ID A0A1V8V399_9PEZI Unreviewed; 1519 AA.
AC A0A1V8V399;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQO30386.1};
GN ORFNames=B0A51_02346 {ECO:0000313|EMBL:OQO30386.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO30386.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory complex
CC required for the internalization of endosomes during actin-coupled
CC endocytosis. The complex links the site of endocytosis to the cell
CC membrane-associated actin cytoskeleton. Mediates uptake of external
CC molecules and vacuolar degradation of plasma membrane proteins. Plays a
CC role in the proper organization of the cell membrane-associated actin
CC cytoskeleton and promotes its destabilization.
CC {ECO:0000256|ARBA:ARBA00025194}.
CC -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC {ECO:0000256|ARBA:ARBA00011159}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton, actin patch {ECO:0000256|ARBA:ARBA00004134}. Endosome
CC membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004125}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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:OQO30386.1}.
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DR EMBL; NAEU01000052; OQO30386.1; -; Genomic_DNA.
DR STRING; 1974281.A0A1V8V399; -.
DR Proteomes; UP000192386; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00052; EH; 3.
DR CDD; cd14270; UBA; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11216; EH DOMAIN; 1.
DR PANTHER; PTHR11216:SF161; EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE CLONE 15, ISOFORM A; 1.
DR Pfam; PF12763; EF-hand_4; 2.
DR SMART; SM00054; EFh; 4.
DR SMART; SM00027; EH; 3.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF47473; EF-hand; 3.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50031; EH; 3.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Reference proteome {ECO:0000313|Proteomes:UP000192386}.
FT DOMAIN 19..105
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 159..249
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 191..226
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 314..405
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 347..382
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1478..1518
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 243..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 562..638
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 282..301
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1519 AA; 158298 MW; 3A3C4B9F227FBB77 CRC64;
MADNTNDPNP AILNLSTDEK RAFGYLFNQA DSDQLGVVTG ERAVSFFQRT SVSPTVLGEI
WQIADTENRG LLTRPGFCIV LRLIGHYQAG REPSTELAFK QGPIPKFDGL TIPGLGGNGS
PAGVPMAQSP TGSGFPPNAL QPQVSGQGPI RVPPLDAQKA QQYAGLFERS GAQGGVMDGG
TAKAIFEKAG LPNEVLGKIW MLSDREQHGA LNQNEFIVAM HLLTSMKSKS MTALPGTLPP
GLYEAAARRG APPPPGSRQV PAQTPVSRQF TGGSIGAPPR AQSPLAKPPG YATPPPQVAQ
PTGLGPHWLI TTQEKAKFDQ FFATVDTGNR GVVTGEQAVR FFSDSGLPED TLASIWDLAD
IRSEGQLNRD EFAVAMYLIR QQRAPNAAPL PAFLPSALVP PSMRKQNIQQ QTQQTTAPAF
DNASNASGLP KSAADDLFGL DEPSAPGPQQ PVLQPQATGA STSRDPFGGS SVPASPSSPQ
QRFQSQAPQS GSVFKPFMPT SAFGASIAQQ NTGGSMTSSQ GQARGFAPPT GPPPPQTRAQ
QSGGMDDLLG DNDAHAAESG KLTNETTELA NMSNQIGNLR SQMEQTQQKK NTTQADVTAT
STQKRDLETR LQQFRAQYEQ EARTVKELEQ QLTVSRESTK KLGQELAMLE GGYQDLQTQH
QTIGQALQAD QTENANLKQR IGQLNADVNR LKPEIDKMKL DARQQKGMVS INKKQLTTNE
SALSGLQREK ADLEQEAAER AEAAARSPPP EPTPVAAPRE AVVSPAGSTM SSTNPFFRKT
STEPQAERSM SPAVASPGAP NPSAFDQLFD PSFAQQGGSR SGTPPATSFG SRPAPALPRD
RAASGDLANS VGTMSSDGRP TPSATPPLSE RAAKESPVGS GLERNADNIP PPPEKGQFTP
AQLPVGGLRP SATSESSSTR VLPPASRAGG TDTPRDSPIE TPGLRGPSGA FGGVSEGLPG
AFPETPAVEQ PRSPGPFGAP NAPPNETSKA VEPSIEAPAP TKDLNTDFDN ASAGFGAPEA
SKSAESRGVD DPFAPKDITP VAGGLQSRGF GSEFPPIRTL EHDEEDSDSD DDSTAGHGFG
DNFGAAAPTS QATAPAVKAP EEAASVPAIA TGSSLAPARP DLHSGVSTAS VLPGVDVQQS
PPGYDASEAQ VGHGDRSGSN QFPQEYSGLL PARDVPTSPT GAASPPPLQG PALASSTTMA
HEVVSASPPP AAVDRVQEIM APPEHAQREE SGRSLTTPST SLFPASAQAA SPFGTASTSE
TFHDAFSRPT SSFTDIGASA NGPMSSSMTA PHAAVPTTAQ PNAFDDFDDF DDLAEAKEAD
KSMSDLDFGF GNHSRENSEF NTAFDSPAAS MTTTTADSQA TPRQLTESSS GFASGFGSST
AQPPPAFGSG TSSLQQTPQN AQHDWDAIFS GLDSSANGDI DTSLNGAAGS TAQHDAWGFA
DSTPASSAAP LSSAAPATTS VPVKSAPDMG RALTPGTEHD DPILKRLTGL GYPRNDALKA
LEQYDYDIER AEDHLLKQI
//
