ID A0A177CXM9_9PLEO Unreviewed; 1221 AA.
AC A0A177CXM9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Fork-head domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CC84DRAFT_1192084 {ECO:0000313|EMBL:OAG11587.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG11587.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG11587.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG11587.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR EMBL; KV441548; OAG11587.1; -; Genomic_DNA.
DR RefSeq; XP_018041952.1; XM_018181225.1.
DR AlphaFoldDB; A0A177CXM9; -.
DR STRING; 1460663.A0A177CXM9; -.
DR GeneID; 28764711; -.
DR InParanoid; A0A177CXM9; -.
DR OrthoDB; 5385885at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0060962; P:regulation of ribosomal protein gene transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd00059; FH_FOX; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR045178; Fhl1/FHA1.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR030456; TF_fork_head_CS_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR21712:SF29; PRE-RRNA-PROCESSING PROTEIN FHL1; 1.
DR PANTHER; PTHR21712; UNCHARACTERIZED; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00089};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00089}; Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT DOMAIN 298..331
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 715..803
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 715..803
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 25..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..467
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..867
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..898
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..972
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1152
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1221 AA; 131267 MW; 615A1847A477D421 CRC64;
MLVNPGDAPP ADALAAHNVA AEPAPIAPST STASMDVAVA SAPDAPPSAP ASMPPPLLDK
AADALPVASA DLNGQAMAAS DAPFPSLDAP ISLTADMSMG PLPMGPEYPM MDADLPFNNG
YASVAPAEQR LSAFARLRFD DGSYYMHTYQ IILGRNVQLA HKDMRRLAKV EQLKAKGEKQ
RAQALLNGGR KRKLKSARSV ISEAGGIVTA PIEMMPVDYQ QRCQSVASQS HSSGSHAQAA
ESNHNVDHAP QEMLMQALPE VPYQIDQQVP EDPNDCPLVP IHPQHITDRT GLKGPKGISR
QHAKIYYDFD SGNFCLAVMG SNGLYHEDRF LAKGANVELS HGDTIIIGMV EMTFFLPDIA
LTEEQRNRQE SGSQSRPMSF SFENGRGESE DVDDSGSEDQ SVNPRHVYHY PVGSEFESDD
DLLIDEDMDD LDDEAYSPVP QPKPNLKIKL KKKKHRPEKH SKGHKRKAIR EPSPEEPPFK
KHKIKIKEKH VHKEPPKEKE VEKEKPKEKE KAKANKAPTK APTKAPAKAP AKEQTPATPK
EEPKDDVSLK DTIEATEKPK SESPVIIRRP QPGVNIEDLD PDGLITPEMC AQYGLPHSLI
GQYVGKRKGP GRPPKDGVMS KRQRSQLIKQ GKEIEKARAA GIDPADLPQP IVKPKVARRK
ESNAGEDDEI RESTEKGDGT VMLGGEKKTN KPAKPTRTPS PEMRIEDYTE EQLQRPTSNY
VVLIHEAISS APSGQMNLQQ IYNYIEKNYP WYKFKTTTSG WQSSVRHNLG QHDAFVKGDK
EGKGYMWRIN SNVSIEKERR KRQVSPPQVN AQRPTYYPPP TGYSPYGQPG YYPGMPPQGM
PPNGPPRPPP VEAAQPRLPP TAPAPSPYAS PWAGGAAGGN PSNSHPPQPY PPSAHAPSAN
PGAPSGQYGV LFPTSAPPSS GSPYTSAPTY TSPFATAGQS PYGMPNGASP YTPYPPAGQP
PKTTPTPTPT PTSGQAPGNQ APQRPESSAP HPSGRYPAST NPDLIRQLEA FRTVYLHTRI
EPGEDKKADN AIRAFVTPEL ESSLTQAEAA LLDSIKTIPM LEQLRGGARP PIKPDESTQP
IEFKTPVEAL ASIPSAPTTT AAIAAADAAA NTAPNHPAPV AESSQPQRFV PPMTATPQPS
ATPAPAPTAP PAVPAIANVQ AQRPSVEPIT PVPGSPAVRN GTPVTRPVQD AAPSAPPDAG
SGAEEKAPKA EIPAPPVNES T
//
