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Database: UniProt
Entry: A0A162R6H6_MUCCL
LinkDB: A0A162R6H6_MUCCL
Original site: A0A162R6H6_MUCCL 
ID   A0A162R6H6_MUCCL        Unreviewed;      1149 AA.
AC   A0A162R6H6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Homeodomain-like DNA binding domain-containing transcription factor {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=MUCCIDRAFT_136222 {ECO:0000313|EMBL:OAD08780.1};
OS   Mucor lusitanicus CBS 277.49.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=747725 {ECO:0000313|EMBL:OAD08780.1, ECO:0000313|Proteomes:UP000077051};
RN   [1] {ECO:0000313|EMBL:OAD08780.1, ECO:0000313|Proteomes:UP000077051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 277.49 {ECO:0000313|EMBL:OAD08780.1,
RC   ECO:0000313|Proteomes:UP000077051};
RG   DOE Joint Genome Institute;
RA   Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA   Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA   Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA   Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA   Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA   Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA   Mccluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA   Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA   Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA   Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA   Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA   De Vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA   Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA   Gabaldon T., Grigoriev I.V.;
RT   "Expansion of signal transduction pathways in fungi by whole-genome
RT   duplication.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OAD08780.1}.
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DR   EMBL; AMYB01000001; OAD08780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162R6H6; -.
DR   STRING; 747725.A0A162R6H6; -.
DR   VEuPathDB; FungiDB:QYA_136222; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000077051; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014012; HSA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029295; SnAC.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF973; ATP-DEPENDENT HELICASE BRM; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07529; HSA; 1.
DR   Pfam; PF08880; QLQ; 1.
DR   Pfam; PF14619; SnAC; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00951; QLQ; 1.
DR   SMART; SM01314; SnAC; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
DR   PROSITE; PS51666; QLQ; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077051}.
FT   DOMAIN          1..35
FT                   /note="QLQ"
FT                   /evidence="ECO:0000259|PROSITE:PS51666"
FT   DOMAIN          198..279
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          377..542
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          685..874
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1024..1094
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          57..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          959..991
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1114..1149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        968..991
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1132..1149
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OAD08780.1"
SQ   SEQUENCE   1149 AA;  133614 MW;  16F6993C0604D6C5 CRC64;
     FLPHQLNALK NQIIAYKLLI KNAPLPPRLQ QAVLAPSNSL LAQSSPPMTP IVTPKVIHQQ
     PHQERPQSVP PTPPTPQHQE FDAYLPPTAL LANPITSYAH ASRHQRILIP SLLPAGIDPQ
     AIRSDREKRM LARMTHQYQQ PATHVQEHIR SKALKLYQKQ SQLRKEFVQG VEKSTVLATS
     AHHTMFKRTK RVSRLDSQQV EAVEQVQRRQ QEAYIQEAKH NRLHALYQHG SALSHESKLK
     RNTLTQLGRA VLHYHQSVAK AEQKKMERIA KERMQALKNN DEEAYLRLLD QAKDTRLTDL
     LRQTDLFLQS LTASVVEQQQ STGIPHQEHL KQQQQHEVSS ADYFRITHKI HEDVSQPAIM
     VGGQLKQYQV RGLQWMISLY NNNLNGILAD EMGLGKTIQT ISLITYLIEK KQQNGPFLII
     VPLSTLPNWT MEFDKWAPSV SKIVYTGPSH QRKELASMVR SGQFQVLLTT FEYIIRDTQA
     LCRTKWLYLI MDEGHRMKNA NAKLTVTLRQ KFHARYRLIL TGTPLQNNLP ELWALLNFIL
     PKIFKSVKTF EEWFNTPFSN QGAHDKVDLN EEEQLLIIKR LHKVLRPFLL RRLKSDVESE
     LPDKVEKVIK CKLSSLQVKL YHQLKNTHVN SNGYFPIAYK KLNNTIMQLR KVCNHPFIFE
     GVENALNPKG KANELLYRCS GKLELLDRML PKLQRTGHRV LIFFQMTGIM NIMEDYLNWR
     HYRYLRLDGN TRSEDRSTLL HHFNQPDSPY FIFLLSTRAG GLGLNLQSAD TVILFDSDWN
     PHQDLQAQDR AHRIGQTKEV RIFRLVTSNS IEERILATAQ YKLGIDGKVI QAGKFDNRST
     EADREALLRT LLEDKMQEEA WDEDASNQEL NNVLKRSDQE LSVFEMMDSE RRSHPSQQGE
     RLIQENELPD VFDIKDHVAV DLSPVMPDTD RSRKAKQNIK YDDGLTDAQF MRAIQEGQLM
     PPRIENKRPL LSTDKSSRKR SKVEPEKTPE VDTVSRLMRK QLTEIFEACY KEVEKSIAVE
     DDGYYRKRCE LFMDLVDKRD YPDYYTLIKN PISMNMIKQR MHSFYYEDIH EFKNDFAVMF
     ENARIFNEEG SAVYEDANEM EKILNDELEK QCPRGVLPPY RKRKTAIEQD FVEDPFDGDD
     HDEDQEDDE
//
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