ID   CAN1C_EMENI             Reviewed;        1041 AA.
AC   Q5BAH2; C8VP77;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Cullin-associated NEDD8-dissociated protein 1, C-terminal part;
DE   AltName: Full=Cullin-associated and neddylation-dissociated protein 1, C-terminal part;
GN   Name=candA-C; ORFNames=AN2458;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH CANDA-N;
RP   CULA AND CULD.
RX   PubMed=21119001; DOI=10.1091/mbc.e10-08-0732;
RA   Helmstaedt K., Schwier E.U., Christmann M., Nahlik K., Westermann M.,
RA   Harting R., Grond S., Busch S., Braus G.H.;
RT   "Recruitment of the inhibitor Cand1 to the cullin substrate adaptor site
RT   mediates interaction to the neddylation site.";
RL   Mol. Biol. Cell 22:153-164(2011).
CC   -!- FUNCTION: Assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
CC       ligase complexes that promotes the exchange of the substrate-
CC       recognition F-box subunit in SCF complexes, thereby playing a key role
CC       in the cellular repertoire of SCF complexes. Acts as a F-box protein
CC       exchange factor when interacting with candA-N (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with candA-N. Interacts with unneddylated cullins
CC       culA and culD. {ECO:0000269|PubMed:21119001}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21119001}.
CC   -!- DISRUPTION PHENOTYPE: Cells show a dark red color when grown on an air-
CC       medium interface that induces development. Cells are able to initiate
CC       the cycle but are blocked in the initial stage of early nest formation.
CC       Cells exhibit reduction in asexual development and block in sexual
CC       development. {ECO:0000269|PubMed:21119001}.
CC   -!- MISCELLANEOUS: In E.nidulans, CAND1 is separated into 2 distinct
CC       proteins: candA-N (AC C8VP82) and candA-C, corresponding to the N- and
CC       C-termini respectively of the protein in other species.
CC   -!- SIMILARITY: Belongs to the CAND family. {ECO:0000305}.
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DR   EMBL; AACD01000040; EAA64164.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF86897.1; -; Genomic_DNA.
DR   RefSeq; XP_660062.1; XM_654970.1.
DR   AlphaFoldDB; Q5BAH2; -.
DR   SMR; Q5BAH2; -.
DR   STRING; 162425.CADANIAP00009174; -.
DR   PRIDE; Q5BAH2; -.
DR   EnsemblFungi; CBF86897; CBF86897; ANIA_02458.
DR   EnsemblFungi; EAA64164; EAA64164; AN2458.2.
DR   GeneID; 2875417; -.
DR   KEGG; ani:AN2458.2; -.
DR   VEuPathDB; FungiDB:AN2458; -.
DR   eggNOG; KOG1824; Eukaryota.
DR   HOGENOM; CLU_007157_0_0_1; -.
DR   InParanoid; Q5BAH2; -.
DR   OMA; MGGTQDD; -.
DR   OrthoDB; 194023at2759; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IDA:AspGD.
DR   GO; GO:1900797; P:cordyol C metabolic process; IMP:AspGD.
DR   GO; GO:1900570; P:diorcinol metabolic process; IMP:AspGD.
DR   GO; GO:0018940; P:orcinol metabolic process; IMP:AspGD.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0010265; P:SCF complex assembly; IBA:GO_Central.
DR   GO; GO:0043935; P:sexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR   GO; GO:0000909; P:sporocarp development involved in sexual reproduction; IMP:AspGD.
DR   GO; GO:1900588; P:violaceol I metabolic process; IMP:AspGD.
DR   GO; GO:1900591; P:violaceol II metabolic process; IMP:AspGD.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR039852; CAND1/CAND2.
DR   InterPro; IPR013932; TATA-bd_TIP120.
DR   PANTHER; PTHR12696; PTHR12696; 1.
DR   Pfam; PF08623; TIP120; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN           1..1041
FT                   /note="Cullin-associated NEDD8-dissociated protein 1, C-
FT                   terminal part"
FT                   /id="PRO_0000422243"
FT   REPEAT          138..176
FT                   /note="HEAT 1"
FT   REPEAT          242..279
FT                   /note="HEAT 2"
FT   REPEAT          339..376
FT                   /note="HEAT 3"
FT   REPEAT          434..472
FT                   /note="HEAT 4"
FT   REPEAT          479..516
FT                   /note="HEAT 5"
FT   REPEAT          525..560
FT                   /note="HEAT 6"
FT   REPEAT          598..637
FT                   /note="HEAT 7"
FT   REPEAT          670..708
FT                   /note="HEAT 8"
FT   REPEAT          710..744
FT                   /note="HEAT 9"
FT   REPEAT          780..817
FT                   /note="HEAT 10"
FT   REPEAT          822..867
FT                   /note="HEAT 11"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..103
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1041 AA;  113518 MW;  DE7144CB71B289CF CRC64;
     MSSDAMSDYS HDDEHDPQTD ELRETALVTL EALISSCSSQ MQSYLPNTIN SALRFLKYDP
     NVADMGEDEE MSGTQDDGSE DDVTEEPDLE DDDFEDFEEE GGYSDIDDMS WKVRRCAAKL
     LYAVISTYGR GRALDDTSLY QQIAPAIVAR FNKEREESVK LELVSTMDAL VRKTAEGSMI
     MTSSGFLESV GSGSKISRKR RRQDSDASMI DFEPSMGTSS AAGTPLAAPS SPQSGPQSEL
     ANALPVIVRS LVTMWKQASI HLKQAIIILL KSLALVRYGG LADHLQQIED PIADVLKSSL
     SGAPSASIGI SASAGTLQIE TLSLISAISE THASDALLPF LIALIPGVIV AVNDKNYKVS
     SEALAAVEQI VKALTPPRVT TASQDLIFQL EKLYDVSHSR ITDTSADLEV RQRAIHVLGV
     LLARTSDEQG SAFLSFEKRS KGLVTLVDRL KNETTRLSAV RAIDDVAVLC SRKDDVDSNW
     VREVTAELGA QLRKSDRVLR SASLETLRSL SMNPNTRAHY DGETMKNLEE CLIPLISVED
     VHLLAPSLII IAKLVPGNAQ LLVNDGLVSA ICSIVRTSLA GTVLKALLLL VKVIGEEGSG
     LTLMQNLLQD VGVNGDTSVV GRSIGTLLVH GGSNVGVRME DFLSELQKTQ DPQRQCLALA
     ILGESALRLG ASCSLTPNVF IPHFNSKSEK VRLASATALG NAAAGNVKAY LPTILGGLEK
     SDPQSYLLLH SVKELLQHPE MVRRDVAPSA LKLWQALLVV SKEEDNRAMG AECVGRLALL
     DPPAYIPQFQ EYLANGDAGI RSIVVSAFRF TLSDSRDVFN DVLRPLIVPL LVNMLSDRDL
     GNHRLALTTL NSAIHNKLAL ILPHLGELLP AVLGDTQIKP ELIREVQMGP FKHKVDDGLE
     LRKSAYETVY AALDTSFSLS HITELYSRIL AGIDDEQDIR TICNLMTSKL ITLAPEETQR
     HLDALSERYT AILNFKPKEN AVKQEIEKAQ EASTGVLKIT RELSKAFPNA ETMGDHHKWK
     AYMEMVRAQF GTQLSNLESE F