ID V9KXB9_CALMI Unreviewed; 447 AA.
AC V9KXB9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Nuclear factor 7, ovary-like protein {ECO:0000313|EMBL:AFP03429.1};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFP03429.1};
RN [1] {ECO:0000313|EMBL:AFP03429.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:AFP03429.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
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DR EMBL; JW870911; AFP03429.1; -; mRNA.
DR AlphaFoldDB; V9KXB9; -.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd13733; SPRY_PRY_C-I_1; 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:SF698; B30.2_SPRY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 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 2: Evidence at transcript level;
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 2..26
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 59..109
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 250..447
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFP03429.1"
SQ SEQUENCE 447 AA; 51035 MW; 3D1F6AF3BEFD9390 CRC64;
DCGHNFCQVC IQNFWAGEKQ SLCPECGESL PDRKVRSNRA LAKLSNKTRT LNLGVRKQEN
KLLCEEHQEE LKLYCETDRK LMCVICLVGK DGEPHKSHNF MLKSQAIEFY KNKMKTNIYS
LRQKKSALQD VEFKQKQVIS EIKERLGSVQ SNIAAEFGKL HESLQEREKQ LVLELSQQEN
LTLDIMMRNL EEIQGNLTSI TQKLAHIQLQ MEQEDILALI KEDANEPSSE EEYRVLVAGG
IMPVGIFKGP LQYSAWKQML DIIIPVPAAL TLDPNTAHPQ LILSEDLTTV RLGDKKQQLP
DMAERFDLCL CVLGSKSFQS GRHYWEIEVL NKTEWDLGVV RKSVNRKKHT TATPGSGYWI
LWLRNGTDYK ATTAPRTTIE VKQKPKKIGV YLDYEEGQVS FYNADDMSHL HTFTDTFTES
LLPFLSPGLN DDGKNAEPLK ICARQEC
//
