ID M1X4K0_9NOST Unreviewed; 990 AA.
AC M1X4K0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Exonuclease SbcC {ECO:0000313|EMBL:CCH66281.1};
GN ORFNames=RINTHH_1260 {ECO:0000313|EMBL:CCH66281.1};
OS Richelia intracellularis HH01.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Richelia.
OX NCBI_TaxID=1165094 {ECO:0000313|EMBL:CCH66281.1, ECO:0000313|Proteomes:UP000053051};
RN [1] {ECO:0000313|EMBL:CCH66281.1, ECO:0000313|Proteomes:UP000053051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH01 {ECO:0000313|EMBL:CCH66281.1,
RC ECO:0000313|Proteomes:UP000053051};
RA Hilton J.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH01 {ECO:0000313|Proteomes:UP000053051};
RA Hilton J.A., Foster R.A., Tripp H.J., Carter B.J., Zehr J.P.,
RA Villareal T.A.;
RT "Diatom-associated endosymboitic cyanobacterium lacks core nitrogen
RT metabolism enzymes.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000256|ARBA:ARBA00009439}.
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:CCH66281.1}.
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DR EMBL; CAIY01000005; CCH66281.1; -; Genomic_DNA.
DR AlphaFoldDB; M1X4K0; -.
DR STRING; 1165094.RINTHH_1260; -.
DR Proteomes; UP000053051; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR Gene3D; 1.10.287.510; Helix hairpin bin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR PANTHER; PTHR32114; ABC TRANSPORTER ABCH.3; 1.
DR PANTHER; PTHR32114:SF2; ABC TRANSPORTER ABCH.3; 1.
DR Pfam; PF13476; AAA_23; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR Pfam; PF13558; SbcC_Walker_B; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Exonuclease {ECO:0000313|EMBL:CCH66281.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00471}; Nuclease {ECO:0000313|EMBL:CCH66281.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053051};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 429..533
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 167..207
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 243..270
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 305..366
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 745..817
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 481
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 484
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 990 AA; 115725 MW; C561BD114652B905 CRC64;
MDFRGLHTVC ICGSNGAGKS SLLEAITWAI WGQSRAGIED DVIHAGAKEA RVNFTFQMSL
MQTYRVIRSH PRGGTSVLEL QVETPDGFRA ITAKGLRATQ ELILQHIKLD YDTFVNSAYL
RQGRADEFMV KRPSDRKQIL AELLKLNQYD DLEESSKDLS RHFKIRAEES SRLLAEMKER
LQEREEISQQ KQDLAQELNQ LQQLQELDQT KLQNLLVIQH QRKTWEEQLE FVYKQHQGLF
HDKERLKKEK SSLQIQLDQM EEILQQKTEI EVGYSQYQQL QSQEEVLAAK FENFTHWQEL
KQQKQQELDQ DFKVLEQELQ EARATLNILT QKEQEIGKIL AKIGEVETAF AKLNSARKNL
AELDQLQMQV SPLLRKRINL QTQIDREQAS LAARLELLEL TQDDLKSCQE NQHQLQQSVT
EVAMQIEGIE KKRVYLQRVQ EKGQERRNFI ERLQAQQLEY EGLLEKLEQK LQMLQTPNAI
CPLCEYPLDE HHWNRVIDKT KEEYRDTEGQ LWVVREQIAF SDREIQVLRQ EYREVSQQLI
HYDYLLERRG QLAAKLENNS YNKQRLQEIS QGREDLKQLV QSKGYLPKQQ QELQELDTYL
QKLNYDEQKH ILARNEVEIW RWSEVRLSQM KDNLKQKAEI QVRKPEIQEQ IVKLESSINQ
YHNSPIYQEM QHIKKQINDI GYDGEKHQKT RLYLRKAQCW QLRYQQLITV TGQYPELQDR
LQELTASLSF RLSEEQRLIE QVNQIQEQLA NTADHLDQIQ VLEEQTAIRR KELDKKIAQL
GSLEQMAMQL EALQKQYEEQ QQQLQEYCRQ NRIYQELAQA FGKNGIQTLM IENILPQLEA
GANQLLSRLS ANQLHVQFVT QKAGRGSRGK KKTAKLIETL DILIADARGT RAYETYSGGE
AFRINFAIRL ALAKLLAQRA GAALQLLIVD EGFGTQDKEG CDRLISAINT IAPDFACILT
VTHMPHLKEA FQVRIEVNKN QQGSQLSLLI
//
