ID M7B975_CHEMY Unreviewed; 464 AA.
AC M7B975;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Zinc finger protein RFP {ECO:0000313|EMBL:EMP24772.1};
GN ORFNames=UY3_18172 {ECO:0000313|EMBL:EMP24772.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP24772.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB598434; EMP24772.1; -; Genomic_DNA.
DR AlphaFoldDB; M7B975; -.
DR eggNOG; KOG2177; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19762; Bbox2_TRIM7-like; 1.
DR CDD; cd16594; RING-HC_TRIM7-like_C-IV; 1.
DR CDD; cd12888; SPRY_PRY_TRIM7_like; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 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; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
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; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF689; E3 UBIQUITIN-PROTEIN LIGASE TRIM7; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF15227; zf-C3HC4_4; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 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; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 17..58
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 91..132
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 276..464
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
SQ SEQUENCE 464 AA; 52869 MW; DDD60C0AF157C72C CRC64;
MAAAAKARQS LQDEASCSIC LEYFNDPVTI DCGHNFCRAC ITQCWEGSDK DFSCPQCRTT
FPQRNLRPNR QLANMVEIAK QLHLQSTKDA GAGRACEKHQ EALKLFCQED QSPICVVCDR
SKEHRAHTVV PAEEAAQEYK GQIRSRLEML KKEMEGIAAL KLNGEITSQE LLQQTESERM
KILSEFEKLH LFLEEKELLL LAQLEVLDKE ILKRQDEFTT RLTQEKTRLG TLISEMEGKC
RQPPSEFLQA IFLPRYETGK FQSPPSLPLE LKRRVKEFSQ KHTLLEHALS KFKAHVTLDP
DTAHPHLILS EDGSSVRWGP ARQDVPDNFR RFDPVPCVLG CEGFTAGRHW WEVEVDGSSW
AVGVARESVR RKGGVSLEPE EGIWAVGQLN PIQYVALTSP WTSLPPDRRP RKVRVALDCK
RRQVAFFNAE NNTQIFTFTE VAFAGRIFPF CWVADKSSQV KMCH
//
