ID A0A0D2R7J4_GOSRA Unreviewed; 983 AA.
AC A0A0D2R7J4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=BED-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=B456_005G013600 {ECO:0000313|EMBL:KJB27864.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB27864.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB27864.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family.
CC {ECO:0000256|ARBA:ARBA00005234}.
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DR EMBL; CM001744; KJB27864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2R7J4; -.
DR EnsemblPlants; KJB27864; KJB27864; B456_005G013600.
DR Gramene; KJB27864; KJB27864; B456_005G013600.
DR eggNOG; KOG0778; Eukaryota.
DR eggNOG; KOG1121; Eukaryota.
DR Proteomes; UP000032304; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR045259; DAYSLEEPER-like.
DR InterPro; IPR025525; hAT-like_transposase_RNase-H.
DR InterPro; IPR008906; HATC_C_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR003656; Znf_BED.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR23272; BED FINGER-RELATED; 1.
DR PANTHER; PTHR23272:SF132; ZINC FINGER BED DOMAIN-CONTAINING PROTEIN RICESLEEPER 1-LIKE ISOFORM X1; 1.
DR Pfam; PF05699; Dimer_Tnp_hAT; 1.
DR Pfam; PF14372; hAT-like_RNase-H; 1.
DR Pfam; PF02902; Peptidase_C48; 1.
DR Pfam; PF02892; zf-BED; 1.
DR SMART; SM00614; ZnF_BED; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
DR PROSITE; PS50808; ZF_BED; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00027}.
FT DOMAIN 67..121
FT /note="BED-type"
FT /evidence="ECO:0000259|PROSITE:PS50808"
FT DOMAIN 775..953
FT /note="Ubiquitin-like protease family profile"
FT /evidence="ECO:0000259|PROSITE:PS50600"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 983 AA; 112607 MW; 3F6B96859404D736 CRC64;
MPTHSSSKVV AAPFNTPEGP HNQIVPNDDP EIGKANKEKL PRTKQRNSRP KTVKANKEKL
PETTQRRLTS AVWEHFDRLL VGGEQVAKCK HCPKVLTGSS NSGTTHLRNH LNVCQKEQNQ
ERSRLNFVKM IIKHRYPLDM ADQEFFKNFV KDMQPMFEFE SKDISSYIRS IYREEKEKLQ
LYFNKLASKF NLTVSLWKNN SGKTAYCCLI AHFIDDSWEL KMKTLGLRTL EHINDTKAVG
GIIQSLVSEW NIGSKVCSIT VDNSFLDNSM VQQIKDNCLS NLVSLSSTHW FINCTLLEDG
FREMDDLLFN LKKSIEYVTE TKHGRLKFQE AVDQVKLHDG KSWDDLSLKL ESDFGILDSA
LRSREIFCKL EQIDGNFKLN PSMEEWENAA ALQSCLRCFD DIKGTQSLTR RLCNSALAVA
SVLDPRLKFK VVEFSYILIY GHDSKVQLNT FRELLTNVYN EYANETKNQT TSASVLDDIN
WLGNNSIWDS FSKFVTANEA SSKSELELYL DEPLLPMDGE IFDILGWWCD KSQKFPILAK
MARDFLAIPV SIFTPCSNIK ATINNPAYNI LNPESMEALV CSENWLESPK GNDGENHEPT
QTTDKGKRKL DEDTCVGKKS KPSNCEKDIA KDSNSNDEPV GEISIGKLQT ENSSKNGCYG
ETSSGNKSKA SNKMMGTISL QDIHQEKSSS EFNHGRNVED VSSGESSSDN DQSDQLQSSS
SESDVEITLK EQGSWFEQDI KAYLLSEFTK KENELIDKWQ KNELKGKRIG RDKCFKIPGE
ILAPLLMVPQ GDETRKEYYI EDLVVNTFFE LLKKRSDKFP NIYINHYSFN SQIATQLIEG
PRTEQEVLAW VKVDELRGVH KMFLPMSLSK HWVLFYADTK EKKISWLDPI ASSRVRSYNV
EKDIILQWFT TLLLPKLGYV DAKEWPFLVR NDIPEQKNSV DCAVFVMKYG DCLTHGDCFP
FKQEDMVHFR RRIFVDIYRG RIH
//
