ID A0A1F5LIG0_9EURO Unreviewed; 1385 AA.
AC A0A1F5LIG0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=SEC7 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENARI_c009G06015 {ECO:0000313|EMBL:OGE52915.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE52915.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE52915.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE52915.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
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:OGE52915.1}.
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; LXJU01000009; OGE52915.1; -; Genomic_DNA.
DR STRING; 1835702.A0A1F5LIG0; -.
DR OrthoDB; 4248238at2759; -.
DR Proteomes; UP000177622; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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 SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48425; Sec7 domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000177622};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 419..579
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT DOMAIN 701..829
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1194
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1385 AA; 153320 MW; 285872F0F0A0031D CRC64;
MHWKGLRLVA DGNSKRQSTI EGQSRRSEHL PRPVPPATEP RLSESIPRSP ALDTPGPQLR
GLQAPEENGV AQSDFAGPSS GDTPSLRRNR FSFMRLRHAS DPQLSKSYAK AGQDAPPVPS
LPPPTIITTA PTSHELDQPV KQRSKLNFLP SSRKQSMEEL PRSSTEQPSG KSRRRGQGSA
DSQVTDSVLA TSQSIPEEPG RLSTTSRGNR DQHSDSQRSS LIDPRFSESS RSDQSYGDQT
VARTNSPRDA AGATATKRFR MPRLKRTRSP LFPLPPKLPQ STQVTDNGPK FPPVDTPNSG
HSDNQDQISP LPSPSRSTVQ LAPASSVPPL FRNDSTNSAR SVRSNPSFKN RGRSSTMGSL
AENQDDLTPT TYLASSGRTS TSTSGRKSFG DMFNITQRLR QNSSPPAPRG SPGGSSTPIS
KPEPPPVPKR EETDTPATYL SRLEMCLSRG MIAGVLAQSD EEFFKVGLRK YMRGFSYFGD
PIDMAIRKLL MEVELPKETQ QIDRFLQAFA DRYHECNPGI FASPDKAYFI AFSILILHTD
VFNKNNKRKM QKPDYVKNCR GEGISEDILE CFYENISYTP FIHVEDANLR DRHLAKPRRA
LFKSTSTENL GRISREPVDP YALILDGKLE SLRPSLKDVM DLDDTYDHFG TAGPPDMENL
HQAFTKSGIL QIISLRSRPD AFMPSSLGNP LDSNPGLVDI KVAKVGILWR KDPKKKRARS
PWQEWGAILT FSQLYFFRNV QWVRSLMAQH EAYVKTGRRG TLVFRPPLSD FKPDAIMSTS
DAVALLDSSY KKHKFAFMFV RHNALEETFL AQSEPEMNDW LAHLNYAAAF RTTGVRTKGM
IATNYEGQRY RKSQRLDSIS SQLSQQTGDL EPDSPSIDTD IVAGFVAARR ELMSHKIREA
NEKLFVSQKQ LEDLLQNARH LQVLTPVHAR AREGVIMAAG RLSAKLKWVR QDIWRNKCYR
QVLLRDLGED EEAASTVGSI AETAQSDAAH MASLSGPSVK SEPSVERAGS VVHTASSRDP
SEHPVNPTDQ TPETGLLTKP SNEVMRRPSI PGSTTSGDIS RIGRRRSIIT LPERAKSYSP
DPTTIQLERE ASVLSRASKW DGASLASRAS KLTSPVSFDD NEERLLREAG LLDVSGSPTA
RKEQDIVPTA TPEKLPEGSS DTPPGDRPSR VRRSLHRTLR DSHTHRHHSH SKKNRSSVSS
IGQEEDDQTS GDGEVLSRKA PSFTVHGKKA SIVTFGSEWQ NIPPEERLKL RKPTPHEEPR
ASEPILGSGE SLMSERDPER PHSLHSMSTT TGLSLRTNDE AEFKDAREEQ PEEDIGRPAS
QVITTFPIPD AESDNSPVSP TTTPNVDYLS APRTGSSHSP SSTSLNERIM DNASSENLRE
QSVGA
//
