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Database: UniProt
Entry: K2RFN7_MACPH
LinkDB: K2RFN7_MACPH
Original site: K2RFN7_MACPH 
ID   K2RFN7_MACPH            Unreviewed;      1048 AA.
AC   K2RFN7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   22-FEB-2023, entry version 39.
DE   SubName: Full=I/LWEQ domain-containing protein {ECO:0000313|EMBL:EKG11692.1};
GN   ORFNames=MPH_11185 {ECO:0000313|EMBL:EKG11692.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG11692.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG11692.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG11692.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
CC   -!- SIMILARITY: Belongs to the SLA2 family.
CC       {ECO:0000256|ARBA:ARBA00010135}.
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:EKG11692.1}.
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DR   EMBL; AHHD01000467; EKG11692.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2RFN7; -.
DR   STRING; 1126212.K2RFN7; -.
DR   VEuPathDB; FungiDB:MPH_11185; -.
DR   eggNOG; KOG0980; Eukaryota.
DR   HOGENOM; CLU_004601_0_0_1; -.
DR   InParanoid; K2RFN7; -.
DR   OrthoDB; 7775at2759; -.
DR   Proteomes; UP000007129; Unassembled WGS sequence.
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:UP000007129}.
FT   DOMAIN          8..138
FT                   /note="ENTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50942"
FT   DOMAIN          805..1048
FT                   /note="I/LWEQ"
FT                   /evidence="ECO:0000259|PROSITE:PS50945"
FT   REGION          267..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1007..1043
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        269..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..318
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1048 AA;  119082 MW;  B9EE9ED535290CF1 CRC64;
     MYGSRNVDMG KQESELAINI RKATSIDETA PKRKHVRAAI VYTWDHKNSD SFWAGMKVQP
     ILADEVQTFK ALITIHKVLQ EGHPIVLKQA QAHIGFLESL QRGVAGGEGM RGYAPLISEY
     VYYLMAKLAF HRQHPEFNGT FEYEEYISLK SINDPNEGYE TISDLMTLQD QIDSFQKLIF
     SHFRNGTNNE CRISALVPLV QESYGIYKFI TSMLRAMHTT LGDDEALAPL RGRYDAQHYR
     LVKFYYECSN LRYLTSLITV PKLPQDPPNL LSEDEDRPAL PARPKKDDDT PKRAASVDPE
     PINEFWKNEQ KRQQEEYEAE QKRLAQQWEE AQRRQQEEQM RAQREFEEQQ RLAAEQARMA
     QEQLAREQFA QQTQGRMAEL ERENLAARNQ YQQDQLLLQQ YDARVKALEN ELQSIQGNFA
     QQSQSKDDQI RALQEQLNTW RSKYEALAKL YSQLRHEHLE LLQKFKSVQL KAASAQEAID
     QREKLQRELK TKNLELADMI RERDRALHEK DRTTGGHKDE VEKLQRELRL ALDRADQADR
     NKGSELSAML SRHNREIADL EEALRNKNRQ LEDLQLRFRE GDSELERQLR EKEDELEIFK
     AGMDQTLLEL NELKMNQQAS NNASDEVFDT VILDNLRKIG DIIDSVLQSG VQRVDDALYE
     LDSSMQAGNQ NASGAYVLSQ IEKASSCAME FSTAYNNFIA DGPNATHAEI IRTVNAFAGS
     IADVLSNTKG LTRFASDEKK GDQLIGAARH SAESTVNFFR SLQSFRLEGM EDLQKTDVVL
     NCNSEVQLNL QKLSKLADAF APKSKISANQ GDLGDLVDRE MANAANAILA ATERLSKLKD
     RSRDSYSTYE LRIHDAILGA AIEVTNAIAR LIKAATESQQ EIVREGKGTS SRTAFYKKNN
     RWTEGLISAA KAVANSTNLL IETADGVISG RNSPEQLIVA SNDVAASTAQ LVAASRVKAS
     FMSKTQDRLE AASKAVTQAC RALVRQVQSI INERNRDGEE AVDYSKLSGH EFKVREMEQQ
     VEILQLENAL SAARHRLGEM RKLSYQEE
//
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