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Database: UniProt
Entry: A0A0D6KPC4_9CYAN
LinkDB: A0A0D6KPC4_9CYAN
Original site: A0A0D6KPC4_9CYAN 
ID   A0A0D6KPC4_9CYAN        Unreviewed;       922 AA.
AC   A0A0D6KPC4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Helicase {ECO:0000313|EMBL:EKF01304.1};
GN   ORFNames=FDUTEX481_07952 {ECO:0000313|EMBL:EKF01304.1};
OS   Tolypothrix sp. PCC 7601.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1188 {ECO:0000313|EMBL:EKF01304.1, ECO:0000313|Proteomes:UP000032761};
RN   [1] {ECO:0000313|EMBL:EKF01304.1, ECO:0000313|Proteomes:UP000032761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX   PubMed=25953173;
RA   Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA   Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA   Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA   Kehoe D.M., Weinstock G.M.;
RT   "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT   Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT   PCC 7601.";
RL   Genome Announc. 3:0-0(2015).
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:EKF01304.1}.
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DR   EMBL; AGCR01000041; EKF01304.1; -; Genomic_DNA.
DR   RefSeq; WP_045871070.1; NZ_JH930362.1.
DR   AlphaFoldDB; A0A0D6KPC4; -.
DR   STRING; 1188.FDUTEX481_07952; -.
DR   PATRIC; fig|1188.3.peg.4953; -.
DR   HOGENOM; CLU_302045_0_0_3; -.
DR   OrthoDB; 9814088at2; -.
DR   Proteomes; UP000032761; Unassembled WGS sequence.
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   GO; GO:0006793; P:phosphorus metabolic process; IEA:UniProt.
DR   CDD; cd18793; SF2_C_SNF; 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; 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   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45766:SF3; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A-LIKE PROTEIN 1; 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.
DR   PROSITE; PS50035; PLD; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:EKF01304.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          121..148
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          236..403
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          573..755
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   922 AA;  106463 MW;  82CB778E50A52925 CRC64;
     MNEEIENEEN GERGTLRESW FERKKALEYI SHYFQTAKKE IRIASGFFTI RGWGLVRRYT
     KGKRVYILVG LDDPGEERAR QALIDDILRD LRTGLDKDRR QTVLDLIEKM LQGRLHLVDA
     RATEHHAKLY IVDHKVVIMA SSNLTQRGLM EQVEAGNIIT KRREVVALAN EFDAYFAEAK
     DITQELLEVL QRWLNFVRPW DVYLKTMLAL EDIQPIKSNY KKQPVSYQVD MIAQTLRQIK
     ESGGSMLVAS TGLGKTVVAV HVALHLRNDD LIDNVMVIGP KAVRSNWTRE MRDAGLPCEY
     FVYQALDKSG SDQDSSLELF EEIQKNLHEQ RWLIIFDESH YFRNRFKQDL FNMKKNPAER
     RAFLRLKELL NKSSNTKVLL LTGSPYARDE SNLNNQLYLL PHTAELSALF DENYVDGARA
     WHINKTDDFI HLPVASQLTT PHVAKYYSQL ENQDNYIIFG TEKRYIPKIV LYSVNFPLLL
     DKELVEAIKK GYFDLDSRNP MFRECIRRLV KIAWASSPLA LRGVLESVVD TPGGKNEYKL
     GKLQFVSAQQ ERQSFLNPLI EKLANLDFKS DLKLEALYII IQELRQNSEK AIIFCERRAT
     VVYLAQALEQ MFPALKVVAT IEQSENEEKY QMKETNEIEK LIKKFAPISN NAENISEESY
     DVFISTDAHG VGVNMQDASA VINYDIDWTP IGPVQRAGRI LRFWHYPRTV KVYTFVPNLT
     QETDLKYDLV RIRQRWENLM LRHGESRKLT DLPVLTIANS QEINMPELAS QVTIKSGQLD
     LDVLADLDIS PFFQHTAKLQ MHRDYARTIL SDIVSAKLTQ DSEPSIYVLV NQNQKYHALV
     YTPKNQQVRE PDIIKILNLI ACNEDTEIAV VDYGLVEELS DACIRTWCNK QGISPEEVER
     ICTLYLKPES EPDGLERLLN AE
//
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