ID D9T577_MICAI Unreviewed; 494 AA.
AC D9T577;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=RNA binding S1 domain protein {ECO:0000313|EMBL:ADL47887.1};
GN OrderedLocusNames=Micau_4374 {ECO:0000313|EMBL:ADL47887.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL47887.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL47887.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000256|ARBA:ARBA00006767}.
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DR EMBL; CP002162; ADL47887.1; -; Genomic_DNA.
DR AlphaFoldDB; D9T577; -.
DR STRING; 644283.Micau_4374; -.
DR KEGG; mau:Micau_4374; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_4_1_11; -.
DR Proteomes; UP000001908; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd05687; S1_RPS1_repeat_ec1_hs1; 1.
DR CDD; cd04465; S1_RPS1_repeat_ec2_hs2; 1.
DR CDD; cd05688; S1_RPS1_repeat_ec3; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 4.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR035104; Ribosomal_protein_S1-like.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR10724; 30S RIBOSOMAL PROTEIN S1; 1.
DR PANTHER; PTHR10724:SF13; 30S RIBOSOMAL PROTEIN S1; 1.
DR Pfam; PF00575; S1; 4.
DR PRINTS; PR00681; RIBOSOMALS1.
DR SMART; SM00316; S1; 4.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR PROSITE; PS50126; S1; 4.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001908}.
FT DOMAIN 39..108
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 126..191
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 212..280
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 297..366
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 431..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 54839 MW; DEA45E13B3A0CF94 CRC64;
MTSSIEATSS ANKVTHDDLG SEEAFLAAID ETIKYFNDGD IVEGTVVKVD RDEVLLDIGY
KTEGVIPSRE LSIKHDVDPA EVVSVGDHIE ALVLQKEDKE GRLILSKKRA QYERAWGTIE
KIKDEDGVVR GSVIEVVKGG LILDIGLRGF LPASLVEMRR VRDLQPYVGR ELEAKIIELD
KNRNNVVLSR RAWLEQTQSE VRTEFLNKLQ KGQVRKGVVS SIVNFGAFVD LGGVDGLVHV
SELSWKHIDH PSEVVEVGQE VEVEVLDVDL DRERVSLSLK ATQEDPWRQF ARTHAIQQIV
PGKVTKLVPF GAFVRVDDGI EGLVHISELA ERHVEIPEQV VQVGSEVMVK VIDIDLERRR
ISLSLKQANE GFVEGEEHFD PTLYGMAATY DDQGNYIYPE GFDPETGEWL EGYDKQRETW
EQQYAEARQR WEAHTKQVQT SRAADAEAAA NPAPATTGTT TSTSAPSRQA EEPAGTLATD
EALAALREKL AGGK
//
