ID A0A135S5C0_9PEZI Unreviewed; 1263 AA.
AC A0A135S5C0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=UBA/TS-N domain-containing protein {ECO:0000313|EMBL:KXH31061.1};
GN ORFNames=CSIM01_07946 {ECO:0000313|EMBL:KXH31061.1};
OS Colletotrichum simmondsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH31061.1, ECO:0000313|Proteomes:UP000070328};
RN [1] {ECO:0000313|EMBL:KXH31061.1, ECO:0000313|Proteomes:UP000070328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS122122 {ECO:0000313|EMBL:KXH31061.1,
RC ECO:0000313|Proteomes:UP000070328};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL Submitted (FEB-2014) 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:KXH31061.1}.
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DR EMBL; JFBX01000686; KXH31061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135S5C0; -.
DR OrthoDB; 12127at2759; -.
DR Proteomes; UP000070328; 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 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 Pfam; PF00627; UBA; 1.
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; 1.
DR PROSITE; PS50031; EH; 3.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endosome {ECO:0000256|ARBA:ARBA00022753}.
FT DOMAIN 19..127
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 146..237
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 293..328
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 294..387
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 1222..1262
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 114..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..416
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..995
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1209
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 132081 MW; 2CCE087727E0BEDA CRC64;
MSAEGVDAAA PNLNLTPEEK RLYGQLFRQA DTESVGVVTG ETAVKFFEKT RLDSRVLGEI
WQIADKENRG FLTPAGFGLV LRLIGHCQAG REPTTEIALQ PGPLPRFDGM PPPAGLASPT
PPPAAALQAQ GTGGGSIRIP PLTPEKVNQY SGLFERQPLQ AGNLLPGDAA KSIFEKSGLP
TEVLGRIWQL ADTEQRGALV LTEFVIAMHL LTSMKTGALR GLPNILPAPL YEAATRRGPP
APRQSPTATG PISAIPRQLS GTAQYRAGSP LGRPPITAQT TGAPASDWLV TPDDKQRFDV
LYNDLDKTQK GFITGEEAVP FLSQSNLPED ALAQIWDLAD INSEGRLNRD TFAVAMYLIR
QQRTRRDGTV SLPASLPPNL IPPSLRTQAR PQTSGSPFDA PPPPQAQAPV PAPAPAPKSA
LDDLFGLDTP PAPAPAQVAL STGGSNANDP FGSGSAVLAP SSPIRPSPTG NQFKPFVPSS
SFGRGLTVHN TGDSNSGRPP APSASEDLLG DGDPEVSKKL TNETAELANL SNQVGSLSKQ
MQEVQGQRTT TQNELNQANS QKKNFEHRLA QLRTMYEKEA KDVESLQVQL NTSRNETKKL
QGECMTLDGT YRDLQTQHQQ VYAALQADQQ ENANLKEKIR NLNAEIAQLK PQIEKLKSEA
RQQKGLVAIN KKQLTTNEGE RDKLQSEITD LHKSNEELSR QVNTSSPVAS SAQVASPTPS
TASGNNPFFK RTGSTDIMGT FTSPPPAKPS SGDKSFDDVF GPAFPPVGTA STPPPATSFN
PQHTGASTAS LGSFSTPPVS MPSSISRQAT FAAEPPAPPQ SRQISSSFLP FADANESLSS
SRAVSPPASR AEGEVETPQA ASLPGAFPLE PTATGQSTAS TSTASFHESA AQGDAKPSST
GAAAAPAAAG VVAGAAAGAT GSAAADSDPF AAMGPNDAKA DFDDAFASFT SAHNNSDKSG
ADTAKPFSAF DSEFPPISEL DRDDDDDDSD TASEGGGFDD DFAPASPQAK KTEPPVEPKD
AASPTVPVAA AAPATEDSVS PTSIHNATTT TATAAPNIPE TSEASITPAP TTTQHPEPKA
QSSFDDLDDE FEGLEDAKEG SADDDFQTIS RSGLDDFNPV FDSSPPPSQA KTESTAFGQE
SSYDFGSVSP NPAAGELAGA ASKSSAAAPD AQDWDAIFAS LDSPSDANAN PTASAPAPAP
APAPPAEDTR PTPGRALTHT GEHDDPILKN LTSMGYSRED SILALEKYDY NLERAANYLA
SQS
//