ID A0A151MIM5_ALLMI Unreviewed; 1099 AA.
AC A0A151MIM5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=RC3H2 {ECO:0000313|EMBL:KYO24329.1};
GN ORFNames=Y1Q_0004350 {ECO:0000313|EMBL:KYO24329.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO24329.1};
RN [1] {ECO:0000313|EMBL:KYO24329.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO24329.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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:KYO24329.1}.
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DR EMBL; AKHW03006099; KYO24329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151MIM5; -.
DR STRING; 8496.A0A151MIM5; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1790; -; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR041523; ROQ_II.
DR InterPro; IPR048575; Roquin_1_2-like_ROQ.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR13139; RING FINGER AND CCCH-TYPE ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR13139:SF6; ROQUIN-1; 1.
DR Pfam; PF18386; ROQ_II; 1.
DR Pfam; PF21206; Roquin_1_2-like_ROQ; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 374..402
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 374..402
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 474..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..525
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1099 AA; 121682 MW; CC69589B8B84D3C2 CRC64;
MCLNKLHRKA CPFDQTTINT DIELLPVNSA LLQLVGAQVP EQQPITLCSG AEDTKHYEEG
KKCVEELALY LKPLSSARGV GLNSTTQSVL SRPMQRKLVT LVHCQLVEEE GRIRAMRAAR
SLGERTVTEL ILQHQNPQQL SSNLWAAVRA RGCQFLGPAM QEEALKLVLL ALEDGSALSR
KVLVLFVVQR LEPRFPQASK TSIGHVVQLL YRASCFKVTK RDEDSSLMQL KEEFRTYEAL
RREHDSQIVQ IAMEAGLRIA PDQWSSLLYG DQSHKSHMQS IIDKLQTPAS FAQSVQELTI
ALQRTGDPAN LNRLRPHLEL LANIDPSPDA PSPTWEQLEN GLVAVRTVVH GLVDYIQNHS
KKGTDQQQPP QHSKYKTYMC RDMKQRGGCP RGASCTFAHS QEELEKFRKM NKRLVPRRPL
SASLGQLNEV GLPSAAILSD EGAVDLPSRK SSALPNGIVS TGSTVAQLIS RGTDSSYDSA
LKPGKIDHLS SSAPGSPPDL LESVPKSSLP ALPVNPHPVP TRGPADLPPM SVSKQMQMVP
RGSQLYPAQQ PDMFYQDPRG AAPPFDPGPY QQGVYYSTQS SQCMPRFVRP PSAPEPGPPY
LEHYPAYLPD RVVNSQYTPP QQYPPMGQPI YPPHYDSRRV YPPAQPYQRE DIVRGSPVPI
EIPQTAVPPY VQESRDRYQQ MEGYCPVAPH LGQIRPSCHR EPCNRFPSSP QPHPSLDELH
RRRKEIMAQL EERKVISPPP FAPSPTLPHT FHPEEYLDED LKVAGKYKGN DYSQYSPWSC
DTIGSYIGTK DAKPKDVVAA GSVDMANVDN KTIRDQRLDM QRRAAETGDD DLIPFGDRPT
VSRFGAISRT SKAMYQSSGP MQAMAVQGAS TKSMNISDYS PYGTHGSWGS SPYLPHQNIP
SQGRFSDRER LSMSDITGHG KPLPSAEREQ QLRLELQQLN HQISQQTQLR GLEAASNRLL
LQREATTLAG QPQPPPPPSK WPGMISSEQL SLELHQVERE IGKRTRELSM ESQSSLDMKS
KLGTSKQTEN GQLEPQNKVP AEDLALTFSS DVPNGSALTQ ENISLLSNKT TSLSLTEDPE
GGGDSHDSQR TGVTPTSAP
//
