ID D8SAB9_SELML Unreviewed; 2030 AA.
AC D8SAB9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SELMODRAFT_444519 {ECO:0000313|EMBL:EFJ18575.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ18575.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000256|ARBA:ARBA00008438}.
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DR EMBL; GL377609; EFJ18575.1; -; Genomic_DNA.
DR RefSeq; XP_002980315.1; XM_002980269.1.
DR STRING; 88036.D8SAB9; -.
DR EnsemblPlants; EFJ18575; EFJ18575; SELMODRAFT_444519.
DR Gramene; EFJ18575; EFJ18575; SELMODRAFT_444519.
DR KEGG; smo:SELMODRAFT_444519; -.
DR eggNOG; KOG0298; Eukaryota.
DR eggNOG; KOG4197; Eukaryota.
DR HOGENOM; CLU_001691_0_0_1; -.
DR InParanoid; D8SAB9; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18070; DEXQc_SHPRH; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002885; Pentatricopeptide_rpt.
DR InterPro; IPR048686; SHPRH_helical_1st.
DR InterPro; IPR048695; SHPRH_helical_2nd.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR NCBIfam; TIGR00756; PPR; 3.
DR PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF20826; PHD_5; 1.
DR Pfam; PF01535; PPR; 1.
DR Pfam; PF13041; PPR_2; 3.
DR Pfam; PF21325; SHPRH_helical-1st; 1.
DR Pfam; PF21324; SHPRH_helical-2nd; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51375; PPR; 5.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 999..1049
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1096..1258
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REPEAT 1554..1588
FT /note="PPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT REPEAT 1624..1658
FT /note="PPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT REPEAT 1659..1693
FT /note="PPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT REPEAT 1694..1728
FT /note="PPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT REPEAT 1764..1799
FT /note="PPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
SQ SEQUENCE 2030 AA; 230059 MW; FC7D4A051EA5C0E9 CRC64;
MLRRSLQSLI VWLRPELSID FFYGPETRSK SQNEVFDPSS LYRGVQRQRD EPCWSVALEG
LLPELRTYQQ QAVFWMVQRE TADPAVEEVV RKRHPLWVLV ESLDKEKSFY YNVFNGMVSR
EPRDCCSYVR GGILADEMGL GKTVEVLACI LANRHEGPAM WEPAVEKLQH RLDDRKNERV
ECICGDDDAG GMMVQCDHCH VWQHTSCVGY SPPKKKKTRK SKEADEDDNA FACDGCFEVI
ASTEVEGVCG ATLIVCPTAI LKQWQEEIVR HTKLDAVKVL VYEGVRRGCI TLGEKNSCLR
KVGAHDLAAA DVVITTYDVL QADLCHDIEE ENQQTLRFEK KYHVIATPLT RLKWWRICLD
EAQMVESSTA KATEMAMRLH AENKWCVSGT PIQRGLDDLY GLLRFLQAEP FDNHTWWQQA
IKHPYEEGKM GAVDFVHFFF REIMWRSMKI DVIDQLDIPP QEERITWLKF SGVENHFYRQ
QHEQCVKRAR EVIEKYSLGD GRPLNHMDAS KLMNPLLRLR QACCHPQVGS SGVRSLQASP
LPMDEVLEVL IEKAKTEGEE AQRDLVASLN GLAGLAIIEE NIPMAVSIYR EALAATEENA
TNFEVDPLQK VHILHNLEES LRNCKDDALS KIPRTLRDDM LISQCDELRK KYVSGQYANL
AAAQQDFYAA HKEIASAQSH DKSSRWSRWW LDAFAWVQSS SQRSDHLLER IKHGLEDVNR
AGGRNASSLV LRYHDLNGLK FLLSQELDAI HETRDHVLSR LLEVDGGMQN PNPDYVQRAG
QCSQCQPRHT GITCVHCAID LMFQKYANRL FYLTSRAAEL DGIVTAEDAF VSQVRSLVKG
NKETETNTGR RKGAAVAAVT HRCSETEMVL KILLAYMKAE TNLEEDEIEA AKKHLEYLEA
LRSEYAAARR LTTAQQLVLT ALDELSMSTT RLCLQGAKAA DGNPFGDEGY EIAIRNAELT
NEKFVAVENL SRVKRQLRYL KGLRNKKDEG HNSLEGEICP VCHDGIESGA MVLPCGHLLC
GKCLNLIVNR QKAPANGADF KRIACPTCRQ QTYVSNIAYA NAEGTSSKIA ENLQEEEEDE
EKSITVAGSY GTKIEAVVRR ILSLKEDDPF VKILVFSTWQ EVLDLLEHAL KSNKLSWVRL
KQRRQMGSSI LEFKKENVQV MLLPIQHGAN GLNLIEAQHV ILVEPLLNPA VEAQAINRVH
RIGQRLKTLV HRFILLVLLL NRGSCDYRPT LAYRFLLATE MGAKFQPLPR FYWTKEQIAA
IRDLCRDDDL YVKTKYGRKL RPPPRPRLSR EQERFVRADP QAGLDRISGQ WVALQHQLGK
KPYTAEEQEG NYVGPILGHK QYRRELHLHR GQKQWNVHAV GDKFLVYETL PPATDTGDDP
PVLCGRDKFV IGRPLSVTMD NRATNVSSSW NSFPVWSLPE EGKEGTIALP GNYMVPSSKV
ALPGLVPGKG ALVFDALYET VKEGGASWSS EMVEKLDRLK RGITHPHQVC VVLKKIKHDA
SLSLKLFTWA KTIPGFKHDL VNYSTMIMIL GDDGNYLMAE ALFVEIQELG LRLDTFAVNN
MIRCYTRVNR IQEALDLYRK MPYFGCHPDN CTFGLLIDWC GKFGSRKELQ RIFLDLRASP
RNADAQTFNT MIHNFCKQRD FANAREAANQ MKAWGIPFSS ATYAILIHMY AKARDSKAAA
ELYADYLRSG LEPNLIVYNN VILSYGSSGF PGHAQNILGD IRKAGLAPDR FTYCTLISSW
ARAGAMLQAR RWFNKACKTK AGPSIEMCNA LIDGYLKARE VEPAKFILTK VMPERGVEPT
LQTYTILLGH YTSSVKVADS RAVREMMKSS SKPAAAAAGR GGGDDHPGVD EFLNEILQGL
RAIKELKSYS REFFRKLRMD KPPRWGRWLA DALVNHLHCF GYAREAFYVW EGVSSTELYP
RGIWEDWQGA WFIWLQDMSS GTAMVALTSG LIVSRRKLAR GFERPERVII VCGYASDKSK
EVTHAVNRTL VALDSPFEPF ISMGRFMCEG NLFRDWLWEK QVAIELTMDA
//