ID M7AM59_CHEMY Unreviewed; 555 AA.
AC M7AM59;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=E3 ubiquitin-protein ligase AMFR {ECO:0000313|EMBL:EMP25589.1};
GN ORFNames=UY3_17329 {ECO:0000313|EMBL:EMP25589.1};
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:EMP25589.1, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KB587772; EMP25589.1; -; Genomic_DNA.
DR AlphaFoldDB; M7AM59; -.
DR STRING; 8469.M7AM59; -.
DR eggNOG; KOG1689; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR CDD; cd14421; CUE_AMFR; 1.
DR CDD; cd16455; RING-H2_AMFR; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR040675; AMFR_Ube2g2-bd.
DR InterPro; IPR016706; Cleav_polyA_spec_factor_su5.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15067:SF4; E3 UBIQUITIN-PROTEIN LIGASE AMFR; 1.
DR PANTHER; PTHR15067; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR Pfam; PF02845; CUE; 1.
DR Pfam; PF18442; G2BR; 1.
DR Pfam; PF13869; NUDIX_2; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00546; CUE; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 62..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 259..297
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 374..416
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT REGION 415..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 63814 MW; FF02777DE3092CE1 CRC64;
MREEFDKIGM RRTVEGVLIV HEHRLPHVLL LQLGTTFFKL PGGELNPGED EVEGLKRLMT
EVLVNTACCF LMLIAKLIQC AVFGPLRVSE RQHLKDKFWN FIFYKFIFIF GVLNVQTVEE
VVMWCLWFSG LVFLHLMVQL CKDRFEYLSF SPTTPMSSHV RVLTLLIAML LSCCGLAVIC
GVIGYTHGMH TLAFMAAELF GNIWLSMASL VIFMQLRYLF HEVQRRIRRH KNYLRVVGNM
EARFAVATPE ELAVNNDDCA ICWDSMQTAR KLPCGHLFHN SCLRSWLEQD TSCPTCRMSL
NITDNHRVRE DHQRENLDEN LVPVAVAEGR PRLNQHNHFF HFDGSRIASW LPSFSVEVMH
TTNILGIAQA SNSQLNAMAH QIQEMFPQVP YHIVLQDLQL TRSVEITTDN ILEGRIQRPD
SVRPASNSPA ERHNSDQEEA ETATQTERVP LELSPRLEEM VEFSEMEAEP SETEDFEARG
SRFSKSVDER QRMLVQRKED LLQQARKRYL NKTSDEDSTS ESPFLSEGAA SDPVTVRRRM
LAAAAERRLQ MQQTL
//
