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Database: UniProt
Entry: A0A2Y9DWQ1_TRIMA
LinkDB: A0A2Y9DWQ1_TRIMA
Original site: A0A2Y9DWQ1_TRIMA 
ID   A0A2Y9DWQ1_TRIMA        Unreviewed;      1605 AA.
AC   A0A2Y9DWQ1;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Rho guanine nucleotide exchange factor 5 {ECO:0000313|RefSeq:XP_004382470.2};
GN   Name=LOC101354281 {ECO:0000313|RefSeq:XP_004382470.2};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004382470.2};
RN   [1] {ECO:0000313|RefSeq:XP_004382470.2}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_004382470.2; XM_004382413.3.
DR   STRING; 127582.A0A2Y9DWQ1; -.
DR   GeneID; 101354281; -.
DR   KEGG; tmu:101354281; -.
DR   CTD; 7984; -.
DR   InParanoid; A0A2Y9DWQ1; -.
DR   OrthoDB; 12272at2759; -.
DR   Proteomes; UP000248480; Unplaced.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd01221; PH_ephexin; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd11940; SH3_ARHGEF5_19; 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; IPR029212; ARHGEF5/35_N.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR047271; Ephexin-like.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR047270; PH_ephexin.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR12845:SF2; DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR12845; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR   Pfam; PF15441; ARHGEF5_35; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1182..1366
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1518..1579
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          16..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          951..1075
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1120..1140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..539
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..758
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        809..823
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..844
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        853..875
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        976..991
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1000..1018
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1605 AA;  174766 MW;  2002447926B5FD16 CRC64;
     METAEPPQEA LAPTAAILGF MRGSQAPAPG PEAPESPSYE EVEGRRHSET SWGELRNASG
     FPAEIMPPFP KDSSADKETY QETPGTNQET PTMDQETPGT NQETPTANQE TPAANQETPT
     ANQETPETPT TNQETPAANQ ETPTTNQETP TANQETPTMD QETLTMDQET PTANQETPAA
     EQGAANSQAR TPAYPELCDH LVPGHSLDVV PDPSEWDSRP EAELVAWGAG HTDEQEGAYP
     DNPALTTLGP PWRECPAGTP QPQEEPQERH GQAGCMHPQG APGWEGQGQQ EVGFQKVQEL
     TDKQVNGRRG EQRQNAEQGQ EGLGTRGLGG LTQGQWGQEE NAARPQGPRR GGQGEAGEMP
     GPEENEVDAQ PEEKLEEVPG KQEDQGLGRE LIPVEEWGEE AGVSEGEEAG VGEGEPGDQA
     GDRLGAGEEQ AEHNGPSTVA PRPPGIPPPC DVFFKASCPI TGVPQAQIDS WAGDMSPSSP
     VPAWVSSDKD ASQKGQGEGH KQGPGARAIS ASTLGTPPWT LDSAPGSPTQ VSPCSITSLP
     ASPAEEIRPA TGSPEASRAS LSMDSPILCE ALETPMATPR GSPSTEATWD LCPSPSGSRP
     QSSLASPSGS PLQSPVAGPS GSPLQNPVAS PSEVGPHLRS SSFTGPPRTK LPPDLAARSL
     SFSHSEPPQR PPKPAIYGSV TPRRNRRSGR DSSITLEPPT ASPALWQSLG VPHSQPEGPG
     GAHPCQHSSA PAPPLVSVDR RVPEPPPPLE KRHVLSPTGE RDTCLQTMPP TLQQPSYPAP
     LALGSGFHGT PKVPADPLVA RQLRPLPSTL DLPHSTQTSL PPRHRYNKPL PPTPDGPQPL
     PSPSSSSRSP RTYKPLPPLP TLDPPTEPPP LPPKARARSR STQRALMSAG GQARLRPGSQ
     DWSAALAPLA GHTSWPPATG LSPNPLAPAS RGRSDMAPSM AFSNVTNLLS LSSPTTAWPP
     EEGSWLTEET GGPTRGPSKR ETTQEGANSP QGSELGWARP PERPGHHPLE KSSSWPHRRD
     TGRPLPGVSG TALREGHSKS KGWNRQGLRR PSILSEDASG TRGPAMERAP GPSDTIIFRE
     KKPKEASGGF SRRCSKLINS SQLLYQEYSD VFLNKEIQSQ QRPDSLAEPP GLASPRQPRK
     ALVSSESYLQ RLSSASSSSL WQEIPVVRNS TVLLSMTHED QKLQEAKFEL IISEASYLRS
     LNVAVDHFQL STQLRAALSN QDHQWLFSRL QDVRDVSATF LSDLEENFEN NIFTFHVCDV
     VLNHAPHFRR VYLPYVTNQT YQERTFQSLL NSNSHFREVL ERLESDPVCQ RLSLKSFLIL
     PFQRITRLKL LLQNILKRTQ PGSLEEAEAT KAHHALEELI RDCNSNVQRM RRTEELIYLS
     QKIEFECRIF PLISQSRWLV KSGELTALEF SASPGLRRKL NTRPVHLHLF NDRLLLSRPR
     EGSRFLVFDH APFSAVRGEK CEMKLHGAHK NLFRLFLLHN TQGSQAEFLF RTETQSEKLR
     WISALALPKE EMDLLECYDS PQVQCLRAYK PRENDELALE KADVVMVTQQ SSDGWLEGVR
     LSDGERGWFP QQQVEFISNR DVCARNLKEA QRVKTARLQL VEQQA
//
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