ID F2SK80_TRIRC Unreviewed; 698 AA.
AC F2SK80;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=ATP-dependent RNA helicase MRH4, mitochondrial {ECO:0000256|ARBA:ARBA00039952};
DE AltName: Full=ATP-dependent RNA helicase mrh4, mitochondrial {ECO:0000256|ARBA:ARBA00039691};
GN ORFNames=TERG_03433 {ECO:0000313|EMBL:EGD87183.2};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD87183.2, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
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).
CC -!- FUNCTION: ATP-binding RNA helicase involved in mitochondrial RNA
CC metabolism. Required for maintenance of mitochondrial DNA.
CC {ECO:0000256|ARBA:ARBA00037267}.
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DR EMBL; GG700650; EGD87183.2; -; Genomic_DNA.
DR AlphaFoldDB; F2SK80; -.
DR STRING; 559305.F2SK80; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_18_0_1; -.
DR InParanoid; F2SK80; -.
DR OMA; HSTIDFI; -.
DR OrthoDB; 1333884at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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 PANTHER; PTHR47960; DEAD-BOX ATP-DEPENDENT RNA HELICASE 50; 1.
DR PANTHER; PTHR47960:SF1; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000008864}.
FT DOMAIN 250..470
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 517..698
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..41
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 698 AA; 77934 MW; 96E587F85B201738 CRC64;
MAESLGAAKY SAEAYPGPAQ ANSKVKKKIL KKAKGNQRRR QRRQHFSEVI EAAAGISEML
SITRASLLPV GEALQPWRQL SRAASTAHAR RKPSRMRLSP NVAKSVLPDE KSKKSDRFEN
SPFGAMNRTS VRLRDNTRPR SDAELRRAAK PKFRDQGKEK EKSEESWMKP LKMQIALTPV
PYNRRMAIKE KIADITSFDQ FPLLDVVREA VYKNALVGME DITPTPIQRV AIPTLLGNNN
KTPDPAAQTD DLAPKYDQFL LAAETGSGKT LAYLVPVLDA LKHAEAFQKE QDKIEADEKA
KKEQEEKERR EKNNIFELES PELTTPDTYQ DVAKPRVIIL VPTSELVNQV GHLVKQLSHT
IKFRSALISS SQTPRRIRNS LFNPAGLDVL ISTPHLVSSI AESNPYILSR VTHIIADEAD
SLFDRSFSPI TNSIIERAAS TLKQLILCSA TIPRHLDNRL RELYPNIRRL VTPNLHAIPR
RVQLGVVDVD KEPYHGKKSL ACADVVWSLG KAGSGDDGDA FARITGTPET KHIIVFVNER
ESAEEVAGFL ASKGIDAVAL TRDTSEKRQA EILNEFTQAK PQLSEEDKKL LMKSKQLDSG
SIPFLRNDEP KKPNSTKSLD NTKVLVITDL GSRGIDTVAV RNVILYDVPH STIDFIHRLG
RLGRMGRRGR GIVLVNKKDR KDVVKGVREA MFRGQALI
//
