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Database: UniProt
Entry: A0A1V4KEV2_PATFA
LinkDB: A0A1V4KEV2_PATFA
Original site: A0A1V4KEV2_PATFA 
ID   A0A1V4KEV2_PATFA        Unreviewed;      1730 AA.
AC   A0A1V4KEV2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN   Name=UBR1 {ECO:0000313|EMBL:OPJ82999.1};
GN   ORFNames=AV530_010441 {ECO:0000313|EMBL:OPJ82999.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ82999.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ82999.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ82999.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ82999.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC       rule pathway. Recognizes and binds to proteins bearing specific N-
CC       terminal residues that are destabilizing according to the N-end rule,
CC       leading to their ubiquitination and subsequent degradation.
CC       {ECO:0000256|RuleBase:RU366018}.
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         ECO:0000256|RuleBase:RU366018};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC   -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC       ECO:0000256|RuleBase:RU366018}.
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:OPJ82999.1}.
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DR   EMBL; LSYS01003385; OPJ82999.1; -; Genomic_DNA.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000190648; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR   GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR   CDD; cd16685; RING-H2_UBR1; 1.
DR   CDD; cd19678; UBR-box_UBR1; 1.
DR   Gene3D; 2.10.110.30; -; 1.
DR   Gene3D; 3.30.1390.10; -; 1.
DR   Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR   InterPro; IPR003769; ClpS_core.
DR   InterPro; IPR042065; E3_ELL-like.
DR   InterPro; IPR044046; E3_ligase_UBR-like_C.
DR   InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR   InterPro; IPR047507; UBR-box_UBR1.
DR   InterPro; IPR039164; UBR1-like.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   InterPro; IPR003126; Znf_UBR.
DR   PANTHER; PTHR21497:SF27; E3 UBIQUITIN-PROTEIN LIGASE UBR1; 1.
DR   PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR   Pfam; PF02617; ClpS; 1.
DR   Pfam; PF18995; PRT6_C; 1.
DR   Pfam; PF02207; zf-UBR; 1.
DR   SMART; SM00396; ZnF_UBR1; 1.
DR   SUPFAM; SSF54736; ClpS-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51157; ZF_UBR; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU366018};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU366018};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW   Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT   DOMAIN          71..142
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51157"
FT   ZN_FING         71..142
FT                   /note="UBR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT   REGION          819..846
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          974..997
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        819..836
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1730 AA;  197502 MW;  6DF62C6CF8038693 CRC64;
     MWCDERFNFQ ATFLQCLAKH VPNIYSAEMD PLVEKQEEMV QAAILYPLEC YLFGEDPDVF
     LEKLQQSGTS QLCGKVFKGG ETTYSCRDCA VDPTCVLCMD CFQNSIHKNH RYKMHSSTGG
     GFCDCGDTEA WKAGPLCTKH EPGASGSAKE NSGCQLKEEI MEHSRRVFPS VIKYIVDMLV
     WEEEKELPPE LVISREKVDS YYCVLFNDEH HSYDHVIYSL QRALGCELGE AQLHTTAIDK
     EGRRAVKAGH YASCQEVKEE IKRHSENVSQ RPLHVEVLHA DVMAHQKFAL RLGSWLNKLM
     SYSSDFRQIF CQICLKEEAG SEKPCFISKL MLWDAKLHKG ARKVLHELIF SSFFMEMEYK
     KLFAVEFVKY YKALQKEYIS DDHDRVLSVT ALSVQMFTVP TLARHLIEEQ NVITTITETL
     LEVLPEYLDK NDKFNFQGYS QDKLNRVYAV IYDLRYVLVS KPTLWTDRLR VRFLEGFVSF
     LRILTCMQGM EEIKRQIGQH IEVDPDWEAA IAIQMQLKNI LLMFQEWCAC DEELLLKAYS
     ECHKAVIRCS TNGRSREKTV FHLCGHTLES RPYRVSADPV SIHLPLSRTL AGLHVRLSKT
     GTISRLHEFV SPEEFQVELL VEYPLRCLVL VAQVVAEMWR RNGLSLISQV FYYQDVKCRE
     EMYDKDIIML QIGASLMDPN QFLLLILQRY ELAEAFKKLK PTKDQDLIKQ YNVLIEEMLQ
     ILIYVVGERY VPGVSNVTKE DVIMREIIHL LCIEPMAHSA ITKSLPENEN YETGLENVID
     KVATFKKPGV SGHGVYELKD ECLKEFNMFF YHYTKTQHSK AEHTQKKRRK QENRDEALPP
     PPPPDFSPAF SNVVRILNCD VMMHILRTIL QRAVELETHL WTEAMIQMVL HLLSLGLLEE
     KQQLQKSPEE EVTFDFYHKA TRMGSSALNA VSVLTLLEKL KRVPQLEAQK DTVSWILQMF
     DTVKRLREKS SLTTVAATSG SEATKVDEST QDKEKAERKR KAEAARLHRQ KIMAQMSALQ
     RNFIETHKLL YENTLEAQGK EDAVMEEESI SSAIDYSRIS LGPKRGPSVA EKEVLTCILC
     QEEQEVKLES AAMVLSACVQ KSTALTQNRS RILEHSGDTL DPLFMHPDLP CGTHAGSCGH
     VMHAACWQKY FEAMQLNFRQ RLHVEQIFDL ENGEYLCPLC KSLCNTVIPI VPLQAQKINS
     EDAEAVAQIL SLARWLEIII ARISGYSVKN AKGEKQNLPA FTNKGMGNSA LEFNSILSFG
     VQSSAKYSNS IKEMLILFAT TVYRVGLKVA PNEADYRIPM MTWSTCAFTV QCIENLLEAE
     GKPLFGSLQN RQHSGLKALV QFAAAQRTTS PQVLIQQHLI RLLGVLLPNF KVEDTPSLLE
     VDMFHILVGV VLSFPSLYWE DAVDLQPSSI SSAYNHLYLF HLTTLAHITQ IVVSSATESP
     SAQSYENSEE AHSAQAFCRE VCQYTSGCFS QDIPGWLVWD CVKKGIMPYL RCAALFFHYM
     LGVSPPEDLL QVSEEGQFKA LCSYLSLPTN LFLLFQEYRD TVNPLLQRWC ADPMVLSCLK
     GKSIAVRYPR KRNSLIELPE DYSCLLNQAS QFRCPRSSDD EQKHPVLCLF CGAMLCSQNT
     CCQELVNGEE LGACTSHALQ CGAGVCMFLK IRECKVVLIE GKTRGCLYPA PYLDEYGETD
     PGLKRGNPLH LCRERYRKLH LLWQQHCIIE EIARSQETNQ IFFGFNWQLL
//
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