ID A0A0V1PEI4_9BILA Unreviewed; 1537 AA.
AC A0A0V1PEI4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=T-complex protein 1 subunit eta {ECO:0000256|ARBA:ARBA00015836};
GN Name=CCT7 {ECO:0000313|EMBL:KRZ94657.1};
GN ORFNames=T08_6889 {ECO:0000313|EMBL:KRZ94657.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ94657.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ94657.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ94657.1};
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 -!- 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:KRZ94657.1}.
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DR EMBL; JYDM01000017; KRZ94657.1; -; Genomic_DNA.
DR STRING; 92180.A0A0V1PEI4; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
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:0070063; F:RNA polymerase binding; IEA:InterPro.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd03340; TCP1_eta; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.20.70.10; -; 3.
DR Gene3D; 1.10.10.440; FF domain; 6.
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; IPR012720; Chap_CCT_eta.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR InterPro; IPR045148; TCRG1-like.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR NCBIfam; TIGR02345; chap_CCT_eta; 1.
DR NCBIfam; NF041083; thermosome_beta; 1.
DR PANTHER; PTHR15377; TRANSCRIPTION ELONGATION REGULATOR 1; 1.
DR PANTHER; PTHR15377:SF3; WW DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR Pfam; PF01846; FF; 6.
DR Pfam; PF00397; WW; 2.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SMART; SM00441; FF; 6.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF81698; FF domain; 6.
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 SUPFAM; SSF51045; WW domain; 3.
DR PROSITE; PS51676; FF; 5.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00995; TCP1_3; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004187};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924}.
FT DOMAIN 48..81
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 154..181
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 262..289
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 391..444
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 456..511
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 768..824
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 826..882
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 883..949
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT REGION 95..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 441..470
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 97..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..729
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1537 AA; 174727 MW; C4A0805EBD651BCA CRC64;
MESFEVVENA EHNITADDAR LIGENDHNLS DAEVTKDNST PSAVLNPPNQ EEVWFEARAD
NGKMYYYNSI TRVSVWEKPI QGRIVTIDER QRMKNAETAH QLQQQQQQQQ QQQQQQQHQH
QQHLQHHALN NSQGNWYGGY SAMHPRINGP GTIWLEYFSP QGRPYYYNSM TGETTWDRPP
EMDVGASMKP ASEPIGAMVK NGAETLTSEV AKTVPEAFND GKPSSVQSSD SAPEATKTTV
QDSVKQDKPR PISSNPVAGC SWCVVWTSDM KVFFYNPDTR MSVWERPPEL YGRPDVDLLL
SHPPEPKKTE VKKEAPPSQS KASVAQSETV SQTSVPKKAK HSADAKAESE QPAKTKQKEK
QPQVKQPVNK PPDPAMEAEM KAAQERAQIP IEVRTKQFRE MLQEKQVSAF STWEKELHKI
VFDPRYLLLT SKERKATFEE FIKEKAENER AEKKRKLKEA KANFAELLQE ADITGKTMFS
EFASEYGNDS RFKALEKSRE RESLFDDFVR DIRNKEREEK HALRAKQKEA FFALLREQEG
ITRRSRWVDF KKELSSDARY IAIEKSSLRE DWFIDYCRDL PREDRSTDGK SAKRDHSRTK
ASGSKGDDAK DNKDRSKDTE SRNEKETSRA EERFMKEEAP KDKQHSKDKP LKDSSKQTEN
RKRKSESSSS VGLFLKHTNE ERIVDNKKVR MAYKEEEDND DHDDDDDDDD DDDEEEDDDD
GDEDEQEEEK ECRNAATVTR QEQSRTEERY EPDVKKNKLP LGEESDEEIS AEGHFKMLLV
DLVTTTDVTW EESKKRLRKD ERWKELSSLD RGQKEELFEE HLRELKRKYR TEYRQLLDQL
PQFNLSCTWK EIKKLIRNDN RYSQYSSSDR KCEREFNDYL MEKLQNAVDN FIELLKETKI
ITHRSKKMML ESEQHLTDIL SILENDERYL VLECVPSERE KVLERYLDQL EKAGTSKEIS
NFRLCDMRLN GDAGRRAREP VGQRSQVGSI IFRRTMSAPI ILFKPGTEHA KGKRHIVGNI
QACQAIADTI KTTLGPRGLD KMIVQSSGTT IISNDGATIL KALEVALPAA NVLVDLAKSQ
DAEIGDGTTT VVLLAAELLA MSKPFIDEGI HPQVIINAYR KASKYALQVV NDVAVDVKGE
SIEIGGKKGM SKKELLIKCA CTTLSSKLVA TQKQHFAELI VEAVMHLDDS MPLNMIGIKK
IRGGSVDESE LILGVAFKKT FSYAGFEMQP KTYVNPKIAL LNIELELKAE RENAEMQIKN
VQLIVDAEWQ ILYQKLEKLH ELGVNVVLSR LPIGDVATQW FADRDMFCAG RVEALDLERT
MAACGGSIIS TVSNITPDML GSCAMFQEKQ IGGDRYNIFT GEAKAKTCTF LIRGGAEQFM
EETERSIHDA IMIVRRALKN DKIVAVYFSS GGGAFEMEVC NRLRKVALEI KDRDQFFVAA
YAKAFEVIPR QLCFNAGMDS TKILNKLREL HAAGQPSAGI NLAESNVVDN IEAFVWEPAI
VKANAVAAAT EAACLILSVD ETIRTPSRSA NIPKGMQ
//
