ID F9FUH5_FUSOF Unreviewed; 577 AA.
AC F9FUH5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=GCR1-dependent translation factor 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOXB_10056 {ECO:0000313|EMBL:EGU79471.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU79471.1};
RN [1] {ECO:0000313|EMBL:EGU79471.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU79471.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GDT1 family.
CC {ECO:0000256|ARBA:ARBA00009190}.
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:EGU79471.1}.
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DR EMBL; AFQF01002678; EGU79471.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FUH5; -.
DR STRING; 660025.F9FUH5; -.
DR PaxDb; 5507-FOXG_03598P0; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR001727; GDT1-like.
DR InterPro; IPR049555; GDT1-like_CS.
DR PANTHER; PTHR12608:SF1; TRANSMEMBRANE PROTEIN 165; 1.
DR PANTHER; PTHR12608; TRANSMEMBRANE PROTEIN HTP-1 RELATED; 1.
DR Pfam; PF01169; UPF0016; 2.
DR PROSITE; PS01214; UPF0016; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..577
FT /note="GCR1-dependent translation factor 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003383361"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 483..501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 521..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 554..572
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 89..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 400..427
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 180..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 60897 MW; 9D70242501D503F5 CRC64;
MKIRTTHSPL VLFLLPAVAN ALASNDIADL PAPGTAITEQ TDSLPRAGVK RHDIPTKYAP
VDGRDGKPHH GPFIEIDDHK KTPEVALDAG SDTAAGSGSG AGAGAGAGTG AGAGTEPKTG
TEAAPKIDSN PDSLPGLKGR PEDPTVVDGE KIPETNDGVM FDTNRVHAQE GTTGTEGGVT
ERYKARKLEE DLAGEETFRK PSSPKEAPPL PHSEEEKIRA SGGDKAKELG DDTGSAKAED
VVPKAAKPVI SNDDKHDYTA GLEKPADLPD RPVGQNKPVQ DSTKTEPIDL SRGKTHDGHH
DDESIIQPFH SFVLSFTMIL VSEVGDKTFL VAALMAMKHD RMVVFTAAFG ALLVMTVLSA
VLGHAVPTLI PKRVTSFLAA GLFFVFGAKL MREGMLMDPN EGVSAEMHEV EQELAEKEKE
MGRKRGDSVS AYTLEMGMNG NGRRSRPSNR LMSPPRSPSQ SPVRDARSGS GAVASIVQGA
TNLCSLLLSP AWVQTFIMTF LGEWGDRSQI ATIAMAAGQD YWWVTLGATC GHAICTGVAV
IGGRAIAGRV SLKVVTVGGA TAFLIFGVIY LLESLYS
//
