ID A0A3M0KAR0_HIRRU Unreviewed; 1599 AA.
AC A0A3M0KAR0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=DUI87_14628 {ECO:0000313|EMBL:RMC08384.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC08384.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMC08384.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMC08384.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMC08384.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) 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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC {ECO:0000256|ARBA:ARBA00004201}. Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|RuleBase:RU000411}.
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:RMC08384.1}.
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DR EMBL; QRBI01000117; RMC08384.1; -; Genomic_DNA.
DR STRING; 333673.A0A3M0KAR0; -.
DR Proteomes; UP000269221; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0030193; P:regulation of blood coagulation; IEA:InterPro.
DR CDD; cd16781; mRING-HC-C3HC3D_Roquin1; 1.
DR CDD; cd02045; serpinC1_AT3; 1.
DR Gene3D; 1.20.120.1790; -; 1.
DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR033829; Antithrombin_3_serpin_domain.
DR InterPro; IPR041523; ROQ_II.
DR InterPro; IPR048575; Roquin_1_2-like_ROQ.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
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 Pfam; PF00079; Serpin; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00093; SERPIN; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF56574; Serpins; 1.
DR PROSITE; PS00284; SERPIN; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000269221};
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 77..117
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 484..512
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 484..512
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 587..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1599 AA; 178880 MW; 146CFE18D54A086C CRC64;
MRGKERDKLL PPLLPLCPQH GWLKAAEQPL LELLQELRVS PVLRSPDPDT ALLTCLTRNE
QTAMPVQAPQ WTDFLSCPIC TQTFDETIRK PISLGCGHTV CKMCLNKLHR KACPFDQTTI
NTDIELLPVN SALLQLVGAQ VPEQQQITLC SGAEDTKHYE EGKKCVEELA LYLKPLSSAR
GVGLNSTTQS VLSRPMQRKL VTLVHCQLVE EEGRIRAMRA ARSLGERTVT ELILQHQNPQ
QLSSNLWAAV RARGCQFLGP AMQEEALKLV LLALEDGSAL SRKVLVLFVV QRLEPRFPQA
SKTSIGHVVQ LLYRASCFKV TKRDEDSSLM QLKEEFRTYE ALRREHDSQI VQIAMEAGLR
IAPDQWSSLL YGDQSHKSHM QSIIDKTPAS FAQSVQELTI ALQRTGDPAN LNRLRPHLEL
LANIDPSPDA PPPTWEQLEN GLVAVRTVVH GLVDYIQNHS KKGTDQQQVS HRVSLTCQPP
QHSKYKTYMC RDMKQRGGCP RGASCTFAHS QEELEKFRKM NKRLVPRRPL SASLGQLNEV
GLPSGAILSE EGGVDLPNRK TSALPNGIVS TGSTVTQLIS RGTDSGYETA LKPGKMDHLS
SSAPGSPPDL LESVPKSSIS ALPVNPHPVP ARAPADLPSV SVTKQLQMVP RGSQLYNAQQ
ADMFYQDPRG AAPSFEPAPY QQGVYYPTQS MSRFVRPPPS GPEAGAPYLE HYGPYVPERV
VSPQYPQAQG YPALAQPVYP PHYDGRRVYP PVPPYQREEV VRGSPVPIDI PQAAVPLYVP
EARDRYQQTE AYCPVAPHLG QIRPSCHRPH PSLDELHRRR KEIMAQLEER KVISPPPFAP
SPTLPHPFHS EEYLDEDLKV AGKYKGNDYS QYSPWSCDTI GSYIGTKDAK PKDVVAARSV
EMANVDSKAM REQRLDMQRR AAETGDDDLI PFGDRPTVSR FGAISRTSKA MYQNSGPMQA
MAVQGAAPKS IISDYSPYET HSGWGGSPYS PHQNIPSQGR FSDRERLSMS DVAGHGKQLP
SAEREQQLRM ELQQVDHQIS QQTQLRGLEA VSNRLLLQRE ATTLAGQPQP PPPPPKWPGM
ISSEQLSLEL HQVEREIGKR TRELSMESQS SLDMKNKLGT TKQTENGQLE PQNKVPAEDL
TLTFRTMRLF VACLLSVWGL AAPERYTVED ICTAKPRDIP VNPICIYRNP EKKPQEGEGQ
EPAKDKLPES TNPRVWELSK ANSRFAVVFY KYLADSKDNG ENIFMSPLSI STAFAMTKLG
ACGSTLQQLM EVFRFDTISE KTSDQIHFFF AKLNCRLYKK ANKSSELVSA NRLFGEKSLV
FNETYQNISE IVYGAKLWPL NFKEKPELSR QIINEWVANK TEKRITEVIP ESGIDDLTVL
VLVNSIYFKG HWKSQFPAPN TKLDIFHKGN GETCQVPTMY QESKFHYTFV SQDKVQVLEL
PYKGDDITMV LVLPSAGTPL ENVERNLTSE KLQGWIDSMK ETSLFVYLPR FRVEDSFSVK
EKLRKMGLED LFSPENARLP GIIAEGRTDL YVSEAFHKAF LEVNEEGSEA SAATAVTISG
RSFPMNRKIF NANRPFLLFI REASLNTIIF MGRIADPCS
//
