MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
Description | RecName: Full=Staphylococcal nuclease domain-containing protein 1; AltName: Full=100 kDa coactivator; AltName: Full=4SNc-Tudor domain protein; AltName: Full=p100 co-activator; |
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MyHits synonyms | SND1_DANRE , Q7ZT42 , Q6DEI2 , Q7SX79 , Q7ZZS7 , Q8AXL0 , 367B9B6428C306A3 |
![]() Legends: 1, VAR_SEQ R -> RYGDFRDDDADEFGYRR (in isoform 2). {ECO:0000303|PubMed:12753931, ECO:0000303|Ref.3}; 2, CONFLICT I -> K (in Ref. 1; AAP23062 and 3; AAH77133). {ECO:0000305}; 3, CONFLICT D -> G (in Ref. 1; AAP23062 and 3; AAH77133). {ECO:0000305}; 4, CONFLICT D -> E (in Ref. 1; AAP23062 and 3; AAH77133). {ECO:0000305}; 5, CONFLICT Y -> C (in Ref. 3; AAH77133). {ECO:0000305}; 6, CONFLICT N -> K (in Ref. 1; AAP23062 and 3; AAH77133). {ECO:0000305}; 7, CONFLICT V -> F (in Ref. 1; AAP23062). {ECO:0000305}; 8, CONFLICT M -> S (in Ref. 1; AAP23062 and 3; AAH77133). {ECO:0000305}; 9, TNase-like 1. {ECO:0000255|PROSITE- ProRule:PRU00272}; 10, TNase-like 2. {ECO:0000255|PROSITE- ProRule:PRU00272}; 11, TNase-like 3. {ECO:0000255|PROSITE- ProRule:PRU00272}; 12, TNase-like 4. {ECO:0000255|PROSITE- ProRule:PRU00272}; 13, Tudor. {ECO:0000255|PROSITE- ProRule:PRU00211}; 14, VAR_SEQ IECPRGSRNMPGGM -> KCQPASACQLYHHL (in isoform 3). {ECO:0000303|PubMed:12753931}; 15, VAR_SEQ Missing (in isoform 3). {ECO:0000303|PubMed:12753931}; 16, CONFLICT GRNTDPSTSL -> VAKYRSVYVT (in Ref. 1; AAP23062 and 3). {ECO:0000305}; 17, ipfam:SNase [T]; 18, ipfam:TUDOR [T]; 19, iprf:TUDOR [T]; 20, ipat:TNASE_2 [T]; 21, ismart:TUDOR [T].
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ID SND1_DANRE Reviewed; 897 AA. AC Q7ZT42; Q6DEI2; Q7SX79; Q7ZZS7; Q8AXL0; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 10-MAY-2017, entry version 106. DE RecName: Full=Staphylococcal nuclease domain-containing protein 1; DE AltName: Full=100 kDa coactivator; DE AltName: Full=4SNc-Tudor domain protein; DE AltName: Full=p100 co-activator; GN Name=snd1; Synonyms=sn4tdr; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, RP AND DEVELOPMENTAL STAGE. RX PubMed=12753931; DOI=10.1016/S0014-5793(03)00445-9; RA Zhao C.T., Shi K.H., Su Y., Liang L.Y., Yan Y., Postlethwait J., RA Meng A.M.; RT "Two variants of zebrafish p100 are expressed during embryogenesis and RT regulated by Nodal signaling."; RL FEBS Lett. 543:190-195(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Abe S., Wang P.; RT "Danio rerio full mRNA for 4SNc-Tudor domain protein, complete cds."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Embryo; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12753931}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q7ZT42-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7ZT42-2; Sequence=VSP_012670; CC Name=3; CC IsoId=Q7ZT42-3; Sequence=VSP_012671, VSP_012669; CC -!- DEVELOPMENTAL STAGE: During the blastula period expressed in all CC blastomeres. At the onset of gastrulation, expressed more in the CC embryonic shield than in other regions. As embryos elongate, CC expression in the shield migrates toward the animal pole and forms CC a longitudinal band in the dorsal midline. At late gastrulation, CC expressed in the dorsal midline extending from the tailbud to the CC animal pole. Expression is under the control of Nodal signals. CC {ECO:0000269|PubMed:12753931}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH77133.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAN76663.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAP23062.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC76713.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC76779.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY272050; AAP23062.1; ALT_INIT; mRNA. DR EMBL; AF422806; AAN76663.2; ALT_INIT; mRNA. DR EMBL; AB098074; BAC56985.1; -; mRNA. DR EMBL; AB110096; BAC76712.1; -; mRNA. DR EMBL; AB110096; BAC76713.1; ALT_INIT; mRNA. DR EMBL; AB110445; BAC76779.1; ALT_INIT; mRNA. DR EMBL; BC077133; AAH77133.1; ALT_INIT; mRNA. DR RefSeq; NP_001280610.1; NM_001293681.1. [Q7ZT42-3] DR UniGene; Dr.76177; -. DR ProteinModelPortal; Q7ZT42; -. DR SMR; Q7ZT42; -. DR STRING; 7955.ENSDARP00000040404; -. DR PaxDb; Q7ZT42; -. DR PeptideAtlas; Q7ZT42; -. DR PRIDE; Q7ZT42; -. DR Ensembl; ENSDART00000100974; ENSDARP00000091746; ENSDARG00000006766. [Q7ZT42-3] DR GeneID; 324404; -. DR KEGG; dre:324404; -. DR CTD; 27044; -. DR ZFIN; ZDB-GENE-030131-3124; snd1. DR eggNOG; KOG2039; Eukaryota. DR eggNOG; COG1525; LUCA. DR GeneTree; ENSGT00510000047270; -. DR HOGENOM; HOG000173592; -. DR HOVERGEN; HBG057234; -. DR InParanoid; Q7ZT42; -. DR KO; K15979; -. DR PRO; PR:Q7ZT42; -. DR Proteomes; UP000000437; Chromosome 4. DR Bgee; ENSDARG00000006766; -. DR ExpressionAtlas; Q7ZT42; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:ZFIN. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0016442; C:RISC complex; IEA:InterPro. DR GO; GO:0004518; F:nuclease activity; IBA:GO_Central. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro. DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central. DR InterPro; IPR016685; Silence_cplx_Nase-comp_TudorSN. DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold. DR InterPro; IPR002071; Thermonucl_AS. DR InterPro; IPR002999; Tudor. DR Pfam; PF00565; SNase; 4. DR Pfam; PF00567; TUDOR; 1. DR PIRSF; PIRSF017179; RISC-Tudor-SN; 1. DR SMART; SM00318; SNc; 4. DR SMART; SM00333; TUDOR; 1. DR SUPFAM; SSF50199; SSF50199; 6. DR PROSITE; PS01284; TNASE_2; 1. DR PROSITE; PS50830; TNASE_3; 4. DR PROSITE; PS50304; TUDOR; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Cytoplasm; KW Reference proteome; Repeat. FT CHAIN 1 897 Staphylococcal nuclease domain-containing FT protein 1. FT /FTId=PRO_0000183183. FT DOMAIN 18 167 TNase-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00272}. FT DOMAIN 194 329 TNase-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00272}. FT DOMAIN 342 499 TNase-like 3. {ECO:0000255|PROSITE- FT ProRule:PRU00272}. FT DOMAIN 528 663 TNase-like 4. {ECO:0000255|PROSITE- FT ProRule:PRU00272}. FT DOMAIN 732 790 Tudor. {ECO:0000255|PROSITE- FT ProRule:PRU00211}. FT VAR_SEQ 561 574 IECPRGSRNMPGGM -> KCQPASACQLYHHL (in FT isoform 3). FT {ECO:0000303|PubMed:12753931}. FT /FTId=VSP_012671. FT VAR_SEQ 575 897 Missing (in isoform 3). FT {ECO:0000303|PubMed:12753931}. FT /FTId=VSP_012669. FT VAR_SEQ 897 897 R -> RYGDFRDDDADEFGYRR (in isoform 2). FT {ECO:0000303|PubMed:12753931, FT ECO:0000303|Ref.3}. FT /FTId=VSP_012670. FT CONFLICT 606 606 I -> K (in Ref. 1; AAP23062 and 3; FT AAH77133). {ECO:0000305}. FT CONFLICT 612 612 D -> G (in Ref. 1; AAP23062 and 3; FT AAH77133). {ECO:0000305}. FT CONFLICT 617 617 D -> E (in Ref. 1; AAP23062 and 3; FT AAH77133). {ECO:0000305}. FT CONFLICT 643 643 Y -> C (in Ref. 3; AAH77133). FT {ECO:0000305}. FT CONFLICT 669 669 N -> K (in Ref. 1; AAP23062 and 3; FT AAH77133). {ECO:0000305}. FT CONFLICT 682 691 GRNTDPSTSL -> VAKYRSVYVT (in Ref. 1; FT AAP23062 and 3). {ECO:0000305}. FT CONFLICT 753 753 V -> F (in Ref. 1; AAP23062). FT {ECO:0000305}. FT CONFLICT 838 838 M -> S (in Ref. 1; AAP23062 and 3; FT AAH77133). {ECO:0000305}. CC -------------------------------------------------------------------------- CC The following FT lines are automated annotations from the MyHits database. CC -------------------------------------------------------------------------- FT MYHIT 342 499 ismart:SNc [T] FT MYHIT 18 167 iprf:TNASE_3 [T] FT MYHIT 194 329 iprf:TNASE_3 [T] FT MYHIT 342 499 iprf:TNASE_3 [T] FT MYHIT 194 329 ismart:SNc [T] FT MYHIT 528 663 iprf:TNASE_3 [T] FT MYHIT 556 662 ipfam:SNase [T] FT MYHIT 692 801 ipfam:TUDOR [T] FT MYHIT 18 167 ismart:SNc [T] FT MYHIT 221 329 ipfam:SNase [T] FT MYHIT 369 498 ipfam:SNase [T] FT MYHIT 732 790 iprf:TUDOR [T] FT MYHIT 103 113 ipat:TNASE_2 [T] FT MYHIT 68 167 ipfam:SNase [T] FT MYHIT 731 788 ismart:TUDOR [T] FT MYHIT 528 663 ismart:SNc [T] SQ SEQUENCE 897 AA; 100535 MW; 367B9B6428C306A3 CRC64; MASAVPAQVQ SSQASAPQLQ RGIVKMVLSG CAIIVRGQPR GGPPPERQIN LSNIRAGALA RRAIQGQPDT KDTPDEPWAF QAREFMRKKV IGKEVCFTVE NKTPQGREYG MVYLGKDTSG ENIAESLVAE GLAMVRREGI RGNNPEQVRL CDLEDQAKSS KKGLWSEGGG SHTIRDLKYT IENPRNFVDS LHQKPVNAII EHVRDGCMVR ALLLPDYYLV TVMLSGIKSP TFKREADGSE TPEPFAAEAK FFTESRLLQR DVQIILESCP NQVILGTILH PNGNITELLL KEGFARCVDW SMAVYTQGAE KLRAAERSAK ERKVRIWKDY VAPTANLDQK DRQFVAKVMQ VVNADAIVVK LNSGEYKTIH LSSIRPPRLE GEEKNKDKDK RFRPLYDIPY MFEAREFLRK KLIGKKVNVT VDYIRAATNA MEMGVPAFPE RTCATVTIGG INIAEALVSK GLATVIRYRQ DDDQRSSHYD ELLAAEARAI KNGKGLHSKK EVPIHRVADI SGETQKAKQF FPFLQRAGRS EAVVEYVFSG SRLKLYMPKE TCLITFLLAG IECPRGSRNM PGGMQVAEPY SEEAMLFTKE LVLQREVEVE VESMDIAGNF IDWLHIDGVN LSVALVENAL SKVHFTAERS SYYKTLVSAE ESARQRKEKL WANYEEKPNE EVAQVTEAKE RGRNTDPSTS LEITDGLHFY AQDVETGTKL ENLMESMRGE IAAQPPVEGS FAPRRGEFCI AKFADGEWYR ARVEKVESPA KVHVFYIDYG NREVLSSTRL AALPPAFSTR TLPPQATEYA FAYIQVPQDE DARADAVDSV VRDIHNTQCL LNVEYSGMVC PQVTLQFADT KEDVGLGLVK EGMVMVDIRK EKYLQKMVTE YLNAQESAKS ARLNIWR // |