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Database: UniProt
Entry: J4I996_9APHY
LinkDB: J4I996_9APHY
Original site: J4I996_9APHY 
ID   J4I996_9APHY            Unreviewed;      1111 AA.
AC   J4I996;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Anaphase-promoting complex subunit 11 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FIBRA_02818 {ECO:0000313|EMBL:CCM00776.1};
OS   Fibroporia radiculosa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Fibroporiaceae; Fibroporia.
OX   NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM00776.1, ECO:0000313|Proteomes:UP000006352};
RN   [1] {ECO:0000313|EMBL:CCM00776.1, ECO:0000313|Proteomes:UP000006352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM00776.1,
RC   ECO:0000313|Proteomes:UP000006352};
RX   PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA   Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA   Diehl S.V.;
RT   "Short-read sequencing for genomic analysis of the brown rot fungus
RT   Fibroporia radiculosa.";
RL   Appl. Environ. Microbiol. 78:2272-2281(2012).
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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DR   EMBL; HE797004; CCM00776.1; -; Genomic_DNA.
DR   RefSeq; XP_012180059.1; XM_012324669.1.
DR   AlphaFoldDB; J4I996; -.
DR   STRING; 599839.J4I996; -.
DR   GeneID; 24095687; -.
DR   HOGENOM; CLU_000315_2_8_1; -.
DR   InParanoid; J4I996; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000006352; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45626:SF47; ATP-DEPENDENT HELICASE ULS1; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006352};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          337..540
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          727..780
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          930..1091
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          40..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          791..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..878
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          140..198
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        40..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..810
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..869
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1111 AA;  125027 MW;  22FE0D3ED60A5CC3 CRC64;
     MGSRQSHACT KDASGTDSAF GDSVSTPSKS KLLHMLDLRV SQSSSASGST ATTPISTPRH
     RHRSVSAAPS SRKSTMKAEY PNTTGSRKRN YTVQDDTDMD ILSSKKLKTE TTKKPLSVAN
     RNTESLGLTT SDAATSTSTA TDTRARLAEV HTQMDRLENT LAKAKQKRSK TDADFVQIVQ
     YQRQLRELRD LKQGYNSMTP STALQTTISG SRDHVSPGML ADAFQAESSS SPVHVGADGS
     SDYALDISGS FVRGDDRFDE DGNFYGRGRD SFAGPVARAD DIDKFLIAAG NAEQFDGNAR
     VDKALDALGL DGLYRPLDGM EVALMPHQAI GVAWMLDKEK SVHKGGCLSD EMGLGKTVQM
     IAVMVRNQSD DPLCKTNLIV APVALLDQWQ LEIETKTNCD VKCLIYHGPG KPKKKKELMK
     YDVVLTTFQT LALEWPDEEA EERKAKQKAK RKRKLDDFIE SNSEDDRKTS KKKTQQLGLL
     FDIDWYRVIL DEAQNIRNRR TRVSRAVTKL HSTYRWCLTG TPIINSLSDA YGLFRYLQTR
     PWYDWTEFNG HISKLEKKNP VLATTRLQAI FSSMLLRRKK DSMLDGKRLI ELPVKETILA
     KLEFSLEERD IYKMASALVE QKSQAIFNRY LRAGTVLKNY HQVLVLLLRL RQVCSHPSLI
     QEGGSAFISA TDLNDRKHDK RYELSRAVQL VSPEFVQKMQ DKMAQIMAQR MEAEKHSADA
     TVEDEECPIC YDAFTDAVVT ACCHVFCRDC IYQVFDNEAA ESADEQVKYK SDERSCPSCR
     GTISKQKLFS RSAFDPNDDD TGDVEKGSEA REATNVLDTL DDVTEEARPK LGRILRKRKL
     RQRHFMDSDD EGDEGDDGDM SDFIVQSDED EEEKDTRRAL KQRLSKRRAI VISDDDDDDI
     DPDVICGAKP DVDAPPEQIK LMPKFLPSTK MKHMMENLRL WAETHSDEKT LVISQWTQCL
     QLVSDYLTEN GFLHVKYQGD MNRKKRDQAV RVFMSRDKAT IMLMSLKCGG VGLNLTRANR
     VISLDLGWSE AVESQAFDRV HRLGQTRQVF VHRLVIADTV EDRVLALQER KKNLADGSLG
     EGTGKKIGRL SVRELANLFG LDHRGRVLSE N
//
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