ID A0A401PJC3_SCYTO Unreviewed; 1649 AA.
AC A0A401PJC3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=scyTo_0006682 {ECO:0000313|EMBL:GCB73227.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB73227.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB73227.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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:GCB73227.1}.
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DR EMBL; BFAA01002295; GCB73227.1; -; Genomic_DNA.
DR STRING; 75743.A0A401PJC3; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR CDD; cd19756; Bbox2; 1.
DR CDD; cd16544; RING-HC_RNF138; 1.
DR Gene3D; 1.10.10.2360; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR022011; IR1-M.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
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; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF697; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12185; IR1-M; 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00160; RanBD; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50196; RANBD1; 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 Reference proteome {ECO:0000313|Proteomes:UP000288216};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 7..69
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 133..178
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 1415..1551
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT REGION 102..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 231..283
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 483..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1649 AA; 180470 MW; 798C742F23536B34 CRC64;
MEASLTCAVC LSVFENPTTL PVCSHNFCKK CILECVTKSF SHSLGYSSGG SSSNNNIWRN
SQLECPLCRK SNFVAEGAVN LPGNTTLAEV VKLFRSQQQQ QTAGAGLEDG EQEEEVGEAG
GARPPRAPAP GPGESELCQR HPQRKLQLFC KVCKQLACGQ CVSENHRGVF HAVNLVDMIY
QEEKLVYFNN LRELRQLNNR LKVEIEDTPS DNEYILDYEK EVVQTKFYTI LEKVELKRKQ
LLDEIENQKQ RKEAERKIRL EGKRTQKERI EEYLKECEGL VNECNPVNFL KVACDLNERV
KSNLAIVLPT LEKHDELTAL QPHQFLIKPV MDSISALQLT KETAKLDSIT VPGNTAGKPC
TDSYRFKATL KMWKQPKDLI EAKFSPENVI EFGHRDHLWC ISSKDEYQDM SLEELRYKHY
QSSRKDWNCF VAEEYSDNEN GPEPSVSSLS TEVLKTPVQQ PQAKLFSFGQ SIKKVKKKFR
GNNSGNFESR LPSSSGSVTS IPAASNSQMS LSNSSEKLKQ KHDPIPSLAQ SKTTSSITSS
VGSLATATAT ASLPAALSSC TTVTGNEKTA ECQQKPLPSS ASGFMVAKCS GSPSAQKNSS
IFSNFSTGPV NPAITSGSSQ FAMASSAFTL GNILASKTGN QRPLPISASL AFEKLNSCST
TSNSTSSLTS VLHCKTTCDP PGTHINHQNG QATCHTSSAC NSKVLSDSTG TETTFRSDYV
TEQSSQENSP FAFRTSAPLG DQGKSAQLFP LFDHRIEKLK FPFNLIPHTK PATKSSESLR
NPESLTSVTH SVVGRDVFKP FTLGQVSRGD DPNERQFSSA TSRSTTVSPD CKSDDAGIAM
PALSLFALPP SDSTSNPTPF EQNFLTSQSS IVPLKSVTSS AESPHVFSRI HSTGSNFVDF
TAGFSKEPSS AASQLQSTAI ADDVNKMKEM LASEISINGE PVVLRGWKSL APAATSVAAG
DVSDPFTFTQ VSRSDVPNLN EKPFLSTVGG SISPSSGFKL KWPGVVRSAP SLLASTLLVS
ASSSSSSFSI PVAQNVLPTQ SRIKPLNPFA SCAETAPVFT GTNSTDTSDM ACTASFSRAL
SSAVSQQQST VTPAEVSEVH EVRTSAVQLT AEPSKLDRAH PCSLKCEDLA HAISRQQGSD
RASSDSGDET CELKETSLVE MLTPKPELFH RTESAGSACV YFRPVFGNYL SSVSQQQTQV
ATIDVGIKTC KTKEASAFEV PLNKQLSVIE KGSAPLLQLN NTTPTCENPL ARFSHNINKE
GKEPLIFSYK SSDVQVSQVS EDPGPSKVEQ DSAVTNNQCH VEHEDSTSAK EDSSHCTKRW
TNTEALNLSH KGDSVFMSQT AESYSSSFSE ANNCRTKEDM QRAAISHSRF TAPSGVFCPV
FTFGASSDFQ FKLGASNLAN STGQQQNNRG DCKALHKPMF PLPPPVYHPL AGLDAENVLF
SNRAKLYCFE RTSSQWKERA FGEIRVLENK VTKLPRLVMW NAINKCCANH WITGDLELKH
PKTSNHTWTW RALDYSENKQ ALLEFAVHFK LKEMAQVFKQ VVERVQNTTE VSRLTEKVWC
CSAENEKIDQ NGDDTPTPLV GAFELEHEGQ FLRGTEEQKE EESDEDVVML REVTPTAEQR
ALALELLLPP TFFCYKNTPG YQSSDDEVP
//
