ID J7RBW3_KAZNA Unreviewed; 1965 AA.
AC J7RBW3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CCK72395.1};
GN Name=KNAG0K00270 {ECO:0000313|EMBL:CCK72395.1};
GN OrderedLocusNames=KNAG_0K00270 {ECO:0000313|EMBL:CCK72395.1};
OS Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 / KCTC
OS 17520 / NBRC 10181 / NCYC 3082 / Yp74L-3) (Yeast) (Saccharomyces
OS naganishii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071383 {ECO:0000313|EMBL:CCK72395.1, ECO:0000313|Proteomes:UP000006310};
RN [1] {ECO:0000313|EMBL:CCK72395.1, ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2] {ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Kazachstania naganishii.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; HE978324; CCK72395.1; -; Genomic_DNA.
DR STRING; 1071383.J7RBW3; -.
DR eggNOG; KOG0952; Eukaryota.
DR HOGENOM; CLU_000335_2_0_1; -.
DR OMA; MCSATEF; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000006310; Chromosome 11.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0010467; P:gene expression; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd18020; DEXHc_ASCC3_1; 1.
DR CDD; cd18022; DEXHc_ASCC3_2; 1.
DR CDD; cd18795; SF2_C_Ski2; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF13; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 2.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006310}.
FT DOMAIN 298..486
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 555..732
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1150..1325
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1363..1568
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1965 AA; 223837 MW; 9656F8EC60443042 CRC64;
MSTSYLADSS KSYMIAMQSM VDAVKTYHMD AIHTPPPPID KEASDTEFEN AEKPKKTQLA
VLAQDRNKWD NIYDKFSDIS FSKLETIVSS LAKDTTNAVY KTLSDLFDKC SSNLDKNVLI
ESVLHIIYSH TGVELQKELL DFLGDENIEL ISFLIEHSST LVSRAFDQTM YLITSSDDPD
KLLTEQDIMR QVSENAKRAK NEKLNQAIKI VKYPHVFRKH EEGSTSSLSF SGHKYSLPIG
TTRTSFQTHE EIIIPPADQK NSVNSLYTKL KKVDDLDHYC KAVFTYETLN QIQSLVFPVA
YNTNENMLIC APTGAGKTDI ALLTILNTIK QHSFINSEQE LDIQYDDFKI IYVAPLKALA
AEIVSKFSEK LAVFDVKVRE LTGDMQLTKG EIMETQVVVT TPEKWDVVTR KANGDNDLVS
KVRLLIIDEV HLLHEDRGSV IETLVARTLR QVESSQSMIR IIGLSATLPN FMDVADFLGV
NRQVGMFYFD QSFRPKPLEQ QLLGCRGKEG SRQSKENIDR VAYDKLLGMI ERGFQVMVFV
HARKETVKSS RNFIKLAQAN HEVDIFAPSP ASKEAFSRQL AKNRDKDLKE LFQFGFGCHH
AGMSRSDRNL TEKLFKDGAI KVLCCTATLA WGVNLPADCV LIKGTQVYDS KKGGYVDLGI
SDVIQIFGRA GRPGFGSSNG TGILCTSSDR LDHYVSLLTQ QHPIESRFGA KLIDNLNAEI
SRGTVTNVDE AIQWLGYTYM FVRMRKNPFT YGLSWEEIAN DPQLHERRRK MIISAARKLH
SLQMIVFDEV SMHFIPKDLG RISSDFYLLN ESVEIFNQMC DPRATEADVL TMISMSSEFD
GMKYREEESK ELKRLTEVSV QCQIGGDMAT PSGKTNILLQ AYISQSRIMD SALASDSNYV
AQNSVRICRA LFLIGVNRKW GNFASVMLNI CKSIEKRLWA FDHPLSQFDL PENILRQVRQ
RNPSMDHLLD LEPNELGELV HNQKMGHKLY RALGCFPKID IDTEIFPITA SVMRIHVSLQ
PTFTWDRRVH GEVQFFWVFV EESDKSQILH YQKFILNRKQ MSNVHEMDFM IPLSDPLPPQ
VVVKVVSDTW IGCESVSAIS FQHLIRPYNQ TLQTRLLRLR PLPIAALKNP LVESMYHFKY
FNPMQTMTFH TLYYTNENVF IGSPTGSGKT VVAELAMWHA LREFPGSKIV YIAPMKALVR
ERVDDWRKKI TPITGDRVVE LTGDSLPDPQ DVRDATIVIT TPEKFDGISR NWQTRKFVQN
VSLVIMDEIH LLASDRGPIL EMIVSRMNYI SSQTSKPVRL MGMSTAVSNA YDMASWLGVK
NNGLYNFPSS VRPVPLKMYI DGFPDNLAFC PLMKTMNKPA FMAIKQHSLT KPALIFVASR
RQTRLTALDL IHLCGMEENP RRFLNIDDEE ELQYYLSQIT DETLKLALQF GIGLHHAGLV
EKDRSISHKL FQNNKIQILI ATSTLAWGVN LPAHLVIIKG TQFFDAKIEG YRDMDLTDIL
QMMGRAGRPA YDTSGTAIVY TKESKKMFYK HFLNVGFPVE SSLHKVLDDH LGAEISSGTI
TSKQEALDFL NWTFFFRRAH HNPTYYGINE DHSPSGISKH LSELIDNTIE RLSNSQCVEI
QGKTIVPTPF LSISSYYYIS HLTIRQLLRH INNEATFKDV LKWLSLAVEY NELPVRGGEI
IMNVEMSAQS RYPVESTFTG DDELPMWNPH LKAFLLLQAH LSRVDLPIAD YIQDTVSVLD
QSLRILQAYI DVASELGYFR TVLTLIKVMQ CIKQGYWYED DPVGILPGVD LKRITDIKFG
ENGYPVEQDR AKFDRLLGLD SIGRFGIKKL QSFAQKYNFD ERYTKKFINV CQRLPVLDGM
QFQQVDNDSS KLLVTAKHVS NKKSRGFEVY CDKFPKTQKE LWFCIGYQRD ELLILKRCQP
RQAGKDIVLK ADIIVPDELL DEELDFILIN DAMDLSYNAH YVPKL
//