ID A0A2K1L2V0_PHYPA Unreviewed; 979 AA.
AC A0A2K1L2V0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=NF-X1-type domain-containing protein {ECO:0000259|SMART:SM00438};
GN ORFNames=PHYPA_003145 {ECO:0000313|EMBL:PNR60352.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR60352.1};
RN [1] {ECO:0000313|EMBL:PNR60352.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c2_24250V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR60352.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c2_24250V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c2_24250V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the NFX1 family.
CC {ECO:0000256|ARBA:ARBA00007269}.
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DR EMBL; ABEU02000002; PNR60352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1L2V0; -.
DR STRING; 3218.A0A2K1L2V0; -.
DR PaxDb; 3218-PP1S135_24V6-1; -.
DR EnsemblPlants; Pp3c2_24250V3.1; Pp3c2_24250V3.1; Pp3c2_24250.
DR EnsemblPlants; Pp3c2_24250V3.2; Pp3c2_24250V3.2; Pp3c2_24250.
DR Gramene; Pp3c2_24250V3.1; Pp3c2_24250V3.1; Pp3c2_24250.
DR Gramene; Pp3c2_24250V3.2; Pp3c2_24250V3.2; Pp3c2_24250.
DR InParanoid; A0A2K1L2V0; -.
DR OMA; KCQSVCH; -.
DR OrthoDB; 1412at2759; -.
DR Proteomes; UP000006727; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IEA:EnsemblPlants.
DR GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
DR CDD; cd06008; NF-X1-zinc-finger; 6.
DR CDD; cd16697; RING-CH-C4HC3_NFXL1; 1.
DR InterPro; IPR034078; NFX1_fam.
DR InterPro; IPR000967; Znf_NFX1.
DR PANTHER; PTHR12360:SF1; NF-X1-TYPE ZINC FINGER PROTEIN NFXL1; 1.
DR PANTHER; PTHR12360; NUCLEAR TRANSCRIPTION FACTOR, X-BOX BINDING 1 NFX1; 1.
DR Pfam; PF01422; zf-NF-X1; 11.
DR SMART; SM00438; ZnF_NFX; 10.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 935..953
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 240..258
FT /note="NF-X1-type"
FT /evidence="ECO:0000259|SMART:SM00438"
FT DOMAIN 292..311
FT /note="NF-X1-type"
FT /evidence="ECO:0000259|SMART:SM00438"
FT DOMAIN 345..364
FT /note="NF-X1-type"
FT /evidence="ECO:0000259|SMART:SM00438"
FT DOMAIN 399..419
FT /note="NF-X1-type"
FT /evidence="ECO:0000259|SMART:SM00438"
FT DOMAIN 452..471
FT /note="NF-X1-type"
FT /evidence="ECO:0000259|SMART:SM00438"
FT DOMAIN 479..498
FT /note="NF-X1-type"
FT /evidence="ECO:0000259|SMART:SM00438"
FT DOMAIN 536..557
FT /note="NF-X1-type"
FT /evidence="ECO:0000259|SMART:SM00438"
FT DOMAIN 565..610
FT /note="NF-X1-type"
FT /evidence="ECO:0000259|SMART:SM00438"
FT DOMAIN 744..762
FT /note="NF-X1-type"
FT /evidence="ECO:0000259|SMART:SM00438"
FT DOMAIN 807..829
FT /note="NF-X1-type"
FT /evidence="ECO:0000259|SMART:SM00438"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 107323 MW; 749629761CA8F0EE CRC64;
MIHARAMDKG SVSHAAGTSS QGRNAWNTPL RNQPQSQASA AIKMPVKNPP LSFTNQPALA
DPIYSSSDED SESGGEGGAR GRDVDALESA IMADYPTTED IDDTGLTKIR SLLLARRSGA
TSCLICLERV RATDPVWDCK AGCHVIFHLI CIQSWARQAL GAAAIRSLGQ LSGQHFPAAQ
AEAEDKACWH CPKCRTDYSK SELPREYRCF CGKQEHPVHD PWLAPHTCGE RCGRALPSKC
GHECVLLCHP GPCPTCPQLL KFSCFCGAES KMRRCGHSKF SCGRECKKVL SCGKHKCENA
CHDGDCPPCS KTAVHKCQCG KTSAIRACAE SNFRCENPCG RQLSCQKHCC QRGCHSGPCG
DCYLTGKRSC PCGKVEHKGV PCDVVIPTCG STCEKVLPCQ IHRCSERCHY GSCKEVCRVV
LVKSCRCGSL KKEVPCHQEL LCERKCQRMK DCGRHACKRR CCDGDCPLCS EVCGRRLKCG
NHKCPAPCHR GLCAPCPINV QISCACGATC IQVPCGTERT QRPPRCVKLC SISPKCNHGS
NCKPHRCHYG ACPECQLPCM TLLPCGHNCK ERCHGAKPVP NPDYTYKTKK KKPIHDGSAS
IGEPCPACSE RIVKKCLGQH QGSERTMVCS QSAEFRCSKL CGNPLACGNH ICRNSCHFVT
IPRIVAGEEV YVKQVVVMPS GIDLAEPTDE PERVWGKYGS SPLNEKGNSN NLVQETSTQP
DNVKVVDSCE QCRLPCQKKR FLRCPHPCTQ ICHIGDCKPC KAVLKRACHC EALVQSFECT
AFNSVSDKER AKLLSCGGPC HKKLPNCSHL CPDICHPGIC PTAADSCRKK VTVRCACQRL
KKEWLCCDAQ AALPKGSQKS AVFGVGLLPC DQECSRLAAE RREKEETELL RHRKSKEPEM
NTAPVKVPKK RRGRNLDDTT KPSAFKENIV KAGRWIMIGF LVVGAFLVLV YGYKGLLALS
RWMDARDAVK PRRRMSGGF
//
