ID H6BN84_EXODN Unreviewed; 1811 AA.
AC H6BN84;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=30S ribosomal protein S1 {ECO:0000313|EMBL:EHY53152.1};
GN ORFNames=HMPREF1120_01350 {ECO:0000313|EMBL:EHY53152.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY53152.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY53152.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY53152.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the cleavage factor IA (CFIA) complex, which is
CC involved in the endonucleolytic cleavage during polyadenylation-
CC dependent pre-mRNA 3'-end formation. {ECO:0000256|ARBA:ARBA00002863}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
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DR EMBL; JH226130; EHY53152.1; -; Genomic_DNA.
DR RefSeq; XP_009153613.1; XM_009155365.1.
DR STRING; 858893.H6BN84; -.
DR GeneID; 20305989; -.
DR VEuPathDB; FungiDB:HMPREF1120_01350; -.
DR eggNOG; KOG1070; Eukaryota.
DR HOGENOM; CLU_000845_0_0_1; -.
DR InParanoid; H6BN84; -.
DR OMA; GQYLRAY; -.
DR OrthoDB; 167902at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd05702; S1_Rrp5_repeat_hs11_sc8; 1.
DR CDD; cd05703; S1_Rrp5_repeat_hs12_sc9; 1.
DR CDD; cd05693; S1_Rrp5_repeat_hs1_sc1; 1.
DR CDD; cd05697; S1_Rrp5_repeat_hs5; 1.
DR CDD; cd05698; S1_Rrp5_repeat_hs6_sc5; 1.
DR CDD; cd05706; S1_Rrp5_repeat_sc10; 1.
DR CDD; cd05707; S1_Rrp5_repeat_sc11; 1.
DR CDD; cd05708; S1_Rrp5_repeat_sc12; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 10.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR045209; Rrp5.
DR InterPro; IPR048058; Rrp5_S1_rpt_hs11_sc8.
DR InterPro; IPR048059; Rrp5_S1_rpt_hs1_sc1.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR008847; Suf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR23270; PROGRAMMED CELL DEATH PROTEIN 11 PRE-RRNA PROCESSING PROTEIN RRP5; 1.
DR PANTHER; PTHR23270:SF10; PROTEIN RRP5 HOMOLOG; 1.
DR Pfam; PF00575; S1; 6.
DR Pfam; PF05843; Suf; 1.
DR Pfam; PF14559; TPR_19; 1.
DR SMART; SM00386; HAT; 7.
DR SMART; SM00316; S1; 12.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 12.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50126; S1; 12.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000313|EMBL:EHY53152.1};
KW Ribosomal protein {ECO:0000313|EMBL:EHY53152.1};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 154..257
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 273..342
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 456..530
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 547..621
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 641..710
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 729..803
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 825..896
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 934..1010
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 1042..1113
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 1129..1198
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 1223..1292
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 1312..1383
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REPEAT 1628..1661
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1464
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1811 AA; 198453 MW; DC30DD9D3D27A66A CRC64;
MASAKRKLTG DEASTKPATK RSKSDSKPKA EAASTSSAQD KKAKPNSVSV LAKEQPAFPR
GGAGVLTPLE RKQIQKKATR DAEREQKQGR DLFDEGSKSL HDTSDEEAPS DVDTEVKKPT
KRQRKKKARS KDAADTTEPE VRIEGLSYKR LTTGSLILGQ ITAVSSRTLT VALPNNLVGY
VPLTSISAQL SEKIQALLNE KDEEEDSNDS GDEDDDDIAL TNYFHVGQYL RVAVTSTEQD
NTAGKAPTKR RIELSVQPSL TNVGIGRANL ALGATVQVAV SSIEDHGLVA DLALEDQNVR
GFIPKSQLPA SLPLSSIKTG SVFLCSVIEL GSSGRVVKLS ADPSKWIPLA TAPSVDTFLP
GTKAEILVEN KTEVGLSGKS MGLVDATADL VHSGSFRDKE AFLAKYEAGK KIHGRLICTF
PLSETKKLGF SVLQHVLDME PTANMDGRPE GTPALSSIVD AAPVIRVEPG LGIYLQLSPN
TVGFAHVSRL SDDKVEMLSE TSGPFKLGSE HKARIIEYNP VDDLYLVSLQ KKVLEQSFLR
YEDVPLGAIV KATIEKLLVG PDGVRGLVVN LAEGISGLVP QIHLSDVELK HPERKFREGQ
TVTARVITTD PQKKRIRLTL KKTLVNSDQK PWLRYEDIES GDSTLGTLTK VDPLGAVVRF
YGPVRGFLPV SEMSEAYIKD ATEHFRVGQV VTVTAISVNP AERRLTVSCR DINKSNPSIE
SSLSSLEPGT IVKGTVFEKS QDDILLRLDG SDAIARLTKD HVSDGSSKKR ESAFNKIRVG
QKLEDVVVLQ VLPKRRLVMV SNKQSLIKAA QEGTLLKSYE QLQPNALVTG FVSNITSDGV
FVSFAGGISG LITKAQVPVE ATDERDFGMT KFQPVTAKVL SIDYKGATPR FWLTMRENPA
NTRPEPAAAA VQDVPALVNP VDTELKTIND LSVGRVTKAR IISVKDTQIN VELAKDVQGR
IDASEIFDEW KDIKDRKRPL KQFSPKQELT VKILGAHDTR NHRFLPLTHR NGKNTVFELS
CKPSTVAAPN NSILKLTDLS VGSSWLAFVN NISENGLWVN ISPSVRGRIR ATDVSDDLSL
AANLEKAFPI GSALKVHVLA VDPEKNRLDL TARSDGLASS LTIKDVSKGL VLPGRVTRVT
DRNILVQLSD QAVGAVDLID MADDYNEANP AKFQKNDILR VCVLKVDVPN KKIQLSTRPS
KVLSSSMKVT DPEITSISQL SVNDVVRGFI SNVSDKGVFV TLGHGVTAFV RVTHLSDSFL
KEWKDHFQRD QLVKGKIIMI DQASGHVQMS LKESALDPNY KAPLTFNDLH VGDIVTGKVV
KVEPFGVFIA VDNSENVRGL CHRSEIAEKR VEDATKLFKE GDAVKAKVLK LDPAQRKVNF
GMKASYFIDT VDDDAESEAD SDTESHVSGG AQLGEDEDED MQDADDSGEE EDASDSDDDE
DDPDNASEVD GETGESDDSE AEEQEVKDSA AASQGKGLNV GGFNWYGMPE APSTTGSKRA
AEESSSDEDA DTAAKVPKKK KKRAGIQVDR TGDLDVDGPQ SIDDFERLLM SEPDSSLLWL
QYMAFHLELG DADQARQIGE RALKSIGLGQ EAEKLNVWVA LLNLENAYGD DETIEAIFKR
ACEYNDPQEI YSRLTSIYIQ SGKHDKADEL FQRMLKKFAQ DPKVWINYAT FLFDRVGDAD
KARALLPRAL QTLPKFTHFD TTLKFAQLEF KSPNGLAERG RTIFEGLISS FPKRVDLFNV
LLDLELKQGD REQIRALFER VFSGRLKPKQ AKYFFKRWLA FEEAEGDERQ VEAVKARAAE
WIRAAGKDVD I
//
