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Database: UniProt
Entry: A0A0K0FMJ3_STRVS
LinkDB: A0A0K0FMJ3_STRVS
Original site: A0A0K0FMJ3_STRVS 
ID   A0A0K0FMJ3_STRVS        Unreviewed;      1544 AA.
AC   A0A0K0FMJ3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Schnurri (inferred by orthology to a D. melanogaster protein) {ECO:0000313|WBParaSite:SVE_1022000.1};
OS   Strongyloides venezuelensis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=75913 {ECO:0000313|Proteomes:UP000035680, ECO:0000313|WBParaSite:SVE_1022000.1};
RN   [1] {ECO:0000313|Proteomes:UP000035680}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A, De Silva N.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SVE_1022000.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   STRING; 75913.A0A0K0FMJ3; -.
DR   WBParaSite; SVE_1022000.1; SVE_1022000.1; SVE_1022000.
DR   Proteomes; UP000035680; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45944; SCHNURRI, ISOFORM F; 1.
DR   PANTHER; PTHR45944:SF2; SCHNURRI, ISOFORM F; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   Pfam; PF12874; zf-met; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035680};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00042}.
FT   DOMAIN          1059..1086
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1087..1116
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1342..1369
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1452..1481
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          581..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          842..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          990..1027
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1227..1256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1422..1444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..858
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1242..1256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1544 AA;  172603 MW;  32E47E44A0ADE79F CRC64;
     MSFISNEGLG SSHPSIPINQ NQDISALLNS GQVSGNLLNS LNNGSTLLQQ TNNNQHTLND
     LSTIILQQQL LSQLQQNSGN SNQSSFIGTG NGQVGNIITN TNPSNNAAIY QQLLNQQHQQ
     QQQQNSILLN AATAQNQQPS LSQLLQLQQV QNQLQNCGNL QNSSLQTQNI QQYNSAFKSQ
     TQIPPQQSPQ QQGSINPTIL QQLINAGVSP AILAKLLSGN SQPTNQVNYS PATATQANFL
     LQQQLHLANQ PQMQQNLQQQ INKMIEAHKQ QQLAEKRAME ERHMLNQLLV AANQNNTVGV
     SLPLPFQGNN NNLAQQLQVQ GISTEEDTQK FIKEYMLKQS GSLNNTPILA QQTHQQLQNQ
     THQVLVSTGN GIINGLQNQP LLQQQQQAQQ LSATINLPQS ISIPQSTSSS TPLTKEPSSV
     QLLKDPKSVT NHIQQLINRN EAIIEPSPVL TRRRPYCRQP SNTTVVDNQL ASISNRSSFS
     DKESPTNQIN SGGIEYNQTI NSNSLESCIR QTSSIEMVNN IPVTSLPSGT GNGSLTNGQP
     FIRDLGKIHP RGFACEFCNL LFPNKAGLQA HSFRCSRNEE GESINKDSSN SGNVVTPTNV
     SLPNNNVDNG IMSSTLIPNP LKQQECDNRG SSNLSTNSSM VGNSLKRSFP SIDCMAEDVI
     KNLPFKLFKM KDLRQMSEQS FSEFAAEAKN IIPTIDQGLL KPGDDENVLI ELRTKMLKHA
     IKKVADYDSN VEENAWNNLL KSDNNLQQQQ QSNAPDFIKQ EIPGVVDGQK NDNNNKTNEL
     SNVVRNSGLL SDNNIRNQSL MDTLSLSPST HQNIKTAVES AVSYVRQNVS AHMPYSVTIN
     NLSSENQGTN ISDESQDAKS SLPNKHRSRN ITSETYFCVN TLPVHEEQID TQSSLFANWK
     APLPEENNFS QYLKSCNLKT RTGNKNTYEY TTAKGDVNCL KMTHSTYWYQ SKNITDGSVK
     KDPMDDNCIK EVVELVPVTE EIKKEEVPIQ QTSNRYPISN ISPQTSENSE KSFTITKPPQ
     QTSTNDNNKR IRIESSNGLA GYKTDEVYVY VRGRGRGRYV CERCGIRCKK PSMLKKHLNS
     HTDIRPFKCI QCNFSFKTKG NLTKHLLSKA HSRKLAEQKS GIELSDQPTT SINNILSSDE
     GQLQIITEDP SEAADIVKMG KHEAAFMNID NESDDEDENR RAPVYERNIY RKYGQEVIIH
     DRRAHTPPSL WCNPFVPEDT PTWAEPEFNR SCQSAPPASF SEHEIENEED TRKKQDFQKT
     IQRIRNESIS MASFLDEMSF ANPINTPTKI NNKHQNLCSN KDLNDNNGCQ INGQINNMKI
     NISNHLNTTT MDSFLAKDVN EYACDICEKK FRKEQEWILH QHTHTIEKNS HRVKNYYCPK
     CRTCTRSKTS MIKHIEAFHT LNASTIKSLF LEKLNNNEEI SLSGHVSPNE NSSNSSTSST
     PTYNMNNGSR TFLCNDCNKG FRTHGVLAKH LRSQQHITKM SILGKLNEDQ TCALRRNPHC
     LTKVDTKDCD AARQSIISKA NEILEDEKNG ITPVMTVIPN DNKT
//
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