ID G3VJ88_SARHA Unreviewed; 780 AA.
AC G3VJ88;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSHAP00000003243.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000003243.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000003243.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000003243.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004672}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004747}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000256|ARBA:ARBA00011823}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase
CC family. Class II subfamily. {ECO:0000256|ARBA:ARBA00010478}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the SAICAR synthetase
CC family. {ECO:0000256|ARBA:ARBA00011020}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; G3VJ88; -.
DR Ensembl; ENSSHAT00000003279.2; ENSSHAP00000003243.2; ENSSHAG00000002861.2.
DR GeneTree; ENSGT00390000010172; -.
DR HOGENOM; CLU_061495_1_0_1; -.
DR UniPathway; UPA00074; UER00130.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0043727; F:5-amino-4-imidazole carboxylate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01416; SAICAR_synt_Ade5; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR HAMAP; MF_02045; PurE_classII; 1.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR044822; Myb_DNA-bind_4.
DR InterPro; IPR033626; PurE_classII.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR InterPro; IPR001005; SANT/Myb.
DR PANTHER; PTHR43599:SF3; BIFUNCTIONAL PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE_PHOSPHORIBOSYLAMINOIMIDAZOLE SUCCINOCARBOXAMIDE SYNTHETASE; 1.
DR PANTHER; PTHR43599; MULTIFUNCTIONAL PROTEIN ADE2; 1.
DR Pfam; PF00731; AIRC; 1.
DR Pfam; PF13837; Myb_DNA-bind_4; 2.
DR Pfam; PF01259; SAICAR_synt; 1.
DR SMART; SM01001; AIRC; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE); 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lyase {ECO:0000256|ARBA:ARBA00022793};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000007648}.
FT DOMAIN 5..69
FT /note="Myb-like"
FT /evidence="ECO:0000259|SMART:SM00717"
FT DOMAIN 163..215
FT /note="Myb-like"
FT /evidence="ECO:0000259|SMART:SM00717"
FT DOMAIN 621..768
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
SQ SEQUENCE 780 AA; 87803 MW; 02FCBC4BF0181D9B CRC64;
MESGAGKHWT EEEVKALLTV WSEKNIRKQL YRTLRNKGIF IHIAKRLQEK GIFRDWKQCR
SKYKNLKYEY RTVKHAHNSG DGSKTMKFFC ELDAILQYEP VSQLTEDEDS RDLASETQLV
TSSASENIKG KPTSILDSNN PTLIPSVANE GGKHWTINEV KALIDIWSDK NIQKQLEGTM
RNKRIFEQIA AKLQKFGIDR DWKQCRTKYK NLKHEYKIVK NCQDLGTTKS MKFFTELDAI
LGHTSEQSQK LENKESQRTT KQTNIKMEIS NRESFEGHAM NAESLNKRKA HEDELVPLPL
KRSTSDTIGH EFHLTTKQKG STVHLCGQET KHIQLLQSAS QVPAGLPLAS AFTTEMATAE
VIKIGKKLYE GKTKEVYELL DNPGKVLLQS KDQITAGNAA RKNHLEGKAA ISNKITSCIF
KLLQEAGIKT AFTKKCGDTA FIAPQCEMIP IEWVCRRIAT GSFLKRNPGV KEGYKFYPPK
VELFFKDDAN NDPQWSEEQV IAAKWCFAGL NIGQTEVDIM SHSTQAIFEI LEKSWLPQNC
TLVDMKIEFG VDVTTKEIVL ADVIDNDSWR LWPSGDRTQQ KDKQSYRDLK EVTPEGLQMV
KRNFEWVAER VELLHKVQSP CRVVVLMGST SDLGHCEKIK KACGNYGIPC ELRVTSAHKG
PDETLKIKAE YEGDGIPTVF VAVAGRSNGL GPVMSGNTAY PVVNCPPLTP DWGAQDVWSS
LRMPSGLGCS TILSPEGAAQ FAAQIFGLNN HLVWAKLRGG MLNTWVSLKQ ADKKIRECSL
//
