GEMI5_DICDI
ID GEMI5_DICDI Reviewed; 1276 AA.
AC Q54IY5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Component of gems protein 5;
DE AltName: Full=Gemin-5;
GN Name=gemin5; ORFNames=DDB_G0288425;
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 -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in
CC a heptameric protein ring on the Sm site of the small nuclear RNA to
CC form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1,
CC SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm
CC complex by the chaperone CLNS1A that controls the assembly of the core
CC snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm
CC proteins from CLNS1A forming an intermediate. Binding of snRNA inside
CC 5Sm ultimately triggers eviction of the SMN complex, thereby allowing
CC binding of SNRPD3 and SNRPB to complete assembly of the core snRNP.
CC Within the SMN complex, GEMIN5 recognizes and delivers the small
CC nuclear RNAs (snRNAs) to the SMN complex. Binds to the 7-
CC methylguanosine cap of RNA molecules (By similarity).
CC {ECO:0000250|UniProtKB:Q8TEQ6}.
CC -!- SUBUNIT: Part of the core SMN complex. {ECO:0000250|UniProtKB:Q8TEQ6}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q8TEQ6}. Nucleus, gem
CC {ECO:0000250|UniProtKB:Q8TEQ6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8TEQ6}. Note=Found both in the nucleoplasm and
CC in nuclear bodies called gems (Gemini of Cajal bodies) that are often
CC in proximity to Cajal (coiled) bodies. Also found in the cytoplasm.
CC {ECO:0000250|UniProtKB:Q8TEQ6}.
CC -!- DOMAIN: The WD repeat domain mediates binding to U1 snRNA and to U4
CC snRNA. The WD repeat domain also mediates binding to the 7-
CC methylguanosine cap that is found both on mRNA and snRNA molecules. The
CC regions that bind snRNA molecules and the isolated 7-methylguanosine
CC cap overlap at least partially. Besides, the WD repeat domain mediates
CC interaction with the 60S large ribosomal subunit.
CC {ECO:0000250|UniProtKB:Q8TEQ6}.
CC -!- SIMILARITY: Belongs to the WD repeat gemin-5 family. {ECO:0000305}.
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DR EMBL; AAFI02000111; EAL63238.1; -; Genomic_DNA.
DR RefSeq; XP_636745.1; XM_631653.1.
DR AlphaFoldDB; Q54IY5; -.
DR STRING; 44689.DDB0302538; -.
DR PaxDb; Q54IY5; -.
DR PRIDE; Q54IY5; -.
DR EnsemblProtists; EAL63238; EAL63238; DDB_G0288425.
DR GeneID; 8626623; -.
DR KEGG; ddi:DDB_G0288425; -.
DR dictyBase; DDB_G0288425; gemin5.
DR eggNOG; ENOG502QPYZ; Eukaryota.
DR HOGENOM; CLU_004491_0_1_1; -.
DR InParanoid; Q54IY5; -.
DR OMA; YWFNRND; -.
DR PhylomeDB; Q54IY5; -.
DR PRO; PR:Q54IY5; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0097504; C:Gemini of coiled bodies; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032797; C:SMN complex; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 13.
DR SUPFAM; SSF50978; SSF50978; 3.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Nucleus; Reference proteome; Repeat; RNA-binding;
KW WD repeat.
FT CHAIN 1..1276
FT /note="Component of gems protein 5"
FT /id="PRO_0000371342"
FT REPEAT 92..139
FT /note="WD 1"
FT REPEAT 183..223
FT /note="WD 2"
FT REPEAT 228..268
FT /note="WD 3"
FT REPEAT 271..336
FT /note="WD 4"
FT REPEAT 364..405
FT /note="WD 5"
FT REPEAT 438..481
FT /note="WD 6"
FT REPEAT 485..522
FT /note="WD 7"
FT REPEAT 530..574
FT /note="WD 8"
FT REPEAT 688..727
FT /note="WD 9"
FT REPEAT 729..771
FT /note="WD 10"
FT REPEAT 863..903
FT /note="WD 11"
FT REPEAT 906..946
FT /note="WD 12"
FT REGION 53..55
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT REGION 138..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 778..829
FT /evidence="ECO:0000255"
FT COMPBIAS 597..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 368
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 413
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 466
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 486
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 528
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 579
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 583
FT /note="Interaction with U4 snRNA and with the 7-
FT methylguanosine cap of RNA molecules"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 732
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 910
FT /note="Interaction with U4 snRNA and with the 7-
FT methylguanosine cap of RNA molecules"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
SQ SEQUENCE 1276 AA; 144531 MW; B7A44B91C55E8A80 CRC64;
MNIDSNIIKN ENLINANNHT DRRDVHDSLA EAPEKITELK KNHWEELLPS SSNWYCTSVA
DCNENQIYIY ACKSNVSIFN IKSKKFIGEL NGHTDRVTSV GFFKRFESKN DESYKWCITG
SDDKTVRIWK FNSNDDDHNE DTEIGDDFKH GSGGGGSDGG GGDDVNNFYG NKSSNFCIYY
HQEHKAGVTC VVASPLVPDL VLSGDKAGAL VIYRTLTNHV FPIPPIIGNN ISISTLAFSP
NHSDLVAIGY LNGIVLIYNF VIRSTVCKIS AHSADVLSIV WFDSTIIQKN NIFHDNNIND
QDDNNSNHRN RIFLATCSKD KAIKIWKQVG EKIESGFTNI YQFNPSKYSI QHSSSSGGGG
INQNDKQRVW LTLSWSPESP QYLLSNSLTA DVLIWDLINF KSPPEKFQSS HQRLIFNITQ
IPNSDGSLAK TTATTETTTK NKIKNKDKKQ SQIKLNNKVI TVSLDRQIII WENLKAKIKI
QGLGGFVYSI DTCSYSPNTF AIGCGDNTIR LWSPTENSKD AYESKTLWKG IQSKVTSLSI
CKDYGFSNSN LIAFGMDDGR VGVYNINTNQ SKIFPGGHKN EIYEIIWKPP PTPTPQKNIN
NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNINNNN NNNSNNEQQP NKLYSIGNNE
IYEWDYNDFN KSFTNMTPII QQLNPKETFS KHKTDINFNL NGDMISIGYS DGTIDIFTSE
FLFLTRIREH KKLINRVQWN HFKENEMILA SASTDKKVII YKLSKIGNQN ENEKKIDNEK
GKENENEKGK ENENENENEN ENENENENEN EIENIVNNNN ENDTEIEIKN INKNENVDKE
EMVENNNNNN IKYKIEILHQ FIGHKNNVCS VSWSNVDPNL LGSASADGTV QVWNIKSKEA
ISNMRGHDGR VFTVCWSLLD PNLLVSGGED QTVRLWNYST QPFKTVTESQ IKKSPQPELS
ISLNKKITEQ QQQQQQPQSP IKSNPDQSNN PSLVPPILLT SVTSTSNTTA TATTITQITE
SLPKKRPIFL LNKDIVQRQD SSQYVVPLAK YFTTNDQDSI NTNETKQEYE FGSNSENNNS
KIEAIFSEKK EIINKLVQKE SLELLKIDDV ENYISLNSWN PANLKQALYQ VIKNGKLTGN
IVSLSIQAGR EIFESICNLY SQQLICIGDY HLAVSYLLMI GKVNEAIEVY RNTLLFQEAI
ILAKSRFLPD DPIINKLFTE WAKQTETSHP IHSIKCYLAT INDQSLNSKQ ELLKLLSSVQ
TKQIIKIQSD LEQILK
