ID A0A8H4RPX6_9HELO Unreviewed; 1925 AA.
AC A0A8H4RPX6;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 18-JUN-2025, entry version 15.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAF4633902.1};
GN ORFNames=G7Y89_g4208 {ECO:0000313|EMBL:KAF4633902.1};
OS Cudoniella acicularis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Tricladiaceae; Cudoniella.
OX NCBI_TaxID=354080 {ECO:0000313|EMBL:KAF4633902.1, ECO:0000313|Proteomes:UP000566819};
RN [1] {ECO:0000313|EMBL:KAF4633902.1, ECO:0000313|Proteomes:UP000566819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 108380 {ECO:0000313|EMBL:KAF4633902.1,
RC ECO:0000313|Proteomes:UP000566819};
RA Buettner E., Kellner H.;
RT "Draft Genome Sequence of Cudoniella acicularis.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPI-coated vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004347}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004347}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004347}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004255}.
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:KAF4633902.1}.
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DR EMBL; JAAMPI010000223; KAF4633902.1; -; Genomic_DNA.
DR OrthoDB; 10261439at2759; -.
DR Proteomes; UP000566819; Unassembled WGS sequence.
DR GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:TreeGrafter.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IEA:TreeGrafter.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR FunFam; 1.25.10.10:FF:000260; Coatomer subunit beta; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.50.10330; Probable inorganic polyphosphate/atp-NAD kinase, domain 1; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR011710; Coatomer_bsu_C.
DR InterPro; IPR016460; COPB1.
DR InterPro; IPR029446; COPB1_appendage_platform_dom.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR055916; DUF7493.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR PANTHER; PTHR10635; COATOMER SUBUNIT BETA; 1.
DR PANTHER; PTHR10635:SF0; COATOMER SUBUNIT BETA; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF07718; Coatamer_beta_C; 1.
DR Pfam; PF14806; Coatomer_b_Cpla; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF24321; DUF7493; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000566819};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 149..199
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT DOMAIN 1545..1684
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..10
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..65
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..161
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1925 AA; 212206 MW; 509C15FD0AF3AE89 CRC64;
MPRPEQPPTP ASSTEIKGKD GSQFSSLQMS FELPPPAVTA MESQPSSASS KSSSASSYHP
TSPKSPAIPA SEMVKIRRRS SVAQAPKDSF ALPPPPTRSR KIIQMKPRGQ AEEVAESVKD
AAKDSPAKTS PAPKRKQPSS TSVAGRKIAR KTAHSLIERR RRSKMNEEFG VLKDMIPACT
GEMHKLAILQ ASIDYVRYLE DCVAKLKAEN TRTGVSSPPI TEQFALPPPV RRESQNTPRQ
YTYEEDGDVE MGGSDGRSPT YSTAVPNSNR PSASPALIPQ DSRHRQDSYS SVSTDHRHYS
FSASSTTSPA LGPTAYDYSR SSVSVGSALT SPALPPQRDL DQEATAALLM LNTDRRGTHG
SISGRGGMSV KDLLSTSRPR KLVKVVIHEL IPPPPEDLEN CPANMATFLD QSYSLVHQDN
AADVPTMSEL RTQLEKGTDE SKVETMKRIL TVMLNGDPMP QLLMHIIRFV MPSKHKALKK
LLYFYYEICP KLDASGKLKQ EMILVCNGIR NDLQHPNEYI RGNTLRFLCK LREPELIEPL
LTPARSCLEH RHAYVRKNAV FAVAAIFQHS PTLIPDAPEL LATFLQTETD HTCKRNAFAA
LVSISHDEAL TYLSSVFDGI PNADELLQLV ELEFIRKDAV QNSQNKARYL RLIFDLLEAG
ASTVVYEAAS SLTALTSNPV AVKAAASKFI ELSIKEADNN VKLIVLDRVD HLRQKNEGVL
DDLTMEILRV LSSPDIDVRR KALTIALEMV SSKNVEEVVL LLKKELTKTV DQEYEKNNEY
RQLLIHSIHQ CAIKFSEVAA SVVGLLMDFI ADFNNTSAVD VISFVKEVVE KFPKLRPSIV
ERLVSTLSEV RAGKVYRGAL WIVGEYSLEA NDIRDAWKRI RASLGEIPIL ASEQRLLDEV
ADGQEAPKEP DQVNGHSKAA PTGSRRVLAD GTYATESALT SQSAVAAKLE AVKAAQKPPL
RQLILDGDYY LASVLSSTLT KLVMRHSEIS QDKARTNALR AEAMLIMISI IRVGQSQFVK
APIDEDSIDR IMSCVRSLAE FAQNKDLETV FLDDTRKAFR AMVQVEEKKR AAKEAFEKAK
TAVQVDDVVS IRQLAKKNAG DGTDEIELDL EKATGGDSTV EDLSSKLSRV VQLTGFSDPV
YAEAYVKVHQ FDIVLDVLLV NQTTETLQNL SVEFATLGDL KVVERPTTQN LGPHDFQNVQ
STIKVSSTDT GVIFGNVVYD GASSTENNVV ILNDVHVDIM DYIQPAVCTE TQFRTMWTEF
EWENKVNINS KAKSLRDFLT QLMACTNMSC LTPEASLKGD CQFLSANLYA RSVFGEDALA
NLSIEKEGED GPVTGFVRIR SRSQGLALSL GSLKGLNKDD ARHLLRSRTD LGPSPSFVTT
TNRSCPLPTT ILFNEDAPAI KEQFDMTTGL AMATDNPFVD PNPSFDESGR GNSFAIDATL
AVGRNASLTL GTDSLIVLDE SFEKRDRSNC CGLWPSGTAN TRAIPFHNIL WAELVDSILT
IQYASPVSKT VVRAATLQYP FEYQMVELVN KWVVRLLDRA YGESQMKKRV KILVNPHSGK
GSAEKWYHWD AEPLLRAAQC TIEMVKTRYR GEAVEIAEKM DIEAFDVVAS CSGDGLPHEV
FNGLGKRPDA KKALEKIAVV NIPCGSGNAM SCNLNGTDSA SLATLAIIKG IPTPLDLISI
TQGEIRTLSF LSQSVGIVAE SDLATEHLRW MGAMRFNYGF LTRLIGKTVY PCDIAIKVAI
DDKPSIREHY RVEQSNYEPA SQRRGYKNLL DDDASGSSGW EDGLPPLRYG SINDKLPDGW
ELVPYDKLGN FYCGNMAYMA SDANFFSPAL PNDGYMDLVC INGDISRLAA IKMMLAVESN
KLFDNPGVWY RKILGYRIIP KNQKDGYISI DGERVPFQPF QAEVHKGLGT VLSKTGHMYE
APGPV
//
