ID A0A0N4U6L7_DRAME Unreviewed; 1342 AA.
AC A0A0N4U6L7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Nucleolar protein 6 {ECO:0000256|ARBA:ARBA00016437};
DE AltName: Full=Maternal transcript 89Ba {ECO:0000256|ARBA:ARBA00031711};
GN ORFNames=DME_LOCUS6935 {ECO:0000313|EMBL:VDN56962.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000257501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000257501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN56962.1, ECO:0000313|Proteomes:UP000274756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the small subunit (SSU) processome, first precursor
CC of the small eukaryotic ribosomal subunit. During the assembly of the
CC SSU processome in the nucleolus, many ribosome biogenesis factors, an
CC RNA chaperone and ribosomal proteins associate with the nascent pre-
CC rRNA and work in concert to generate RNA folding, modifications,
CC rearrangements and cleavage as well as targeted degradation of pre-
CC ribosomal RNA by the RNA exosome. {ECO:0000256|ARBA:ARBA00035000}.
CC -!- SUBUNIT: Part of the small subunit (SSU) processome, composed of more
CC than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3.
CC {ECO:0000256|ARBA:ARBA00035020}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the NRAP family.
CC {ECO:0000256|ARBA:ARBA00006674}.
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DR EMBL; UYYG01001157; VDN56962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4U6L7; -.
DR STRING; 318479.A0A0N4U6L7; -.
DR WBParaSite; DME_0000257501-mRNA-1; DME_0000257501-mRNA-1; DME_0000257501.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR CDD; cd09232; Snurportin-1_C; 1.
DR Gene3D; 1.10.1410.10; -; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR InterPro; IPR005554; NOL6/Upt22.
DR InterPro; IPR035082; Nrap_D1.
DR InterPro; IPR035367; Nrap_D2.
DR InterPro; IPR035368; Nrap_D3.
DR InterPro; IPR035369; Nrap_D4.
DR InterPro; IPR035370; Nrap_D5.
DR InterPro; IPR035371; Nrap_D6.
DR InterPro; IPR024721; Snurportin-1_N.
DR InterPro; IPR047857; Snurportin1_C.
DR PANTHER; PTHR17972:SF0; NUCLEOLAR PROTEIN 6; 1.
DR PANTHER; PTHR17972; NUCLEOLAR RNA-ASSOCIATED PROTEIN; 1.
DR Pfam; PF03813; Nrap; 1.
DR Pfam; PF17403; Nrap_D2; 1.
DR Pfam; PF17404; Nrap_D3; 1.
DR Pfam; PF17405; Nrap_D4; 1.
DR Pfam; PF17406; Nrap_D5; 1.
DR Pfam; PF17407; Nrap_D6; 1.
DR Pfam; PF11538; Snurportin1; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000274756};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 123..274
FT /note="Nrap protein"
FT /evidence="ECO:0000259|Pfam:PF03813"
FT DOMAIN 289..423
FT /note="Nrap protein"
FT /evidence="ECO:0000259|Pfam:PF17403"
FT DOMAIN 430..586
FT /note="Nrap protein"
FT /evidence="ECO:0000259|Pfam:PF17404"
FT DOMAIN 602..770
FT /note="Nrap protein"
FT /evidence="ECO:0000259|Pfam:PF17405"
FT DOMAIN 773..925
FT /note="Nrap protein"
FT /evidence="ECO:0000259|Pfam:PF17406"
FT DOMAIN 929..991
FT /note="Nrap protein"
FT /evidence="ECO:0000259|Pfam:PF17407"
FT DOMAIN 1049..1078
FT /note="Snurportin-1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11538"
SQ SEQUENCE 1342 AA; 156103 MW; 366F41D961936CE9 CRC64;
MKRKAEISTI QLEGDLNESR RLMNVMMDDF TSDFTLSPIS RSKLQCFVEH LKSLILSKDT
HIAESELSDN SWLLKKGICF PLSLPFGLKV SELKCHGKCR WKLPESVNVF GYWRMNTRED
VFIDMNVVMS KEYFGSRDFL NFTYHIKRAY YVCGVAIILK QGEIDLDFTI EDHDQMKPML
IAYMKEGRKF EINNRALLSL FYMQIKFVKK NNINRKIGVR IHFSPPDSFA KPFRFRPTNN
NLRPSFCFQN KKYDENSPTP FYNNGIIADL VRDRLEVHFE NFFKKKAIFI KAVMLIQCWL
QNRNFDKRSD GFGDFLLYAW FIYLYNEKVI GEHMAISDIL ITFFQSVVSV NWNDAQLGLA
KDIDSSLYAQ FGEYFDYTFL DVTGFYNLAA NLSCSAFNCI KDAAKSAIVK LNSFKDFDLL
FVKEMPFTNY FDIYIRISVP ETYISSDLPS LFPLEYIDCC GNYSRIIVRY LTNLLLKAWN
DRVDLFDFKQ IFNLGIKWKV GEGWNRKIES LIVGARVIQG WNNIITRGPF AKSNDAVKFQ
DFWGKDICEL RKFPDNTICE TIKWCDSKFA SSVLCRICSH VALRHMRLSG QLLVRSSIPN
FNGGHSRSFT YITNAYNRLY QFLRQLQDLP LQITNIHPIS PHLRKTLSFF ELSYFSVFVQ
FYISVGLTME SSGKWGDNRE AVALLKTAFY IALAQILNEQ FSRAIPYQDY LIVVLDQVLF
RLSILYQREV HLMQKDMNSG LITSDETYLK LQEREIIIKP RLSAYLYSVS QLYPAFAATC
RLAHQWLSSH MLTDYINDII LETITAYIFV HPFTSVPPRS YYSGFLNFLI LLSSHNWLMK
PLIVNFNNEL TEDEMNEMET TFIKMRPVLP SMVIFTPADS TGIRWTREEP QPLILKRIVC
LASSSAILLQ RNLDSIPVVI KSIFATDINV YDVIITLNNE HIVRKRNRCR RFVATKYLPV
FDYDPVEKFL QSLRANFATV AFFFFDKSKD NQKSGSNTCV SSVTYFTMEN EELLNGSMVY
NEVFDVDGLI MKFSGDAIEL SPQSVSSGHP RYTFYKNVAR AEEVQRKRRA EFLERQKECV
FIIFKHQNIN TRNLFLDKAD KADQEAMDVV EISSNKNKRN EKYADVLMLS EWLVDIPTNL
SSEWIMVPCP VGKRLKGVTS AYNKKGNRFK QFRSYLPGSI RSKGSENATL LDCILSYETN
TFYCLDVIVW NGIIQSDVTF DCRLFFINSR INENQNFGER SKENPFVFKS LPYCYCQINA
MENLLKSNLD FTIDGILFYH SQVFYRSGQS PLVGWLKPWM LPEILNVTVP QRLMDGKETE
IGASQKFIDN YNIEHNHISS LK
//