ID A0A0V1MMR3_9BILA Unreviewed; 1323 AA.
AC A0A0V1MMR3;
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:KRZ72882.1};
GN ORFNames=T10_11173 {ECO:0000313|EMBL:KRZ72882.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ72882.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ72882.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ72882.1};
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:KRZ72882.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDO01000071; KRZ72882.1; -; 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 778..859
FT /note="AARP2CN"
FT /evidence="ECO:0000259|SMART:SM00785"
FT DOMAIN 1018..1293
FT /note="Ribosome biogenesis protein BMS1/TSR1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01362"
FT REGION 557..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..996
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1323 AA; 149297 MW; CDB919EB3031F60D CRC64;
MNFRKSVGNF NTVWHLNLLK MAPGGIPRVG FARLLKDGAR HYRGVEESLF RNIEACLGIA
ATVRSSFGPK GMNKMVVNHL GKLYVTNDAA VILRELEVEH PAAKLLVMAS EMMDSQIGDG
TNSIMILSAS LLDSAKELIR MGLNVSQIIS GYNMASKKAL EVLPKFVCKS VNDVRDVEAV
KTVIRSAIAT KVYGQEDMLS DLVVQACIIA LGANYSTYHV DNVRTCKVLG SNVEASTVMN
GMAFQDCVSG EIKLIEKPKV AVYSCAFSVT KLENPSSIVI NTAKELMQFS KHDEEHIENY
IKSLHNVGIN VVVSGGKFGD LHLHFLNKYK MMAVKISSKF DIRRLCRCVQ ATIIPDMSRV
PTADMIGSCT KVQVREIGSD QLVFFEQNLK GGNLSTIIIR GSSQNVLGEV EKAVDDGVNT
FKQLLKDNRL LPGAGAVELA VAREIRQFGL TCPTLERYAI EKFAVALESL PKQIADNIGA
KWVEIYPHLM KKHQNGENNY GIDIKAPKGG IVNAVSAQIV DCFPVKEWAI KLAVNAVNTI
INVDQIVLAK PAGGPPIQSF SHRSGPWKQQ NKRHNPGRHR SRNSEQANAF QIDKNRLLQM
PMEDRCLMSR LARRNREWQL RAQKVEKVKR NKSEYGSFKS PPIAVVFLPL APRIIGEQVI
STILASQSDA VVTSCDRNIH FLSVPSMKKR FCFLIPDHRN VIEVLDAFKI ADVAVFLWDC
DAVKLHDQFA SLLTAVAAQG MPYHFNIPLT SRITYNYDKK RLSSLVERWG LRAKFCRDFA
LLLKLIANCA KQPLSLQQHH SRIIVECCSI VEQNDDLSSC TLKIDGYVRG PPLDVNRLLH
IPGWGDFQMG KIEVITDPHP LHRNGSNDVI ETTTFAVADP EKQENLESQA AVDEMNSDQI
WPTEEEIVQS QRDTEHLIRR LPEGTSSYQA CWILEDENEA NVSQLSQENE CNTIVFNLDE
DMDSLIAVSR AESVDDQESE VEMSEDDETE CSDENDVDEV ERCRREREER ENEKFPDEVD
TPLDISAAER FQKYRGLASF RTSYWNAEEE LPPEYGRIFQ FQNFKATYKR IAGWFTSVHV
LNVPLKLVEE CKKLKKEPLV AYELLPHEQK MSVVNVTIRK NHLFNETVKS KDRLLFQIGY
RRFFAAPIFS QHTIGDKHKF QRFLPADEVT VASMYAPIIF GPAGVVVLKV EQDGSTRLVA
TGNVLSVDPT RLNIKRAVLS GVPSKINRTH AVIRHMFFNR DDVLWFKPVE LRTSSGRRGH
IKEPLGTHGR MKCVFNGQLT SQDVVFMDLY KRVFPKWIYD PDVTIQLRKF KEEKERDELM
ESD
//
