ID J9I2M8_9SPIT Unreviewed; 1281 AA.
AC J9I2M8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Kelch motif family protein {ECO:0000313|EMBL:EJY71884.1};
GN ORFNames=OXYTRI_07122 {ECO:0000313|EMBL:EJY71884.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY71884.1};
RN [1] {ECO:0000313|EMBL:EJY71884.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY71884.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
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:EJY71884.1}.
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DR EMBL; AMCR01015614; EJY71884.1; -; Genomic_DNA.
DR EnsemblProtists; EJY71884; EJY71884; OXYTRI_07122.
DR OrthoDB; 179183at2759; -.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19769; Bbox2_TRIM16-like; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45632:SF26; BTB DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45632; LD33804P; 1.
DR Pfam; PF01344; Kelch_1; 2.
DR Pfam; PF13418; Kelch_4; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00612; Kelch; 6.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 3..55
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 138..179
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REGION 408..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 241..268
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 419..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1281 AA; 144817 MW; 5C3B9EEB0B2A900F CRC64;
MLCPNCQLEF NSTVQIPRIL IFCGHTFCQS CIESLLQQST DEAQGKTYLN CPECDTQNVA
NDGINSFPKN LVLLQMYTQI TNPSQQPKPQ NNNDNSGLIQ QNSFQNQIPS NENKLLRESS
QKSSSNASQP QNNHDLNQVK VLCSIHGKKL EAFCEKDLQV LCIDCILSDA HKSHEIISVQ
KAAEKQRQIL YEEVNNAQKT EEKLRFIMSD IRRHVSEMHS TADKNRKELS SIYSYVRDLI
LEREQTLKRQ ISENLTKEEQ ESEAKQSEIN DFMGGINQLK QELFQQNQEH DIDILIKAKQ
RDLISGEVNG LRARELVSFN IQSVSSCSLS LQEIKREQEL SQLSKIINPT YKGPSIGQTI
GVSSNLYSHT ASTANKMKKA NTQLPTQASN NFPLGITGAQ NPFQNENKLQ REETRKIGKS
NQNVSSSLNT NQVKTKVSPH RVQQKKGDIS SNQNKKQNVM VLDQNKQKSA NTQLNKNSSK
CQGSFGNIAM QNQINLHNFN QFGHHQQSTQ PTLGAQHDDL TEDLLGNMGA EDVSSIYPLE
TNDCYFQYQG DNQQNQKYTF AKRDESVGNL NDLLESLNKS SSGQQDLGGI IDNDKQLGTS
TASETGGSHS DINIKTPPPQ DFKLKQVKSS VESPKIKKGN PWKNQPVQQK KKSGKKNNFK
KDNSTTDLDE LKSKQQISNN QEVYTALEET KNEIRSGSLQ RYGNNGILDN DNQNSISKKH
NYQNLKNEDN DNKRHKFSQQ NEFNNNHQMC SLSQERAKRK QMKMGLQSQE QSPCKIEKVN
AKDNAIMEML QECTKNIDKL EFRPTQMKQQ NLKTNSTQES PIKLVSQNSG KAAVCVVDLT
RRDDIEEFNV RKNEDKDQIC YNEEEEGTHL KNIPNMTKPK DQSPLKKQFE RQQSSSNSPN
KKLNMLKSTE SLDNLMVQVI KNQDTSLEIS RTNQLNFGSE TFLQQSVSVD TSVSDPFRAF
CKIREEFIFV FSGFNDQKLL TCEALDVQRG TWKEVCQIGK ARTKFSAVPI SKSRILIFGG
KQADGQRTGE IEEYNLKTNK FKTLPFKLPK PRSGFSSCVK REEGKIFFCG GNSGSVLKKF
DCLDLKKGKW SRWPEMIQKR DELAVALGPD GKIYAIGGYG GGSASNSTQQ TIEDNKDNNS
TKGTSNQTSN CLRTAERFDF NTGEWEMLPE MNEARRALAA VALPDGIYAI GGYDGKQYLS
SVEKFDLQKQ QWIPVKSMNT SRCTLSAAVS SDCQYIYAIG GFNGNSLDLV ERYNTMTDEW
EFMTPMISKR FMHEAVCLVT H
//
