ID A0A2H3GQW0_FUSOX Unreviewed; 1833 AA.
AC A0A2H3GQW0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=SEC7 domain-containing protein {ECO:0000259|PROSITE:PS50190};
GN ORFNames=AU210_011735 {ECO:0000313|EMBL:PCD29194.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD29194.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD29194.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD29194.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD29194.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD29194.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
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:PCD29194.1}.
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DR EMBL; MABQ02000008; PCD29194.1; -; Genomic_DNA.
DR STRING; 327505.A0A2H3GQW0; -.
DR OrthoDB; 204547at2759; -.
DR Proteomes; UP000219602; Chromosome 10.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProt.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.220.20; -; 1.
DR Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032629; DCB_dom.
DR InterPro; IPR015403; Mon2/Sec7/BIG1-like_HDS.
DR InterPro; IPR032691; Mon2/Sec7/BIG1-like_HUS.
DR InterPro; IPR046455; Sec7/BIG1-like_C.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR10663:SF375; LD29171P; 1.
DR Pfam; PF20252; BIG2_C; 1.
DR Pfam; PF16213; DCB; 1.
DR Pfam; PF01369; Sec7; 1.
DR Pfam; PF09324; Sec7-like_HDS; 1.
DR Pfam; PF12783; Sec7-like_HUS; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF48425; Sec7 domain; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 4: Predicted;
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000219602};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 625..813
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT REGION 202..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1523..1542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1551..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1804..1833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1833 AA; 206492 MW; 7DBC9D2CCE833062 CRC64;
MSSLKFVVSS LEAIASSKDA QRNKQLADST TKALDAIKEQ DQLPDPEIVF APLQLASRST
NVQLTTTALD CIGKLISYSY FSVPSNPPEG TEEGAEPVPP LIERAIDTIC NCFQGETTAV
EIQLQIVKSL LAAVLNDKIV VHGAGLLKAV RQVYNVFLLS RSTANQQVAQ GTLTQMVGTV
FERVKTRLHM KEARLNLEHL KHGASNATFD QADTPNGAND NNDRDESPAE HSEAVNASAE
PPESGAKLTL KDLEHRKSFD DSNLGDGPTM VTRLQPERKE TGTPVSDQAG QESSPPEDGE
VLDAEDEVYI RDAYLVFRSF CNLSTKVLPP DQLYDVRGQP MRSKLISLHL IHTLLNNNIA
VFTSPFCTIK NSKSGEPTSF LQAIKFYLCL SITRNGASSV DRIFNVSSEI FWLMIKYMRA
DFKKEIEVFL NEIYLALLAR RTAPLSQKLQ FVTILNRLCA DPKALVEIYL NYDCDQTVDN
IYQTIIEDLS KFSTTPLTIT TINEQVYEEM RLKTTPASEW QLKATLPPPL TVAHIAPHQE
TEPDYPKEYA IKRLSIEALV ETLRSMVNWS APIRGDPEPP RSENHDPKAS LDLRPSIDPS
INDSISRVET PLPPSTPILE DDPDQLEKEK ARKTALMKGI NQFNFKPKKG IQMLLRDGFI
PSDSPKDIAE FLIKEDKLDK AQIGEYLGEG DQKNIDIMHA FVDTMEFAKR RFVDSLRQFL
QSFRLPGEAQ KIDRFMLKFA ERYVLGNPNA FANADTAYVL AYSVILLNTD LHSVKIAKRM
SKEEFIKNNR GINDNADLPD EYLLGIYDEI AANEIVLKSE RDAAAAAGNT PAPSTGIAAG
LGQALSNVGR DLQREAYMQQ SEEIALRSEQ LFKDLFKSQR RKAGTKYILA TSFKHVSPMF
NVTWMSIFST LSSQIQKSHN LEVNKLCLEG MKLATQIACL FDLSTPREAF MSALKNTTNL
NNPQEMLAKN IEALKVVLEL GQTEGNVLRE SWKDILMCIS QLDRLQLISG GVDESAVPDV
SKARFLPPQR SEPSDSRSSS NSKKATRARA GTASKGFSTE IALESRSDEV IRSVDRIFTN
TATLTGESMV YFARALTEVS WDEIKVSGSN DSPRTYSLQK IVEISYYNMN RVRFEWSNIW
EVFGEHFNRV GCHNNMNIVF FALDSLRQLS MRFMEIEELA GFKFQKDFLK PFEHVLANSH
NVTVKDMVLR CLIQMIQARG DNIRSGWRTM FGVFTVAARD PHESIVNLAY ENVNQVYKTK
LGVVISQGAF TDLIVCLTEF SKNLKFQKKS LAALELLKSL IPTMLKTPEC PLSQKYNNIP
PPDGAMQNSE KRSRSNTSVE EGYWFPVLFA FHDVLMTGED LEVRSNALEY FFETLLKYGG
TFPSEFWDIL WRQQLYPIFM VLRSRPEMSN VLSHEELSVW LSTTMIQALR NMITLFTHYF
DALEYMLDRF LELLALCICQ ENDTISRIGS NCLQQLILKN VTKFKPEHWN KLVGAFVELF
ERTTAYQLFT ATAINNTASI SPPPNGLEFS STASGTTPMD ETSLKINGKE ELEDDHTVPP
PSAEDELQTP TADAPHIALE EFKPSSNLQQ QPVVVTAARR RFFNRIISRC VLQLLMIETV
NELFSNDTVY AHIPSAELLR LMSLLKRSFQ FARRFNEDKE LRMRLWREGF MKQPPNLLKQ
ESGSAATYIS ILFRMFADNA PERLESRPAV EDALVPLCKD IVHGYTTLEE ESQHRNIVAW
RPVVVDVLEG FVTFPEDAFK KHIPDFYPLA VELLTKDLTA DLRSSLLLVL RRVGEVGLGI
EGMTQAGQRR DSEASRATAE PVGDREADAR RML
//
