_TRYCR 
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
//
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