ID C4R6N6_KOMPG Unreviewed; 1548 AA.
AC C4R6N6;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Helicase {ECO:0000313|EMBL:CAY71261.1};
GN OrderedLocusNames=PAS_chr4_0035 {ECO:0000313|EMBL:CAY71261.1};
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY71261.1, ECO:0000313|Proteomes:UP000000314};
RN [1] {ECO:0000313|EMBL:CAY71261.1, ECO:0000313|Proteomes:UP000000314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; FN392322; CAY71261.1; -; Genomic_DNA.
DR RefSeq; XP_002493440.1; XM_002493395.1.
DR STRING; 644223.C4R6N6; -.
DR EnsemblFungi; CAY71261; CAY71261; PAS_chr4_0035.
DR GeneID; 8201127; -.
DR KEGG; ppa:PAS_chr4_0035; -.
DR eggNOG; KOG0298; Eukaryota.
DR HOGENOM; CLU_001592_2_0_1; -.
DR InParanoid; C4R6N6; -.
DR OMA; QLFEQMC; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000000314; Chromosome 4.
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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18070; DEXQc_SHPRH; 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; 2.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00487; DEXDc; 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; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:CAY71261.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000000314};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1228..1266
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1344..1514
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 804..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1548 AA; 177159 MW; 661F6C6665177238 CRC64;
MSSILHQNVE VVIFEIENIA QVLAYKSKLK LSKEEPVSRK RGYNQLQDDH EPNPIPISPE
LAEISKNSVD LAQVDFCGTI DEPEGCSLLR QLGDELTIKD IELSLSDDIL IVKSIRKQRL
SSLPLLSIRL GKIKELVISH LPFFKRVRIV HRSDHIIIVR PQIKFLFSEN APLAFHLEYK
ISVHQGIFIN FPQNWSTHIL NLITKLSWSN PTLFESTSTE YSVPDVPMFY SLVSNATSNW
TPPFPEKLIR VPGLNANLFK FQSKTVNWLL GHEGVEFNHD TKTTTQLPFY SPPESCDTDT
FHNYLIECLN KLSFGWNRIR IDEEVYFYNQ YSGNIVSPDK IIAYFKTLAP TNAQGLLSEE
MGLGKTVEMI ATIMLHPRPE LELESQIFDP VAGRNVRKCK SSLIVCPESI LKQWRDDIYN
FNPHLKVIFY KGISNNKQFK DPSIIAEHLA EHDIILTTYN TVAKEVHYAM YNPTDRPLRK
AAKDGRMKAQ IEEENATSIP NENDAAKSER IASTLRKQSS DEFVERYDYS SPLVLLQFWR
VILDEVQMVT SKISNAAKIC KMIPRAHAWG VSGTPIRNNL DDLQAILSFL RFHPFDDNDS
QKRVRIKNPN WELVKSAKPP LTFVRLWSKI ALRHTKLMVA DDIKLPPQQR IQLSISLTPV
ERDNYDNLFK SFLSDVALND KGEPLLENWE PNSTVLTTMR VWLEKLRRIC CHAQIGSGNI
KKQMFELVGL KTMDAVLDDI LLKVDQDVDT SKRLEILSRC KQGMIYEYMK APTSALEIWE
SCLTEIEKQI KALNDLLNGI NEGSPVKLEP LDEKEEMEET DSSDENGDFS KKGLLKHRLR
SWLELLHRCY FFIASAHNQI YNPKLTEEEK ESGSRQNLDE VPDELLDRDS LEHRKIERLY
YAKAEDIRKE LLKERLKQVD NSDKDLLTKT RAFLKNNGFM KETRKAHHKK DTDFKDRKDI
DVKESDTHLK VDRVNLLKLI QVPDVTGGHF FSFQDDLEGL YHRLNSQAEY VNKWIKVVFS
LLTKSIVETE ETTGNEMSSY AEEQDKIDKY LSVIQLALTD RGVCLKASRN RGVPTTYRIP
SSTKEEESEF QKARVMTGVS ITLTQLLDRI SLEAGNNDSE TLKNAFLEIK ALVSSQVDEL
TKNLNSASKI VTVFNNSFNS RVNYFKGLQQ ISENVMPYSP TGLDPAAQLR GAEGEENRYK
QQVAQAQLRS NYLRSLGDNA QNNDERLCII CRSDITIGAL TKCGHQYCKE CLKEWLKKSS
TCPLCKAHLD HFSIYFFTFT RDDLKASLLT ANEADTEAEK EEFKKEIYSI YKPMNDETLQ
EIQDIPIQKM YGSKVDLIVK QALWLKNKIS NVQIVVFSQW LELLEVLAIA LKQNGLKCIG
AKNSLKLEKG SGRNKEKLTD VELFKSDPSI TCFLLNARAQ AAGLTLVNAS HVFLCEPLVN
TALELQAISR IHRIGQQHKT TIWMFTIKDT VEESVLRLST RKRMRLVENK STEDDGKVLD
QNITSDIIDQ EELSKTTKGM VHKNIIGGEV VSNEDLWGSI FSAKAQSF
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