ID A0A0P9EXX2_RHOGW Unreviewed; 1127 AA.
AC A0A0P9EXX2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=FYVE-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=RHOBADRAFT_56143 {ECO:0000313|EMBL:KPV72006.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV72006.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV72006.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV72006.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; KQ474089; KPV72006.1; -; Genomic_DNA.
DR RefSeq; XP_018268055.1; XM_018418210.1.
DR AlphaFoldDB; A0A0P9EXX2; -.
DR STRING; 578459.A0A0P9EXX2; -.
DR GeneID; 28978658; -.
DR OMA; RASHMIE; -.
DR OrthoDB; 53554at2759; -.
DR Proteomes; UP000053890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF159; RAC GUANINE NUCLEOTIDE EXCHANGE FACTOR JJ; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053890};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 226..587
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 620..724
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 940..1021
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..54
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 119270 MW; 67861014712D78A7 CRC64;
MSHHRAAARA SAHQPAPTLV IPDRDADLAP SAVPFPSPTR PDASPSPTSP SFPSTSRPSS
PDMLISPAAS SSRRSPSPGP HAPAKRPTFM RVRQTSLPAS LVQSRHHSIV GSAGLSAMVA
SAASGGAKRV SVASFASFDS LPEEEEGQGD VDGAEMGRLG LSRRSLSPPA TPPRPVAAKR
SSLPALSSAL ACGVSVVRPR TLSARTSSPS RWSVMSEGER EKHAQTRWRI AEELRESERA
YVRVLEDVDS LYYQPLIEAL PADDPLSRRS SKRYSTATQP DSRTTSPRHS LYGAPQPRYR
TSTAESLLST APSSASTTSP PPIQPILSRR EINKVFSNFS DVLNLAHVML LALEEAVPPR
PSQPVSIQTG VAAVPASEST TTCSAPATAE TSVEASSVEN GIEASALSRS GGTVESEGPE
TPDQSPPTKA TPKVVPRQRP LSTRSTERRR STPVAPPVRL GKALLPILPF FKQYSLFIAN
FSASLALLSR LDGSSSITSS ASSASRWQAF VASRQQHPGG EHGGEPHSQA SKIGLAGLLL
NIVQRVPRYR LLLKDLLRHT DDEHPDARDL QAAFDLVDGV ASHLDSQIAA HTSALALLDL
QRSFLPGSFP SSPLVAPGRT LFKSGPLSQV SHSGPPRPRT LFLFSDLLIV AAAEEVWIGD
EDRYRLVGRY ELDEVTVVGN EEVDQEGRRR CGFQVLSRER SFAVYADTRG DRDTWLDAIR
NAKATLSTAR ATIQRSAPST PLAPVSTSPL LSKLDRRISL PPPSASSTTP HPLARTRSTS
SHLGVPPSRQ VSLPPSLGFI PPSPAEELDK LIFPSTSSAA CEIVQSPLEG PPLAERVEAR
AGSPAVASSS GTSSRAAILS SPTTSSPTAS SSTSTSSSPP AARPSLARSR RWSELPTSSA
FAALSSIFLP SPPSSSPDLA SGETAYPVID AYQAPVWVPD SRAPRCQNCA RDFGLWRRRH
HCRLGGCVVC WECSTKYFVI PAAVFSSPSL DPSSGPAAPP TLSTEPDRLA RACDSCFTSV
FAPTTPASRF LDAHPTATDT FPRLGMRGGG TGSVKWTGTW RMSKALGPAG GGLAPLWDLE
ELAAAAAGSD GSGARQSTPT AASAGQGEAR RTRERSAVKQ LKALLGE
//
