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Database: UniProt
Entry: A0A3B4H0A7_9CICH
LinkDB: A0A3B4H0A7_9CICH
Original site: A0A3B4H0A7_9CICH 
ID   A0A3B4H0A7_9CICH        Unreviewed;       673 AA.
AC   A0A3B4H0A7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=TRIM67 {ECO:0000313|Ensembl:ENSPNYP00000029072.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000029072.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000029072.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
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DR   AlphaFoldDB; A0A3B4H0A7; -.
DR   Ensembl; ENSPNYT00000029782.1; ENSPNYP00000029072.1; ENSPNYG00000021896.1.
DR   GeneTree; ENSGT00940000154071; -.
DR   Proteomes; UP000261460; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; 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; cd00063; FN3; 1.
DR   CDD; cd12889; SPRY_PRY_TRIM67_9; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 4.10.830.40; -; 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; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR017903; COS_domain.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003877; SPRY_dom.
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; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR   PANTHER; PTHR24099:SF21; TRIPARTITE MOTIF-CONTAINING PROTEIN 67; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00622; SPRY; 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; SM00060; FN3; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS51262; COS; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50119; ZF_BBOX; 2.
DR   PROSITE; PS00518; ZF_RING_1; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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          163..212
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          225..267
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          375..433
FT                   /note="COS"
FT                   /evidence="ECO:0000259|PROSITE:PS51262"
FT   DOMAIN          438..532
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          514..673
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
SQ   SEQUENCE   673 AA;  74578 MW;  6EDA80913EBA019C CRC64;
     MIAVTALVYW QKRGSDEETM EEELKCPVCG SLFKDPILLP CSHNVCLGCA RNITVQTPEG
     ETPVQSRASG SSDYDYLDMD KMSLYSETDS GYGSYTPCQL KSPNGVRVFP PAIPHRQCTL
     TCPLCHRSVS LDERGLRGFP RNRLLEAIVA RYQQTRGASS SSSNAVKCQL CDRNPVDAAV
     MCEQCDVYYC NACQQRCHPS RGPLAKHRLV PPGGGGGQQP PATARKPATC VDHEAENFSM
     YCSSCKAPVC MKCLEEGKHA KHDVKPLAVM WKQHKCQISQ ALNGVSDKAK DAKEFLVQLK
     NMLQQIQENG VEFEACLVAQ CDSLIEALTR QKAKLLTKVT KEKEYKLKVV RDQITHCTMK
     LRQTTGMMEY CLEVLKENDP SGFLQISDAL IKRVTSSQDQ WVKGALEPKV GPDFDLTLNT
     DSLLQTILQL DFCQGKVPPA PLLQLEKCCT RNNSATLAWR VAMPTINPIE GYILELDDGN
     GGQYREVYVG KETVCTVDGL HFNSSYNARV KAYNSIGVGP YSKTVMLKTS DVAWFTFDPT
     SAHRDIVLTN DNQTVSCNSY DDRVVLGTAA FSKGIHYWEV SIDRYDNHPD PAFGIARINT
     MKDMMLGKDD KAWAMAEGGI TKGSTVGVLL DLTKRTLTFY INKEQHGPTA FENLDGVFVP
     AVSLNRNVQV CVC
//
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