ID A0A1D1VJ88_RAMVA Unreviewed; 1539 AA.
AC A0A1D1VJ88;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Phorbol-ester/DAG-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=RvY_12367 {ECO:0000313|EMBL:GAV01695.1};
GN Synonyms=RvY_12367.1 {ECO:0000313|EMBL:GAV01695.1};
GN ORFNames=RvY_12367-1 {ECO:0000313|EMBL:GAV01695.1};
OS Ramazzottius varieornatus (Water bear) (Tardigrade).
OC Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX NCBI_TaxID=947166 {ECO:0000313|EMBL:GAV01695.1, ECO:0000313|Proteomes:UP000186922};
RN [1] {ECO:0000313|EMBL:GAV01695.1, ECO:0000313|Proteomes:UP000186922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAV01695.1,
RC ECO:0000313|Proteomes:UP000186922};
RX PubMed=27649274; DOI=10.1038/ncomms12808;
RA Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT "Extremotolerant tardigrade genome and improved radiotolerance of human
RT cultured cells by tardigrade-unique protein.";
RL Nat. Commun. 7:12808-12808(2016).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAV01695.1}.
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DR EMBL; BDGG01000007; GAV01695.1; -; Genomic_DNA.
DR STRING; 947166.A0A1D1VJ88; -.
DR Proteomes; UP000186922; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20815; C1_p190RhoGEF-like; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 3.30.60.20; -; 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 InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR PANTHER; PTHR13944; AGAP007712-PA; 1.
DR PANTHER; PTHR13944:SF21; CYSTS, ISOFORM C; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000186922};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 323..370
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 561..750
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 232..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1350..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1421..1452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1475..1539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1207..1304
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 395..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1384
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1539 AA; 169113 MW; 8994D9276ECFC3F6 CRC64;
MEAWSQEVLE ATVVIKLNGA MMGDADWQEE SWTDTMKPAS HVAALLADEQ PKYPSNAVLQ
ILSDPSSLPS LMSSDTASLS RSLSLPFLDT LGAKDEEGGN GVNWVDTVIH PHLERESPVT
DAMAHSAQEV SWPEGQVQRR SAQAAPQPLA RALHQRQPVT LPMPMPFLKS LSTPQLLSAS
PCQTMSAQQI VPIATGNHDE TLPAAAIGQA LPCDGGAPVA MRQRAAPVIP LRRSQLENSE
RSGSEQEAPM AAEEISETRE GRVEHPAITP TASPPSQGWS HSVVVERRKE KKSRTLRHGS
AIFLFGASRY KKSKEDIRRS RESHHFVPVS ISTSAVCWSC RKPLAHKLTV KCQRCNLICH
EGCLEQIEVC SASLLPPSTS LHHSSVGGLA SDMGQRRRLN STGNDLSSDE LQPPLNGKSS
PSVMLEPQQM AVEHGDEGSR LQPTLPPQSL KRLSVPASYP QHTKSTGLGA AQSDSNLSPS
KSGSTDSQGA DYDSPAEDVS LSEPTSQTGA ASAAGKADSV IHLLPMLRFD GDLRLELDEP
EAWVSLVEPS VLGQLPEEEV KRQSMIHELI FLEKNYQIIL LIIDQLYIAG LQRELQWSEA
DVRLFFPSFE GIVSVHKTFL GRLRARQAQG VVIVQIGDVF LQQFEGDEAE KMKRAYADFC
CHKKQAEAEY KQRLKTDAKF AAFDKKWNEN IGNRNLRFDS VMQTITQRIT KYRILVDNIF
KKTNKSSGDY GLMARACHYV DDVISHVNRE LDQQKLKEEL GRIYRSFDSK STLVGRDGTP
YGPAEEWKKH NLLDRRTLLF EARQVQIQRS SKEEEKKALS VTLLVMSDVL VLLSNSAGRD
KYSWASIDSK RDRAVIHLQD LVLRLKPETA GAEERSLYLV SQELRTPYEL TCETAKERDK
LRKEIEAARD HGGNLRASSA MDGDDLADAL FLDNYTAHIK RIDDVVAACR LRDDGIRRLC
LEKEQLLQQM ASCAGMTNYR LHRPPLLDME EGNLQEGGEE LLQSAQEAVR QADKLCCFLT
AAALPSEGQG QRRDDGKEEV QRRIPSWPYG ELLGQASPEP LPTVHLGVSA QAPARRHETF
GGFDNKSEMP ALTSTAGRST SMKNPPRQRR SASPLNGTLS PACQPEQSEA QAVPLDQVSL
AVSRTSLSPS TLSGRESGDG SSPSASSSPR LSAVLSDEQA TLVPALIQLA HHLNQLTDGL
AQHLTAVEAL RHKYAAAQHK MAVMEGRDKR LNKHSGQLEE LRALQEALAR DKCQWQAQRD
DERQQLDKLR KQLDADMMKA KQEREDVEKQ RQAMFAQCEK LVENGLEVKL SSSAPYAQIF
HRQQPPPEAA MSSELLLQSL AETGPLLEQD PRLAHLPPRP LSHQPAHYPP PLSTDGPPLQ
RLTSPPPLAA VLANGGPRSA LAARSLLLPF NSFSSLPVAP ALDTGATPPP SGLCGPAGRQ
PSQSSLLLPT GPPVLPKHSF SWKGSMESLC DKLRNPREGS ALAPADRPDS AAPPRPTLRA
NSEAKLGIGN LMHLSEKDQA LDHPPSTRKK GSAKKRYAF
//
