ID A0A178EX06_TRIRU Unreviewed; 1760 AA.
AC A0A178EX06;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=A7C99_4066 {ECO:0000313|EMBL:OAL64632.1};
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551 {ECO:0000313|EMBL:OAL64632.1, ECO:0000313|Proteomes:UP000243015};
RN [1] {ECO:0000313|EMBL:OAL64632.1, ECO:0000313|Proteomes:UP000243015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCC(F)T1i {ECO:0000313|Proteomes:UP000243015};
RA Zhan P., Tao Y., Liu W.;
RT "Genome sequencing of Trichophyton rubrum CMCC(F)T1i isolated from hair.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAL64632.1}.
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DR EMBL; LHPM01000015; OAL64632.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:TERG_05024; -.
DR VEuPathDB; FungiDB:TERG_05025; -.
DR VEuPathDB; FungiDB:TERG_05026; -.
DR Proteomes; UP000243015; Unassembled WGS sequence.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IEA:UniProt.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:UniProt.
DR GO; GO:0043596; C:nuclear replication fork; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd17757; MCM6; 1.
DR Gene3D; 1.20.58.870; -; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008049; MCM6.
DR InterPro; IPR041024; Mcm6_C.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF43; DNA REPLICATION LICENSING FACTOR MCM6; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF18263; MCM6_C; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01662; MCMPROTEIN6.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF103481; Multidrug resistance efflux transporter EmrE; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000243015};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1640..1662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1674..1694
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1700..1718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1073..1281
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 99..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1393..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1520..1581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1721..1760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1528..1581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1760 AA; 193063 MW; DBFF8E089DAEDD68 CRC64;
MDDAGSAPSH SRSVSIPPAE AASRHLELAL QRLVNHRAKS NRAAHTAKMI EQRQAATETA
VSAPGKVLLA GGYLVLDRDY TGTVCALDAR IHVVVQQQSV KRRPSAAETQ TEGHAQLNSG
QAAADGAVGA AEIPPATVSG GAQEEAVQDT VTVKSPQFVD AVWKYKIQRS DNGGGVRAVQ
CDDGPRNPFV ETALNYALTY VSYVSASHNI GSLVVTILAD DDYYSETTAS GSPNSGYAGF
KKFGVRLQDA HKTGLGSSAA LVTALVSALV VHRTVQPEKL SQNKAKLHNL AQAAHCAAQG
KIGSGFDVAA AVYGSCYYRR FSPSVLAGLG EPGSAGFEDR LFAVVEDVNA GAPWDTECHD
VGFKLPMGIR MVLCDVDCGS QTPGMVKKLL RWRDENREEA DILWANLQLN NEKILFELRK
LLHSPGADFN ELRNLLLKSR MWIKTMTKKS EVPVEPMVQT ELLDSLGKLD GVIGGVVPGA
GGYDAIALLM IDDPGVYNEV RAHLNDWQST VEDDFGGKIE RVRLLGVGYG SEGILNELPV
RRELYATFFF LLLIKTSTFN PKDEQKRTTR DIDDTGCCSR SIFLLLHVNA NENFVMSSIL
DQLMTSEADG GPMLGSSQRS DAPPTSSRLP LASESNAPMS EAPEFADDQV VGAGSRSSRR
PRHPMYGPGP PPVRDVAGEK VQQAFEEMLE THVEDPMSSG APPTSSEMLS DKYYISQIHG
MQKLQLSTLY VDFTHLNSNQ VLADAIINQY YRFQPYLTKA LHNLIAKYEP QYFRAHKQLG
SHSSQAGTST VALDSTEPDS LAGKTRYQQT DKVFTLAFYN LPLVSRLRQL RTAQIGTLCS
ISGTVTRTSE VRPELALGTF ICGNCNNVCP DIEQSFKFTE PTQCTSATCG NRIGWRLDIR
KSTFVDWQKV KLQESAHEIP TGSMPRTMDV ILRGEMVDRA KAGERCIFTG MLVVIPDISQ
SGLPGVRPEA TKDYGNFRGG DVGGNGVSGL KSLGVRDLTY RLAFLACMVT PDLSTPGQSS
NQNLSGQAPN ILSSLNQVEA PDDVEEEAQT ALLHSLTPYE VQDLKQMVHS DYIYARLIDS
IAPMIYGHHQ IKKGLLLQLV GGVSKRTVEE SMQLRGDINI CIVGDPSTSK SQFLKYICKL
HPRAVYTSGK ASSAAGLTAA VVKDPETGEF TIEAGALMLA NGGGICAIDE FDKMDISDQV
AIHEAMEQQT ISIAKAGIHT TLNARASILA AANPIGGRYN PKTTLRGNLN FSAPIMSRFD
LFFVIRDDPN EAVDRNLADH IVNVHMNRDE AVKPELSTEQ LQRYIRFART FRPVFTEEAR
ALVVEKYKEL RADDAQGGMG RSSYRITVRQ LESLIRLSEA VAKANCVEEV IPRFVKEAYD
LLRQSIVTVE KDDVDVDDEE VPPAATNQPD TEDHNMMDED ENTQQNTDVP QANGENRTQK
VKITYDKYMR VLNVLVRRVN DDENRSGEGV EEEDLILHYL EQVESELNNE EELEQERSLV
TKILRRMVKD NILMQIRGDG LMETDGGEQP AEEPKVDNER QPTETDPQWE QAEKWRGEGM
SRASRAGKEE PELHEPRKDE KMSQHSKWLM LALASGAFAA TNGLFAKLTT TELTTSISRA
ISHIFSSSEA TTTLDVIVEY LVRAAFFGLN LLSNFIMWTL FTRALTASPS TTKVTITNTT
ANFLVTGILG MLVFREKVNA QWLIGATLMA AGCIIVGMRE KQKDEESPGT SAGMNEGEDI
GLAENRKSDE DDDLIALEED
//
