ID A0A0V1AD47_9BILA Unreviewed; 1531 AA.
AC A0A0V1AD47;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=T-complex protein 1 subunit eta {ECO:0000256|ARBA:ARBA00015836};
GN Name=CCT7 {ECO:0000313|EMBL:KRY22612.1};
GN ORFNames=T12_14462 {ECO:0000313|EMBL:KRY22612.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY22612.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY22612.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY22612.1};
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:KRY22612.1}.
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DR EMBL; JYDQ01000008; KRY22612.1; -; Genomic_DNA.
DR STRING; 990121.A0A0V1AD47; -.
DR Proteomes; UP000054783; 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; NF041082; thermosome_alpha; 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; SSF81995; beta-sandwich domain of Sec23/24; 1.
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:UP000054783}.
FT DOMAIN 54..81
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 159..186
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 267..294
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 396..449
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 461..516
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 764..820
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 822..878
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 879..945
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT REGION 93..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 446..475
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 97..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..725
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1531 AA; 174171 MW; 567AE0120C2B988A CRC64;
MESFEVVENA EHNITADDAR LIGENDHNLS DAEVTKDNST PAAVLNPPNQ DEVWFEARAD
NGKMYYYNSI TRVSVWEKPI QGRIVTIDER QRMKNAETAH QQQQQQQQQQ QQQQQQQQQQ
QQHQHQQHLQ HHALNNSQGN WYGGYSAMHP RINGPGTIWL EYFSPQGRPY YYNSMTGETT
WDRPPEMDVG ASMKPASEPI GAMVKNGAET LTSEVAKTVP EAFNDGKPSS VQSSDSAPEA
TKTTVQDSVK QDKPRPISSN PVAGCSWCVV WTSDMKVFFY NPDTRMSVWE RPPELYGRPD
VDLLLSHPPE PKKTEVKKEA PPSQSKASVA QSETVSQTSV PKKAKHTADA KAESEQPAKT
KQKEKQPQVK QPVNKPPDPA MEAEMKAAQE RAQIPIEVRT KQFREMLQEK QVSAFSTWEK
ELHKIVFDPR YLLLTSKERK ATFEEFIKEK AENERAEKKR KLKEAKANFA ELLQEADITG
KTMFSEFASE YGNDSRFKAL EKSRERESLF DDFVRDIRNK EREEKHALRA KQKEAFFALL
REQEGITRRS RWVDFKKELS SDARYIAVEK SSLREDWFID YCRDLPREDR PTDGKSAKRD
HSRTKAAGSK GDDAKDNKDR SKDTESRNEK EMSRAEERFM KEEVPKDKQH SKDKPLKDSS
KQTENRKRKS ESSSSNEERI VDNKKVRMAY KEEEDNDDHD DDDDDDDDDE EEDDDDGDED
EQEEEKECRN AATVTRQEQS RTEERYEPDV KKNKLPLGEE SDEEISAEGH FKMLLVDLVT
TTDVTWEESK KRLRKDERWK ELSSLDRGQK EELFEEHLRE LKRKYRTEYR QLLDQLPQFN
LSCTWKEIKK LIRNDSRYSQ YSSSDRKCER EFNDYLMEKL QNAVDNFIEL LKETKIITHR
SKKMMLESEQ HLTDILSILE NDERYLVLEC VPSEREKVLE RYLDQLEKAG TSKEISNFRL
CDMRLNGDAG RRAREPVGQR SQVGSIIFRR TMSAPIILFK PGTEHAKGKR HIVGNIQACQ
AIADTIKTTL GPRGLDKMIV QSSGTTIISN DGATILKALE VALPAANVLV DLAKSQDAEI
GDGTTTVVLL AAELLAMSKP FIDEGIHPQV IINAYRKASK YALQVVNDVA VDVKGESIEI
GGKKGMSKKE LLIKCACTTL SSKLVATQKQ HFAELIVEAV MHLDDSMPLN MIGIKKIRGG
SVDESELILG VAFKKTFSYA GFEMQPKTYV NPKIALLNIE LELKAERENA EMQIKNVQEY
QLIVDAEWQI LYQKLEKLHE LGVNVVLSRL PIGDVATQWF ADRDMFCAGR VEALDLERTM
AACGGSIIST VSNITPDMLG SCAVFQEKQI GGDRYNIFTG EAKAKTCTFL IRGGAEQFME
ETERSIHDAI MIVRRALKND KIVAGGGAFE MEVCNRLRKV ALEIKDRDQF FVAAYAKAFE
VIPRQLCFNA GMDSTKILNK LRELHAAGQP SAGINLAESN VVDNIEAFVW EPAIVKANAV
AAATEAACLI LSVDETIRTP SRSANIPKGM Q
//
