ID A0A0V1MNF9_9BILA Unreviewed; 1316 AA.
AC A0A0V1MNF9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Pre-rRNA-processing protein TSR1 homolog {ECO:0000256|ARBA:ARBA00040070};
DE AltName: Full=CCT-theta {ECO:0000256|ARBA:ARBA00029602};
DE AltName: Full=T-complex protein 1 subunit theta {ECO:0000256|ARBA:ARBA00016981};
GN Name=cct-8 {ECO:0000313|EMBL:KRZ72878.1};
GN ORFNames=T10_11173 {ECO:0000313|EMBL:KRZ72878.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ72878.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ72878.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ72878.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required during maturation of the 40S ribosomal subunit in
CC the nucleolus. {ECO:0000256|ARBA:ARBA00037087}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC {ECO:0000256|ARBA:ARBA00008020, ECO:0000256|RuleBase:RU004187}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Bms1-like GTPase family. TSR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00038288}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ72878.1}.
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DR EMBL; JYDO01000071; KRZ72878.1; -; Genomic_DNA.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro.
DR CDD; cd03341; TCP1_theta; 1.
DR Gene3D; 3.50.7.10; GroEL; 1.
DR Gene3D; 1.10.560.10; GroEL-like equatorial domain; 1.
DR Gene3D; 3.30.260.10; TCP-1-like chaperonin intermediate domain; 1.
DR InterPro; IPR012948; AARP2CN.
DR InterPro; IPR039761; Bms1/Tsr1.
DR InterPro; IPR007034; BMS1_TSR1_C.
DR InterPro; IPR012721; Chap_CCT_theta.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR NCBIfam; TIGR02346; chap_CCT_theta; 1.
DR PANTHER; PTHR12858:SF1; PRE-RRNA-PROCESSING PROTEIN TSR1 HOMOLOG; 1.
DR PANTHER; PTHR12858; RIBOSOME BIOGENESIS PROTEIN; 1.
DR Pfam; PF08142; AARP2CN; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF04950; RIBIOP_C; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SMART; SM00785; AARP2CN; 1.
DR SMART; SM01362; DUF663; 1.
DR SUPFAM; SSF52029; GroEL apical domain-like; 1.
DR SUPFAM; SSF48592; GroEL equatorial domain-like; 1.
DR SUPFAM; SSF54849; GroEL-intermediate domain like; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004187};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004187};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843}.
FT DOMAIN 762..843
FT /note="AARP2CN"
FT /evidence="ECO:0000259|SMART:SM00785"
FT DOMAIN 1002..1286
FT /note="Ribosome biogenesis protein BMS1/TSR1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01362"
FT REGION 541..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..980
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1316 AA; 148387 MW; 1D1470960D0963D8 CRC64;
MNFRKSVGNF NTVWHLNLLK MAPGGIPRVG FARLLKDGAR HYRGVEESLF RNIEACLGIA
ATVRSSFGPK GMNKMVVNHL GKLYVTNDAA VILRELEVEH PAAKLLVMAS EMMDSQIGDG
TNSIMILSAS LLDSAKELIR MGLNVSQIIS GYNMASKKAL EVLPKFVCKS VNDVRDVEAV
KTVIRSAIAT KVYGQEDMLS DLVVQACIIA LGANYSTYHV DNGSNVEAST VMNGMAFQDC
VSGEIKLIEK PKVAVYSCAF SVTKLENPSS IVINTAKELM QFSKHDEEHI ENYIKSLHNV
GINVVVSGGK FGDLHLHFLN KYKMMAVKIS SKFDIRRLCR CVQATIIPDM SRVPTADMIG
SCTKVQVREI GSDQLVFFEQ NLKGGNLSTI IIRGSSQNVL GEVEKAVDDG DNRLLPGAGA
VELAVAREIR QFGLTCPTLE RYAIEKFAVA LESLPKQIAD NIGAKWVEIY PHLMKKHQNG
ENNYGIDIKA PKGGIVNAVS AQIVDCFPVK EWAIKLAVNA VNTIINVDQI VLAKPAGGPP
IQSFSHRSGP WKQQNKRHNP GRHRSRNSEQ ANAFQIDKNR LLQMPMEDRC LMSRLARRNR
EWQLRAQKVE KVKRNKSEYG SFKSPPIAVV FLPLAPRIIG EQVISTILAS QSDAVVTSCD
RNIHFLSVPS MKKRFCFLIP DHRNVIEVLD AFKIADVAVF LWDCDAVKLH DQFASLLTAV
AAQGMPYHFN IPLTSRITYN YDKKRLSSLV ERWGLRAKFC RDFALLLKLI ANCAKQPLSL
QQHHSRIIVE CCSIVEQNDD LSSCTLKIDG YVRGPPLDVN RLLHIPGWGD FQMGKIEVIT
DPHPLHRNGS NDVIETTTFA VADPEKQENL ESQAAVDEMN SDQIWPTEEE IVQSQRDTEH
LIRRLPEGTS SYQACWILED ENEANVSQLS QENECNTIVF NLDEDMDSLI AVSRAESVDD
QESEVEMSED DETECSDEND VDEVERCRRE REERENEKFP DEVDTPLDIS AAERFQKYRG
LASFRTSYWN AEEELPPEYG RIFQFQNFKA TYKRIVNEEK HGAPAGWFTS VHVLNVPLKL
VEECKKLKKE PLVAYELLPH EQKMSVVNVT IRKNHLFNET VKSKDRLLFQ IGYRRFFAAP
IFSQHTIGDK HKFQRFLPAD EVTVASMYAP IIFGPAGVVV LKVEQDGSTR LVATGNVLSV
DPTRLNIKRA VLSGVPSKIN RTHAVIRHMF FNRDDVLWFK PVELRTSSGR RGHIKEPLGT
HGRMKCVFNG QLTSQDVVFM DLYKRVFPKW IYDPDVTIQL RKFKEEKERD ELMESD
//
