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Database: UniProt
Entry: A0A022MN89_9ACTN
LinkDB: A0A022MN89_9ACTN
Original site: A0A022MN89_9ACTN 
ID   A0A022MN89_9ACTN        Unreviewed;      1565 AA.
AC   A0A022MN89;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=CRISPR-associated protein Cse1 {ECO:0000313|EMBL:EYT83384.1};
GN   ORFNames=CF54_07860 {ECO:0000313|EMBL:EYT83384.1};
OS   Streptomyces sp. Tu 6176.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1470557 {ECO:0000313|EMBL:EYT83384.1, ECO:0000313|Proteomes:UP000020060};
RN   [1] {ECO:0000313|EMBL:EYT83384.1, ECO:0000313|Proteomes:UP000020060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu 6176 {ECO:0000313|EMBL:EYT83384.1,
RC   ECO:0000313|Proteomes:UP000020060};
RA   Olano C., Cano-Prieto C., Mendez C., Salas J.A.;
RT   "Draft genome sequence of Streptomyces sp. Tu 6176, producer of the
RT   cytotoxic benzoxazol nataxazol.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated
CC       nuclease Cas3-HD family. {ECO:0000256|ARBA:ARBA00006847}.
CC   -!- SIMILARITY: In the central section; belongs to the CRISPR-associated
CC       helicase Cas3 family. {ECO:0000256|ARBA:ARBA00009046}.
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:EYT83384.1}.
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DR   EMBL; JFJQ01000233; EYT83384.1; -; Genomic_DNA.
DR   HOGENOM; CLU_250011_0_0_11; -.
DR   Proteomes; UP000020060; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   CDD; cd09641; Cas3''_I; 1.
DR   CDD; cd09729; Cse1_I-E; 1.
DR   CDD; cd17930; DEXHc_cas3; 1.
DR   Gene3D; 1.10.132.100; -; 1.
DR   Gene3D; 1.10.3210.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR041372; Cas3_C.
DR   InterPro; IPR006483; CRISPR-assoc_Cas3_HD.
DR   InterPro; IPR038257; CRISPR-assoc_Cas3_HD_sf.
DR   InterPro; IPR013381; CRISPR-assoc_prot_Cse1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR006474; Helicase_Cas3_CRISPR-ass_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01587; cas3_core; 1.
DR   NCBIfam; TIGR01596; cas3_HD; 1.
DR   NCBIfam; TIGR02547; casA_cse1; 1.
DR   PANTHER; PTHR47963:SF9; CRISPR-ASSOCIATED ENDONUCLEASE_HELICASE CAS3; 1.
DR   PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 1.
DR   Pfam; PF18395; Cas3_C; 1.
DR   Pfam; PF18019; Cas3_HD; 1.
DR   Pfam; PF09481; CRISPR_Cse1; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51643; HD_CAS3; 1.
PE   3: Inferred from homology;
KW   Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          28..236
FT                   /note="HD Cas3-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51643"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          964..1008
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1237..1265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..981
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1565 AA;  169848 MW;  2743CD5BA5D6B810 CRC64;
     MTAHSRSEPA PHALSASARS AWAKHDRKTD GWLPLWRHLR DSASVAGKLW EDWLPASVRR
     LVSEPFPGGE DDAARLLRFL AASHDIGKCT PAFACQVEQL AGRMRDHGLD MPTAKEYGQD
     RKLAPHGLAG QLILQEWMGQ RFGLGARVAG QFAVVAGGHH GVPPGSQQIH DLQLRPYLMR
     HPGPSEDVWR RTQAELLDWC AESTGMTSLL PTWHSVRLPQ PVQVLLTAVV ILSDWIASAP
     ELFPYAPESW HPVGAEGERR RLLAAWEGLD LPGPWQPRLP ASAPQELFRQ RFPTLRDAAL
     RPVQREAVRL AQEMDPGGLL IVEAPMGEGK TEAALAAAEI LAARSGAGGL LMALPTRATG
     DAMFARLLSW LDALPADGSR TRSVVLAHAK AALTESWSGL LREGSRSIAA VEPDALRHEV
     TPNGKDQETP RHPGALHAHQ WLRGRKKQLL ASFAVGTVDQ VLFAALKSRH LALRHLAVAG
     KVVVIDEVHA YDAYMNRYLD RTLEWLAAYR VPVVLLSATL PAGRRRALAA AYAGEDGAAS
     VTAEAGAYPL LTAVSPGREA LTVRPDPASD RGTAVVMERV NDDLAALAER LDAELADGGC
     ALVVRNTVGR VLETADALKD RFGEDQVTVV HSRFLAADRA ANDAALLARF GPSGERPARH
     VVVASQVVEQ SLDVSFDLLV TDLAPVDLVL QRMGRLHRHR SPRPDRLSTP RCLVTGVDWT
     ASPPAPVAGT QAVYPGDWPL LRSLAAFAPH LDGVPVRLPH DISPLVQSAY GEEPLGPAAW
     AGAMAAAGER HRALLTEKRR RADGFLLGPV QRPGRPVYGW LEAHAGDADD SRTGRAQVRD
     SEETLEVLVV QRQTDGRLTT VPWLDEGRED GRGGLELPVD FPPSRRAAEA VAASALTLPG
     RFGKPWMIDR TIADLEKFLV PAWQAKECPW LAGELILVLD ERCQTRLAGF ALSYSRAEGL
     RVTAPRTAGS DQQQTAASAA SEESGGVAKD AGRESDMVSP PARLSGRCAT DDDGPAAFNL
     VREAWVPVQH LDGTVTELSL YEVFAQADTL RGLVGDVPTQ NPVLLRLLLA VLHDALEGPA
     SLEDWEDLWH SPAPFTVAAD YLRSHADRFE LFDVERPFFQ VAGLRTGKDE IAPLSRIVAD
     VPTGSALFSM RRPGVNRLSF AEAARWLLHA HAFDTSGIKS AMKGDETRSR AGKVYPLGVG
     SLGHLGCVFA EGDTLRETLL LNLVPFEEAY AGSEFAEQTG EDRPVWRQDE PYGPGPRGER
     AGGAEPLGLR DLYTWQSRRI RLCATGGAVT GVVLGYGDPL LLSAPWVLEP MSGWRRSPAQ
     EKKQSRALVY TPDRHDPNRS AWRGLGALLP ARAQAQESEA RGEPPERLRS GVTRWYTQVI
     TESEIDPGKL IRLRLTGVVY GTQQSVIDEI VDDSVVLPVV TLHRTNPVYG AAAVDAVSDA
     EEAVTALGHL AANLVRAAGG DRPEAAAAAA RDLGYGILDG PYRAWLRELA RQPDLVAARR
     TWRESVRRQM LRLARQEVRS AGPAAGEGRV IDLPGRGECL MDAGRAELWF RARLRRVLGP
     SPITT
//
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