ID A0A165P3F2_EXIGL Unreviewed; 412 AA.
AC A0A165P3F2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RNA polymerase II-associated protein 3 {ECO:0000256|ARBA:ARBA00040133};
GN ORFNames=EXIGLDRAFT_717977 {ECO:0000313|EMBL:KZW01586.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW01586.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW01586.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW01586.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the RPAP3 family.
CC {ECO:0000256|ARBA:ARBA00038275}.
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DR EMBL; KV425893; KZW01586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165P3F2; -.
DR STRING; 1314781.A0A165P3F2; -.
DR InParanoid; A0A165P3F2; -.
DR OrthoDB; 1353681at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR025986; RPAP3-like_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR46423; RNA POLYMERASE II-ASSOCIATED PROTEIN 3; 1.
DR PANTHER; PTHR46423:SF1; RNA POLYMERASE II-ASSOCIATED PROTEIN 3; 1.
DR Pfam; PF13877; RPAP3_C; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT REPEAT 73..106
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 301..393
FT /note="RNA-polymerase II-associated protein 3-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF13877"
FT REGION 124..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..289
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 43984 MW; 9AD8A1BEC4DFA711 CRC64;
MSGAAKAAKD KGNAAFKSGD FVAAVGHYTD AALADRLEPT YPLNRAAAYL KLGKYADAER
DCSTTLALSH GNVKALYRRA QARIALRKLD DAEKDLNDAL KREPANDAVK QELVKLKQIR
AEASAPKKAP ISVSTPLPAA TASSATTKPI RRRIPIKIVD DDAPASIATH ASTSASKAGE
DFMTPVATRS LSGSSSSSTP PPKSILKKPQ PTEPTQPPSQ TPATSFQAAK DARDQARKPK
VGGGIFKANG THTLFKGSTT AQEEATPRIV EVTAPEPAPA PPAPRTRQLP LPQSPDTALT
TTLFNLQREW RNRPTAEARW ELLCSVPPSS LPKLCGTSLE PAFLVAVLDT FRTLAVSGVA
QADARNAMRD YLNSFATVPR FDTVLMFLSA QEKEVVRDTI RSLGLKSWAG VS
//
