GenomeNet

Database: UniProt
Entry: A0A167MUB9_PHYB8
LinkDB: A0A167MUB9_PHYB8
Original site: A0A167MUB9_PHYB8 
ID   A0A167MUB9_PHYB8        Unreviewed;       585 AA.
AC   A0A167MUB9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PHYBLDRAFT_112357 {ECO:0000313|EMBL:OAD74004.1};
OS   Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS   33097 / NRRL 1555).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX   NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD74004.1, ECO:0000313|Proteomes:UP000077315};
RN   [1] {ECO:0000313|Proteomes:UP000077315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG   DOE Joint Genome Institute;
RA   Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA   Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA   Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA   Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA   Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA   Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA   McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA   Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA   Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA   Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA   Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA   De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA   Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA   Gabaldon T., Grigoriev I.V.;
RT   "Expansion of signal transduction pathways in fungi by whole-genome
RT   duplication.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KV440980; OAD74004.1; -; Genomic_DNA.
DR   RefSeq; XP_018292044.1; XM_018428273.1.
DR   AlphaFoldDB; A0A167MUB9; -.
DR   STRING; 763407.A0A167MUB9; -.
DR   GeneID; 28989179; -.
DR   VEuPathDB; FungiDB:PHYBL_112357; -.
DR   InParanoid; A0A167MUB9; -.
DR   OrthoDB; 1459320at2759; -.
DR   Proteomes; UP000077315; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000077315}.
FT   DOMAIN          3..457
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          122..322
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   585 AA;  65361 MW;  BBDAB0F9FDA711FD CRC64;
     MVAIHKILIA NRGEIACRII RTCNRMGILT VAVYSDSDEN APFVKMADEA YHIGDSIAAH
     SYLDSQKLIH AALASGSNAI HPGYGFLSEN SDFTDQVTRA GLIFIGPRAD SIRTIGDKSA
     AKEFITNYTS SMPLIPGYHD EDQNMERLES EANKIEFPIL LKASAGGGGK GMRVVYNTTK
     LREEIEAAKG ESLRSFGSDK LLIEKYFESV RHVEIQIFGD QYGNVYDINE RDCSIQRRHQ
     KIIEETPSPA VDVTLRKAMA TAAVELGRQL RYEGAGTVEF ILDESTKKFY FLELNTRLQV
     EHPITEAISG LDLVELQILV AQGANLKTLG VLENIKFNGH AIECRLCAED PESDFGPRTG
     VIHKWSPANA ARQLQGVRYD TGVEDGSIIS IFYDSMIAKI IVHAPTRAEA IQKMATTLAR
     TVILGVATNQ KFLLSIMNNS CFQSGTFDTN FINKEKSVLF PPLSDTLNSS MVAALVYDWV
     RRKEEKIILR NIPPRWRNVH VNNPCMMFMI GHQQEAKIEY VYQGVKDKRH RFQCYINIAK
     DSTESQMLDV VLFETDMEKE VPGPNGIQGI KGLIRLAISK KEKSL
//
DBGET integrated database retrieval system