ID A0A452I825_9SAUR Unreviewed; 1009 AA.
AC A0A452I825;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000023671.1};
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:ENSGAGP00000023671.1, 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:ENSGAGP00000023671.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A452I825; -.
DR Ensembl; ENSGAGT00000026968.1; ENSGAGP00000023671.1; ENSGAGG00000017339.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11857; SH3_DBS; 1.
DR Gene3D; 1.20.58.60; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR035532; DBS_SH3.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR PANTHER; PTHR22826:SF146; PROTO-ONCOGENE DBL; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..88
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 509..689
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 707..823
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 925..986
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 849..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 115786 MW; A8F8DA7641BE61D8 CRC64;
MAEASPAGGV LGLRRNAASF PGNLQLVMVL RPTGFFQRTF TDIGFRFSQE DFLLKLPVVM
LSSVSDLLMY IDEKQLTPEF GGTLEYRHSE WVIFRTAIES FALTVKEIAQ MLQSFGTELA
ETELPDDVYS IERILALRTE KYCQLKGDIT VVTKEGNVLL SSLEEPDANE RSQKQHHDRP
GDWETVNRLL AQLHEMETAF DGFWEKHQLK MEQYLQLWKF EQSFQELQSA IAFLMGQQAK
LPDTGDSVAE VKQRLKDLGN LDGMAQDLVG KAQVVMLHGH QLAANHHYAL SLICQQCNEL
RHHSDVLSEE IKRKHVRLRM TLELHTRLQQ ALECCDEGAN LLANQQVDKC QSKEGAQKAL
QDIDKFLDSS LPYLSYDPQV LCCDFESVLT PEIKVQIQAV WIKLENVRSM FENQQTCFKK
LVDKQVRPVQ LVAPRPENPP RSKSPLFSPK HGMDFNSSLK FSFDISLPGK KTSRKSLNSR
KIEVMHDYQE KRNSLQSFIS ESEDNLDILK GHVINELIET ERVYVEELFT VLMGYRAEMD
NPAMVILMPP ALRNREDILF GNMPEIYDFH NKIFLHNLES CVGAPERVGL CFLERREDFQ
MYEKYCQNKP RSESLWRQCS ESTFFQECQR KLEHRLGLDS YLLKPVQRLT KYQLLLKELL
KYSTSCDGVK ELQEALVAML DLLKSVNDSM HQISITGYDG DLSELGKVLM QGSFSVWAGH
RKGPTKMKDL ARFKPMQRHL FLYEKALVFC KKREEHGDGY DKTSSYSFKH FLKMNAVGIT
ENVKGDHRKF EIWYSGREEV YVVQAPTVDV KMVWLSEMRK ILFKQQELIK VEKKPSGLFT
DQIQLSPQLS DGKQHRASIS SEENDSECTS PIMLDSISSS PQNKPNQSWS RMSQSVEICE
GLEDWSSNNY LSNCSDTEEE DGSQLSPGKY KALADCKKRG SEDLLVKNGD VIQLLHEDGE
GQWLVKNLNR RKEGWIPVNS LQIVIGDCRF RNAKVADAAL CNTRKFSFP
//
