ID G4UWA6_NEUT9 Unreviewed; 1132 AA.
AC G4UWA6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Ribosomal protein S2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=NEUTE2DRAFT_159933 {ECO:0000313|EMBL:EGZ69470.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ69470.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ69470.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000256|ARBA:ARBA00006242}.
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DR EMBL; GL891258; EGZ69470.1; -; Genomic_DNA.
DR AlphaFoldDB; G4UWA6; -.
DR STRING; 510952.G4UWA6; -.
DR eggNOG; ENOG502QVK2; Eukaryota.
DR HOGENOM; CLU_009026_0_0_1; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd17781; CBS_pair_MUG70_1; 1.
DR CDD; cd17782; CBS_pair_MUG70_2; 1.
DR CDD; cd06409; PB1_MUG70; 1.
DR CDD; cd01425; RPS2; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
DR HAMAP; MF_00291_B; Ribosomal_S2_B; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR001865; Ribosomal_uS2.
DR InterPro; IPR005706; Ribosomal_uS2_bac/mit/plastid.
DR InterPro; IPR018130; Ribosomal_uS2_CS.
DR InterPro; IPR023591; Ribosomal_uS2_flav_dom_sf.
DR PANTHER; PTHR12534:SF0; 28S RIBOSOMAL PROTEIN S2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12534; 30S RIBOSOMAL PROTEIN S2 PROKARYOTIC AND ORGANELLAR; 1.
DR Pfam; PF00571; CBS; 4.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00318; Ribosomal_S2; 1.
DR PRINTS; PR00395; RIBOSOMALS2.
DR SMART; SM00116; CBS; 4.
DR SMART; SM00666; PB1; 1.
DR SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 2.
DR SUPFAM; SSF52313; Ribosomal protein S2; 1.
DR PROSITE; PS51371; CBS; 4.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 106..164
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 173..229
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 276..333
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 342..399
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 485..585
FT /note="PB1"
FT /evidence="ECO:0000259|PROSITE:PS51745"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1132 AA; 122648 MW; CFCBDD11FD907207 CRC64;
MSTHPGSTAR GPSRAGGSIA QPQNRSATPY GQNHAGSAIP RPVLETNHAA TGSEVGSASV
SVSRQKQSKR DEAIRRKMES DLSKKKHLTS RARHTRKAPP GTVLALKPSP ALQIKAATTV
SEAAQLMAAK REDCVLVTDD DERIAGIFTA KDLAFRVVGG GLKANTVTIA EIMTKNPLCA
RTDTSATDAL DLMVRKGFRH LPVMDENQDI SGILDITKCF YDAMEKLERA YASSRRLYDA
LEGVQSELGT SQPQQIIQYV EALRSKMSGP TLESVLNGIP PTTVSVRTSV KEAAQLMKEN
HTTAVLVQDQ GAITGIFTSK DVVLRVIAPG LDPATCSVVR VMTPHPDFAP MDMTIQAALR
KMHDGHYLNL PVMNDAGEIV GMVDVLKLTY ATLEQINTMG SGTDNEGPAW NKFWLSLDHE
TESMVSGDGS LHHTHHGPRS LMSPDIARSE RIVDSVAPGD SASHAGVESP SHSQLGGIQE
VNPADIPFPF KFKAPSGRVH RLQVTASHGM AEFVAAVAAK LGAEVDAIGG TPEVENGRLS
GGFALSYLDD EGDSVSITTD QDLLEAILLA RHGLREKVDL FVHDPSEPAI SHAPTPAPVI
ETIPATPPAS SVVRERRKKV EEESEEVSEE EEPVHRRPTR TRTMSQPQEQ PRVIAGVPNE
LLLPGAIVTL AVVIVSVFTV SRLTSSPADS QRLPDDDVSD PSISTMIVRN IGARLGRRAL
ATPLSRASFQ AQSRFLSQDN FTAPPPPTNT KKQAAKTAFA EPTLEEQAEF YAESIEKPTP
EFAASPAAEA WSAPSATATE TVTTWDPSLV DEEALKLKQQ IEAIPGNFKL FKQTKAQTQK
LGAGVEVRYI PEQYLRNPPS DASLEDLMAA QAHMGHNTSL WNPANARYIY GVRQGIHIIS
LETTATHLRR AARVVEEVAY RGGLILFVGT RPGQRPIVVR AAELAKACHL FTKWRPGTIT
NREQLLGGVP LTVVDELDRP LSGFEDHLHD RRPLAPDLVV CLNPKENMTL LYECSLAKIP
TIGIIDTNTN PSWVTYQIPA NDDSLRATAL ISGVLGRAGE RGQKRRLEAA QRGVVTWKTP
ADVQGYFELA SARAADARRR QAQDNSVEEQ KEKDTFLSED ALKAMFGGDA RV
//
