SKB1_SCHPO
ID SKB1_SCHPO Reviewed; 645 AA.
AC P78963; O42946;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein arginine N-methyltransferase skb1 {ECO:0000303|PubMed:11278267};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P38274};
DE AltName: Full=Shk1 kinase-binding protein 1 {ECO:0000303|PubMed:8943016};
DE AltName: Full=Type II protein arginine N-methyltransferase {ECO:0000250|UniProtKB:P38274};
DE Short=Type II PRMT {ECO:0000250|UniProtKB:P38274};
GN Name=skb1 {ECO:0000303|PubMed:8943016};
GN Synonyms=rmt5 {ECO:0000312|PomBase:SPBC16H5.11c};
GN ORFNames=SPBC16H5.11c {ECO:0000312|PomBase:SPBC16H5.11c};
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 [GENOMIC DNA], AND SUBUNIT.
RX PubMed=8943016; DOI=10.1073/pnas.93.24.13802;
RA Gilbreth M., Yang P., Wang D., Frost J., Polverino A., Cobb M.H.,
RA Marcus S.;
RT "The highly conserved skb1 gene encodes a protein that interacts with Shk1,
RT a fission yeast Ste20/PAK homolog.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13802-13807(1996).
RN [2]
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 [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11278267; DOI=10.1074/jbc.c100096200;
RA Bao S., Qyang Y., Yang P., Kim H., Du H., Bartholomeusz G., Henkel J.,
RA Pimental R.A., Verde F., Marcus S.;
RT "The highly conserved protein methyltransferase, Skb1, is a mediator of
RT hyperosmotic stress response in the fission yeast Schizosaccharomyces
RT pombe.";
RL J. Biol. Chem. 276:14549-14552(2001).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-arginine N-
CC methyltransferase that can catalyze both the mono- and symmetric (type
CC II) dimethylation of the guanidino nitrogens of arginine residues in
CC target proteins (By similarity). Positively modulates the shk1 kinase
CC function. May be a mediator of hyperosmotic stress response
CC (PubMed:11278267). {ECO:0000250|UniProtKB:P38274,
CC ECO:0000269|PubMed:11278267}.
CC -!- SUBUNIT: Interacts with the N-terminal regulatory domain of shk1. Shk1,
CC cdc42 and skb1 are able to form a ternary complex in vivo.
CC {ECO:0000269|PubMed:8943016}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11278267}.
CC Note=Localizes to cell ends, sites of septation, and nuclei.
CC {ECO:0000269|PubMed:11278267}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR EMBL; U59684; AAC49571.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA17909.1; -; Genomic_DNA.
DR PIR; T39614; T39614.
DR PIR; T48644; T48644.
DR RefSeq; NP_595936.1; NM_001021844.2.
DR AlphaFoldDB; P78963; -.
DR SMR; P78963; -.
DR BioGRID; 276637; 39.
DR IntAct; P78963; 1.
DR STRING; 4896.SPBC16H5.11c.1; -.
DR MaxQB; P78963; -.
DR PaxDb; P78963; -.
DR EnsemblFungi; SPBC16H5.11c.1; SPBC16H5.11c.1:pep; SPBC16H5.11c.
DR GeneID; 2540099; -.
DR KEGG; spo:SPBC16H5.11c; -.
DR PomBase; SPBC16H5.11c; skb1.
DR VEuPathDB; FungiDB:SPBC16H5.11c; -.
DR eggNOG; KOG0822; Eukaryota.
DR HOGENOM; CLU_010247_0_0_1; -.
DR InParanoid; P78963; -.
DR OMA; IKYAWYE; -.
DR PhylomeDB; P78963; -.
DR Reactome; R-SPO-3214858; RMTs methylate histone arginines.
DR PRO; PR:P78963; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0071521; C:Cdc42 GTPase complex; IPI:PomBase.
DR GO; GO:0005938; C:cell cortex; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990463; C:lateral cortical node; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:PomBase.
DR GO; GO:0061246; P:establishment or maintenance of bipolar cell polarity regulating cell shape; IGI:PomBase.
DR GO; GO:0034969; P:histone arginine methylation; IBA:GO_Central.
DR GO; GO:1903359; P:lateral cortical node assembly; IMP:PomBase.
DR GO; GO:0035246; P:peptidyl-arginine N-methylation; IEA:InterPro.
DR GO; GO:1903360; P:protein localization to lateral cortical node; IMP:PomBase.
DR GO; GO:2000100; P:regulation of establishment or maintenance of bipolar cell polarity regulating cell shape; IGI:PomBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR007857; Arg_MeTrfase_PRMT5.
DR InterPro; IPR035075; PRMT5.
DR InterPro; IPR035248; PRMT5_C.
DR InterPro; IPR035247; PRMT5_TIM.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10738; PTHR10738; 1.
DR Pfam; PF05185; PRMT5; 1.
DR Pfam; PF17286; PRMT5_C; 1.
DR Pfam; PF17285; PRMT5_TIM; 1.
DR PIRSF; PIRSF015894; Skb1_MeTrfase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..645
FT /note="Protein arginine N-methyltransferase skb1"
FT /id="PRO_0000212346"
FT DOMAIN 300..608
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 422
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT ACT_SITE 431
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 316
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 325..326
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 379
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 406..407
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT SITE 319
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000250|UniProtKB:P46580"
FT CONFLICT 45
FT /note="F -> L (in Ref. 1; AAC49571)"
FT /evidence="ECO:0000305"
FT CONFLICT 134..138
FT /note="PTSPM -> SNFTQC (in Ref. 1; AAC49571)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="A -> G (in Ref. 1; AAC49571)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="G -> A (in Ref. 1; AAC49571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 645 AA; 73167 MW; 288FEE7BDF61558D CRC64;
MLLRDGRIPQ YSIYPLPVPP MNSKTPTLGI VCSEGTISLS LEEGFEFVGV PLSGEGLKLR
VEALAPSERL QEFLDDEVAY HPEENVHKVV GLSSAWLELD SEDTLIADRS EEVLLKEASY
ASYCGLSSII LNGPTSPMNV MRYARAVSSA LNSTMNLKFL VQLAIESGHE DYFETWKMWD
TIRSACGYHP RLKVALELPP ACSPPIELVN RWYAEPIEMI TMSCMAFVPN PNGYPVLGRK
LRAIYALYLR LNPRILLWDN DAPEKIGDSP DYSIYMKHLF DSQPPAPLVE DLADSYKDYL
QVPLQPLSYN LENITYEIFE RDPVKYAQYE QAIFSALMDR DESSVTRIAV VGAGRGPLVD
CALRAAISSS RTVDMIALEK NPNAFSMLLM RNRQDWAGKV TLVFGDMRTW NPDYKIDILV
SELLGSMGDN ELSPECLDGV QHVLDEETGI CIPSSYISYV TPIMSPKLWS EARNMNDPNA
FERQYVVLMN SFDFLAADDE FRFQSLWSFH HPNKDSEVYT KNLHNKRFAS VRFQASSPGI
LHGFAGYFEA TLYKDISLSI MPATMEAKSP DMFSWFPIYM PIKKPMYVPE NSQLEFHMWR
LTDGMRVWFE WCANAYLVLR NGSQIKLSST EVHNISGKAF SCNMY
