GenomeNet

Database: UniProt
Entry: A0A0A2V655_PARBA
LinkDB: A0A0A2V655_PARBA
Original site: A0A0A2V655_PARBA 
ID   A0A0A2V655_PARBA        Unreviewed;      1287 AA.
AC   A0A0A2V655;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Cyclin-like domain-containing protein {ECO:0000259|SMART:SM00385};
GN   ORFNames=PAAG_11395 {ECO:0000313|EMBL:KGQ01822.1};
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779 {ECO:0000313|EMBL:KGQ01822.1, ECO:0000313|Proteomes:UP000002059};
RN   [1] {ECO:0000313|EMBL:KGQ01822.1, ECO:0000313|Proteomes:UP000002059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
CC   -!- FUNCTION: Component of the SRB8-11 complex. The SRB8-11 complex is a
CC       regulatory module of the Mediator complex which is itself involved in
CC       regulation of basal and activated RNA polymerase II-dependent
CC       transcription. The SRB8-11 complex may be involved in the
CC       transcriptional repression of a subset of genes regulated by Mediator.
CC       It may inhibit the association of the Mediator complex with RNA
CC       polymerase II to form the holoenzyme complex. The SRB8-11 complex
CC       phosphorylates the C-terminal domain (CTD) of the largest subunit of
CC       RNA polymerase II. {ECO:0000256|ARBA:ARBA00025278}.
CC   -!- SUBUNIT: Component of the SRB8-11 complex, a regulatory module of the
CC       Mediator complex. {ECO:0000256|ARBA:ARBA00011612}.
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KN293995; KGQ01822.1; -; Genomic_DNA.
DR   RefSeq; XP_015703315.1; XM_015847053.1.
DR   AlphaFoldDB; A0A0A2V655; -.
DR   STRING; 502779.A0A0A2V655; -.
DR   GeneID; 9099230; -.
DR   KEGG; pbl:PAAG_11395; -.
DR   VEuPathDB; FungiDB:PAAG_11395; -.
DR   eggNOG; KOG0834; Eukaryota.
DR   eggNOG; KOG2069; Eukaryota.
DR   HOGENOM; CLU_276213_0_0_1; -.
DR   OMA; MEEVAMS; -.
DR   OrthoDB; 4848277at2759; -.
DR   Proteomes; UP000002059; Partially assembled WGS sequence.
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; cd20545; CYCLIN_SpCG1C-like_rpt1; 1.
DR   CDD; cd20546; CYCLIN_SpCG1C_ScCTK2-like_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; IPR006671; Cyclin_N.
DR   InterPro; IPR019194; Tscrpt_elong_fac_Eaf_N.
DR   PANTHER; PTHR10026; CYCLIN; 1.
DR   PANTHER; PTHR10026:SF51; CYCLIN-T; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   Pfam; PF09816; EAF; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
PE   3: Inferred from homology;
KW   Cyclin {ECO:0000256|RuleBase:RU000383};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491}.
FT   DOMAIN          646..752
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   DOMAIN          765..852
FT                   /note="Cyclin-like"
FT                   /evidence="ECO:0000259|SMART:SM00385"
FT   REGION          157..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          865..1273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..206
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..235
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        870..902
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..939
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        954..997
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1022..1081
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1101..1174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1175..1196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1217..1231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1232..1248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1259..1273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1287 AA;  142695 MW;  446F72BDF8606A67 CRC64;
     MATLASSATP LPNGGLIDPT KQAEYPILLG DKLARREEAS SNGFISVTYN HKSKSASRQQ
     RATITASKSS RHLYKLTLQD KGPNADQNIV HTYQGSVDPT SPVSVSETGN LVLVFDPKRK
     AFILEPVMTR LNFNLRSAPG KSTQQVTEQY PQLNVLSGED HVSGDDLLLE KPGEDDSEGA
     PDDSNPYDFR HFLPKSKADD DIPESITPDP HQVTASQPAS RLAPPQPPPL SSGKPRPKPA
     AKAKPQTNPL RPLKRLPKSI TNPKIPTIPK PQSAPLVEEV GLVLDSASDG ASDGASDGAS
     DEEEEETTTQ NVVDNTASQP AASPGANIIV DGDLIIDMGS PPPARPAFKI NPRHFSSNNT
     SANEADYDSD DEGEIEDLRL PSPAGASYHG HEEDEKEEDE EEEQERERER GETRQDDVID
     DDDLAAEMEA AFEESAREEE QERAQQLLLQ QQMQHHIVSE DESERSNVDP DRNYPSSNSL
     TFTFIFRVST PTYNAKHSRK APYLLEFTTT TPGRELLRSA IIPHDLSGSC PLQGTCVLSE
     REMTSDHLTL IVTLRQHLQL VSELAVLPCE VAQYRLLALF LRLSNMSATS TSKRMSLPPV
     PSPSNPILVA TQSQWIFTDS ELHRTPSILD GMTMEAEHTS RSKGVNFITQ VGILLKLPQL
     TLCTASVYLH RFFMRYSMKD LPQRPGMHPY SVAATSLFLA TKVEENCRKM KELIVACCRV
     AQKKPSMVVD EQSKEFWRWR DTILHNEDLL LEALCFDLQL EQPYRLLYDF ICYFKVQGNK
     RLRNSAWAFL NDSTYTVLCV QFPARTIAAA ALYAAARHCE VTFEDDALNR PWWEQLDVDL
     NEMRRACNRM ADIYEFVSVP VPGQQYAHLS TGDDGATDQT RTSHQPKSES SMDISANSMS
     PGEINGRKRE RDNHSDSFSQ YPISLPANGT TSGTQDPQPS PKRQRREGSE VDADTAPFSQ
     TQPPLSSQTS FVQAAPNLNM RTATNDPSSQ IPSEINGHPR NVSPPKSRIP QAARIPANVA
     RQEHPLPPPP PVTVPPLPHQ HSPPPRRASY ANNPPPPPRG PPLSSGPSMF HPPPPPPPSN
     SSSVDELQQR IDAIIQQGLP RDNDRSHEPR GSYHYHPPSR DRDGNREKDR DRYLDSDIDR
     SRERDRYRER GIDKDREKEK DKGRDYDRDF NCSRRQSSEA SGSVAISASL SAPSFSGAPP
     ATVLPPPLAP SADTRKESGQ DQQEKGEAVN EDTTTKTTVS QVIGNNSAEP DDGGSEEEQW
     VVDDGHNVDS VKRPFRDKGT LRFYADI
//
DBGET integrated database retrieval system