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Database: UniProt
Entry: A9NH67_ACHLI
LinkDB: A9NH67_ACHLI
Original site: A9NH67_ACHLI 
ID   A9NH67_ACHLI            Unreviewed;       986 AA.
AC   A9NH67;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Putative DNA/RNA helicase {ECO:0000313|EMBL:ABX81697.1};
GN   OrderedLocusNames=ACL_1087 {ECO:0000313|EMBL:ABX81697.1};
OS   Acholeplasma laidlawii (strain PG-8A).
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Acholeplasma.
OX   NCBI_TaxID=441768 {ECO:0000313|EMBL:ABX81697.1, ECO:0000313|Proteomes:UP000008558};
RN   [1] {ECO:0000313|EMBL:ABX81697.1, ECO:0000313|Proteomes:UP000008558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG-8A {ECO:0000313|EMBL:ABX81697.1,
RC   ECO:0000313|Proteomes:UP000008558};
RX   PubMed=21784942; DOI=10.1128/JB.05059-11;
RA   Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA   Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA   Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA   Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA   Ladygina V.G., Govorun V.M.;
RT   "Complete genome and proteome of Acholeplasma laidlawii.";
RL   J. Bacteriol. 193:4943-4953(2011).
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DR   EMBL; CP000896; ABX81697.1; -; Genomic_DNA.
DR   RefSeq; WP_012243028.1; NC_010163.1.
DR   AlphaFoldDB; A9NH67; -.
DR   STRING; 441768.ACL_1087; -.
DR   GeneID; 66294072; -.
DR   KEGG; acl:ACL_1087; -.
DR   eggNOG; COG1061; Bacteria.
DR   eggNOG; COG3886; Bacteria.
DR   HOGENOM; CLU_005588_1_1_14; -.
DR   OrthoDB; 9802848at2; -.
DR   Proteomes; UP000008558; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR   CDD; cd09204; PLDc_N_DEXD_b2; 1.
DR   CDD; cd18799; SF2_C_EcoAI-like; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR021835; DUF3427.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR025202; PLD-like_dom.
DR   PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR   PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR   Pfam; PF11907; DUF3427; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000313|EMBL:ABX81697.1};
KW   Helicase {ECO:0000313|EMBL:ABX81697.1};
KW   Hydrolase {ECO:0000313|EMBL:ABX81697.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:ABX81697.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008558}.
FT   DOMAIN          249..399
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          448..606
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   986 AA;  113985 MW;  F04219E50F3E6FB7 CRC64;
     MKINQQPVEL LTNNLKSSFY HYLKDALKRC QSFSFSVAFI SDSGLQLIID DLIDAGKRGV
     KGKLITTNYE FGTTPRALEM IGDQNYIEAK LYDALTSIRK FHTKAYIFDM GNHFEIVVGS
     SNMTQYALKN NHEWNLKYVA KNDDKTKENI IDNFDELFND PKSLQLTPKV IKEYKTLYES
     KRMVDEGKKA MLDFFFEFIK RNPDHEIVDA MQGFNIDENN ELKDFIEQVD VNEIKPNEMQ
     EMALEGLNNI RNSGGNKALI IAATGTGKTY LSAFDVFQLR PKKVLFVVHR GKILRDALRT
     FKTIMPEVSM GEFVGSKKDL ESDYLFASVQ TISKIDNLNL FDPSYFDYII IDEAHRSAAD
     SYQRITSYFT PKFLLGMTAT PERTDSRNIY ELYDNQIAVE IRLRQALEKE LVVPFHYFGI
     EDATTDIQNI NLNTEIDKLA EKLNIKARVE LIIENIKKYK HSGDKTKALG YCVNIAHAEY
     MANAFNERGL VSIALTGGTA ELDREDTIRR LEDPNDPLSY IFTVEIFNEG IDIPSVNLIL
     MLRPTNSSII FTQQLGRGLR KYKDKEYLTV LDFIANHNKN FLLPIALIGD KAYDKDDLIV
     STANDFFDIP GDTFISLNKV SKERILAQLE ATDFNEITYL KEAYLDKKKN LGRVPRLTDF
     AFDEFDPIRF IKKKKSYISF VASQEKGILE DSSLHDSFIK LIGYLDSMLP IKRPYEYAIL
     RELTHYKALE MNELFSKMKK YIDNPNLDSF NHSVKNLLLE FGSVTDKKNN IKVIEKSNSQ
     IRVSDDFSNI FENVRYTDII NNTISYGLAR YHHEFDRKVA PYPFVDLYHE YSKTEIYTLS
     LFDKNVSGLL MSGLIRIEKE YYLTVNLVKG DVHDSINYDD YFIDQNTFHW QSPGSTRTTN
     ETGKNLVNHK ELGFNLHLFV RKSATEATKG KGYSRDFTYL GKVFVEEYVG EAPISFKLKF
     EHRVPNDIYQ RLTYDYTKEK ENEKTN
//
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