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Database: UniProt
Entry: B5RTD0_DEBHA
LinkDB: B5RTD0_DEBHA
Original site: B5RTD0_DEBHA 
ID   B5RTD0_DEBHA            Unreviewed;      1390 AA.
AC   B5RTD0;
DT   04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=DEHA2C17028p {ECO:0000313|EMBL:CAR65592.1};
GN   OrderedLocusNames=DEHA2C17028g {ECO:0000313|EMBL:CAR65592.1};
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:CAR65592.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAR65592.1, 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; CR382135; CAR65592.1; -; Genomic_DNA.
DR   RefSeq; XP_002770229.1; XM_002770183.1.
DR   STRING; 284592.B5RTD0; -.
DR   GeneID; 8998405; -.
DR   KEGG; dha:DEHA2C17028g; -.
DR   VEuPathDB; FungiDB:DEHA2C17028g; -.
DR   eggNOG; KOG1703; Eukaryota.
DR   eggNOG; KOG2710; Eukaryota.
DR   HOGENOM; CLU_001321_1_0_1; -.
DR   InParanoid; B5RTD0; -.
DR   OMA; QCSAKFF; -.
DR   OrthoDB; 1329523at2759; -.
DR   Proteomes; UP000000599; Chromosome C.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd09392; LIM2_Lrg1p_like; 1.
DR   CDD; cd04397; RhoGAP_fLRG1; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR14963; RHO GTPASE ACTIVATING PROTEIN 18,19-RELATED; 1.
DR   PANTHER; PTHR14963:SF1; RHO GTPASE-ACTIVATING PROTEIN CONUNDRUM; 1.
DR   Pfam; PF00412; LIM; 3.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00132; LIM; 3.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 3.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          263..328
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          331..391
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          682..748
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          1093..1303
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          985..1014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1356..1390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..864
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        875..905
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..920
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        921..935
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1356..1373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1374..1390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1390 AA;  157136 MW;  54FC7336750981CB CRC64;
     MSNPSDSKNI PTNKKPYKNS HTSPYKLQAS DIYNPNDSPL INKPASKHNG MRLHLRSHSY
     GYSNDKKDFA GGGIPAPNYA HNNTPNWKTL IPPMPSYPQP TYKTDKRSYS PSQLQKKSFQ
     SQPNTQIPIH VQQAPSHGNS PHARAPQSKP QSDGDHHLSK PNQRHSIAVS PSSEKSNFMG
     NASPSPALNQ SHQFHNAPQS PPPRIQNQRS KTQIPQAPIQ EIPPFQRQMS SNIPDLSRES
     LDQTDIQSRP SQIRQKSMHK KKKFCKGCGL EITGQFVRAL SSAFHIECFR CSECGNQCSS
     KFFPYEMLDE PTGIKYQVAL CEYDYFKKLN LICFNCNNAL RGPYITALGN KYHLEHFKCA
     VCQVVFESDE SYYEHEGEIY CHYHYSKLYA THCEGCHSSI VKQFVELFRG GRNQQWHPEC
     YMVHKFWNVC ILADSVGLRQ HFNINDSNVS NITIFLNESN LKAELLIAIE QHVENTIMNC
     WLTLSGYEET TAACISDMLL NACTSNQSAG LIATGKLILN VEVLFNALDV VQDLCSVVNS
     NVTSKSTSPN TSTSIKNTAS SEDLTFLEMD IFQPLRKEPR NISGKIMSYL AILRKSMQTT
     LSGSLSTELL AVVTGCAHYL KLLIRIGLNN ALKVNKLQGT TDATDKFLSL MKIYEEFNSS
     GDNKVNRELI KSRLSIPTNA TDSCQTCVKS IEKSCIRLDN KRWHTKCFIC YNCSKPIASV
     RATISQSAYN ISNSQVYCTE CFNRNDKTFI LGFELVSDLS QLVYLLKIAL YRSKSVMKVE
     NKSVSQVRQA SLKSKNMSII DEESAARNAT ADDYSKTLND VTRLRASRQS QKLSNSIKQN
     ARKSVILEAP EADKAKRDET NAEGLVDDFE GSNEDIINKP NQTERKASIS SQLSYIQQPE
     NDQFNISSRR SKKSLRIKDE PQKQTTNNNL DRTSDLLQNE KSLTLDDIPR IVAAEQAREQ
     RPNAFKHHNS LYQKHAPMES VRTIPAASTS NASNRNRTSS KSNNNVDNTS NDVPAADYEI
     SSSRLKYYSE LDKSEHFILR HIAVEALIQI SNYNKDELLG LIQTRKLPTF WDKFKFGGTN
     DPKKDKHLNV FGVDIQDLTK RYGVDSELGV GPSKLRIPIV VDEIINALRQ KDMSVEGIFR
     LNGNIKKLRE LTDQINKNPL KSADISSQTA VQLAALMKKW LRELPNPLLT FNLYDLWISS
     QQQKDPLLCK RILQLAYCML PRSHRNLLEV LLYFFSWVAS FAEIDEETGS KMDIHNLATV
     ISPNILISKK ASQSDQSPPQ TGDNYFLGIE VVNQLIELHE ELCIIPDDLL LFFEKCKFNE
     NKSENISTKE IMNKLEKTSK EIPNFFLSFE TKNNNYNTSA QPNVQTNKIS RGHSKVTNES
     HGETSDVQHP
//
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