ID A0A0V0U0N7_9BILA Unreviewed; 971 AA.
AC A0A0V0U0N7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=T-complex protein 1 subunit theta {ECO:0000256|ARBA:ARBA00016981};
DE AltName: Full=CCT-theta {ECO:0000256|ARBA:ARBA00029602};
GN Name=Tsr1 {ECO:0000313|EMBL:KRX44822.1};
GN ORFNames=T05_6701 {ECO:0000313|EMBL:KRX44822.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX44822.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX44822.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX44822.1};
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 -!- 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 -!- 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:KRX44822.1}.
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DR EMBL; JYDJ01000088; KRX44822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0U0N7; -.
DR Proteomes; UP000055048; 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; 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; PTHR11353; CHAPERONIN; 1.
DR PANTHER; PTHR11353:SF19; T-COMPLEX PROTEIN 1 SUBUNIT THETA; 1.
DR Pfam; PF08142; AARP2CN; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SMART; SM00785; AARP2CN; 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:UP000055048}.
FT DOMAIN 766..847
FT /note="AARP2CN"
FT /evidence="ECO:0000259|SMART:SM00785"
SQ SEQUENCE 971 AA; 107997 MW; 5638E9AA71D10B6E CRC64;
MHNNKKMAPG SMPRVGFARL LKDGVKHYRG VEESLFRNIE ACLGIAATVR SSFGPKGMNK
MVVNHLGKLY VTNDAAVILR ELEVEHPAAK LLVMACEMMD FQIGDGTNFV IILSASLLDS
AKELIRMGLN VSQIISGYNM ALAKALELLP KFVCKSVHSV RDDEAVKAVV RSSIATKVYG
QEDMLSDLVV QACTLALGAD YSTYHVDNIR ICKILGSNVE ASTVMNGMAF QDCVSGEIKL
IENPKVAVFS CAFAVTKLEN PSSIVINTAK ELMQFSKHDE EYIENYIKSL HNAGVNVVVS
GGKFGDLHLH YLNKYKMMAV KISSKFDLRR LCRCTHSTII PDMSRVPTPD MIGSCTKVQV
REIGSDQLVF FEQNLKGGSL STIIIRGSSQ NTLTEVEKAI DDGVNVFRQL LKDGRLLPGA
GAAELAIARE IRQFGLTYPS LERYAIEKFA IALESLPKQI ADNIGAKWVE IYPHLMKKHE
NGENNYGLDI KAPKGGILNA VSAEIFDCFS VKEWAIKLAV NAVNTIINVD QIVLAKPAGG
PPIRQPKSQE DDDTNFSQWK RIFLIDVVRG SSRTRSTILA DIEAKAAPNK KWIKTDWFIF
HWKIELQLRA QKVEKVKRNK NQYGSARSPP IAVVILSLSP IIDSNSVIGN ILACRPDATV
TSCDRNIYFL SSPNLKRRFC FLIPDHWNMI EVLDAFKVAD VAVLLWDCDT VTLHNHFSSL
LSAVSAQGMP YHFNISLNAK MSFNHDKKRL ASVVERWGLR PKFCRNYDLL LKLIANCAKQ
PLSLQQHHSR IIVESCSIVE QNDDLSVCTL KINGYVRGPP LDVNHLLHIP GWGDFQMDKI
DVITDPHPLH KYGKSHVIET CTFAVADPAK QENLESQATV DEMNVDQTWP TEEEIAQSQK
DTEHLIRRLP EGTSTYQACW ILDNGSDDDV SEPEQENECN TVLLNLDEDM DSLIAVSRAE
SVDQDGGGGN E
//
