ID A0A183R401_9TREM Unreviewed; 691 AA.
AC A0A183R401;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
OS Schistosoma rodhaini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6188 {ECO:0000313|Proteomes:UP000050792, ECO:0000313|WBParaSite:SROB_0001069201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SROB_0001069201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
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DR AlphaFoldDB; A0A183R401; -.
DR STRING; 6188.A0A183R401; -.
DR WBParaSite; SROB_0001069201-mRNA-1; SROB_0001069201-mRNA-1; SROB_0001069201.
DR Proteomes; UP000050792; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR045124; Su(sable)-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR13119:SF12; PROTEIN SUPPRESSOR OF SABLE; 1.
DR PANTHER; PTHR13119; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEI; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR SUPFAM; SSF90229; CCCH zinc finger; 3.
DR PROSITE; PS50103; ZF_C3H1; 3.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 134..161
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 163..190
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 191..214
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 134..161
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 163..190
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 191..214
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 77809 MW; EB9C61F74D6EA206 CRC64;
MTSVDFEEGE VEDLSGSDHE DSGHEYTNYG PTKVSLHKSS KRKRHTERNA DRFRCSRRES
TVLLGLRAVE LPHVDGRNAN SKRSKERSKL PLLEFLSEDE DDTYLMNHEE PDKTKSSERS
RKRKKRKKDA PHRSASQSRC KYYMDGRCSK GCSCPFLHDF TPAKKNELCK FYAVGMCSKE
SACSFLHGEF PCKFFHLTND CHHGSDCKFS HAPLTEFTRS LLEKISSKHS VDRCSKPGLV
RQPDSKSFMS GRPRNDDHGD VDYRFDQNLP QMNIPSEKEL ATPGFSPQRM PVLTPNLFAP
VCTPSPRHFR PEHEISRARG MRPFNMVPGE QMPQTVYPKN DRCFPSPVPY GPVPFQSQHV
MSNATCSPTV NGFRPPSLLD TPLRCPPSRI MPPRMRTMDP GSMRFPRFRP RCETFYGAGV
RPSPPIRPNF DAVREEAIVS SELDMMAALL ASSKTMNDDC KNGSTIPPSS PTCVGEHSLQ
LESASPPQLF SKTETEAIPP NIVVEDRSAP EFTTTTQVGG VTPSQGPAPW RLIPLDMTVK
IPYPLMELPV DDLPYRFEDP RLRGQLTTFR LQPPSKPSSV SDPENSRCND EPEAQNHNET
NPIGTNGDNP GGLTQRRPIK LQLHEMANTF ANTSSDHLHA PSRQGDRSYL DDPRFRRRRI
MVPAPTSQSA SNVLNQDNPN NTPQTTQECS N
//