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Database: UniProt
Entry: Q6BPM2_DEBHA
LinkDB: Q6BPM2_DEBHA
Original site: Q6BPM2_DEBHA 
ID   Q6BPM2_DEBHA            Unreviewed;      1159 AA.
AC   Q6BPM2;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   24-JAN-2024, entry version 109.
DE   SubName: Full=DEHA2E12452p {ECO:0000313|EMBL:CAG88087.2};
GN   OrderedLocusNames=DEHA2E12452g {ECO:0000313|EMBL:CAG88087.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88087.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88087.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC   2968 {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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DR   EMBL; CR382137; CAG88087.2; -; Genomic_DNA.
DR   RefSeq; XP_459848.2; XM_459848.1.
DR   AlphaFoldDB; Q6BPM2; -.
DR   STRING; 284592.Q6BPM2; -.
DR   GeneID; 2902522; -.
DR   KEGG; dha:DEHA2E12452g; -.
DR   VEuPathDB; FungiDB:DEHA2E12452g; -.
DR   eggNOG; KOG3508; Eukaryota.
DR   HOGENOM; CLU_002973_1_0_1; -.
DR   InParanoid; Q6BPM2; -.
DR   OMA; WFVGLNY; -.
DR   OrthoDB; 22721at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   CDD; cd05137; RasGAP_CLA2_BUD2; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR039360; Ras_GTPase.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR001936; RasGAP_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   PANTHER; PTHR10194:SF60; GTPASE-ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   DOMAIN          367..490
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          576..836
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   REGION          617..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..975
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1159 AA;  132065 MW;  597C5F62AAD21ADC CRC64;
     MKYPTPFHEV ISKIKGIFEG RNFLVSNDSI SWHYVHSLRI TDEGQMTSTD EEGNQYILLK
     SLQSCYVQII PHLNNKQQQQ PPARRILTRK ASSLSNNSDN SVSEEPPVVY IKTYDNEKLY
     IKIPIKTNFV NLMPCLLVWQ ALKPQTLAKK WYCENKVTST NGSDVHEVLV CRFKIYGPIP
     SKSKNIKVVP GAKAPVYQPK GDSTFDSQID GINGNSNVNY LQGDNVNEGW FYTMGVLKSN
     GVLNFITELD GTLLYSIDMK QILSSEIRQV HHSIFDNSNV LFVGNIKELR SNNCIKTISY
     PNDTSSFLFK DGKTVASNQR VLIEFPLHID LEDWFVGLNY FSMREYIGSY SPGSSPLNQP
     SNPVKETPAT VPLSDYSKEN LRVSKKVFID IIEAKLDEFP NTSSNPGKIY AEVIMWGLPW
     SRTALVSYSE NPFWKEEFVT DLPISTQMIH ILIKKSSLNE STYSSNDKLI GTVYLTPDIL
     TKQMNTSSTM MMGSALGNSI NVNGLQSADN ATNNDTVRLA IYDSSNLPIG KLLLNVKLRE
     HHILPPKVYK PLENMLLNAP MKDLIKFCNE NVQTSEFENV SLIMLDIFQS LGIEDRWFKS
     LMEVELVSVD KMTRKNYASN RRSRDNRAQT NNNSSSSNNV FNTLFRGLSI FSKSLEMYNL
     RIGQEYLEKV FGEFMGKISY EEKDCETDPR YIRLQLKAER KGRTIDDSDL ESDDSDDYDS
     DIEKENEELI KERVNTNFGN LYHYAEEVWN KIYITSNDLP QQIKSQLKNF RTKVELSCDP
     DDKVTALNCL SSFIFLRFFC PAILNPKLFY LTKDHQTGKT QRTLTLIAKI LLNLANRQEF
     SAHKEPHLVR MNAFLESHKE DLFEYFDKIT GRKNDFNEKI LDLSHEVKRF DLGISGDKSS
     SELPTTPYLI DKYLRLTELI YLLDFSNAKS ISHLNTPSPQ NGLVNSGSSV SIESTISYNG
     QSGNGNQNNN GSFDEIHLNN ERNVYQIGSL EFEKSEFLDL AGDNDTEGFI KSLCRSNENI
     FSFITSDITL KDLQKQSQNL TNIITNLEAL LERYEYPSNY LSNTALWDVF TADILSRVYL
     DTTRNCIIHL DRLDTSVPSN LKKLTENAFS ALKLKFPETR FESESSYGAG ITQSLSTNSL
     GSIMKSSSKN PFKKWLRKA
//
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