ID   PAF1_XENLA              Reviewed;         524 AA.
AC   A2BD83;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=RNA polymerase II-associated factor 1 homolog;
GN   Name=paf1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
CC       functions during transcription by RNA polymerase II. PAF1C associates
CC       with RNA polymerase II, is involved in transcriptional elongation and
CC       in histone modifications including methylation on histone H3 'Lys-4'
CC       (H3K4me3) (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the PAF1 complex, which at least consists of
CC       cdc73, paf1, leo1, ctr9 and rtf1 (By similarity). The PAF1 complex
CC       interacts with PHF5A (By similarity). {ECO:0000250|UniProtKB:Q8K2T8,
CC       ECO:0000250|UniProtKB:Q8N7H5}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PAF1 family. {ECO:0000305}.
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DR   EMBL; BC130057; AAI30058.1; -; mRNA.
DR   RefSeq; NP_001086458.1; NM_001092989.1.
DR   AlphaFoldDB; A2BD83; -.
DR   SMR; A2BD83; -.
DR   BioGRID; 103138; 1.
DR   IntAct; A2BD83; 1.
DR   MaxQB; A2BD83; -.
DR   DNASU; 446278; -.
DR   GeneID; 446278; -.
DR   KEGG; xla:446278; -.
DR   CTD; 446278; -.
DR   Xenbase; XB-GENE-5797702; paf1.L.
DR   OMA; MRPDGIY; -.
DR   OrthoDB; 599989at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 446278; Expressed in internal ear and 19 other tissues.
DR   GO; GO:0016593; C:Cdc73/Paf1 complex; ISS:UniProtKB.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR   GO; GO:0016570; P:histone modification; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR   InterPro; IPR007133; RNA_pol_II-assoc_Paf1.
DR   PANTHER; PTHR23188; PTHR23188; 1.
DR   Pfam; PF03985; Paf1; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..524
FT                   /note="RNA polymerase II-associated factor 1 homolog"
FT                   /id="PRO_0000326405"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          351..384
FT                   /evidence="ECO:0000255"
FT   COILED          412..442
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        359..375
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..432
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..447
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..478
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  59605 MW;  FDB5F8BCF3658A99 CRC64;
     MAPTIQTQAQ REDGHRSSSH RTVPERSGVV CRVKYCNTLP DIPFDPKFIT YPFDQNRFVQ
     YKATSLEKQH KHDLLTEPDL GVTIDLINPD TYRIDPNVTL DFADEKLLEE EIQAPSSSKR
     SQQHAKVVPW MRKTEYISTE FNRYGVSNEK PEVKIGVSVK QQFTEEDIYK DRDSQISAIE
     KTFDDAQKDI SQHYSKPRVT PVEVMPVFPD FKMWINPCAQ VIFDSDPAPK DASGTAALDM
     MSQAMIRGMM DEEGNQFVAY FLPGEDTMRK RKRDQEEGLD YMPEDIYDYK IAREYNWNVK
     NKASKGYEEN YFFIFREGDG VYYNELETRV RLSKRRVKAG VQSGTNALLV VKHRDMHEKE
     LEAQEARRAQ LENHEPEEEE EIEVDRDTQG SDAEEGEKGS GSEKEGSGAE QSGSESEREG
     AEEEEKEDEQ EKESSEDDRA ARDKEEIFGS DDDDDDDDSD EDGHNESGQD GEDSGSDEEE
     EKGQGRRSRS ASSSPFGSDR SQQENEDQSA SDQGSGSSDG SDSD