ID A0A0L6UX58_9BASI Unreviewed; 1144 AA.
AC A0A0L6UX58;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE RecName: Full=FYVE-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VP01_357g4 {ECO:0000313|EMBL:KNZ52425.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ52425.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ52425.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ52425.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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:KNZ52425.1}.
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DR EMBL; LAVV01008590; KNZ52425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6UX58; -.
DR STRING; 27349.A0A0L6UX58; -.
DR VEuPathDB; FungiDB:VP01_357g4; -.
DR OrthoDB; 53554at2759; -.
DR Proteomes; UP000037035; 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 CDD; cd00160; RhoGEF; 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; 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:SF270; DH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 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:UP000037035};
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 322..551
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 581..733
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 942..994
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1144 AA; 126188 MW; 9974D86D89A788F9 CRC64;
MVPMSLIPGR RACSEDTLPS SSNLNPKRML ARSPAPSSSR SYAAIEFPSG VDPQIISLKA
GDVVNLPPGV ETGSCQAHCT VASGSTLPES GASAVDSIED ISHRTPLDRR ISLPLLGIDL
GRSGPSYGQT LKRMSVAVYG LASDAFDAQD NHAMSSHSKR PIAFPQDIST GYPAHFSLKT
TARPSFTDAE QFTPQKSVTH IGGLDANAGI ADTNRLDTAL PPSRQSSDTT VQLAFSTRSK
SLRSSRPPRL KTERHQSSRN VNLPFKTNIK FPLKGPKLPE EARSHSDSSD VNHNLHTPRL
SLDLTSLNLP DQALLSQKNW HKQRLVIKEL IETERRYFEL LNQIHSNYIL PIQASQQPND
HQRVILSKKT TANIFSNFAA ILGLSGQFLN SLENLGQHHQ LFEESSFPRS LTTPPVGGYH
KRQPLPSLKT STCGIKKLNI GEILLEFLPF FKLYTTFTSN FSVSQSTLQL HSAKRGPSPA
FVTLLEDCRG RGVDSGLGLA HMLLGIIQRV PRYELLIKEL VKYSAETACD HRQLQSAQTM
VGCVARRLEI GMNEQAATKT ILTIQRAMEG LAFPLVIPSR KLVKIGQLKK IGRKGDLQDR
VFFLFNDCLI YCGILKNGNV ESVEKWLGQL TAAFNNSNRT DSPPTGPVNV LTIKHISSSF
LLPFTHTDDN SPRLIFCRKM DLHDVTTVGA VGGRKNEYST GFQIISSAKS FVVYANNAEE
KENWIYNLRE TKSELLDSRR TLFIKDDFSQ RENDAPSNKH TSILEGPPSR GYSWLSLASS
EDDSNSSTTG KPAEKTPQRS KDISPSTISF PTRPPNCKSP VNGSVFTKLL SPRSRLYSTP
SKSSIFNWKP LVNLSFPPLA NQMTQILEGI HEAHAGSLAE TISPQAEPTA LTPEPKKLSP
TKQNDEIHPP RKHISVKHVA ENYCAPVWVP DNHVDRCMGN SCQAWFSVLK RRHHCRLCGG
VFCSGCSSRI FVIKNQEHGN LLARACEACF ESVFLGVHDG RSQPSRRENG VYRPILSNQP
QDDHDVLLRR EKRDHLRHAH RQSLPIDMGS AYFRHSSTLA NLAHDDQQHL IVSAGTSVAG
DSACGLITSK GFDDPIIDSS SLDLSFSPRD SRSHTPGAPS CPSPPLSQTH ARQRLSSLLH
SKSR
//