ID A0A0C3QEA2_9AGAM Unreviewed; 1920 AA.
AC A0A0C3QEA2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIO23299.1};
GN ORFNames=M407DRAFT_214873 {ECO:0000313|EMBL:KIO23299.1};
OS Tulasnella calospora MUT 4182.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Tulasnellaceae; Tulasnella.
OX NCBI_TaxID=1051891 {ECO:0000313|EMBL:KIO23299.1, ECO:0000313|Proteomes:UP000054248};
RN [1] {ECO:0000313|EMBL:KIO23299.1, ECO:0000313|Proteomes:UP000054248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUT 4182 {ECO:0000313|EMBL:KIO23299.1,
RC ECO:0000313|Proteomes:UP000054248};
RG DOE Joint Genome Institute;
RA Kuo A., Girlanda M., Perotto S., Kohler A., Nagy L.G., Floudas D.,
RA Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUT 4182 {ECO:0000313|Proteomes:UP000054248};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the BLM10 family.
CC {ECO:0000256|ARBA:ARBA00005739}.
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DR EMBL; KN823088; KIO23299.1; -; Genomic_DNA.
DR STRING; 1051891.A0A0C3QEA2; -.
DR HOGENOM; CLU_000772_3_0_1; -.
DR OrthoDB; 68480at2759; -.
DR Proteomes; UP000054248; Unassembled WGS sequence.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IEA:InterPro.
DR GO; GO:0016504; F:peptidase activator activity; IEA:InterPro.
DR GO; GO:0070628; F:proteasome binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032430; Blm10_mid.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR035309; PSME4.
DR InterPro; IPR021843; PSME4_C.
DR PANTHER; PTHR32170; PROTEASOME ACTIVATOR COMPLEX SUBUNIT 4; 1.
DR PANTHER; PTHR32170:SF3; PROTEASOME ACTIVATOR COMPLEX SUBUNIT 4; 1.
DR Pfam; PF16507; BLM10_mid; 1.
DR Pfam; PF11919; DUF3437; 1.
DR Pfam; PF02985; HEAT; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Reference proteome {ECO:0000313|Proteomes:UP000054248};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 383..897
FT /note="Proteasome activator Blm10 mid region"
FT /evidence="ECO:0000259|Pfam:PF16507"
FT REPEAT 1769..1804
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1834..1920
FT /note="Proteasome activator complex subunit 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11919"
FT REGION 41..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1920 AA; 216093 MW; 7129E55F5B9EED63 CRC64;
MDALVDSLIQ QFQDSSSTAS IAVAMADDSI DDMDLELEDE LDLSSGGVTT STRQPETDEE
KQQRIMDGYI SALPFPSESP EEMREELNRI VSKMLIAAEG RHWDHLLAWT GAFNSYVFIP
SLELQYIHSF ASTLIRLIGN RLGSKRKLEL NELTLPWARL WKLLELEMWP KKRMVMTNMS
RNLHNVLLHL AEACCDYFAP SEIPKMLDTF LPLITKETAP SMFTVLAAFL PASHAHTYLP
FMFKSWESFH SYKIEDSMIS QFAALSVAHV AGTASEYGPE GSLPWKDVGI YSDTEWDMIM
RTCLASMSAS KGGSSTAVHA DRSNPSVFKK NGQRHAWLAQ IIVYSMSVDG PVRPLASEDA
KPESTTEKSF LAGSKALDSL DRRVLLTFVH RLAAEFSTRW NDELLPSCKT PLAQRITVDI
KRSFVQVLRT PVLLSMFAKD PIATTYAQAA LKHLSILEPD LIMPQLLERA FSGLETVNET
HRTTAAIGAL AAVPSALTIR SVWLKGQKHL VSLLEMCLPG IDINDAIKTI STSLFITTAL
QFIKIGDLNV EGAVPLAHDA PGEDVVMKLE GAETPMMERL KRKEMTDEEL EEDSLVKHST
AGFADWVVSF FRRVFALYEN LPEEGGKSGK TGGKTEETVL KSLNAALDVV CANLSDKLFT
LVLNLVYEYC TTNARSNSVR SIGNLVNSMA RTRPRETISK FLPFTKQQIE IELAAGASSV
RTTSNTAAAL PSDTTFHWNL AVIRAALAYG GADLVEFKDD LLSLMNTLRK AKNERGYSGF
GRLVNRTLAT LTGTYPLEQR IVNPRQWKDP YFDRSHHYSW GKQFSNPKDV EVQWHVPSAK
ELEFAVEIFQ KIITPAIVDL EALIQVPPTS RDGVWRNDFC RMMYLVRSAW SGASCLLIEG
EKTGGDLCID ENYIAGITPS FKRPRAAFAL SDPADPRYQS VKALKDRFGK LLHHSFLALT
QEAEAKSEAA DAVDASIQLV RALDIYLLDY GVSRDTIVAL KRQFTMARDS VKTHPKQRSF
PRMVWIKRAA LYGYSRMFQH TNYRDRSALD DQLLLDLVEL SLSPYTRVRK HAQSTLLAAS
AYYRRAWRFV LPRIIEELKR ETAKGKDADP DRQKGMSTPT PPFTLAQALT SVVTGALHIL
SDKTVQSICC NQKVSKPSIQ KLVARITSDS LSCFTEESLA VTVYLVPLPD VAGACATAHL
VNGMSPAEQP NLAESKSRTA FQAEIRQKRL GKLVSRVVHV EWRYREYSIR YLSYLLCRDH
PLLPDVATLL SDYAISEHPY TRAYSQRGLT KLLLHVKMRS FSRDSEQLWG SQWLNPLRQD
IPINDPNKFL QDLERPFAGG SSDVFFVDKE QQGFLTWSNA AKAYRPPPRT GPVLVWSSDT
QPSLQAIRSV INQQWIQKFI ILNSQEGSKA ATASSVDLRL ENVIFLKSLF KTFEAEFLEP
LLNHVDILIF SDDKYQQRAG FEVLAGALRG SKHWALDTQA QVWEWFSTRL PRLFEHIKPD
AVVMWDAFLN MQLVERDPRR MQPLVDFILS QKIDFNADSA FTVTKRLTTI GILADGLGTR
IESQVSRMID LYFDNIQTPY AEVRAQIAVN LGVLMGIQWH PRYRTAGELV AACSTDNDAL
QIRKADHLPR IQYFIANFDQ WRQERLPPPR VSQSTYDRVG LTLLQWVWGT AHSARASSVF
PYVMPLLPEI FKMAELNDSS ELQLYSSAVL IVLSTISPPH EYVEPIIDSL IGAVKSSPSW
RIRLSVLPVL QVFYFRNLLN LPDTSVQRVM EVLLECLRDE NVEVRETAAK TLSGVIRCSQ
RQSIPLLKDR FTRLARRTKL PKRSDKEQLA TAIRTLHSAV LGLCALLDAY PYSVEPWAPE
IIETLARYST DPVPISTSIR KCASRFKQTH QDTWAMDQLA FNEDQAQALS TIVSGTSYYA
//
