ID A0A0N5AI60_9BILA Unreviewed; 627 AA.
AC A0A0N5AI60;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Fip1 domain-containing protein {ECO:0000313|WBParaSite:SMUV_0000409201-mRNA-1};
OS Syphacia muris.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000409201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMUV_0000409201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the FIP1 family.
CC {ECO:0000256|ARBA:ARBA00007459}.
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 AlphaFoldDB; A0A0N5AI60; -.
DR STRING; 451379.A0A0N5AI60; -.
DR WBParaSite; SMUV_0000409201-mRNA-1; SMUV_0000409201-mRNA-1; SMUV_0000409201.
DR Proteomes; UP000046393; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR InterPro; IPR007854; Fip1_dom.
DR PANTHER; PTHR13484; FIP1-LIKE 1 PROTEIN; 1.
DR PANTHER; PTHR13484:SF0; FIP1-LIKE 1 PROTEIN; 1.
DR Pfam; PF05182; Fip1; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 122..164
FT /note="Pre-mRNA polyadenylation factor Fip1"
FT /evidence="ECO:0000259|Pfam:PF05182"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..89
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..328
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..369
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..431
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 69041 MW; 54CA1A5596BBF7AB CRC64;
MSAIPGFGGE EIYEEPLPPH DPSDEEHADS DSGTPQVTLA SKEQDDEKKD DSSADNANDT
CNADALDLDG EGGDEEGGGG DEDDDDDSDA SFVVTIGQKV AASGGKLDLD AVPSINGQPI
YDLDLASMEE RPWRKPGADI NDYFNYGFCE ETWNMYCERQ RKLRDEYGTQ SAVNKALFSS
INLVNPVSQD TGGRQLQTIP IIGQENKGNI DLSSFKAVEQ QPVIRTVLTA GQPPRSIGTG
GTAGTSIGTS EGEPASSLSN TSLNPPSSTV EVDFSKPPPP LDTIASAPTK NVLAMPSLGV
APSLPPPPVS DGPPGVDEPA PPGSTTPPPG FGELISRQIP TLSATVDTSI PPPAFNPLLP
PPNLSAPPPA VRLGLPNTNV PPPSYTVPPP GFTQPPPGFP PRFGAPGVGG PPQINRPPPL
MGRPAYPPPG LETPRDSRDN EEKDRDRGRD RDRERERDRD SGESDADDYV GRRRRSRRRS
RSYSPRSGRR HRDDRDRERD RDSDRYRDKG DRDRDSRSRR HRSRSSSPYE ILMKQLQILG
SRSSRRREDR NEKDKDKKRR GDKDREETDD KEKDKKDREK DNDSSKERER DKDKERKKRR
HNKSDDEGSE KREKEKKKPK AKEEATS
//