ID A0A1Y1HTG7_KLENI Unreviewed; 965 AA.
AC A0A1Y1HTG7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative Sterile alpha motifdomain-containing protein {ECO:0000313|EMBL:GAQ80301.1};
GN ORFNames=KFL_000510010 {ECO:0000313|EMBL:GAQ80301.1};
OS Klebsormidium nitens (Green alga) (Ulothrix nitens).
OC Eukaryota; Viridiplantae; Streptophyta; Klebsormidiophyceae;
OC Klebsormidiales; Klebsormidiaceae; Klebsormidium.
OX NCBI_TaxID=105231 {ECO:0000313|EMBL:GAQ80301.1, ECO:0000313|Proteomes:UP000054558};
RN [1] {ECO:0000313|EMBL:GAQ80301.1, ECO:0000313|Proteomes:UP000054558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2285 {ECO:0000313|EMBL:GAQ80301.1,
RC ECO:0000313|Proteomes:UP000054558};
RX PubMed=24865297; DOI=10.1038/ncomms4978;
RA Hori K., Maruyama F., Fujisawa T., Togashi T., Yamamoto N., Seo M.,
RA Sato S., Yamada T., Mori H., Tajima N., Moriyama T., Ikeuchi M.,
RA Watanabe M., Wada H., Kobayashi K., Saito M., Masuda T.,
RA Sasaki-Sekimoto Y., Mashiguchi K., Awai K., Shimojima M., Masuda S.,
RA Iwai M., Nobusawa T., Narise T., Kondo S., Saito H., Sato R., Murakawa M.,
RA Ihara Y., Oshima-Yamada Y., Ohtaka K., Satoh M., Sonobe K., Ishii M.,
RA Ohtani R., Kanamori-Sato M., Honoki R., Miyazaki D., Mochizuki H.,
RA Umetsu J., Higashi K., Shibata D., Kamiya Y., Sato N., Nakamura Y.,
RA Tabata S., Ida S., Kurokawa K., Ohta H.;
RT "Klebsormidium flaccidum genome reveals primary factors for plant
RT terrestrial adaptation.";
RL Nat. Commun. 5:3978-3978(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000256|ARBA:ARBA00010304}.
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DR EMBL; DF237000; GAQ80301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1HTG7; -.
DR STRING; 105231.A0A1Y1HTG7; -.
DR OrthoDB; 23465at2759; -.
DR Proteomes; UP000054558; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035312; F:5'-3' DNA exonuclease activity; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR CDD; cd09487; SAM_superfamily; 1.
DR CDD; cd16273; SNM1A-1C-like_MBL-fold; 1.
DR Gene3D; 3.40.50.12650; -; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR23240:SF6; DNA CROSS-LINK REPAIR 1A PROTEIN; 1.
DR PANTHER; PTHR23240; DNA CROSS-LINK REPAIR PROTEIN PSO2/SNM1-RELATED; 1.
DR Pfam; PF07522; DRMBL; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054558}.
FT DOMAIN 455..518
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 965 AA; 105686 MW; CC5822D646EA91FF CRC64;
MDESWHRRSN DTTSSYGQTF KRSKMVLNTG DDLVHFNSSP LDASTGPKSC FEPGKIGAAL
ETPLLEQYRS ALSDLNGRAF PKEKGVSGGF ARRKENQEPH FQPVSSFRVR SQKSFPAEPS
RQHYNHLAGS CAEASNCQDG DLKLLSAHPP VSPVSLDWQD SQVKLSQSET RCLGEPNAGP
AYKGGCTNSE TSDEEEDDAD LFYDWRAAAG AATQEDSASE KAHAESGAAT DRPSKQGFEA
TQCSRNGAIW EVGVTVQSLG GQCWSQNESL PSCQDAKQDP EEQKAQADSD LENDSQEGAL
SQLLEMVDED VLKPGSDIEA DCVGPNTEPE FMRISDVNSA RCELPLLMEN TSTSGQKGRV
LSREERSRFI LEASQAVLTD SGDQSGGEES EGEDDEALEC PVCGVSLKQM EAASRDAHTN
RCLDGAEGED DHHADSAKAA SPPDPSATDV NRCGLDNAPL VAWLDRLQLG RYAEAFVKEE
VDFDALHCLK EEDLESMGVV TLGPKRKLLA AIETLRRRSE GESTPAGSAH QDAAADAPPV
HKPAAAANRQ ITDFFPAPSG GVSATAASSK GLITNFFTTP DGKRLPPPSP AVAPAAGRGR
GAFVPKKGNP PGKRGGAWKQ ISGDPHEWHL VPGTDFRVDG FRFQSPHCRY WFLSHFHADH
YQGLTRNFRH GVIFCTPITA RLVHMKLGVP LEKLRPLPLN ERTRVDNCHV TLLEANHCPG
AAMMLFEPDG AKPTLHTGDF RYCPAMARYP ALRAVEIGTL ILDTTYCDPQ YDFPEQDAVI
QFVIDAIQAE TFNPKTLFLI GAYTIGKERV FLEVARELNT KVYVGAARRK VLACLDLPAE
DMARLTTNEN ESNVHVVPLW SLANFKRLTT IAKHYQGRYN TFVSFSPTGW SFGRGKKRTT
GTRRQQGTIV RYEVPYSEHS SFSELRAFVR VVRPGYILPH VNNDGGPKAE AMLRELLKER
EPDAQ
//
