(data stored in ACNUC7421 zone)

SWISSPROT: B4SJ53_STRM5

ID   B4SJ53_STRM5            Unreviewed;      1104 AA.
AC   B4SJ53;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   SubName: Full=Non-specific serine/threonine protein kinase {ECO:0000313|EMBL:ACF50221.1};
DE            EC=2.7.11.1 {ECO:0000313|EMBL:ACF50221.1};
GN   OrderedLocusNames=Smal_0516 {ECO:0000313|EMBL:ACF50221.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50221.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50221.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50221.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001111; ACF50221.1; -; Genomic_DNA.
DR   RefSeq; WP_012509992.1; NC_011071.1.
DR   STRING; 391008.Smal_0516; -.
DR   EnsemblBacteria; ACF50221; ACF50221; Smal_0516.
DR   KEGG; smt:Smal_0516; -.
DR   eggNOG; ENOG4105C0D; Bacteria.
DR   eggNOG; COG0553; LUCA.
DR   HOGENOM; HOG000294304; -.
DR   OMA; LRTHDWT; -.
DR   OrthoDB; 325071at2; -.
DR   BioCyc; SMAL391008:SMAL_RS02640-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd00079; HELICc; 1.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR007527; Znf_SWIM.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50966; ZF_SWIM; 1.
PE   4: Predicted;
DR   PRODOM; B4SJ53.
DR   SWISS-2DPAGE; B4SJ53.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Kinase {ECO:0000313|EMBL:ACF50221.1};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ACF50221.1};
KW   Transferase {ECO:0000313|EMBL:ACF50221.1};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT   DOMAIN       51     91       SWIM-type. {ECO:0000259|PROSITE:PS50966}.
FT   DOMAIN      636    796       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      924   1081       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   COILED     1043   1063       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1104 AA;  122665 MW;  69278AD74D2D5A1D CRC64;
     MTPTFTDEDL FRWIDEWTLQ KSEQCLGGVR NRQLRDGLLT AEVQGSARHP YYVEIDLTAS
     TRTARSRLQS ACSCPVGRTC KHVAAVLVSY MLDSLAMDDE SPLTEQNLTQ PPRPELLAEL
     SRWQSARIQP AQPRRNGVIF ELSTYNHHPA VLVRRVKYGT DGAISTGKWM DITADLLLDP
     PAYLTPTDLA VMIQLRTQRQ PATKDEWIDF AATLQLIVSS GHGWVSCGTH GDVPARSGAP
     RRGELGWTVG MTQGATLLEP ALSVEGGARG VVLGRSACYL DPVTGEVGPL LLDVRAEDAD
     AFLSLPNLLP NEEAVVAQML QQIDPALPRP GASDTLPTLQ ISAMIPVLRL HTIEFRPAWL
     GRRDPSQWAD IATVAFEYDE HVRFLDDPSL FAHDTEGRLA LLPRDLAEEA RREGELRSVK
     LHRDPQPRAV LDGAGPQFQL RTHDWTGFLL GDVPRLEALG WKVETDDDFR HRITRVDEID
     LDIQADPEDA GWFNLGLEIQ VDGRKVSMVP LLQQVLHADP RWSRGQLDAI GDDENILLTA
     SGNTRLALQA SRLKPIMALL ADLFTQRGAP LRLSAHDRGR LQALQDDAHL QFRGHKDTQA
     LVQRLLQAPA PEDVAPPAGL QATLRSYQRE GLSWLQYLRQ QGLGGVLADD MGLGKTLQTL
     AHLLVEKESG RLDRPALLVV PTSLLHNWQS EAARFTPGLR VLTLHGPARE ALFEAIPEHD
     LVLTTYPLLW RDEQALQSHS YHLLILDEAQ QVKNPKSRAA VTLRTLQARH RLCLTGTPLE
     NHLGELWTQF DFLLPGLLGS EKLFNQHWRH PIERGSDQRR AQLLAQRLRP FILRRRKDQV
     AAELPPKTLI TRAVTMEGGQ RDLYETVRAA MEKQVREAIS DSGLARSHIR VLDALLKLRQ
     VCCDPRLLPG ETPARNAGSA KLELLREMLP SMVEEGRRIL LFSQFTGMLA LIAQALDGLG
     LAYVTLTGDT QDRVTPVQRF MQGEVPLFLI SLKAGGVGLN LTAADTVIHF DPWWNPAAEN
     QASDRAHRIG QQQPVFVYRL IAAGSIEERI AELQERKAML AESILEGGGS AGPRFSEEDV
     QALLAPLPGA LPARRKAGRQ SKVR
//

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