ID A0A077Z0F6_TRITR Unreviewed; 699 AA.
AC A0A077Z0F6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Cyclin N domain containing protein {ECO:0000313|EMBL:CDW53917.1};
GN ORFNames=TTRE_0000218601 {ECO:0000313|EMBL:CDW53917.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW53917.1};
RN [1] {ECO:0000313|EMBL:CDW53917.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW53917.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cyclin family.
CC {ECO:0000256|RuleBase:RU000383}.
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DR EMBL; HG805873; CDW53917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077Z0F6; -.
DR STRING; 36087.A0A077Z0F6; -.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd20538; CYCLIN_CCNT_rpt1; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; CYCLIN; 1.
DR PANTHER; PTHR10026:SF155; CYCLIN-T; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR Pfam; PF21797; CycT2-like_C; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; Cyclin-like; 1.
PE 3: Inferred from homology;
KW Cyclin {ECO:0000256|RuleBase:RU000383}.
FT DOMAIN 53..152
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 268..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..691
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 77507 MW; 19E21D3AC53072D9 CRC64;
MSDGAAHFLP ESSRLSASSS RWLFTAERLS DSPSVRDGMS VAKELHCRQQ AASHIQEMSQ
KLSLTQLCMN TAIVYMHRFY VFHSFCRFPK FDLAAAALFL AAKVEECPRK LEYLVKVSHA
LQHRGEPTLD TRSDKYMQEV QKIVTYENVL LQTLSKYIYI CRLFLSHSFA SLNCLGFDLQ
VEHPHPYVVR CCQMIKGKDN NRLTMIASAK FFLPFQHLIP QSHEGKPWFY YVDKRLTTET
LEALADEFAT ICEKTPERWR LRRMGLRRDE DDSAESVEGQ QSSSASLQGK ASASSPTIDG
GQNVPICSIE RKSNELPDER LPRWRPPSDN NKESMRSVKV EPTKGESSSL VAAANANTNT
GSCTSAVDAT VLGEMQATST KRPCHSPAVI DIKMYKERRE KELASMGKSA ADLLNQQSTS
QRKSFIPDVS NVKAATAATA ANSVTTTDGH CNGSFSSKSH REDLGKKRPF PEHSSSSSSS
SSSYGYSKLK VSRTTEERNK MNGLGSSILR PFSGDLPLPP STKLPARPDD NDSSKGLYKD
QWSSLARSSF HHQSKNGQHY GAERLKQNVA APHLHTYSDH SRTTRMQEVD YYKKGLVNNT
DRRSTTTTGR SDYVAKKQVA VDGERTSSTT HKYGKIGGGI PKPPPMEFYP PPPPLPPPPP
PPPPPPDTKK PPPPPMPPPP APPPPETPSN PHLTQPAIT
//
