ID A1HQI3_9FIRM Unreviewed; 1050 AA.
AC A1HQI3;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Type I restriction enzyme endonuclease subunit {ECO:0000256|RuleBase:RU364115};
DE Short=R protein {ECO:0000256|RuleBase:RU364115};
DE EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
DE AltName: Full=Type-1 restriction enzyme R protein {ECO:0000256|RuleBase:RU364115};
GN ORFNames=TcarDRAFT_1194 {ECO:0000313|EMBL:EAX47788.1};
OS Thermosinus carboxydivorans Nor1.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Thermosinus.
OX NCBI_TaxID=401526 {ECO:0000313|EMBL:EAX47788.1, ECO:0000313|Proteomes:UP000005139};
RN [1] {ECO:0000313|EMBL:EAX47788.1, ECO:0000313|Proteomes:UP000005139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nor1 {ECO:0000313|EMBL:EAX47788.1,
RC ECO:0000313|Proteomes:UP000005139};
RG US DOE Joint Genome Institute (JGI-ORNL);
RA Larimer F., Land M., Hauser L.;
RT "Annotation of the draft genome assembly of Thermosinus carboxydivorans
RT Nor1.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAX47788.1, ECO:0000313|Proteomes:UP000005139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nor1 {ECO:0000313|EMBL:EAX47788.1,
RC ECO:0000313|Proteomes:UP000005139};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Richardson P.;
RT "Sequencing of the draft genome and assembly of Thermosinus carboxydivorans
RT Nor1.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC activities, but not for modification. {ECO:0000256|RuleBase:RU364115}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give random double-stranded
CC fragments with terminal 5'-phosphates, ATP is simultaneously
CC hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000256|ARBA:ARBA00000851,
CC ECO:0000256|RuleBase:RU364115};
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S. {ECO:0000256|ARBA:ARBA00011296,
CC ECO:0000256|RuleBase:RU364115}.
CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC ECO:0000256|RuleBase:RU364115}.
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:EAX47788.1}.
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DR EMBL; AAWL01000007; EAX47788.1; -; Genomic_DNA.
DR RefSeq; WP_007289287.1; NZ_AAWL01000007.1.
DR AlphaFoldDB; A1HQI3; -.
DR eggNOG; COG0610; Bacteria.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000005139; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR CDD; cd18030; DEXHc_RE_I_HsdR; 1.
DR CDD; cd22332; HsdR_N; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR004473; Restrct_endonuc_typeI_HsdR.
DR InterPro; IPR040980; SWI2_SNF2.
DR InterPro; IPR021810; T1RH-like_C.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF15; TYPE I RESTRICTION ENYME HINDI ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF18766; SWI2_SNF2; 1.
DR Pfam; PF11867; T1RH-like_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364115};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364115};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364115};
KW Reference proteome {ECO:0000313|Proteomes:UP000005139};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 283..447
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 475..502
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1050 AA; 120241 MW; EDA3082AA97AC3D7 CRC64;
MSRYSEDALV EQPAINLFRE LGWETVNCFH ETLGAAGTIG RETTSEVVLT RYLRNALEKL
NPGLDSEAIN LAIEEIVKDR SSLNPVQANR DVYKLLKDGV KVTYKNADDE EIDEVVKVID
WNCPENNHFL LASQLWISGE IYKRRADLVG FVNGIPLVFI ELKSTARRLE HAYYDNLRDY
KNTIPQLFWY NGFIILSNGS QSRIGSMSAS WEHFAEWKKV SSEGEEGVVS LETMFRGTCD
KVRLLDIVEN FTLFSDAGGS LVKLVAKNHQ YLGVNNAIEA VKKIRENKGR LGVFWHTQGS
GKSYSMLFFC QKILRKIPGN WTFVIVTDRT ELDDQIYKNF AAAGAVIEER VQAESCQHLK
ELLAEDHRMV FTLIHKFQSD NDGEYPKITD RDDIIVLVDE AHRSQYDTLA ANMRSAMPNA
SFIAFTGTPL MAGEEKTREV FGDYVSIYNF RQSIEDRATV PLYYENRIPE LQLINEKLND
DIQDIIDNAA LSEEEEKKLE REFAREYHLI TRDDRLETIA EDIVKHFMTR GEMGKAMVVS
IDRFTAVRMY DKVQKYWQKY MDELQKQLAK CHPEEAAEIK KKLDYMQETD MAVVISSGQN
EVEAFQKKGL DILPHRKRMV TEDLDKRFKD PNDPLRIVFV CAMWLTGFDA PAVNTIYLDK
PMKNHTLMQT IARANRVFKD KTCGTIVDYI GVFRNLQKAL AIYATPVAGG SVDTPVKDKT
TLIDELKKAI AATTAFCNEK GIDVGRLLNT SGLELVRLLD DAVERLVVND ETKQRFQSLV
GNIVKLYKAI LPDPKASEFA KQKNLFACIS DKIRSLTPPA DISDIMGEIE EVLDQSIASE
GYIIHEAPAG YNTKVDLSQI DFEALRKFFD KSKKHTEVEK LKGLINAKLN KLVRLNKSRI
DFAERFQKLI DEYNSGSLNV ELMFDKLLAF AKELTEEEKR GLAEQLTEEE LALFDILTKP
EPKLTDKDKA QVKKVVRELL DTLKREKLVL DWRKRQQTRA VVLITIQDFL DRELPRAYTP
EIFNRKCDLV YQHIYDCYYG AGQSIYSRAG
//
