ID A0A093H625_STRCA Unreviewed; 403 AA.
AC A0A093H625;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Cyclin-L1 {ECO:0000256|ARBA:ARBA00019921};
DE Flags: Fragment;
GN ORFNames=N308_07909 {ECO:0000313|EMBL:KFV78043.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV78043.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV78043.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV78043.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
CC Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin L subfamily.
CC {ECO:0000256|ARBA:ARBA00010589}.
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DR EMBL; KL206022; KFV78043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093H625; -.
DR STRING; 441894.ENSSCUP00000003407; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
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; cd20592; CYCLIN_CCNL1_rpt2; 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; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; CYCLIN; 1.
DR PANTHER; PTHR10026:SF64; CYCLIN-L1; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF036580; Cyclin_L; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
PE 3: Inferred from homology;
KW Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584}.
FT DOMAIN 76..191
FT /note="Cyclin C-terminal"
FT /evidence="ECO:0000259|SMART:SM01332"
FT DOMAIN 80..164
FT /note="Cyclin-like"
FT /evidence="ECO:0000259|SMART:SM00385"
FT REGION 192..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..290
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..325
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..403
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV78043.1"
FT NON_TER 403
FT /evidence="ECO:0000313|EMBL:KFV78043.1"
SQ SEQUENCE 403 AA; 46935 MW; 4FE6A73E8832EA57 CRC64;
SFQIVAMACI NLASKIEEAP RRIRDVINVF HHLRQLRAKR TPSPLILDQN YINTKNQVIK
AERRVLKELG FCVHVKHPHK IIVMYLQVLE CERNQTLVQT AWNYMNDSLR TNVFVRFQPE
TIACACIYLA ARALQIPLPT RPHWFLLFGT TEEEIQEICL TTLKLYTRKK PNYEFLDKEV
EKRKMALQEA KLKAKGLNPD GTPALSTLGG FSPASKPSSP REIKTEEKSP VSLNTKTIKK
EPEERQQAAK SPYNGMRKES KRSRSSRSAS RSRSRTKSRS RSHTPRRHYN NRRSLSGTYS
SRSRSRSRSH SGSPRRHHNH GSPHLKTKHS REELKSASRH GHKRKKSRSR SQSKSRDHSD
VAKKHRHERG HHRDRRERSR SFERSHKGKH HSSSRSGHSR HRR
//
