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Database: UniProt
Entry: V5I3J7_IXORI
LinkDB: V5I3J7_IXORI
Original site: V5I3J7_IXORI 
ID   V5I3J7_IXORI            Unreviewed;       901 AA.
AC   V5I3J7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Serine/threonine-protein phosphatase 1 regulatory subunit 10 {ECO:0000256|ARBA:ARBA00022330};
OS   Ixodes ricinus (Common tick) (Acarus ricinus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB82438.1};
RN   [1] {ECO:0000313|EMBL:JAB82438.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB82438.1};
RX   PubMed=25765539;
RA   Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT   "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT   and midguts when blood feeding on the vertebrate host.";
RL   Sci. Rep. 5:9103-9103(2015).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00649}.
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DR   EMBL; GANP01002030; JAB82438.1; -; mRNA.
DR   AlphaFoldDB; V5I3J7; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR   InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR   InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR   InterPro; IPR017923; TFIIS_N.
DR   InterPro; IPR000571; Znf_CCCH.
DR   PANTHER; PTHR46557:SF1; SERINE/THREONINE-PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 10; 1.
DR   PANTHER; PTHR46557; SERINE/THREONINE-PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 10-RELATED; 1.
DR   Pfam; PF08711; Med26; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00509; TFS2N; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR   PROSITE; PS51319; TFIIS_N; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00649};
KW   Protein phosphatase inhibitor {ECO:0000256|ARBA:ARBA00023272};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT   DOMAIN          71..144
FT                   /note="TFIIS N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51319"
FT   DOMAIN          868..895
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         868..895
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          146..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          820..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..442
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..479
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..768
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        822..836
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   901 AA;  96542 MW;  9CDC76ECA1486338 CRC64;
     MAPIDPLQLL KALSPLLSAE GGIRSSDEVS RLSSLMKKFS RKLVSRCIYC NVLRATSSDI
     LEVFLDLDGW STIHMWLQEA KTADNRPFLL ELLKLCQVLP MSLERLKENS SPKLIKGLTK
     CSSEEVRLMA EKVVTGWMKL IKGDSKEAVK PVKDTAEPGA KKKKTKSPVG APAVSPKGAL
     KRERSKGSQD ESPQEQVAPK GNTTPVHPST RTGPAGKDSP PTPKESPVAP KKPKAQDRPK
     TVKTFQTRFR STGLEESPLP PPVKAGAKKV VRPAVDKNAL LSARQRLAPT VHAERRVKPS
     SLVSMGGDGK EAAGPGIRLI APKPVHVLQE DGGFMDALTA VPVVPAVPGK RKRKNSAAGG
     SPATPTNAKE KGATPPTSSS PTSPPPVAPK FQFYKDTLET GEGAEAAEEE EDIGKRVKRR
     KRGQAKEGKE EASEKEGAEE SAASPEGDSP PTPTGEEEEG TAEKEEETVE KKEEEVEVGA
     GDASAGSDKL ASDRPASILS MTRKKTKKTV RWVEESKLKQ FHFFDLDETE RVNVNNMQNF
     GDLKTLEMKR ERQVVETARR MMGDRMEEAL PYRMPRLLER PEPLAEPGSG SHEKEVQKLR
     QQKTLQEIYF SKDMIPDSPY EPDAEQVSGQ EPKQIPLEDE NSPSATLDYS NMEVPKASSL
     PSILSNLVLS IASKTQGGPQ GPPQQGGQAP QGHMMPGGHV RMPGQQHHQG PMPGQMQGQM
     PPQSMMPDMQ GPPIHMGGGG GNLLGGDPQC QNGPPNFMHP NNMQGQGMNM MGPPVSMAGG
     GGFPNMGMPM GHGGGNGGGG GDWGMMPPMG AEGDFFRGPP PGMGGGGPPM GMGGGAPPPP
     MGSAVQHMMD MARGNMPPHG GGRNSRMRTP RVPCKYYMTS TCRFGTSCSF LHPGVNGPPL
     Q
//
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