ID A0A3M0L4Z7_HIRRU Unreviewed; 563 AA.
AC A0A3M0L4Z7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Cyclin-dependent kinases regulatory subunit {ECO:0000256|RuleBase:RU311113};
GN ORFNames=DUI87_03583 {ECO:0000313|EMBL:RMC18984.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC18984.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMC18984.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMC18984.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMC18984.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to the catalytic subunit of the cyclin dependent
CC kinases and is essential for their biological function.
CC {ECO:0000256|ARBA:ARBA00002449, ECO:0000256|RuleBase:RU311113}.
CC -!- SUBUNIT: Forms a homohexamer that can probably bind six kinase
CC subunits. {ECO:0000256|ARBA:ARBA00011253}.
CC -!- SIMILARITY: Belongs to the CKS family. {ECO:0000256|RuleBase:RU311113}.
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:RMC18984.1}.
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DR EMBL; QRBI01000095; RMC18984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0L4Z7; -.
DR STRING; 333673.A0A3M0L4Z7; -.
DR Proteomes; UP000269221; Unassembled WGS sequence.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0035368; F:selenocysteine insertion sequence binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.30.170.10; Cyclin-dependent kinase, regulatory subunit; 1.
DR InterPro; IPR000789; Cyclin-dep_kinase_reg-sub.
DR InterPro; IPR036858; Cyclin-dep_kinase_reg-sub_sf.
DR InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR InterPro; IPR004038; Ribosomal_eL8/eL30/eS12/Gad45.
DR InterPro; IPR040051; SECISBP2.
DR PANTHER; PTHR13284; GH01354P; 1.
DR PANTHER; PTHR13284:SF9; SELENOCYSTEINE INSERTION SEQUENCE-BINDING PROTEIN 2; 1.
DR Pfam; PF01111; CKS; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00296; CYCLINKINASE.
DR SMART; SM01084; CKS; 1.
DR SUPFAM; SSF55637; Cell cycle regulatory proteins; 1.
DR SUPFAM; SSF55315; L30e-like; 1.
DR PROSITE; PS00944; CKS_1; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|RuleBase:RU311113};
KW Cell division {ECO:0000256|RuleBase:RU311113};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000269221}.
FT DOMAIN 375..468
FT /note="Ribosomal protein eL8/eL30/eS12/Gadd45"
FT /evidence="ECO:0000259|Pfam:PF01248"
FT REGION 67..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 474..501
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 67..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 64033 MW; 9FBB83845A9403AC CRC64;
MAHKQIYYSD KYFDEQYEYR HVMLPRELSK QVPKSHLMSE EEWRRLGVQQ SLGWVHYMIH
EPVAGSQCQS NNSTHCNGSG IGSESAEQTY PVRQENKSLS KQRRSKEGEK KLDKKKHDGG
EASVKIVNRT SFQASTHSRE SVKPDRFNKT TNKKSTETAK PESCPVPTFE TSFLNFHKSQ
SLESSEILNE HHKGTPVEES QVTPEHKYVL EDTSTKSKAL PKASDEAGDN LYPSSLDGRV
SFPEAPADGS AQPHVSWAVI LSQPPKKIVS SPESEGLSRG KGKQESEPKQ SGTKDIASET
EPEEGSEKKK KKKKKKKKLK SRTDIERPQS DSNIVQHHRR LSYCSQVLSK EVDSCVTDLL
KELVRFQDRL YQKDPVKAKI KRRLVMGLRE VLKHLKLKKL KCVIISPNCE KIQSKGGLDE
TLHNIIDCAC EQNIPFVFAL NRKALGRCVN KAVPVSVVGI FSYDGAQDHF HRMVQLTTEA
RKAYKDMIAA LEEEAKAGLR ETQPNILTPE SEKNGLLETC KTSSKTQMRM YQITLKSGRE
NLKKNITHML WSWKKVQLLT WRY
//
