ID A0A1V9ZH29_9STRA Unreviewed; 544 AA.
AC A0A1V9ZH29;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=C3H1-type domain-containing protein {ECO:0000259|PROSITE:PS50103};
GN ORFNames=ACHHYP_12217 {ECO:0000313|EMBL:OQR97298.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR97298.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR97298.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR97298.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR97298.1}.
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DR EMBL; JNBR01000118; OQR97298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9ZH29; -.
DR STRING; 1202772.A0A1V9ZH29; -.
DR OrthoDB; 56980at2759; -.
DR Proteomes; UP000243579; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.1370.210; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF14608; zf-CCCH_2; 1.
DR SMART; SM00582; RPR; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000243579};
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 367..394
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 410..437
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 367..394
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 410..437
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 136..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..255
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..308
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..358
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..531
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 58956 MW; 28D6AE57356D7DA7 CRC64;
MALSWKEGEA DLKEALAPIA TPKGTSATKV KTASALCLRM VKDYKRVVHA VETLMWKSEH
RLGFLYLIDA IIRQSQAKFG SEKDLFAPRF SQHLSHTISS LKQLPDDGQE HAHRIVYDWV
TRRVFTKEQI IKAGGADYVQ SPPPQHSPPA AAAPLNSDAE KEKLAILLDN IKRLKQQQEE
KVPDVAHTSY APPASDPRAF APSPRASYPS SPRSRTSYAP PQQGGPSYAP PRPSPSNYAP
PAATNYAPPP ATSYAPPQQS YAGYAPQSYG SAPPAPRYSQ PRRESPPRKQ RDRSRSRSPR
RSRMRSRSRS PPRRQETGPP PYNGGPPLRQ PSPTYPPPHA AFSGPPPSYP PPGPAQSNTP
FGQPQGGYGK GICRDYTLGR CFRGAACRFL HEGPTSQPPE AARAPLRPGQ LKTRLCMNFP
AGGCRFGDRC TFAHGEAQLG TTVDAMPPRS SPPPPDAFVP SNASYPSSNS MADNTFGAPH
NTLPAAPKPA GEAESPAKRP RPSRWGAKST APPAEAAPVV AKPPPEEEEP APAPEFTLEY
DDDE
//
