ID C9SG55_VERA1 Unreviewed; 1401 AA.
AC C9SG55;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=E3 ubiquitin-protein ligase SHPRH {ECO:0000313|EMBL:EEY18069.1};
GN ORFNames=VDBG_04178 {ECO:0000313|EMBL:EEY18069.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; DS985217; EEY18069.1; -; Genomic_DNA.
DR RefSeq; XP_003006225.1; XM_003006179.1.
DR STRING; 526221.C9SG55; -.
DR GeneID; 9534868; -.
DR KEGG; val:VDBG_04178; -.
DR eggNOG; KOG0298; Eukaryota.
DR HOGENOM; CLU_001592_2_0_1; -.
DR OMA; QLFEQMC; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000008698; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008698};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 255..456
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1055..1093
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1164..1316
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 957..984
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1401 AA; 157294 MW; 2B99669A49BEDDC0 CRC64;
MAPRAEETLN LPEPAIRNDV GSHLQLSYVS SQWSSKQLKL SVPSAGIAGR AALALRPDSV
SQALGACINI HSKESRVDEG AIWTTVGLRI ERQGKNVLVV FDLELYWNAT FSPFRLRTPR
QRETSQMVLS TFFNNDETTT TTTTQVAEAT WTPLDFYEAA FVPPATDGSA LAIEVPGLNA
SLYPYQKRTL KWLLHREGTR WVPPSNGSAA GLKSVEETGT LQPARSFGEI SSPSNVQWYL
SHLYHAITPE TSAFLSAEKV VRGGILSEEM GLGKTLEIIG LILLHRRQPA NEDSYLHFNN
ERLVKSGATL IVCPESLRQQ WMDELERHAP HLLVSYYPGR AQFRNQTEEE VFRNMAAHDV
IVTTYKTLTA EIHYATKPPE RSRRREREYE RPKSPLTQIS WWRVCLDEAQ MIETGVSAAA
LVARVLHRVN AWGVTGTPVK KDVQDLLGLL LFLRFEPYCS SPQVWKALTK NHKPLFHNLF
HDIAIRHTKN LVRDELELPA QKRFVITLPF TAVEEQHYQS IFAEMAEVCD VDLDGNPMSA
DWDPKRYEEA MRTYLNRLRQ AALHPEVGVQ NRRALGHRAG PLRTVDEVLT AMIEQSDASI
RTEQRAYFTA RLNYGQLLEN GPLVQEALVI WDQTRREVEE VVGKCRQELD VAMNAAKRAI
SENGSVSNTN GTSDEDVIEG LDEYQASPEV GEALMRLRSA LEVQHRAIFF CANARFQIKS
NRDFTEPDSA EFSALQKLEE EGYETAKGVR REILSENHRK ATKAMRKLGN DAVSQNFVTI
PELIPNPVKG LESATVVEKV EELYGFLNLQ ANLIDEWREV IVGLLLQPLV DEENETETTG
DEFVNSTAIQ EQLMVHVQVL RATIADRQDA ISGLQNMLVK HETQTTKALA MDGEGPAPKT
LIELLDVRNK VKPSLEKHGC LRGAIGELRA LAARLPPHEP GKDSRANMEH AVVNRQIKDI
QAQIQAQTKA SQRLERECDE FTNAMNLRLD YYRQLQAISD SVDVYEGPKT QDILAKWVNA
AETAHRKLSS AEAKQRYLVS LRDGGASKAN EPKMCIICQT DFTIGVLTVC GHQFCKHCLM
LWFKAHHNCP MCKRKLKITD LHTITLKPRE LTLHTEDVPT STPGKKRSAA QNKSAIYSEF
GADKLAQIRD VDLEGPPLTT KVDSVVRHLL WLRESDPGAK SIVFSQYRDF LQVIGSALSR
SRIGYTSIDK PNGVQRFKED AGLECFLLHG RAQSSGLNLV NASHVFLCEP LLNTAIELQA
IARVDRIGQQ HETTVWLYLI EGTVEESIYN LSVKRRLQHL SSVTKGKSKD STPDVLGPTL
EAANTFEMEN ARLSKLMSKD RSAGEAVDKE DLWECLFGHV ARAANSESRE ERGENPAVMN
LLAAEAAETR RMMENASKLE T
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