ID A0A178AEL5_9PLEO Unreviewed; 1072 AA.
AC A0A178AEL5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 30.
DE RecName: Full=Importin N-terminal domain-containing protein {ECO:0000259|PROSITE:PS50166};
GN ORFNames=IQ06DRAFT_381136 {ECO:0000313|EMBL:OAK96064.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK96064.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK96064.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK96064.1,
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: tRNA nucleus export receptor which facilitates tRNA
CC translocation across the nuclear pore complex. Involved in pre-tRNA
CC splicing, probably by affecting the interaction of pre-tRNA with
CC splicing endonuclease. {ECO:0000256|ARBA:ARBA00025147}.
CC -!- SIMILARITY: Belongs to the exportin family.
CC {ECO:0000256|ARBA:ARBA00009466}.
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DR EMBL; KV441721; OAK96064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AEL5; -.
DR STRING; 765868.A0A178AEL5; -.
DR InParanoid; A0A178AEL5; -.
DR OrthoDB; 169519at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005049; F:nuclear export signal receptor activity; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006611; P:protein export from nucleus; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR041123; CRM1_repeat.
DR InterPro; IPR041235; Exp1_repeat_2.
DR InterPro; IPR013598; Exportin-1/Importin-b-like.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR045065; XPO1/5.
DR InterPro; IPR014877; XPO1_C_dom.
DR InterPro; IPR040485; XPO1_repeat_3.
DR PANTHER; PTHR11223; EXPORTIN 1/5; 1.
DR PANTHER; PTHR11223:SF2; EXPORTIN-1; 1.
DR Pfam; PF08767; CRM1_C; 1.
DR Pfam; PF18777; CRM1_repeat; 1.
DR Pfam; PF18784; CRM1_repeat_2; 1.
DR Pfam; PF18787; CRM1_repeat_3; 1.
DR Pfam; PF03810; IBN_N; 1.
DR Pfam; PF08389; Xpo1; 1.
DR SMART; SM01102; CRM1_C; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 26..92
FT /note="Importin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50166"
FT REGION 1041..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1066
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 123039 MW; FF5A5F08BB7F8CD0 CRC64;
MSLSIEELDA TVRAFYEGRG EPQKQAQATL NQFKENPDAW LLVDKILQDA QYPQTKYLGL
QVLDNVIMTR WKVLPRDQCQ GIRNFVVNFI IQLSNNDDSR RTDRTLLNKL NLVLVSVLKQ
EWPHNWPTFI NEIISSCHSS LGICENNMVI LRLLSEEVFD YSEEQMTSSK RRELKQSMCD
EFTSIYQLCS EVLRTATEAS LIKATLETLL RFLNWIPLGY IFETPPSGQS LIETLRSRFL
EVPEFRNITL KCLTEIAGLH TEPAYDDKLV SMFTETLTAI SKIIPLSLDL KSTYASSNGR
DQEFVLNLAL FLTNFFTMHL NVIENLMNRD FLTHGHFYLI RISQIDDREV FKICLEYWTK
LVSELYDEMQ ALPITDMNPL LNMGISSSGP RDSNMMANYP LRKNKYTEIL SNLRTVMIEK
MVRPEEVLIV ENDEGEIVRE FVKESDTIQL YKSTRECLVF LTHLDVNDTE QIMSEKLARQ
VDGTEWSWAN CNTLCWAIGS ISGAMNEETE KRFLVTVIKD LLGLTEMKRG KDNKAVVASN
IMYIVGQYPR FLKAHWKFLK TVVNKLFEFM HETHEGVQDM ACDTFIKIAN KCRRHFVALQ
PGESEPFIDE IVRNLRKITA DLSPQQVHTF YEACGYMISA QGQKSMQERL IHDLMALPNS
AWDNIIAQAN QNPACLQDSE IIKIVGNIMK TNVAACGSIG SYFYPQIGRI YFDMLTMYRA
SSQLIDEAVQ REGNIATKMP KVRGLRTIKK EILKLINTYV EKADDLEMIH NNIVPKLLEA
VLVDYKNNVP DAREAEVLNV MTTIVNKLHS MMEDQIINIM DSVFECTLEM INKDFSEYPE
HRVEFFKLLR TINLRCFPAL LRLDARSFKF VIDSCMWASK HDNREVESAG LSMCFELVSN
MADTDAQTCN AFFQTFFTTI LQDVFFVVTD SDHKAGFKSQ SMLLAKMFWL VDSDKLQGPI
YTSPDMAPAG TPNREFLRNF VGNLLATAFP NLQTAQIASF IDGLFATNSD LNRFKVILRD
FLISLKEFSG DNAELFAEER EQAASKAKEE ERERAMKVGG LLKPSEMDDD EL
//
