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Database: UniProt
Entry: A0A452HUE9_9SAUR
LinkDB: A0A452HUE9_9SAUR
Original site: A0A452HUE9_9SAUR 
ID   A0A452HUE9_9SAUR        Unreviewed;      1315 AA.
AC   A0A452HUE9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=DH domain-containing protein {ECO:0000259|PROSITE:PS50010};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000018749.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000018749.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   Ensembl; ENSGAGT00000021372.1; ENSGAGP00000018749.1; ENSGAGG00000013870.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR039919; ARHGEF10/ARHGEF17.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR12877; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR   PANTHER; PTHR12877:SF14; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 10; 1.
DR   Pfam; PF19057; PH_19; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF19056; WD40_2; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50010; DH_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020}.
FT   DOMAIN          367..554
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   REGION          1..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1171..1202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1221..1246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          537..568
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        22..39
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1181..1195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1221..1240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1315 AA;  147308 MW;  69E7CE5F65030050 CRC64;
     MEAEDFPPPP PEVLENELKG CGTNDEEEEE GEQFDFDSGD EIPEADRQAL VPSASDSGIN
     VEHEDTNSTG DDNIGRTEKI QTTESCAESS PTKVNPYSVI NISPIQEKDH SSSPEPNPQD
     ENASSNLSGG YSVPVPCGYA VPSNLPLMLP AYSSPIIIRS VSVDEEVGMQ SVTEDGNSNS
     LSSEDPPNSE DNQVCKEEDA LAKWVADPAN TSWMENPDEV IYDDVPKEDS DTEPEEMIYD
     DVENGDDGGN SSLEYGWSSS EFESYEEQSD SECKDGFPSS FLRGNHKRQM QKLMRAAREG
     TKDGYEKTKA AVKKGRSFIR TKSFITQDHK SSCMEEEELN LFIDVDCMHT EAIMTPMPEG
     LSQQQVVRRY ILGSVVDSEK NYVDALKRIL EQYEKPLSEM EPKLLSERKL KMVFYRIKEI
     LQCHSMFQIA LASRVSEWDS VEMIGDVFVA SFSKSMVLDA YSEYVNNFST AVGILKKTCA
     TKPAFLDFLK QCQELSPDRI TLYGLMMKPI QRFPQFILLL QDMLKNTTKG HPDRLPLQMA
     LTELETLAEK LNERKRDADQ RCEIKQIAKA MNERYLNKLL SSGNRYLIRT DDMIETVYNE
     KGEIVKTKER RLFMLNDVLM CATVSARSSY ESSGIMATGL RYLLKWSVPL GQVEVIEYGS
     NEGQGENCRF PPQHSAENVI VNVKPNKLYM GPGQLYHDLQ NLLHDLNVVS QISQLICSLK
     GNYQNLNQSV AHDWTSGLQK LILKKEDEIR AADRCRIQLQ LPGKQDKSGR PTFFTAVFNT
     FTPAIKQSWI TNLQMAKLAL AEENLLGWFC VEDDGNHIKR EKHPLLVRHM PVMVAKQQEF
     KIECVTYNPD PYLCSETESD SCSMEHGFLW IGSCTNQMGQ IAIVSFQNSS PKVIECFNVE
     SRILCMVYIP EEEKQKELNV APESENMATK TLKVPTVCLG MEEGSISIYK SHQGSKKVRL
     QHFFTPEKST VMSLTYLSQY LFAGLVNGNI AIYTKAEDGA WNSEPQKVVK LGVLPVRSLL
     MMEDTIWAAS GGQIFIISTE THTVERHFEA HQEEGMVISH MAVAGVGIWI AFTSGSTLRL
     FHTETLKHLQ DINIATPVHN ILSGQQRISV TSLLVCHGLL LVGTNLGIIV ALPVPRLQGI
     PKVTGRGMVS YHAHNGPVKF LVMVTAVNKK NKSKSRNSLP PNCEAKEDDQ KNVLHNDRPS
     SFLSNTHDTA VWLGGSAGSI AQRSDKSSSS GSLTLSHGSN SLERRPEDST IYELLKDQNI
     SLKNKRQRSR KMKASSVLVI SGGQGHRRVN KKSKQQRQDE LVSSVMVWQI PLLNI
//
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