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Database: UniProt
Entry: A0A168MKY2_ABSGL
LinkDB: A0A168MKY2_ABSGL
Original site: A0A168MKY2_ABSGL 
ID   A0A168MKY2_ABSGL        Unreviewed;       670 AA.
AC   A0A168MKY2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-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   Name=ABSGL_04285.1 scaffold 5264 {ECO:0000313|EMBL:SAL98729.1};
OS   Absidia glauca (Pin mould).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL98729.1};
RN   [1] {ECO:0000313|EMBL:SAL98729.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL98729.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00000600};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000256|ARBA:ARBA00000600};
CC   -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007913}.
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DR   EMBL; LT552303; SAL98729.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168MKY2; -.
DR   STRING; 4829.A0A168MKY2; -.
DR   InParanoid; A0A168MKY2; -.
DR   OMA; TIIHGPP; -.
DR   OrthoDB; 170190at2759; -.
DR   Proteomes; UP000078561; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0003723; F:RNA binding; IEA:InterPro.
DR   CDD; cd18044; DEXXQc_SMUBP2; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 2.40.30.270; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   InterPro; IPR048761; SMUBP-2_HCS1_1B.
DR   PANTHER; PTHR43788:SF19; DNA-BINDING PROTEIN SMUBP-2; 1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF13086; AAA_11; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF21138; SMUBP-2_HCS1_1B; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022806};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078561}.
FT   DOMAIN          188..456
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|SMART:SM00487"
FT   DOMAIN          206..552
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   670 AA;  74507 MW;  511E9E713BBCE3A1 CRC64;
     MEAFIDHQVQ LVQEEKRIDV EDTQKLLSSY SPIQLQKRGM ALLGLRVTAM RTGLGGKSLI
     DLELGQSNRQ IPTFPTHKIT TGDIIGLDEY KKDKPSKKAA PWSGVVLRVT DTRITVALSQ
     DMDEDLPPEV QDRCQIVKLA NNVTYERMIK GLEQLKVNAM AGSSRMTEVL LGKQKPATVE
     DVPDLAFFDT TLNDSQKEAV RFALGAQDIS LIHGPPGTGK TYTLVEIIRQ LSVKQNKKVL
     VCGPSNVSVD NLVERLARHR MNLVRVGHPA RILPTVLEHS LDVITRTCDS GKIVADVRKE
     MDDTLGKIGK SKSRAERRLL YGQIKELRKD YRVRERKVVD EVISGAQVVL STLNGCGSRT
     MMKREFDIVI IDEATQALEA ECWIALQKGQ KAILAGDHLQ LPPTIKTPSK PMKKTGSKNG
     LSTTSDLSTT LFDRLLAMYG NKIKKMLMVQ YRMHQKIMEF SSKELYDNLL VADDSVASHL
     LQDLPDVSSS ENTEVPVVLL DTSDTGLGHE VTDDDSLDDQ SKANELEVSL AVHHVEALLE
     DGLTQDQIGI ITPYAAQVSR LVRDVRDKWP AIEIGTVDGF QGREKEAILL SLVRSNDDGQ
     VGFLQEKRRL NVAMTRAKRH LCVICDSETL AGNKGGTASS SSRVDGGFLK RWMNWLCEES
     DLRFSDFVLQ
//
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