ID A1CB16_ASPCL Unreviewed; 1174 AA.
AC A1CB16;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=DNA repair helicase rad5,16 {ECO:0000313|EMBL:EAW12934.1};
GN ORFNames=ACLA_013710 {ECO:0000313|EMBL:EAW12934.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW12934.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW12934.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; DS027049; EAW12934.1; -; Genomic_DNA.
DR RefSeq; XP_001274360.1; XM_001274359.1.
DR AlphaFoldDB; A1CB16; -.
DR STRING; 344612.A1CB16; -.
DR EnsemblFungi; EAW12934; EAW12934; ACLA_013710.
DR GeneID; 4706192; -.
DR KEGG; act:ACLA_013710; -.
DR VEuPathDB; FungiDB:ACLA_013710; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_3_3_1; -.
DR OMA; CDEMGFG; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45626:SF17; HELICASE-LIKE TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:EAW12934.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 444..639
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 984..1141
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..948
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 132744 MW; D439C7A01D98B103 CRC64;
MDLDPSQRTE NMNMESEPET LDIDPVLLES IESRRQMSAM DAFARLRQVQ KTAMAFGPRF
AGTTFEPALP EPLTLGDWTE PLPQDNQLFA EPSTEKNLTA DLEQLPHSKA TDSGSVSQPN
CTTDMSLGET RHHSTNSCSE DIWKPQIGTQ GTQLVVASSP ARLNAPRVLA TTSLGEPSVE
NDVLEWPEMP EEDPTTFSKV ESWYKSLKNP SPWDRVQFER ATQQEARRKE RVASRLALEQ
YDPENNEGLQ NTSDRGSGSA LAETSHNRNH TAQHGSQAKK RKRKNKISAD EQRRSMQLGL
NFLLRPKLTS TKRIRKRRAN QVDTNDEMQH LRESPKNMKY AEFDLDAFLG SEDVVAEGHE
NAALPACPVF TSNVKMKALT QLVASIPAAD QEEAKSDKRK ILEGTRKFTT RVKCDGQNGW
RIKGMKTSLL SYQLLGAGFM RDREKSPEPP QGGLLCDIMG YGKTIQALAN IVDGRCVDPD
DPVKATLIVV PSHLVGHWEY QISKHCDQDA IGDVLIYEAR HRLRTLDVIQ SMQRYNVVIT
TYDEVRRSYP LSKINSNGSN DDELTSSWED FYLSTVGPLH KIKFLRIILD EGHVIKNHLS
TTSIAVRALT SKYKWILTGT PAINGITDLY ALFNFLGHRY AQEYDSFVGD FLCVSANDKQ
GLQRLRNICR TCTYRRTYSS RLFGLPLVQL PDISRTVVTI EFCDIERKIY SEVRENYVAN
INELSNEPNP RYSQSRCFLA MILRLRMISS HLLTNQDVVK DLLTSETFAQ QVYKLGAESG
DPEHPSAKIA RCLTGLKNGI FVPAARQEHE ELGGLCKELS GDQEELVNEF KEFMNQLHEE
QQWLERLERV TCPRCGMPPT EPIVTDCMHL YCEECFFEND IIAGNGTPKC QAQFCGKIIQ
KAALFGSVES IVQESTAPAT QTHMPLQGGK KKVRRVTPIR KPEKPKPKNK RSNLRFNSSS
FDKDQDTDWI SACGGEMPSA KLTKIRELIQ NWIEENPEVK VVIFTLSLDF VRIATMMCER
EGWQCYAFTG KMPIPAREQS MKEFRENPEA KVLVASLKAG GIGLDMTMAN KCILVDLWWN
EAIHEQAFCR LYRIGQQKEV EIVILIVRDT IDEYICQLQL KKTAEINSAM GEEELSKRDT
IIELFRMFAE VEVNAKGGIT INLDGKGKQA NRKG
//
