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Database: UniProt
Entry: A0A319ETV5_ASPSB
LinkDB: A0A319ETV5_ASPSB
Original site: A0A319ETV5_ASPSB 
ID   A0A319ETV5_ASPSB        Unreviewed;       368 AA.
AC   A0A319ETV5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   SubName: Full=Cyclin {ECO:0000313|EMBL:PYI11525.1};
GN   ORFNames=BO78DRAFT_446626 {ECO:0000313|EMBL:PYI11525.1};
OS   Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI11525.1, ECO:0000313|Proteomes:UP000248423};
RN   [1] {ECO:0000313|EMBL:PYI11525.1, ECO:0000313|Proteomes:UP000248423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI11525.1,
RC   ECO:0000313|Proteomes:UP000248423};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ826318; PYI11525.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319ETV5; -.
DR   STRING; 1448318.A0A319ETV5; -.
DR   Proteomes; UP000248423; Unassembled WGS sequence.
DR   GO; GO:0000795; C:synaptonemal complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IEA:InterPro.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR042448; CCNB1IP1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR14305; E3 UBIQUITIN-PROTEIN LIGASE CCNB1IP1; 1.
DR   PANTHER; PTHR14305:SF0; E3 UBIQUITIN-PROTEIN LIGASE CCNB1IP1; 1.
DR   Pfam; PF14634; zf-RING_5; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          12..53
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          207..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          123..167
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        251..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   368 AA;  41020 MW;  4C9FABDFD2EB858B CRC64;
     MDFYLRCNSL KCRTQLKERA VVTTCSHIFC LHCAGNLGLS HPTENERTCP ACQTVLVNPD
     DAVATVLNPT EDYKTSVLSG LDPNTIMECA GRALLFWTYQ TTQEIFYQEF LAKTLTDKYT
     NLNTQLDKVI HNANSEISAL QARVSDMQTT QEQLRKKNQE LVDMYREKCK KFTQMTNLYN
     LLKSRAMRSQ MQTAATDTVS QALNSLTASR NDPSGLASIP PEASGPPQTP LSRQPNVYPV
     NQEGVEQLHR HQRSGTGSSK GAKQKADNSA MPPPSRPMEN PRKSNHPAAT PQHRTRLMGP
     SRPSTAKPQL PHDSIMLERF QGESGPIDSL ITAQDSLSRR DIGMQPRGQT RDPTEPPGMR
     SFFDSTII
//
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