ID   F4W7P7_ACREC            Unreviewed;      1311 AA.
AC   F4W7P7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=G5I_01463 {ECO:0000313|EMBL:EGI69920.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI69920.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; GL887844; EGI69920.1; -; Genomic_DNA.
DR   STRING; 103372.F4W7P7; -.
DR   eggNOG; KOG2242; Eukaryota.
DR   eggNOG; KOG4692; Eukaryota.
DR   InParanoid; F4W7P7; -.
DR   Proteomes; UP000007755; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   CDD; cd16541; RING-HC_RNF123; 1.
DR   Gene3D; 2.60.120.920; -; 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; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR045129; RNF123/RSPRY1-like.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13363:SF5; E3 UBIQUITIN-PROTEIN LIGASE RNF123; 1.
DR   PANTHER; PTHR13363; RING FINGER AND SRY DOMAIN-CONTAINING; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00449; SPRY; 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; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          94..274
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   DOMAIN          1245..1283
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   1311 AA;  148849 MW;  103AC3616FCC383E CRC64;
     MDMDKVLYRI FGANPLSVER TAAGRSKDDH LGQSSYSISQ IKLGLFDTYL HKTKESISLD
     PHTSNSALTS NAGEKQIIEN LNWVNEHIRK SLLNLYIDMW NSEDNREGRI GPPFVKFDIS
     IQHGLCIISP DRLSVNSQSS FSTIRANTGV FKGKWMYEVQ LGSKGVMQVG WGTAQCKFNQ
     QYGVGDTPNS YAYDGNRMRK WNVSTHKYGE AWLTGDIIGC ALDMDDGTID FYRNGRSLGR
     AFENIPMGAG IAYFPTVSLA FTENLTANFG SIPFRYPIED YKSLQAPPMK QVRQAMLLFQ
     WLSQVIELLE YSKNVDKQNI LLDDKTMSAH AFLMCLARSI LKHIGPLLTI PYVTETVFVP
     FIQMLCNLTT DDSATKSSYS NIHSTRSIVC LDLLWTFLEE HEIKMCLEST VLHLLSAFRH
     VSLLLEYPDQ CKSLILLTKI CQHTVTRQYF LQYLLFDRVR FANFVHVKPL DEGGLTNVVE
     KVWWETNPLD SSIETNKTSY LYACERIKAA ISEIEALQVK LLVILLNNTD GTAKRPTSRA
     IFLKKFKRFV QENLISNRTP LPITLCCFHR LLVAFRILWD AEIGTSPVYI PCRAFYDASI
     DYSGIDRLGG VITHLNKTFR NELLRLLGSH HEVIVAMEQQ QHTTTATNEA TNNAYAVTDT
     VIRQIVDLPV TVPAAIYPRL ININPSTAST SQVGSSMILE RFGFFSYRDR IREDRTPIRH
     GPVDPATSLM ELLDDIILFY HVAAKKQLAK VAGLRDSMSA YINAIANTKA RLEHVKGETS
     PGKNSNAKAI QRELLRTTDI FNKKLSEQAR HMAWIRAAVY SEEKQAQLAW LLKVITLTLQ
     TASQQGNMFS FVPDFYLETL SDLSVSLRAH MHPTVPIENI PDYRTILCNA AEFLCDHFLD
     PRIVHANSKD VLILALAGFV SNPLMLEALE NVPRKSRIKI VTNLLKPYEN RAWAQSNWVL
     LRFWQGNGFA FRYEKSPHLS KIGMKQQESV YQLIKPCPSV IYQAHVRDVL LGNPQASTQF
     LNSLLNQLNW AFSEFIGMVQ EIHNVSSRPE RVFIESRQLK ICATCFDLAI SLLRVLEMIS
     TVAWDVFSDP KQPSSDILLA RLCQLLCQVL NRMSSQTNCF QHVMLLEIPD LESVDHFPIL
     AAVIGILLAL LEKEMKDFGA KSTIEILRVT RSLLTEPSFQ ISSLRFVLSD TKLKNTKTKN
     IKPFSLLNYV TADEINRVKQ MITYLDTCHT LLPDTKLISD DDNACTICYA FPITAIFRPC
     NHQTCRTCID RHLLNTRECF FCKTIIDKVE DLSGNILHDF TSEFPISRTT S
//