ID V5EWE9_KALBG Unreviewed; 1730 AA.
AC V5EWE9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=M-phase inducer phosphatase {ECO:0000313|EMBL:EST09900.1};
GN ORFNames=PSEUBRA_SCAF1g00347 {ECO:0000313|EMBL:EST09900.1};
OS Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST09900.1, ECO:0000313|Proteomes:UP000019377};
RN [1] {ECO:0000313|Proteomes:UP000019377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA Goldman G.H.;
RT "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT high producer of endo-1,4-xylanase isolated from an insect pest of
RT sugarcane.";
RL Genome Announc. 1:E0092013-E0092013(2013).
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DR EMBL; KI545851; EST09900.1; -; Genomic_DNA.
DR RefSeq; XP_016294889.1; XM_016435909.1.
DR STRING; 1365824.V5EWE9; -.
DR eggNOG; KOG0952; Eukaryota.
DR HOGENOM; CLU_000335_2_2_1; -.
DR OMA; MCSATEF; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000019377; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase 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; cd18795; SF2_C_Ski2; 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; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
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; 1.
DR Pfam; PF02889; Sec63; 1.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
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:UP000019377}.
FT DOMAIN 168..362
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 393..598
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 36..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1609..1632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1667..1708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1686..1708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1730 AA; 192419 MW; E5E7D28D99CFBC94 CRC64;
MSIQDHLQPH IPGSQVVVQT QEERQQARRF KNDLRKANRQ QVVDPSDSIR TYTPEELERI
REESLAAAAN RPLYTGTATG GDDVRYPHVF SSGAQGNVLS VFGQRFALPL GTLREEKEFY
EEVTIPPPRT VPMRTDERYI PIPEMDPICR GAFPGYKSLN RLQSAVYPLA YKTNENLLVC
APTGAGKTDV AMLTVMRAIS QYARNLEPTA GNAAAGFDIQ KNDFKIIYVA PMKALAAEIV
RKFSKRLQYL GIKVRELTGD MQMTRQEIAE TQMIVTTPEK WDVVTRKPTG EGELATKVRL
LIIDEVHLLH DERGSVIETI VARTLRLVES SQSLIRIVGL SATLPNYVDV ADFLRVNRWQ
GLFYFDSSFR PVPLQQHFIG VKGKVGSQQS RANLDKACFE KVSELVQAGH QVMVFVHARK
ETVKTSQTLR EMFRDEDMSD IIRDATEANP RKAFFKRELQ SSRNREMKEL FDYGFGIHHA
GMLRSDRTLS ERMFEAGVTR VLCCTATLAW GVNLPAYAVV IKGTDVYDSS AGKFVDLSIL
DVLQIFGRAG RPQYEDLGVG YILTSQDRLS HYVDAITSQH PIESKFIGGM IDSLNAEISL
GTVASIRDGV SWLGYTYLFT RMKRTPLTYG MTHDEVADDP HLGAKRQQLV NVGVKKLVEA
KMVEHDPVTD HLKVTDLGRI AAKYYIGYKT IETFNERMHS NMSEADVLGL LSQAADFEQI
VPRDAEEKEL KKMLEAAPCE VSGGIVTSPG KVNILLQAYI SRTYIEDFAL VSDSAYVAQN
GGRIIRSLLE IALSRRWART ASALISMSKA LEKRMWPFDH PLQQSHLNPD TLYAVTERAD
DVEIEELAEM APAEIAKLIR VNARMGQAVK QAARSFPRIS TSASLRPLSH DLLRIDVVVD
RTFEWSERDL GRLHGFYIWI EDEEGSEILQ WVTHLTRVSD SHLSNVTFTV PLRDELPSGL
NLRWMSESWL GSEGTEWISF DDLVVPDKPP AHDSLLDLPL LPVRSALQDE LLCEMYAQKF
SAFNALQTQS FHTLMHTSAN TVLCGPTASG KSTVATMAVW RALQRGDRKC IVIVHNKRDS
LASAMRSTMV AALKQKGIEV KRSSLSKEVL PFVCNDGAGA RVLVTTATSL LRAMEARNDL
VDHVSLLLAE DIHLLDPGYE LMLSKFMWCS ARWNANDTPN TVAAPRIVAT SASLNDVSSL
SQWIGADEFS TYNFHPKDRP SILNTGFQAF DLPHSSGLLK TMVKPAFDKM KETRANGPAI
VVVPSIWQCF TTASDLITKA AAELDTDGFL GLPSEEIESI LPHILDTSLH EALVHGIGIV
HEKTSPQDRT VIEHLYEQGL VKLIIITREC LWSTTLRAAL VIVMSTQYVR ITKTHGTGVS
DRELVDYTLA ELGRAQSLAV RPGTLSNPNP PGKCLVLCQT DKAIMLEKML QTGMPLHSSL
LQDEHRGAPL LPTVLGEIVE GVLTSEEQVI DLLSWTILPS ELMRNPTYYD CAANSTESVA
ARLTQVGIDL VQTLRDLRLI DKTGLKATDL GRALHVQPGS TLLHVVRWFT NLSSKPNRAA
KEMDTFAPSP RNRRDKEVVE DTAVREVIEA TLIQLPVEWR SAFRLSASTA ASNEGEAAEG
DVREGEGEKK DITHGTKHRL LLCLYFAKME LITPATARVL GMSRRARKRL QHEQEQGQNE
GGEANGDAPH GDEEEATDAA HGKAIEKLEQ EQAAEVLALL SSISSVGGRN
//
