ID K9IMF5_DESRO Unreviewed; 580 AA.
AC K9IMF5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Desmodus rotundus (Vampire bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC Desmodontinae; Desmodus.
OX NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA48307.1};
RN [1] {ECO:0000313|EMBL:JAA48307.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:JAA48307.1};
RA Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA Ribeiro J.M.C.;
RT "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT Desmodus rotundus.";
RL Submitted (NOV-2012) 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 {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
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DR EMBL; GABZ01005218; JAA48307.1; -; mRNA.
DR AlphaFoldDB; K9IMF5; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19809; Bbox1_TRIM45_C-X; 1.
DR CDD; cd19785; Bbox2_TRIM45_C-X; 1.
DR CDD; cd16588; RING-HC_TRIM45_C-VII; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR047153; TRIM45/56/19.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR25462; BONUS, ISOFORM C-RELATED; 1.
DR PANTHER; PTHR25462:SF291; TRIPARTITE MOTIF-CONTAINING PROTEIN 45; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 29..98
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 130..176
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 186..222
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 394..497
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT COILED 249..316
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 580 AA; 63959 MW; A796D12EE94190C5 CRC64;
MSEKRKPLLG FVGKLPSGTA LGNLGKTHCP SCLGLFKNPR LLPCLHTVCT TCLEQLEPFS
VVDIRGGDSD TSSEGSIFQE LKPHGLQPQI GILCPVCDAQ VDLPMGGVKA LTIDHLAMND
VMLESLRGEG QGLVCDLCSD REVEKRCQTC KANLCHFCCQ AHRRQKKTTY HTMVDLEDLK
GYSRIGKAIL CPAHPAEELR LFCELCDQPV CRDCVVGEHR EHPCDFTSNV IHKHGDSVRE
LLKDTQPHVE ALEDALAQIK ETSSALQQRV EAVAADIRTF SEGYVKAIEE HRDKLLKQLE
DIRIQKENSL QLQKAQLEQL LADMRTGVEF TEHLLTCGSD LEILITKGVV VERLMKLNQV
EYTAHPRVND KICFSPQEKA GRCRGYEVYG VINTKEVDPA KCVLQGEDLH RAREKQTTSF
TLLCKDAAGE SMGRGGDNVQ VAVVPKDKKD SPVRTMVQDN KDGTYCVSFT PKEPGIYTVL
VCIKEQHVQG SPFTVTVRKR HRSHPGVFHC CTFCSSGGQK TARCACGGTM PGGYLGCGHG
HKGHPGRPHW SCCGKFTEKS ECTWAGGQSA ARSLLRTVAL
//
