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Database: UniProt
Entry: A7TG42_VANPO
LinkDB: A7TG42_VANPO
Original site: A7TG42_VANPO 
ID   A7TG42_VANPO            Unreviewed;      1982 AA.
AC   A7TG42;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=RNA helicase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Kpol_1028p75 {ECO:0000313|EMBL:EDO18799.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO18799.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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DR   EMBL; DS480385; EDO18799.1; -; Genomic_DNA.
DR   RefSeq; XP_001646657.1; XM_001646607.1.
DR   STRING; 436907.A7TG42; -.
DR   GeneID; 5547115; -.
DR   KEGG; vpo:Kpol_1028p75; -.
DR   eggNOG; KOG0952; Eukaryota.
DR   HOGENOM; CLU_000335_2_1_1; -.
DR   InParanoid; A7TG42; -.
DR   OMA; MCSATEF; -.
DR   OrthoDB; 57056at2759; -.
DR   PhylomeDB; A7TG42; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
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; 2.
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:UP000000267}.
FT   DOMAIN          301..489
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          525..735
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1153..1328
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1366..1570
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   1982 AA;  225601 MW;  1B61642D39B1311A CRC64;
     MTTEYSIHSA GSYMQAMQAM MHSVDQYDMK IGVSELPEIN GESDEQVGKT TLIKLAQDRN
     EWDDIFDDFK DLNYEKFVKM VDDVKKCNGV NGGDSSGSTV FKRLVRLAST CSSSLSTGTL
     LKSVLEITFA NEKGQLAEQL LDLVGAENVE LISFVLENRQ LITAHSLEDV IQMTRDIIDS
     SEFDYLTEQE MKDQVIQNAY DAKNQKLDPA RRVIKYPHVY RKYEDGNTSS LAFSGQKFSL
     PIGTTRQSYQ SHEELIIPAA DPDTNKKVFH TRLMSIDSLD HYCRAVFKYK TLNKIQSLVF
     PVAYNTNENM LICAPTGAGK TDIALLTILN IIKQFSQVNE HNELDIQYDD FKVIYVAPLK
     ALAAEIVEKF SEKLAIFDIQ VRELTGDMQL TRAEIQTTQV IVTTPEKWDV VTRKANGDND
     LVSKVKLLII DEVHLLHEDR GSVIETLVAR TLRQVESSQS MIRIVGLSAT LPNFMDVADF
     LGVNRQVGMF YFDQSFRPKP LEQQLLGCRG NAGSRQSREN IDRVSYDKLI EMIQRGYQVM
     VFVHARKETV NSARTYIRIA EQNSEITEFA PDADMKNKYS KELAKNRDKD LRELFQFGFG
     IHHAGMARTD RNLTEKMFKD GAIKVLCCTA TLAWGVNLPA DCVIIKGTQV YDSKKGGFID
     LGISDVIQIF GRAGRPGFGS EHGTGILCTS NDRLDHYVSL LTQQHPIESK LGSKLVDNLN
     AEISLGTVTN VEEAVQWLGY TYLYVRMRKN PFTYAIDWEE LASDPQLYDR RRKMVVTAAR
     RLHSLQMIVF DEISMHFIPK DLGRVASDFY LLNESVEIFN QMCNPRATEA DVLSMISMSS
     EFDGIKFREE EAVELTRLSE SAVECQIGGA LDTAQGKANV LLQAYISQSK IFDSALNSDS
     NYVAQNATRI CRALFLIGIN RRWGNFAKVM LDVCKSIEKR LWAFDHPLCQ FDLPDPIIRQ
     IRDRNPSMDH LMDLEPEEIG ELVHNRGIGN KLFNLISKFP SISISAEIFP ITTNVMRIHV
     NLIPDFKWDF RVHGDVQFFW VLVEESDKSQ VLHFEKYILR KAQLNTVHEM DFMIPLSDPL
     PPQVVVKVVS DTWIGCESTF PISFQHLIRP YNETLQTKLL RLKPLPTSAL NNPLVQSIYP
     FKYFNPMQTM TFHTLYNTND NVFVGSPTGS GKTVVAELAI WHAFRDFPGK KIVYIAPMKA
     LVRERVDDWR KRITPVTGDR VVELTGDSLP DPKDVRDATI VITTPEKFDG ISRNWQTRKF
     VQNISLVIMD EIHLLASDRG PILEMIVSRM NYIASQTSNP IRLLGMSTAV SNAYDMASWL
     GVKSNGLFNF PSSVRPVPLN MYIDGFPDNL AYCPLMKTMN KPAFMAIKQH SPVKPALIFV
     SSRRQTRLTA LDLIHLCGME DNPRRFLKID DDGELQYYIS QITDDTLKLS IQFGIGLHHA
     GLVEKDRDIS HQLFQKGKLQ ILVATSTLAW GVNLPAHLVV IKGTQFYDKK VLGYVDMDLT
     DILQMMGRAG RPAYDTTGTA IVYTRENKKM FYKHFLNVGF PVESSLHKVL EDHLGAEINS
     GTVCNKQDAI DFLRWTFFFR RAHHNPTYYG ILEDTSAAGV HKHISELIDK SIEELVSSRC
     VEVYGEDIEA TPFLSIASYY YISHKTIRTL LAQIKDNARF IDVLKWLSLA EEYNELPVRG
     GETIMNEEMS AQLRYPAETI FTGEYELPIF DTHVKAFLLL QAHLSRVNLP IADYIQDTVS
     VLDQSLRILQ AFVDVASELG YFNTVLTIIK AMQCIKQGYW YEDDPASALP GCELKRFNDI
     EFLESGHPLD AKSQSSKVNL NGIARMGFKK LQNLAIQNDL SYADLKNDDE VSEEVLAERI
     QRKFISVCQR LPALDDVKVE KQEDNTKVVI TSKHHSKQNN REFEVYCDKF PKMQKESWFC
     IGYKNNELYM IKRCHPQQDK DKTVNITCEF IVTEELRGKD MDFLLINDAL SLEYHINHQL
     LK
//
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