ID A0A178AV38_9PLEO Unreviewed; 1426 AA.
AC A0A178AV38;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=UBA/TS-N domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=IQ06DRAFT_375851 {ECO:0000313|EMBL:OAL01557.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL01557.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL01557.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL01557.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV441710; OAL01557.1; -; Genomic_DNA.
DR STRING; 765868.A0A178AV38; -.
DR InParanoid; A0A178AV38; -.
DR OrthoDB; 12127at2759; -.
DR Proteomes; UP000077206; 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; 1.10.287.1490; -; 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; IPR018247; EF_Hand_1_Ca_BS.
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; 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; PS00018; EF_HAND_1; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT DOMAIN 21..97
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 151..241
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 299..388
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 332..367
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1384..1424
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 237..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 532..650
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 256..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1426 AA; 152596 MW; C50F8BDBC6F971F8 CRC64;
MADLAASGEL NQPVLNLTPE EKRIFQYLFQ QADTEKLGVI TGEIAVKFFE RTKLQPAVLG
EIWQIADTEN RGLLTMAGFC QVLRLIGHYQ AGRDPAPELA FRPAPLPKFE GLSIPAAPSA
APSFSPQTTG SIQPQMSGNG PIRVPPLVPA KAAEYAGLFE KSGAVNGVLS GENAKEIFEK
ARLPNEVLGR IWNLSDTEQR GALNVTEFII AMHMLASYRT GNMKALPNTL PPGLYEAASR
RGGVLPPPHG RPDQSATIPR QFSGQNAPRT QSPLSRPPFG APPQTSQATG SDWLIGPQEK
ASYDNLFNNV DKAGRGFITG DQAVRFFSDS GLPEDVLAGI WDLADINSEG QLSKDEFAVA
MYLIRQQRKG DQLPTTLPPS LIPPSLRTAA NQAGASQLQP AAPIPQPKSA ADDLFGLDAF
SAPPPAPQQA AQSTGGSASF SRPFDNDPFA SKAASPTSPH PFQPSPRNPA STFKPFMPSS
SFGQTLTSQS TGQSGSSGVQ GRGSAPSAMD DLLGGENDAE INKKLTQDST ELANMSNQMT
TLRNQMQEVQ NKKVTTASDL NSVNTQKRDL EIRLTQFKNQ YEQEVKSVKE LEDRLAASRN
ETRKLQQDVA MIEGTLQDLQ NQHRQVGGAL EADQRENGNL KERIRQINAE VGQLRPQLEK
MRNDARQQKG MVAINKKQLA TNESERDKIK NEMNDLSKAP EEGFRSPATQ TPSVVSPATS
TASHNTNPFF RKSPQPATEN TMSPSGFARD GPHKDFDSVF GSFASPQNAA PPVSFRSDSQ
SQVPAFSAPS GQSVRSSEGP DVPTPSTSPP LSSYQESPRG TEPPAPPESR QFGSAFLPLR
DAVPRSDSFS SSVKVSAPAS RYGGPGNETP TVSKASPAGT PVPEKPTMER SETNRTETDN
FNPSLFDRNV STASPVASVT SDTQRSTRPE DRKDNFANFG PPSQVTQDLP GAFPRDTASP
LQQMQTGESN LSGQSKNNNR SDPFGSSSGE QARAGGKVDF DAAFAGFGSS RQNTTGPSTS
NGPIDNSNRF NKEFPPIEDL AHDDDSDSND GQGFDDNFTS ASPQQKRAST GIDSQAQQQR
PGTASTTDDL YSRPAPASRL DSNLSDLPTP NAQKSPPTYE SSVPQRSGSN QFPPEFGGLL
PSRDVPGSPT TSQGPEKSFN PAGGHGAALF GGSQSKPATT SPPPLDTPSS TVPSDAYHSA
VSYGTNETNK GPSPPANHSQ LGRSAFTDDF DAGFDDLTDA KEDDKTDDDF MFSSQRTEGL
DEFNPVFDSP AASKANTMAS QQTPTGKQRG DDSFSDFEHL SHTFGQPQAP QPAASNQDWD
AIFSNLESSS TDKNSQQAST EFGKSSVFDT LDKEEAAASS SKGALSPQSA QMPQLGRAIS
TGTEHDDPIL KKLTGMGYPR NDALDALEKF DYDINKAADH LTSGQR
//
