ID G2R2Q0_THETT Unreviewed; 1050 AA.
AC G2R2Q0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 22-FEB-2023, entry version 53.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AEO65011.1};
GN ORFNames=THITE_2111501 {ECO:0000313|EMBL:AEO65011.1};
OS Thermothielavioides terrestris (strain ATCC 38088 / NRRL 8126) (Thielavia
OS terrestris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides;
OC Thermothielavioides terrestris.
OX NCBI_TaxID=578455 {ECO:0000313|EMBL:AEO65011.1, ECO:0000313|Proteomes:UP000008181};
RN [1] {ECO:0000313|EMBL:AEO65011.1, ECO:0000313|Proteomes:UP000008181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38088 / NRRL 8126 {ECO:0000313|Proteomes:UP000008181};
RX PubMed=21964414; DOI=10.1038/nbt.1976;
RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA Tsang A.;
RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT Myceliophthora thermophila and Thielavia terrestris.";
RL Nat. Biotechnol. 29:922-927(2011).
CC -!- SIMILARITY: Belongs to the SLA2 family.
CC {ECO:0000256|ARBA:ARBA00010135}.
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; CP003010; AEO65011.1; -; Genomic_DNA.
DR RefSeq; XP_003651347.1; XM_003651299.1.
DR AlphaFoldDB; G2R2Q0; -.
DR STRING; 578455.G2R2Q0; -.
DR GeneID; 11518304; -.
DR KEGG; ttt:THITE_2111501; -.
DR eggNOG; KOG0980; Eukaryota.
DR HOGENOM; CLU_004601_0_0_1; -.
DR OrthoDB; 7775at2759; -.
DR Proteomes; UP000008181; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:InterPro.
DR CDD; cd17007; ANTH_N_Sla2p; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 1.20.1410.10; I/LWEQ domain; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR035964; I/LWEQ_dom_sf.
DR InterPro; IPR002558; ILWEQ_dom.
DR InterPro; IPR030224; Sla2_fam.
DR PANTHER; PTHR10407; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR10407:SF15; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR Pfam; PF07651; ANTH; 1.
DR Pfam; PF01608; I_LWEQ; 1.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF109885; I/LWEQ domain; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50945; I_LWEQ; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000008181}.
FT DOMAIN 8..137
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT DOMAIN 808..1050
FT /note="I/LWEQ"
FT /evidence="ECO:0000259|PROSITE:PS50945"
FT REGION 267..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 310..619
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 983..1036
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1050 AA; 118683 MW; 3DA22684D584C5D6 CRC64;
MATIRSLDHT KSEAELAINI KKATSPEETA PKRKHVRSCI VYTWDHKSSQ SFWAGLKVQP
ILADEVQTFK ALIMVHKVLQ EGHPVTLREA MANRGWIDSL NRGMIGEGVR GYGPLIKEYV
YYLLAKLSFH KQHPEFNGTF EYEEYISLKA INDPNEGYET ITDLMTLQDK IDQFQKLIFS
HFRNVGNNEC RISALVPLVT ESYGIYKFIT SMLRAMHSTT GDNDALEPLR QRYDAQHYRL
VKFYYECSNL RYLTSLITIP KLPQDPPNLL ADDDTAPALP ARPKQEIEKQ PTPPPAPKSD
EPDEITEFWK SEIDRQNREF EEQQRVLEAQ QQAALLAQQQ AQLQAQREFE EQQRRLLEQQ
QREQEALRAQ QAQWQTQGRL AELEQENLNA RAQYERDQLM LQQYDQRVKA LEGELQQIQS
NYGQQIASKD DQIRALQEQV NTWRTKYEAL AKLYSQLRHE HLDLLQKFKA VQLKAASAQE
AIDRREKLER EIKTKNLELA DMIRERDRAL HEKDRLQGSN KDEVEKLKRE LRMALDRADN
LERSKGNELS AMLSKYNREV ADLEEALRNK SRALEEAQAK LRDGNSDLEA LLREKEEELE
VYKAGMDQTL IELNELKNNQ GTTEQVLDGQ IDALVLAQLA KINEIIDSVL QAGVQRVDDA
MYELDSTMQA GNQSASPSYV LSQIEKASAS ATEFATSFNN FIADGPNSTP ADLIKNVNIF
AGAIADVCGN TKGLTRLATD EKMSDSLING ARQSAHATVK FFRSLLSFRL EGMEPLQKTD
VVINSNHDVQ MNLQRLNKAV EAFAPGYGKL AAKGDLGEIV DKELSKAADA IEAAVARLNK
LKSKPRDGYS TYELRVHDSI LDAAMAITTA IAQLIKAATI AQQEIVQAGR GSSSRTAFYK
KNNRWTEGLI SAAKAVASST NTLIETADGV LSNRNTPEQL IVASNDVAAS TAQLVAASRV
KAGFMSKSQE NLEQASKAVG AACRALVRQV QDMIKDRNAE EEQVDYSKLG QHEFKVREME
QQVEILQLEN ALAAARHRLG EMRKISYREE
//
