ID A0A0K3CHY7_RHOTO Unreviewed; 1845 AA.
AC A0A0K3CHY7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=BY PROTMAP: gi|342321538|gb|EGU13471.1| Pirin domain-containing protein [Rhodotorula glutinis ATCC 204091] {ECO:0000313|EMBL:CTR08573.1};
GN Name=FGENESH: predicted gene_8.289 {ECO:0000313|EMBL:CTR08573.1};
GN ORFNames=BN2166_0044340 {ECO:0000313|EMBL:CTR08573.1};
OS Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR08573.1, ECO:0000313|Proteomes:UP000199069};
RN [1] {ECO:0000313|EMBL:CTR08573.1, ECO:0000313|Proteomes:UP000199069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Single colony {ECO:0000313|EMBL:CTR08573.1};
RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the RRN3 family.
CC {ECO:0000256|ARBA:ARBA00010098}.
CC -!- SIMILARITY: Belongs to the pirin family.
CC {ECO:0000256|RuleBase:RU003457}.
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DR EMBL; CWKI01000008; CTR08573.1; -; Genomic_DNA.
DR STRING; 5286.A0A0K3CHY7; -.
DR Proteomes; UP000199069; Unassembled WGS sequence.
DR GO; GO:0004518; F:nuclease activity; IEA:InterPro.
DR GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; IEA:InterPro.
DR GO; GO:0006361; P:transcription initiation at RNA polymerase I promoter; IEA:InterPro.
DR CDD; cd02910; cupin_Yhhw_N; 1.
DR CDD; cd09870; PIN_YEN1; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 2.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR003829; Pirin_N_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR007991; RNA_pol_I_trans_ini_fac_RRN3.
DR InterPro; IPR006086; XPG-I_dom.
DR PANTHER; PTHR12790:SF0; RNA POLYMERASE I-SPECIFIC TRANSCRIPTION INITIATION FACTOR RRN3-RELATED; 1.
DR PANTHER; PTHR12790; TRANSCRIPTION INITIATION FACTOR IA RRN3; 1.
DR Pfam; PF02678; Pirin; 1.
DR Pfam; PF05327; RRN3; 1.
DR Pfam; PF00867; XPG_I; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000199069}.
FT DOMAIN 126..239
FT /note="XPG-I"
FT /evidence="ECO:0000259|Pfam:PF00867"
FT DOMAIN 1586..1692
FT /note="Pirin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02678"
FT REGION 178..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1401..1422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..662
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1076
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1526
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1845 AA; 201723 MW; 813E384C1F66FAB2 CRC64;
MGVPKLWEEL EAGHRTTSWS QLVEPAFQRP GIRSLRVGVD TPLWLFHMGR MHTIVDPETG
LPQNVGPNAD LRMVFFRACD FLRRGILPIF VFDGPKRPSF KRDRNVGGNY RGRSENDLTR
LFALMGFEVR KAPGEAEAEL AAMQERGEID AVLTLQIIRN PSKTLSANHS KKYLERQASM
PAASQPGPSQ SQSSQAIEYM SVPPSHDKAV TTYSATDIAA DAGVDRNGMI LIALISGADY
DTKGSFRVGI TISAALARAG YGASLVEGVE RIRSSPAARD FPASAKAALD SFLTEWRESV
ANELRTNVNK LFSKRHLKVA DELEADSSFP RLDILDFYLS PVVSDPTLPS YVTPTWSRDV
NLEGLASYVI SKFEWSHVEV LARFRNLLWL GLAVQHIRRA ALAEDASTHL ARVLPEGFIA
LVESRKCAES TDFVPSYRVE LDPSVFNPHI AAALPGDDPF EFPDYTQLSQ EQIEAVKAVR
KAEGRAQEPP PSPRGATVFR HWVPVGVLEA CEEGREAVQT WRDLAGRKKR AKEDEERRKE
ERRRAREAGS SSPVKKGSPL KKLAFAESSG SMARRKPARM VAPPEDSSDS DEDVHETVSQ
EKQGLLAFSS TKPGTSSQST KATTVSPLFA GDSDSDVFLH SPPKPASKRP VPSPPPDRRD
TLSPPTSEPS DDDLYRSKHV SKATRTSSAK TSPSKTRKAK APPAVLELSS DSSPEKVKKK
ASPKKKKQDN GEGESLTDWL RWRKADKAAA EERRTAKMVA PSAPTAKATA HSRPKQIKRT
RMPPPASVAA APPQLSSVVK GKRPRPSDGV SDLEKEKPRR VKSLRGQKRS EATEGRSKEA
AAALAAGDGG GAYRRVMFAS FINQAFEKRY KGDNEEYNQI IGQFRALLPS ATASQTASTS
SGQPTVTPLT QLRAWLEALT SVVSKLDQSH APLVETILAV PWAVMEDAFV SAYMRFVGAI
VSARPEWLKG VLDKCVKGFK YHVLTLVVER ALNIDVEIQG EPEDWEDVEE EMMAAAEASE
GVEGKKRLVD GAVNDLVDRP VEEDPADSDS DSDDDDEEGG IDLDNLSSDD DEPDPVNDED
AAKRANGAKQ GMSEAAIRKV LDSRAKLDGI LKVILDHLAS AHADKRGLER NNTSTVQPPA
TPTTDVFDKA FAAAPVPAES GSREATPTAD DVLTADVVER RLNLFRTLLD IFDRTLLRTF
KTRNVQFVLF YLCSLDSAST DHFIGVLLGR ALFDQDAPPV TRVAAAGYVA SFIARAKYVD
AAMTRKVVRH LCGYLEGQME DYARTSALAT SIAGAKAPGG GSELPVFYAV AQAVFYIFCF
RWKDLLDEDD ADDEAALFGL DAGRRWMMGL ETVKKAVSSS FNPLKVCAQP VVNQFASIAH
KTGFMYCYAI LDSNRRANSY RDASAASTPT QPMPPPPLRS VSTSSLLNTL TAAQLHLSTP
SPSGTPGPPS IPATASRQLI VAEEMDSFFP FDPFKLPLSS AYIDGIYREW EGADDDESTT
SGDASSSVAD SDDDTGESDA TTGDEDEDEP AWVKTRGGLA VPGSGRPGAE DDDDEVSRTL
YTSLSPSTMS ASALKFIPRR SATRGWADHS WLKTYHTFNF ASYYDPNYES WGPLRVINED
RVDAGTGFGT HRHREFEIWS YIVDGELEHK DSLGNTEIMK RGDVQMTSTG TGIAHSEYNR
NTKQQVHFLQ IWALPNKSGL SPKYYNRHFT DEEKRDKLVK VVAPAGSEGC SDERNASGPT
PVHAALTMYA SILSPKSSLK HTLAPTTTKA LVHNIMRSGY RSPTTAASDK YEDGGAMVQL
NNGLILEEGD GAFVQVSKTS DGSREVEIKN VGERDAEFLV FEMED
//
