ID   W6MV44_9ASCO            Unreviewed;      1784 AA.
AC   W6MV44;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=SEC7 domain-containing protein {ECO:0000259|PROSITE:PS50190};
GN   ORFNames=KUCA_T00005755001 {ECO:0000313|EMBL:CDK29762.1};
OS   Kuraishia capsulata CBS 1993.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX   NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK29762.1};
RN   [1] {ECO:0000313|EMBL:CDK29762.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK29762.1};
RA   Genoscope - CEA;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDK29762.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK29762.1};
RA   Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA   Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA   Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA   Gabaldon T., Wincker P., Dujon B.;
RT   "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT   features among budding yeasts (/Saccharomycotina/).";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HG793131; CDK29762.1; -; Genomic_DNA.
DR   STRING; 1382522.W6MV44; -.
DR   HOGENOM; CLU_000691_1_1_1; -.
DR   OrthoDB; 204547at2759; -.
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   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          625..813
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1784 AA;  200197 MW;  80916066A7F9E533 CRC64;
     MDIATDPVEL PTEPNGEGSD IRESLEQSVP PIVVTKTNGA ANGSTNGSTN GSTKTRSATK
     AGPRMGGATT NFIKVSLESI AAIKEVTKKH SELVKSCQAA LSKLNEPELP DNATIFEPLR
     LACATDIVEA KIIALDCLSK LFTFNVFDDP SEVVVSTKRQ AKYVVDADME TGSAALSPGT
     DRIPLIDAAI ATIADCFEGE GTDEKVELQV IRVLMAAILN ESMPAHGSTL LTAVRQIYNI
     FLLSLSPINQ GIAQATLTQV VNIVFERVVT VRAERSEISR NASIVEVGES QTKVSEANSE
     ATSQPKLTLS NMENINELKL AEISTNDASE IAVKDAFLLF RAMSKLSVKP IDNDALDMRS
     HAIRSKLLSL HIIHLILKNH IDCFMDRGAV ISSNNNETSL LDAIRQYLCL TLSGNAASAL
     APVFEISLEI FWFMISQLRS EFKREIPVFW DEIYFPVAEM KTSTAHQKRY LLSIIKRLSE
     TPRALVEFFL NYDCDATMPN ICESLIDYLT KLALTRIDVT PTQKIGYREN LTRPLATYNL
     SQLPMLSIGK LGGHPPDPDA NLNFPVEYAL KMNSIECLVG VLRSLSLWAD DDSLLKRPRS
     HTNGSVSTPS LQEDSFVAEE DEPAQFETQK QRKTQLLEGI REFNFKPKRG LQRLVDKGFI
     ASKEPKDIAH FLLTTDGLDK QVIGEFLGEG DELNIATMHA FIDEMVFTNT PFVSAMRTFL
     QAFRLPGEAQ KIDRFMLKFA ERYVSGNPTV FANADTAYVL AYSVIMLNTD QHSAQVRKRM
     TVDDFIKNNS GIDDGQNLPQ EFLVQIFDEI QHHEIKLQSE QHAALISGDV QPTQQGFFFG
     GRNISREMYM QASREMSSKT EQLVRTIGKL SKDSSRTVYY VATNNVDHVR SMFDTLWMSI
     LAGLTPPFKE YDDEDTAKLL LEGIRISVHL ACLFELDYAR ASFIGAIVQF SNLSNPEELK
     PKNLSAMYVM LEVAVSEGHA LKSSWKDVLV SISQMERLKL LATGVDSGVV PDVANARVAN
     RDSVDSSRSS QQNGFFAALA SIGTKKSTLA EQAYHHHQNQ KLNPEILSMI VSTNLDVAMD
     KVFTHSSDIV GDGITDFVQA LTDVAWEEIE SSGQSEHPRM FSLQKMVDVC YYNMGRIRVQ
     WSAIWAVMGE KFNRFGCHSN IRVAFFALDS LRQLSQRFFE LDELSHFKFQ KEFLKPFEYI
     IANNQEISVK DMVLDCVQYL VQKRGDQVRS GWVTVFDILT DDAKLTDEGL VTKGFGFASD
     ITNHHFDSVF NQGAFTNLVV CLTEFAKNQR FQKTSLQALQ ELKRLVKKVV GLTLPGKTAV
     SDEKRTSNDG DDKNGVIFVT EDFLDKMWFP VLFSFHDVIM TGDDLEVRSR ALNFMFDTLV
     QYGGHFQPEF WDKICNLLLF PIFGVLSTHW EINQFDSQDD MSVWLSTTLI QALRNMIALF
     AHYFDTLNRM IDGYLKLLVS CICQENDTIA RIGRSCLQQL ITQNMGKFTQ DHWDKINGSF
     DELFEHTTAK ELFKADPLNN GTVPALAVEA GSENVEASAS EAENGLDFSA EEMNVSSPAY
     NSQKQSAQEE ERLQKTKEKS TIVVKCVLQL LMIETLAELF EDGELYETIP VDNLIRLAGL
     LERSYRFARE FNDDYNLRVR LWNAGIIERL PNLLKQETSS SAVYIAIMLR LYTDPEKTGP
     KQKEHIAATL LPMCSGIIER YVALEDVTQL RNINSWRPVV VEILQGYVEL DEQDFLKNAP
     TMYDLVMQMF DKSLPAELRT AMRLFLVRVG DVYLSGQESK KEES
//