ID Q1RLF4_CIOIN Unreviewed; 852 AA.
AC Q1RLF4;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Zinc finger protein {ECO:0000313|EMBL:FAA00111.1};
DE Flags: Fragment;
GN Name=Ci-ZF(Bbox/RING)-3 {ECO:0000313|EMBL:FAA00111.1};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|EMBL:FAA00111.1};
RN [1] {ECO:0000313|EMBL:FAA00111.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16519883; DOI=10.1016/j.ydbio.2006.01.024;
RA Miwata K., Chiba T., Horii R., Yamada L., Kubo A., Miyamura D., Satoh N.,
RA Satou Y.;
RT "Systematic analysis of embryonic expression profiles of zinc finger genes
RT in Ciona intestinalis.";
RL Dev. Biol. 292:546-554(2006).
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DR EMBL; BR000080; FAA00111.1; -; mRNA.
DR AlphaFoldDB; Q1RLF4; -.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19803; Bbox1_TRIM9-like_C-I; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd16576; RING-HC_TRIM9-like_C-I; 1.
DR CDD; cd12889; SPRY_PRY_TRIM67_9; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 4.10.830.40; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR PANTHER; PTHR24099:SF15; E3 UBIQUITIN-PROTEIN LIGASE TRIM9; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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 210..257
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 283..325
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 431..489
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT DOMAIN 493..586
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 569..762
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 73..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:FAA00111.1"
SQ SEQUENCE 852 AA; 94424 MW; 044D5AFBBD38BB1C CRC64;
MEEELQCPVC HCIFNDPVIL PCTHNVCFQC ANTLIHKVID LPPAYNIETS FPHHEPDKVS
LLSETVLSDS DSGYSASSAS SGTSDTPTPS SSTPTIVTSD PFSSLVPTHT VTQASTTTTP
TGVNLPALPD SISCLTCPIC HRASFVDDRG VNGLPRNKAM NSIVGRYTRT IDSSLRPPTL
SPNASPVRKP PISPKKPATP VLRRHTKTVH NCQICEGDPA NEASVKCLQC EVLYCASCRD
RCHPPRGPLA RHTLVDVDAD KPEPTRRPAY PTLPNKPSLK NGVRLPSCSH HPTEKTSLYC
SSCHLPLCVL CQDEGRHKNH DLKPIGALYK SRKSQLSQQM GSLSSKARQA KDLVMSLRGM
PSEIEKFSTE LESKTVTQLD HLMSLLQRKK DELLQKIAKE RETSIVQDQL QQSTMKLRNT
TGLLEYCIEV MKDNDPSAFL QVSQSLTERV SCNEQQWNGR NLISKTKPEF DMDIVTSPLA
MEIENLDFFQ MKVPGKPSIR ADECGARNNT VTLSWLPAPN SIVDSFRLEM DDGNNGNYRE
VYAGKETVCT VDGLHFNSVY RARVRAVNKA GPSPHSDPLQ LQTSEVASFQ WDPTQGHCDV
RLSNNNCTVT SNSFDDRVVL GSVGFSRGIH YWEFSVDRYE GRPDPSFGVA FYDVDKSQLL
GKESRGWGMY IDESRSWLMH ANEHSNRHEV GIKVGSRVGV LLDIARSLLS FYVDGKPQGN
PMTLPTSQGN YHPSGRKQAL YFPAISVNRN VEVTLHTGLR SPIQPLQLYR NRMQESSSYS
GFSRIQKSPD CPHRGRNLSS SDLRLPSMEA KKFPPPPPIR RGGSTGNMST RSDGESSDST
SAKSLRSFFH KK
//