ID K5W651_PHACS Unreviewed; 1531 AA.
AC K5W651;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Sec63-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHACADRAFT_137065 {ECO:0000313|EMBL:EKM59388.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM59388.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM59388.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM59388.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
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DR EMBL; JH930469; EKM59388.1; -; Genomic_DNA.
DR RefSeq; XP_007391949.1; XM_007391887.1.
DR STRING; 650164.K5W651; -.
DR GeneID; 18908378; -.
DR KEGG; pco:PHACADRAFT_137065; -.
DR HOGENOM; CLU_000335_2_2_1; -.
DR InParanoid; K5W651; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000008370; 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:0010467; P:gene expression; IEA:UniProt.
DR GO; GO:0090304; P:nucleic acid 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; 1.
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; IPR014756; Ig_E-set.
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; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
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; 2.
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:UP000008370}.
FT DOMAIN 215..406
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 437..640
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1073..1243
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 425..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1531 AA; 171177 MW; 8599D819B974938C CRC64;
MLQDGSHSNL MTTLLSKSQA APLLVSLQSL LSSSRPNESI SEELADIIGF EDIELAMEIL
ESRSSLNREI TQYFANNSSS GFRKVAPDAA FNIDQNGFDE ESARMRMEEA LRANAVRPLY
TGIAHDGPEV LPHVYTSSSM ASGNVLSHLG SRFMLPVGTT RVDHEGYEEV TVPPARPVPP
RVNERSIPVP ELDQLCKGSF PGYSSLNRIQ SIVYPTAYHS NENMLVCAPT GAGKTDVAML
TVLRVLDQYR TVSPTTQSSA SAIGRDDFKI IYVAPMKALA SEIVRKLGRR LQWLSIRVRE
LTGDMQMTKA EISETQIIVT TPEKWDVVTR KPTGEGELAS KVKLLIIDEV HLLNDERGAV
IETIVARTLR QVESSQSVIR IVGLSATLPN YVDVADFLHV NRHIGLFYFD SAFRPVPLEQ
HFIGVRGKPG SPQSRKNLDR TTSEKVSELV HQGHQVMVFV HARKETVKTA LALKEAAMVE
GSLDEFSCED HPSYSMFKRD IGQSRNKEMK QLFDNGFGIH HAGMLRTDRN MMERMFEARA
IKVLCCTATL AWGVNLPAHA VIIKGTQVYD SAKGAFTDLS VLDVLQIFGR AGRPGMESSG
VGYICTTHDK VDNYLDAVTA QNPIESKFTT GMIDALNAEV ALGTVANVHD AIRWVGYTYL
FVRMRKNPLQ YGISWDEVQE DPYLHSKRTS LVNQAANKLA EARMIAFDRP LGNFVITDLG
RIAAKYYIRH NSIEIYNKEF RPKMTEADIL AMLCMSTEFH QIQVRENELK ELEQLMEVVP
CKVKGGTDTS QGKVNILLQA YISGYRPDDF ALVSDQAYAA QNGGRIVRAL LEIAISRKWA
NATSVLMGMS KAIEKRLWPF DQPLKQFPLK QDVFYGLERF ADEYTVAELA DMTAAELGKL
VRLNEKHGMA IRDAVLRFPA AGITYNLRPL GPDVLKISTH VTREFKWDSK VHQTAEPFWL
WVEDHEGLTI FQLSHLVFWQ TTEALDVDFV ISIPSTKPPP SVTIRYVSDR WIGAEGELEI
LLDDLVMPSM TECHAPRLDM PFLSLDVLHD QVLHDALSAR IHSLNGIQSQ IFWSVVNTRL
QSLICAPAGS GKSMIGQLVL WCTLRDAPQG SWALLIAPQR TLLNEFLADL RPVCRLLDIA
TEVISTDFSF ARPPRKSIRI VTANALRALM SKIPPNSRNN FFDALRLVVC ENMELLDSSY
ELAVSTLLHL TQQLPTRFVG ISSSLNDPGD LATWLNADPQ ALHSFRPVDR DQSLTILTHT
FTIPHAAALL KAMAKPAHTA IQGTPREPAI VFVPSRGQCR PVALDLITQC ALEMETTKGY
LSDDVSSDAL ESYLTRLRDR SLVDFVTRGI GFFHEGILRQ DQILILELYA EGIIRILVVP
HDSCWSLPVR AATVVVMGTQ YVHVAPGTSE RHTRDYRLEE LVRMQGRAVR HNGAGHFHLF
CQAEAKDTIL RFLSDGLPLE STLLEGDDLR SWYTDQRERG AIRNRQDGVD ALSFTFLSHR
LQTNPVFYDA PSEGDKSYRL SRIVDDLENS L
//
