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Database: UniProt
Entry: A0A120E8Q9_9BASI
LinkDB: A0A120E8Q9_9BASI
Original site: A0A120E8Q9_9BASI 
ID   A0A120E8Q9_9BASI        Unreviewed;      1105 AA.
AC   A0A120E8Q9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=KTI12-domain-containing protein {ECO:0000313|EMBL:KWU46053.1};
GN   ORFNames=RHOSPDRAFT_32533 {ECO:0000313|EMBL:KWU46053.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU46053.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU46053.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU46053.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
CC   -!- SIMILARITY: Belongs to the KTI12 family.
CC       {ECO:0000256|ARBA:ARBA00025768}.
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DR   EMBL; KQ954469; KWU46053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A120E8Q9; -.
DR   STRING; 1305733.A0A120E8Q9; -.
DR   OrthoDB; 375350at2759; -.
DR   Proteomes; UP000062823; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd12226; RRM_NOL8; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR013641; KTI12/PSTK.
DR   InterPro; IPR034138; NOP8_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR12435:SF2; PROTEIN KTI12 HOMOLOG; 1.
DR   PANTHER; PTHR12435; UNCHARACTERIZED; 1.
DR   Pfam; PF08433; KTI12; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00176}.
FT   DOMAIN          369..452
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          252..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          704..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          795..988
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1069..1105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..731
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..858
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        876..897
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1075..1089
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1105 AA;  117989 MW;  69B9D1A81941D87F CRC64;
     MAMVTLCGYP CSGKSTRAQQ LAAFLDRKLA DPSTPTHLQR ALRRVVVVND EGLSISKHAY
     DDARAEKPAR AALFSAVQRS LAKEAIVIVD AMNYIKGSRY QMYCEAREVG VRTCTVFVAT
     PPDQCRERNA LRPHSTAYAP ATLDNLISRF EEPQSAARWD APLFTIAADD PPFDEPAATS
     QTGGEAVPLG STEAERIWTA ITEGVIKPST VATQLATTSS TSYLTRLDSS SSALISSLLS
     LQSISPLSGP TTLSVPLSSP SSSSTITTQK KNAAADSSTT IRVTVDLNRP VTLPMLQRLK
     RQFIQLNART ASGTEFGEKE IVSLFAHEHA HLSFISVATT SRSTARLGKM GGKKASTAAA
     RSSTEPVTKR VHVGNLAPSV TAKDLVQRFS SFGTVIDGEH GVQGLGKTDT GTARAFAFFS
     LETTDAQFAR CMSMLNGSTW KAHKLRIGPA KPDWQSRLAA EREAAAAAAN EGNGSSAAGS
     GRPKKRRKRS KDPNVGVAAT HFELVDKDNI QRHRGWLLDP KPVPTPLFPI IIRPSHPVGP
     PPAAPTTAWS RAPTKAKPSK AARAAARLGG AGALERPSIT RAKRMRIDPR RWGRQKIVFD
     LMGAPEGKGH QQRGAAAGAG APNMHAIGTW ECEEPEEGAP RDQEQVTWVF KTRDGQVRRR
     ETVRLTQRTA HTDRFTTLLE RLHQSSSVPT TSTAPTQYVQ DDDSTAADAD DVTPTVNDSA
     APASATATRA RSLSPPPYVP VAPRTLIYNE EDEFQLVATA LNDDERALAH ARERAEYRKL
     ALSALAEIQD LDQVEVPSTD TTGEGAATAK PLPKVEGFAQ ADDEDDDEIF ETLRLRGGAG
     GEASDSSSDS SSEESSSDSD SSSDSDSDSD SDEASHQQAD TAGASSSSSS HAQQGPAALK
     ETLTALFKPG SAATGAAAPT AADGGGGFSL FADMDLDLDG EAEPADEGVA IPLAPPIDTV
     PVTRPLPSSL GLGPMRNTSR YGPQVSSGLG LGGPSKPFFL FPSGPFEDAN RPGEVDEVEV
     AKLGLPAVSL ERAKDESRRR IQDAPAKDFW RHDSQDEIDE NHLKMRETLR GVARKRHREA
     VKRTRKPGGT GRRGATSIPL DLLDE
//
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