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Database: UniProt
Entry: A0A068RKJ8_9FUNG
LinkDB: A0A068RKJ8_9FUNG
Original site: A0A068RKJ8_9FUNG 
ID   A0A068RKJ8_9FUNG        Unreviewed;      1782 AA.
AC   A0A068RKJ8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Chromatin remodeling complex subunit {ECO:0000313|EMBL:CDH50157.1};
GN   ORFNames=LCOR_01879.1 {ECO:0000313|EMBL:CDH50157.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH50157.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH50157.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the actin family.
CC       {ECO:0000256|RuleBase:RU000487}.
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:CDH50157.1}.
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DR   EMBL; CBTN010000005; CDH50157.1; -; Genomic_DNA.
DR   STRING; 1263082.A0A068RKJ8; -.
DR   VEuPathDB; FungiDB:LCOR_01879.1; -.
DR   OrthoDB; 196861at2759; -.
DR   Proteomes; UP000027586; Unassembled WGS sequence.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 3.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR024977; Apc4-like_WD40_dom.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR46362; GEM-ASSOCIATED PROTEIN 5; 1.
DR   PANTHER; PTHR46362:SF1; GEM-ASSOCIATED PROTEIN 5; 1.
DR   Pfam; PF00022; Actin; 2.
DR   Pfam; PF12894; ANAPC4_WD40; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   SMART; SM00320; WD40; 9.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW   WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT   DOMAIN          1263..1353
FT                   /note="Anaphase-promoting complex subunit 4-like WD40"
FT                   /evidence="ECO:0000259|Pfam:PF12894"
FT   REPEAT          1391..1424
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          426..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          315..342
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        527..542
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1782 AA;  201378 MW;  A0F6FCA42B4AB33A CRC64;
     MQKVKSQQEC DLFSIHPLPF TSLPPMTEVP IYHLEEKEYD APYYQIRTDY EDNFFNSNTP
     LVIDNGSYQC RAGWATQSNP ALIFDSVVSR YKDRKANVNM LAVGMDAYAD PAGRSNARSP
     FDGNVVCDFD RMETMLDYIF TTLGIATDSI NHPIVMTEPV CVPQLSRKQM SELLFEAYNV
     PSVMFGIDSL FSFYANGGMR DTDGDEADIV VSAGHSNTHI IPTLHGKGLL ERTKRISYGG
     TQATDYMLKL MQLKYPTFPT KMTNTQAQDL VHSQVMVADD YQEALKKIEN RDTFGEFDRI
     VQFPYTPPVI EEKTEEELAR QAAKKEENAR RLREAAAKSR LEKLVRREQE FEAFTELKNS
     RAIMNKKEWM ARLKEAGFKD EADLDDTIKQ TDAAIQRARN KELGIEENEE KGPPVTTLID
     IPDDELSEAE KKEKRKQKLM KANYDARERA KKAKEEAKAR EEEEARLEEE RRLRDPEKWI
     AEVKQKRQGV VDRIKKRRRL NMELADRRSR ASQLRMRSIA NLASDTPAGK RRRRGQEEDT
     FGADDEDWMI YREISREDES DEEEEDLSML NQYESMLLQY DPDFLPEHSF EATSSPTNTL
     MHLLARGQYP PYDPTDVGQM HQLHVNVERV RVGEVLFQPS IVGLDQAGLV ETMHDIVRTF
     NPDRRMQTVK TIFVTGGFSS LPGFSNRIFT SLRAILPVGA SFQVKRAENP LLDAWRGAAM
     IAKESGYKQY AVTRQEYEEY GGEYIKEHGL GNVFRNMLQA YPPVPNWYTS HCACVVDTLN
     YYIYASRNAI VVLDLATFAF AKTFLGAMQR INAIAAYQQF CYIAEGNRIR AWNLIDSRLL
     VAYKAIHKND ITVIQCIRGG TTLVSGDKSG ALVLQLVSGD QCWRSEKVNS EIKTIAPMCH
     AGQDYLAIAY ANGMIYIEKV LADLKTETVY QMTHAHVNNL AWQYQEENQA TVTTAWPLLA
     SSTRRNREIY IWNVPSESKH AIVKIPPPSP KWTEQQRNTL WIELAWSPLE KDRLWVSSYM
     GNIISFKINN GSGASKGRLP DIHSRIAFSL MWVDQGRRMV SYGLDKQIVY WDMYDSVARV
     QMVTQAAFPY TIDISAWNPG QAAVGMGDSN IKVWQFSSTM TSGKDNFYQA SLMWKEMQGQ
     IRHVKWHPEQ DSKIAYSNEY GRIGVYDISK TKNMRFKGYH DAGTVSIAWA GDLSLGEHGM
     VQDTLISCGV DGKILVFNAG KPHFAPVLLE DILAQANPAW AKANQAKVNT KRCTIDVDPG
     NRFLAIGNTD GVVEVYRLDT LKIIYVCNAL TVNVTAMAWG GKDQSYLAVG YKSGNITIHK
     ISIQENSPEV PIPDSTALHK SDFHKKPINS LAWSHHVDKM YLASASEDDS VGVYGVKAEN
     DSTHVTPEAH FKQHRGRVLT VCWGYEDTDV LISGAEDRFI YLWKWTDYLY PKGKHDRTSA
     RERELAMITK SASMGNKSEA ATEVASTSMT ATTDTNQEVV QHAKKKRRVP NALMIASRRS
     QQVLTQDVML RRSLLLAASI YGGDPLSAIE HVKSKIPAHI NPALYDAYVG SPYEGDSEVL
     DLFFGDKNDV RRLLDLEESQ MAQVKERSWP LPGSENFDLK LALDIIRSNT QESQSSSNMI
     DWIALALSPT AGKEAWLAMM ENTATQLARA GQTVLAATCY LACSKVYDAV NVYRKAKMYR
     EAIAVAKLRL PAIDPLIPTL YAEWGDMLKN STTEEEFAAL CFIKGQVPGS TVQAINLLAR
     KQKDGHLFWA ACLACLLNDS TADERISQYI QALEKRATRG SG
//
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