ID A0A1X7R660_9SACH Unreviewed; 1910 AA.
AC A0A1X7R660;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Similar to Saccharomyces cerevisiae YDR170C SEC7 Guanine nucleotide exchange factor (GEF) for ADP ribosylation factors involved in proliferation of the Golgi {ECO:0000313|EMBL:SMN21064.1};
GN ORFNames=KASA_0L00825G {ECO:0000313|EMBL:SMN21064.1};
OS Kazachstania saulgeensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1789683 {ECO:0000313|EMBL:SMN21064.1, ECO:0000313|Proteomes:UP000196158};
RN [1] {ECO:0000313|EMBL:SMN21064.1, ECO:0000313|Proteomes:UP000196158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FXLY01000007; SMN21064.1; -; Genomic_DNA.
DR STRING; 1789683.A0A1X7R660; -.
DR OrthoDB; 204547at2759; -.
DR Proteomes; UP000196158; Unassembled WGS sequence.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000196158};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 733..921
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..66
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1648..1662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1910 AA; 216621 MW; 7091A870C6687B52 CRC64;
MSDQTNHEEN DLQESVSSVN LNSDDASSFA EPQPPNEVEE DNNSGADGEN TEAQEEENEE
EQQQDTTTEE PIASHDNDND DDVNNNGEER TETETHQKEV EEVEEVEQVS EQHDNETTNH
TQITSNHVRN VSTASTTIAS NAKSTLLLVK TTLEELVDEK EVKKIPGTHK IIQRTITKIE
DTLKESNNSS IEVDSILLFE ALRAASRTKS SRITSKSLDT LSKLFSFRAI DEAILVNPPD
SMASNDQEAT NDNSGITPPP KQRLIDAAID TIADCFQGEG TDERVELQII RSLSGCILVE
DENSLCHGAS LLKAIRTIYN IFVFSLNPTN QGIAQATLTQ IITAVYDKIE IKKIQPYQVS
INESKKSLPS SDVTGNDPIT LQNMENLNDE EERRMDAQQY DDVSEDEQLD KNASEKDLAI
KDAFLVFRAM SKICAKPLES ELDMRSHAVR SKLLSLHIIY SIIKDHVDIF LSSDVILPGK
ESVSLMNAVR QYLCLSLSRN AASPIPPVFE ITLEIMWLII ANLRADMVKE IPVFLTEIYF
PITELKTATS QQKRYFLTVI QRICNDPRTL IEFYLNYDCN PGMPNIMEIM VDYLTKLALT
RVEITPTQRS YYEEQLSKPL STFNFDELPL LTTSTLPSNI DPNQGALLFP VDFALKMTAL
NCTISILRSL GSWAHKALNP NAHVVNPAKN NNQLGQSMDG ANTNTSLTLG DENSASESNV
NINQLQDVDD PTQFENLKQR KTQLSDSVAI FNNKPKKAIP GLISRGFIND DSPSSIAKWL
LETDGLDKTV VGDYLGEGNE KNIAVMHAFV EEFDFKGLSI VDALRDFLQA FRLPGEGQKI
DRFMLKFAER FVEQNPGVFS KADTAYVLSY SLIMLNTDLH SSQIKRKMTL EEFLDNNRGI
DNGRDLPEEF LVGLFKEIEG NEIKLLSEQH QAMLSEDNTA TIGTPQAQPA FNFFSSRDLA
RESYLQVSKE ISSKTELVFK NLSKSKGKQD TEVYYAASHF EHVKSIFETL WMSFLAALTP
PFKDYDDIET TNKCLEGLKI SIKISSIFVL DDARKSFIGA LVQFCNLQNV QEIKVKNVNA
MVDLLEIALA EGNYLKDSWK DVILVVSQME RLQLISKGID RDTVPDVAQA RLVNPRASLE
STRSANQSIF DIWGKKSTPM ELAQEKHHNQ KLSSEMSKFI SSSDLVVLMD NIFTKSSELS
GNAIIDFIKA LTAVSLDEIE SSQNASTPRM FSLQKMIDVC YYNMDRIRLE WTPLWAVMGS
AFNKIATNPN LAIVFFAIDS LRQLSMRFLD IDELSGFEFQ SDFLKPFEYA VQNTTNTEVQ
EMIIECFRNF ILTKQQHIKS GWKPILESLQ YTAASNDERI VLKTQRLVGD DIVGKNFESV
FGQEGAFYEL VGIFKEITKN KKYQKAALHA LESLKRITEQ IAKICFINDD TNGNTKIDTE
TREHYEQLLR GKDVFQDVWF PMLYCFNETI MTADDLEVRS RALNYMFDSL VAYGGEFDDA
FWEKICTKLL FPIFGVLSKH WEVNQFNSHD ELSVWLSTTL IQALRNLIAL FTHYFESLSG
LLDGFLDLLV SCICQENDTI ARIGRSCLQE LILQNVDKFN ETHWQHIGEV FTKLFRLTTA
NELFDNDPLR QGRRASNVNN HNNIEGTQET VERAHVEAGS EDVGGETAEN EEQQQQQEEV
EVESKPVNLS TPEQRKLQED DTQDTRRRRI NIKNSIVVKC VLQLLMIELL NELYEDENFA
RCIPYNESIR LTELLEQSYG FARDFNADYG LRTRLVEARV VDKIPNLLKQ ETSAAAVLID
IMFKLYFNSN DDEESKNIEL LDRLVHICSG VVSAYVALDD RTMERSINSW RPVIVEILQG
YYELDDDDFR KHCSAMYTLI IEILDKSVPQ DLRYAIKLFL GRVGTLYLEK
//