RMP_DICDI
ID RMP_DICDI Reviewed; 489 AA.
AC Q54HG4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=RNA polymerase II subunit 5-mediating protein homolog;
DE Short=RPB5-mediating protein homolog;
GN Name=rmp; ORFNames=DDB_G0289477;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase II subunit 5-mediating
CC protein family. {ECO:0000305}.
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DR EMBL; AAFI02000141; EAL62718.2; -; Genomic_DNA.
DR RefSeq; XP_636221.2; XM_631129.2.
DR AlphaFoldDB; Q54HG4; -.
DR SMR; Q54HG4; -.
DR STRING; 44689.DDB0302504; -.
DR PaxDb; Q54HG4; -.
DR PRIDE; Q54HG4; -.
DR EnsemblProtists; EAL62718; EAL62718; DDB_G0289477.
DR GeneID; 8627159; -.
DR KEGG; ddi:DDB_G0289477; -.
DR dictyBase; DDB_G0289477; rmp.
DR eggNOG; KOG3130; Eukaryota.
DR HOGENOM; CLU_558284_0_0_1; -.
DR InParanoid; Q54HG4; -.
DR OMA; EVETECR; -.
DR PRO; PR:Q54HG4; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0019212; F:phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR Pfam; PF02996; Prefoldin; 1.
DR TIGRFAMs; TIGR00293; TIGR00293; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome.
FT CHAIN 1..489
FT /note="RNA polymerase II subunit 5-mediating protein
FT homolog"
FT /id="PRO_0000328598"
FT REGION 141..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..258
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..298
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 57567 MW; 6F02BEAD3C1BBC64 CRC64;
MSSQEIFKKY EQKVVEYQDH IEELKSTKND YKQLIDTLQH LPDTLQPKIM VPMGKLAFFE
GNLKNTNEIL ILLGDNYFAK RSSKQTIDII QRRDKDIDTS INDLREQIKG LKQRVSMTTD
LSKALHEKEY DNIVEIKEEY NSDEEREKEK KRKQKPQKST TTTTTTTTSK DKPKTEEEKK
KSKEMDEEFD KMLKRLSILE EKENKMGDDY DEEEFNKKFN KKLDITGSDE EYDDDNYNNN
NDDDDDNDED DDREYYQEEG FEDEKPENSN YNKNIEEDDH DDDDDYYDEG EEIVEYYDEN
GNIVDINDPN VEYIQGDDDN DDNDNEEDEV DVELNESELE EIKDFHMDKK GQDLSEKEVK
ELTDFYHSKQ KKRISYIDTP QPPTPEATTS ITPKSILKTN SSGNLMSTIP KSYNENDEND
IRRYIKNLDK QEKFENQKTI SVPNPPKDVA FSGDIVEKET DLFPFDEIPK PTPPSNAKQS
RFKSSRQNK
