YG58_SCHPO
ID YG58_SCHPO Reviewed; 661 AA.
AC O60059;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Pumilio domain-containing protein C56F2.08c;
GN ORFNames=SPBC56F2.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; THR-104; SER-105;
RP SER-482; SER-486; SER-488 AND SER-490, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329671; CAA18887.1; -; Genomic_DNA.
DR PIR; T40536; T40536.
DR RefSeq; NP_596709.1; NM_001022634.2.
DR PDB; 6NWW; X-ray; 2.06 A; A/B/C/D=1-79.
DR PDB; 6NX5; X-ray; 1.55 A; A/B/C/D=1-79.
DR PDB; 6NY5; X-ray; 3.00 A; A/B=109-485.
DR PDBsum; 6NWW; -.
DR PDBsum; 6NX5; -.
DR PDBsum; 6NY5; -.
DR AlphaFoldDB; O60059; -.
DR SMR; O60059; -.
DR BioGRID; 277429; 184.
DR STRING; 4896.SPBC56F2.08c.1; -.
DR iPTMnet; O60059; -.
DR MaxQB; O60059; -.
DR PaxDb; O60059; -.
DR PRIDE; O60059; -.
DR EnsemblFungi; SPBC56F2.08c.1; SPBC56F2.08c.1:pep; SPBC56F2.08c.
DR GeneID; 2540913; -.
DR KEGG; spo:SPBC56F2.08c; -.
DR PomBase; SPBC56F2.08c; -.
DR VEuPathDB; FungiDB:SPBC56F2.08c; -.
DR eggNOG; KOG4574; Eukaryota.
DR HOGENOM; CLU_415129_0_0_1; -.
DR InParanoid; O60059; -.
DR OMA; MARHCCE; -.
DR PhylomeDB; O60059; -.
DR PRO; PR:O60059; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; EXP:PomBase.
DR GO; GO:0000932; C:P-body; EXP:PomBase.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:PomBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:PomBase.
DR CDD; cd12340; RBD_RRM1_NPL3; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR034166; Npl3_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR033133; PUM-HD.
DR InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00806; PUF; 3.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00025; Pumilio; 5.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50302; PUM; 4.
DR PROSITE; PS50303; PUM_HD; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..661
FT /note="Pumilio domain-containing protein C56F2.08c"
FT /id="PRO_0000310365"
FT DOMAIN 1..74
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 129..482
FT /note="PUM-HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00318"
FT REPEAT 191..226
FT /note="Pumilio 1"
FT REPEAT 227..263
FT /note="Pumilio 2"
FT REPEAT 264..302
FT /note="Pumilio 3"
FT REPEAT 374..410
FT /note="Pumilio 4"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT STRAND 1..5
FT /evidence="ECO:0007829|PDB:6NX5"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:6NX5"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:6NWW"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:6NX5"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6NWW"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:6NX5"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:6NX5"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:6NWW"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:6NX5"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 131..143
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:6NY5"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 255..265
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:6NY5"
FT TURN 290..293
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 328..339
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 349..359
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 367..375
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 379..382
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 388..397
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 402..413
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 419..426
FT /evidence="ECO:0007829|PDB:6NY5"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 431..439
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 447..463
FT /evidence="ECO:0007829|PDB:6NY5"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:6NY5"
FT HELIX 472..476
FT /evidence="ECO:0007829|PDB:6NY5"
SQ SEQUENCE 661 AA; 72822 MW; ACA0E4E4127ACBCC CRC64;
MLYVSNLPVG TSSSAIHALF SAYGNVKDIW MLSPDNSAIV SYESLSSAIV ARDALHNRPV
FENHGPVQVM LAKPSSNYEP GNITAAVSPP ASTSSKDGVV CSPTSTGASQ LLKSRVDILE
VARQFEMRIN LDIVDSMIAS AIENNKVATE ILPPVETLRS RQFEASKLRE IRKNIDSGFY
TQEEIEVIAR SMLDDVAELS SDYLGNTVVQ KFFEYCSDPI KEAMLERIAP YLAAIGIHKN
GTWAAQKIID VASTEKQMDL IVKHLRPYTA LLYFDQFGNY VAQCCLRFKY PKNTFLFEVM
ARHCCEIGQS RFGARAIRAC LENENATFEQ QALVVASIII NSHLLATNSN GMLLLTWLLD
NSFFRNRHRL LAIHLATHLH TTCTHKLAST LIFKLINNKQ EPESRNLLLK NLFFSEKDNV
LTYILQDQAV GPSFIHKVIT YPSIGREFLA QFHLVIKRVL INIHAQPNAV YCRLMEEVGM
TSKSISPSLS GISAPSASVD SSASRLARDF GSLSLSSNSL LGSLGGLEST PAYPSYPSHI
PLGTASLPLK GNLYQISRSD DIKSGAPVLD TSSLVNPTLA KSASLNNSSL LNPSSSLLRR
EVPAGKLTMP AYPYTTQLMN HTAGADYGLP RLSSKLPQVF PGNYPRLQQS LFPRQGELRF
N
