ID A0A2P5I3N1_9PEZI Unreviewed; 1077 AA.
AC A0A2P5I3N1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 28-JUN-2023, entry version 20.
DE RecName: Full=Importin N-terminal domain-containing protein {ECO:0000259|PROSITE:PS50166};
GN ORFNames=DHEL01_v204503 {ECO:0000313|EMBL:POS77108.1};
OS Diaporthe helianthi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=158607 {ECO:0000313|EMBL:POS77108.1, ECO:0000313|Proteomes:UP000094444};
RN [1] {ECO:0000313|EMBL:POS77108.1, ECO:0000313|Proteomes:UP000094444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7/96 {ECO:0000313|EMBL:POS77108.1,
RC ECO:0000313|Proteomes:UP000094444};
RA Baroncelli R.;
RT "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL Submitted (SEP-2017) 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}.
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:POS77108.1}.
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DR EMBL; MAVT02000300; POS77108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5I3N1; -.
DR STRING; 158607.A0A2P5I3N1; -.
DR InParanoid; A0A2P5I3N1; -.
DR OrthoDB; 169519at2759; -.
DR Proteomes; UP000094444; 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:UP000094444};
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 1043..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1070
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 123394 MW; 884BADED694170ED CRC64;
MAISIEELDV LVRSFYEGRG EQQKAAQAAL NQFKEDPDAW LMVDDILSKA TYPQTKYLAL
QVLDNVISTR WRVLPREQCQ GIRNFIVSFI LQCSSTEESL RSQRTLLNKL NLVLISVLKQ
EWPHNWPTFI NEIIQACHSS LSVCENNMII LRLLSEEVFD YSAEQMTSTK TRSLKTTMCN
EFSQIFQLCQ EILNTATQPS LVLATLETLL RFCNWIPLGY IFETPLISLL RTRFLEVPEF
RNITLQCLTE IGGLQTGGPA GNNYDEQLVK MFTEVLTTVS TIIPIQMDLK TTYPQSNSRD
QQFVQNLALF LTNFFSMHLN LIENLPNRDY LSHAHYYLIR ISQIDDREIF KICLDYWLKL
VQELYEEMQS LPIGDNPLIA MGAMSGGAPN PALLNNYPLR KHKYQEVLSN LRVVMIEKMV
RPEEVLIVEN DEGEIVREFV KESDTVQLYK TIRECLVYLT HLDVVDTEQI MTDKLAKQVD
GTEWSWHNCN VLCWAIGSIS LAMNEETEKR FLVTVIKDLL GLTEMKRGKD NKAVVASNIM
YIVGQYPRFL KAHWKFLKTV VNKLFEFMHE SHEGVQDMAC DTFIKIAKSC KRHFVALQPS
EHEPFIEEIV RNLPKITGDL TPQQVHTFYE ACGYMVAAQG NRNQQERLLA ELMQHPNAAW
DEIIKQATVN PAILQDADTI KIIGNIMKTN VSACSSVGSY FFPQIGRIYH DMLQMYRATS
QLISESVAKE GEIATKMPKV RGLRTIKKEI LKLIETYVDK AEDHTAVRTQ MVPPLLDCVL
VDYNRNVPGA RDAEVLRAMT AVISKLSSLM EDQVPTIMEN VFECTLDMIN KDFSEFPEHR
VEFFNLLRAI NLNCFPALLK LDNRQFKFVI DSCMWASKHD NRDVEAAGLN MCLELINNIA
EKTDVQTSNA FFNQFFTPIL QDVFFVVTDQ DHKAGFKTQS MLLMRMFYFV QPADGTASKI
QGPIYQPDMA QAGTSNREFL GNFVATLLAN AFSNLQAPQI TAFVEGLFAL NTQYDKFRLH
LRDFLISMKE YAGDNAELYQ VEKEKEDAAK QQADLDRRSK VGGLMKPSEL ENDDDEL
//
