ID A0A163J1X8_ABSGL Unreviewed; 516 AA.
AC A0A163J1X8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=SEC7 domain-containing protein {ECO:0000259|PROSITE:PS50190};
GN Name=ABSGL_04621.1 scaffold 5475 {ECO:0000313|EMBL:SAL99050.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL99050.1};
RN [1] {ECO:0000313|EMBL:SAL99050.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL99050.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT552383; SAL99050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163J1X8; -.
DR STRING; 4829.A0A163J1X8; -.
DR InParanoid; A0A163J1X8; -.
DR OrthoDB; 1369677at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR PANTHER; PTHR10663:SF402; ARF GUANINE NUCLEOTIDE EXCHANGE FACTOR SYT1; 1.
DR PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1.
DR Pfam; PF01369; Sec7; 1.
DR SUPFAM; SSF48425; Sec7 domain; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000078561}.
FT DOMAIN 353..512
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT REGION 51..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 57238 MW; 55F2E53FAB9AF808 CRC64;
MRPSSPSDTS RGTKSKHFLS RFLANPTHVY TYDGTASSTD PTYNLQTEHN AETRGSANWN
TDSSSAHRHH STPTVTTNVS TPLMGPRIDH PTSTTNSVVS TNKGIVSAKA TTAEKAQRRR
SATLPSVMYS PPLTPSPPTA KLDAAATHTT MHYKGDNVTT DTTTTVSNSS HDNLAAQKDV
IQIKVHNSDD GDGDDSSSDE SFVDASDELE SDQPTKQHSD NKKRSSITHR LSAGYFGSAG
GLVVNMHHSL RNRQSRQSMA QQQLRNSPPP DDLAKAMLDW KRKSVGDGTI DKRFSINSTD
PAGATSPPQD EHDAPELSKE DKEALRAHAE SILMGNDNST LPPPPLPTTG HLHHERSRSI
KALSEMFSKT LDEAWNNTDA ASQLSHLDQV HDPRVLTAWT RPTLLSTKAQ ETARRIWDCD
ESFLPVDRYA EWLGQSQELT RLGLHASHRT HYNAETLVCY MDLFYFTDMK LDSAFRKLCS
KLYFKAEAQQ IDRILEVFAH RFWDCNPNSD FKCPGK
//
