ID A0A176VWA8_MARPO Unreviewed; 1258 AA.
AC A0A176VWA8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN ORFNames=AXG93_4452s1030 {ECO:0000313|EMBL:OAE25037.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE25037.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE25037.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE25037.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the NEMF family.
CC {ECO:0000256|ARBA:ARBA00008318}.
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:OAE25037.1}.
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DR EMBL; LVLJ01002427; OAE25037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VWA8; -.
DR OrthoDB; 129892at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:UniProt.
DR Gene3D; 2.30.310.10; ibrinogen binding protein from staphylococcus aureus domain; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR021846; NFACT-C.
DR InterPro; IPR008532; NFACT_RNA-bd.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR15239; NUCLEAR EXPORT MEDIATOR FACTOR NEMF; 1.
DR PANTHER; PTHR15239:SF6; RIBOSOME QUALITY CONTROL COMPLEX SUBUNIT NEMF; 1.
DR Pfam; PF11923; NFACT-C; 1.
DR Pfam; PF05670; NFACT-R_1; 1.
DR Pfam; PF05833; NFACT_N; 2.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 1012..1026
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 192..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1258 AA; 140303 MW; F55F1999736E400C CRC64;
MVKVRMTTAD VAAEVRCLRR LIGMRCANIY DLSPKTYVIK FAKSSGVAES GESERALVLL
ESGVRLHTTE FSRDKSSTPS GFTLKLRKHL RTRRLEDVRQ LGIDRVVDFQ FGLGEGAFHI
ILELYSQGNL LLTDSHHNVI TLLRTHRDDE KGLLMMAHHQ YPINSCRLFE RTKKEAISTL
LKEQTRLKAD EAVEEQQAAS KEVHTGSVNE DAKKTKWKPE GKGSKSASQE VSGNGKKGAG
LPTLKFLLVE GLGYGPSLSE HIILSAGLQP GLKMNSSILS RDEFEALAAA IKRFEDWLEA
VVSGDIVPEG YIYMQKVGMG KAKSAASDVK EEFDRVYDEF SPLDLKQMKD RESMKLATFD
AAMDEYYSKV EGQRADQQRR TQEESALTKL DKIRADQTNR VKALKREVDQ SVHMAELIEY
NLDDVDAAIL AVRTALASGM DWKDLGRMIK EEKKAGNPVA GVIHSLQLET NQITLLLSNN
LDDMDEEEKT RPVDKVEVDL SLSAHANARR WFEMKKKHAT KQEKTLAAHE KAFKAAEKKT
QQQLAQAKTV AAITHIRKMH WFEKFNWFIS SENYLVISGR DAQQNELVVK RYMKKGDLLV
RSPWSVQHSN KKQRSYKTHT ALHYKPSGVV HREFKLQILF YYSRLMSQVC RSQAWDSKIV
TSAWWVHPHQ VSKTAPTGEY LTVGSFMVRG KKNFLAPNPL VMGYGLLFRL DESCIAAHLN
ERRIRGDGEG EESERAAFVE AGHPEVGKSS NRNNDDDEEN IEVPSEDQDQ EVRADTSDND
DEGFQEKSRS GSDRSDGMGS ELMTAVHGTN ISEGGDDSGF DALLDKAFEL RSAHKVTSNK
YGLELVNVTT DADRNVDSAP GNVKMSKAVQ REKPYVSRAE RRKLKKGSKH GKDDERNGVA
GDEELATVEG QERLDNLDIS DELSALGTVE GGPDSSPGGS KPSRGRKGKL KKIKEKYAEQ
DEEERQLRMS LLASAGRKES KQPKALGVNG KASTSSKTTF NEQDAGLKEK VCYKCKKTGH
IVRDCPYETA SLSAKDERPT YVGDSQNLAT ERIQKASTDD DAREGIMQPI VRNEAEKPKD
GLSRRAYSKA AKEEIAAIMA EENVVELGDD DKEKLIELDS LTGIPHSSDV LLYSVPMCGP
YSALQAFKYR VKLTPGPAKK GKVYGLDFEL EFEALNSKLI FAKMRGDGLD HNAAAKVAID
VFSHMPETTV REKELMKAVT DPELVACMLG NAKVTAPGLT KLKKTQKKWK KVASKEVG
//
