ID A0A136IZ25_9PEZI Unreviewed; 1156 AA.
AC A0A136IZ25;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ribosomal protein S2, flavodoxin-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Micbo1qcDRAFT_149042 {ECO:0000313|EMBL:KXJ90181.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ90181.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000256|ARBA:ARBA00006242}.
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DR EMBL; KQ964253; KXJ90181.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136IZ25; -.
DR STRING; 196109.A0A136IZ25; -.
DR InParanoid; A0A136IZ25; -.
DR OrthoDB; 1328303at2759; -.
DR Proteomes; UP000070501; 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; PTHR13780; AMP-ACTIVATED PROTEIN KINASE, GAMMA REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR13780:SF125; MEIOTICALLY UP-REGULATED GENE 70 PROTEIN; 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:UP000070501};
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 98..157
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 165..221
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 268..326
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 334..391
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 471..572
FT /note="PB1"
FT /evidence="ECO:0000259|PROSITE:PS51745"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1156 AA; 124323 MW; 1582CE4C61460575 CRC64;
MSGTMRGTPK GRGNMPFNNT PSSPAGGSGI PRPVLETQAS HQPPPSEAPS GVSASRQKQS
KRDEAIRRKL ESDLSKKKGL TNRARHSRKA PPGTVLALKP SPALQIKPST TVSEAAQLMA
AKREDCVLVT DDDDRIAGIF TAKDLAFRVV GAGHKASNIT IAEIMTKNPL CARTDTSATD
ALDLMVRKGF RHLPVMDENQ DISGILDITK CFYDAMEKLE RAYASSTKLY AALEGVQSEL
GTSQPQQIIQ YVEALRSKMS GPTLESVLNG MPPTTVSVRT SVKEAAMLMK ENHTTAVLVQ
DQGQITGIFT SKDVVLRVIA PGLDPSNCSV VRVMTPHPDF APMDMSIQAA LRKMHDGHYL
NLPVMNDSGE IVGMVDVLKL TYATLEQINT MGNGDSEGPA WNKFWLSLDN ETESMVSGDG
SHHHTMASRS LMSPDHGRDR IGDSVAPGDS ASHVGEGSML EPLTPDVPPA DVPFAFKFKA
PSGRVHRFQV TASQGIEQFV ASVAAKLGKE AEALGGTPTV EDGSLSISGF AMSYLDDEGD
TVSITTDEDL LEAIMLARHS HREKVDLFVH DPAQPPVTVT APQPDVLPTP PGSTAASAAR
RRRGIVEESD EDDSDDDEDL STVRRRRRGN HHAEPEQVIA GIPNELLLPG AVAALAVVII
GVFSISRLSS NRNATLLRIH IMIIREMGVR QARRALAAPL RQATSQVSTS RCVRALSTET
TTTPSQTSTD ASQPPSLFIR TAKPYSKNKK SNVPDNTAAE FRKAQNLKSY IGRAGAVTEK
IYHPDDIFRN PPGPADISLE LLMAAQVHMG HNTSLWNPAN ARYIFGIREG IHIISLEQTA
SHLRRAASIV DGVAYAGGNI LFVGNRPGQT RMVVQAARMA KGFHLFTKWP AGAITNSDVL
LRGLPVHMMD EHDQVIESLN YHNMEAQPIK PDLVVCLNPL ENYVLLHECA LANIPTIGVI
DTNAEPTWVT YPIPANDDSL RSVGTIASIL GRAGQEGNKR RLQAAKAGRV TWETPSPVSG
YIKKEAKRAQ ELAEKKAIQA QLLHEAAALG SPTSSSSASS FAPSNTITSS TATAAATPEP
TATSTTTQAQ GKPEDQFVDP KSRGSVLQQE LMDKEAAEAV AEVKRANPEM DEVQVVDETT
GEVMQKGEGS GKNESS
//
