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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//