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Database: UniProt
Entry: C5FP37_ARTOC
LinkDB: C5FP37_ARTOC
Original site: C5FP37_ARTOC 
ID   C5FP37_ARTOC            Unreviewed;       804 AA.
AC   C5FP37;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   SubName: Full=ATP-dependent RNA helicase Prh1 {ECO:0000313|EMBL:EEQ31890.1};
GN   ORFNames=MCYG_04709 {ECO:0000313|EMBL:EEQ31890.1};
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ31890.1, ECO:0000313|Proteomes:UP000002035};
RN   [1] {ECO:0000313|Proteomes:UP000002035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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DR   EMBL; DS995704; EEQ31890.1; -; Genomic_DNA.
DR   RefSeq; XP_002846972.1; XM_002846926.1.
DR   AlphaFoldDB; C5FP37; -.
DR   STRING; 554155.C5FP37; -.
DR   GeneID; 9230088; -.
DR   VEuPathDB; FungiDB:MCYG_04709; -.
DR   eggNOG; KOG0922; Eukaryota.
DR   HOGENOM; CLU_001832_5_11_1; -.
DR   OMA; KVKVWRH; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
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   CDD; cd17917; DEXHc_RHA-like; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF243; ATP-DEPENDENT RNA HELICASE DHR2-RELATED; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000313|EMBL:EEQ31890.1};
KW   Helicase {ECO:0000313|EMBL:EEQ31890.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000313|EMBL:EEQ31890.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002035}.
FT   DOMAIN          116..304
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          370..543
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          69..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   804 AA;  88727 MW;  5FDB13BFC70A2CB6 CRC64;
     MDSLDSKAEK KEDKEILTSK RKRKRKRSNR HNKGKDENKK PRIVENGDES SPASEGMIKN
     VAASYKKDIP GMKSHSKNGA ANSASNGSSA NLREKAKALY EARKKLPIFG HADEIRAHLR
     RTDVMLLIGE TGSGKSTQVP QFLVDEDWCR PKSAKIKNGK TASVGGCIAI TQPRRVAAVS
     LARRVAEEVG CPLGSASPAS KVGYAVRFDT SVSPNTRIKF MTDGMLLQEM LGDPWLTNYS
     AIVVDEVHER GINVDLLLGF LRNIATGSKE GRGGIPLKIV VMSATADMES LMEFFTEGFS
     QGSKRENESR TEENTDADVR KTGRQSKREK NNQVLSDQIS VCHIKGRQFP VTTIYSPSPV
     PDFVDAALKT IFQIHYKEPL PGDILVFLTG QETVETLEYL VNDYASTMDK ELPNVLAVPL
     FAALPQVAQQ RVFLPTPPRT RKVILATNIA ETSVTVPGVR YVIDCGKAKT KQFRTRLGLD
     SLLVKPISKS AAIQRKGRAG REAAGQCYRL YPEKEYLALP ETNTPEILRC DVSQAILTMK
     ARGVDDIVGF PFLTPPPRDA IEKALLQLFN INALDETGKI SPIGSRIAKL PLTAPLGRVL
     LAGAEKGARC LRDVIDVISC LSVENIFLNT SSEEKKEQAD LARRDLYRRE GDHLTMLATV
     RAYAAENTDR KAWAERHLVS HRAMQAVMDV RKQLLTQCKQ SKLFSDTSFE VDDSTPLGNE
     DPVPILTSFL TGFATNTARL FPDGSYRTLV GNQSVAIHPS SVLFGRKVEA IMYNEYVFTS
     RSYARGVSAV QMNWIGEVHQ GIAE
//
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