ID A0A0G4KED2_9PEZI Unreviewed; 1024 AA.
AC A0A0G4KED2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=C2H2-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN1708_001906 {ECO:0000313|EMBL:CRJ81481.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRJ81481.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRJ81481.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRJ81481.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC EC=2.3.1.225; Evidence={ECO:0000256|ARBA:ARBA00001870};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CVQH01000002; CRJ81481.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4KED2; -.
DR OrthoDB; 118267at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0016409; F:palmitoyltransferase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.1170.60; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR041298; UBZ3.
DR InterPro; IPR001126; UmuC.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45873; DNA POLYMERASE ETA; 1.
DR PANTHER; PTHR45873:SF1; DNA POLYMERASE ETA; 1.
DR Pfam; PF01529; DHHC; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF21704; POLH-Rev1_HhH; 1.
DR Pfam; PF18439; zf_UBZ; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR PROSITE; PS50216; DHHC; 1.
DR PROSITE; PS50173; UMUC; 1.
DR PROSITE; PS51907; ZF_UBZ3; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT TRANSMEM 18..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 463..724
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT DOMAIN 943..978
FT /note="UBZ3-type"
FT /evidence="ECO:0000259|PROSITE:PS51907"
FT DOMAIN 948..975
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 95..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 113624 MW; FD8116AB4EECF385 CRC64;
MTESQESHKA IARWTSRVIP AILAGVLGYA TYVVVSRLCI EYLSKERGET GTAIAVLILY
ILFLFLSLVT YIRTIWTINT DTGLVPLGPE AQRARTGAEK SISKGGKQSG RRADDLESQP
YQPGPDQDPD SPGLERFYSK NAFICENDGR PKWCSECRNW KPDRAHHSSE IGRCVLKMDH
YCPWVGGMVS ETSFKFFSQF TCYCAAMCAV VLSTAAYCLA RQQQEGRSLD GQIVAVIALS
AFFGLFTFTM TTTSWYYVFL NVTNIDMLKK AWVYQVAVRV PRGTPSSQHF STVTYPLPKH
SETPSSQSSG GTILPTSSAP HSGGQQLSAR DLAATRTFAI LRTEPDENPW HLGWKENWKQ
VMGNSIIDWL LPIRKSPCAL HENADSDYPM GHVLQSLAKR NGIPTLADEE GILTEMYETM
TTSSPQFRES SPLMGTRSPK SQFTYRQLSL LASYAVSSPL RVIAHIDLDA FYAQCEMVRL
NTPEDQPLAV QQWQGLIAIN YPARSFGIGR HCTLAEARKL CPDLIAQHVA TWREGDDKWA
YRDDAAANIT SDKVSLDPYR LQSRRILALI KETLPSDLQK VEKASIDEVF CDLSAHVHSI
LLERFPELNN PPPYDDPTER LPRPPVVALD WQADALIDLD EDAENQDPDW DDVAILIGSE
IIRGVRARIH EVLHYTCSAG IANNKMLSKL GSAHKKPNQQ TVIRNRAIQQ FLSDFKFTKI
RNLGGKLGDT IVNTFNTDTV KDLLPTPLDQ MKARLGDETG IWVYNTIRGI DQSEVNSRTQ
IKSMLSAKSF RPSIHTPDQG XGQRIPAAAA PGPGQAYGQQ AAAAYGGAPG YYPQRSSICR
VDDNRRRRNP QTGQAVQGYY ITAYRNLTTA MIDDLKADSA RDGGIHRFLT RSVSTDEDVA
AHDAAMTEGS KSSDDKQQRL TTGATSPRIK DAGEIETNDS NPWALPVHLC SRCNASFQDS
DDFQSHQDWH IAKDLQDEER GKSAFVQTPP SASHAAGPRK AATSAKRGGR SGKLEHGQRK
LKFG
//