ID A0A177D4C2_ALTAL Unreviewed; 1521 AA.
AC A0A177D4C2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=ATP-dependent DNA helicase {ECO:0000313|EMBL:OAG13819.1};
GN ORFNames=CC77DRAFT_1100372 {ECO:0000313|EMBL:OAG13819.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG13819.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG13819.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG13819.1,
RC ECO:0000313|Proteomes:UP000077248};
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|ARBA:ARBA00004123}.
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DR EMBL; KV441505; OAG13819.1; -; Genomic_DNA.
DR RefSeq; XP_018379240.1; XM_018530066.1.
DR STRING; 5599.A0A177D4C2; -.
DR GeneID; 29115660; -.
DR KEGG; aalt:CC77DRAFT_1100372; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1100372; -.
DR OMA; QLFEQMC; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000077248; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18070; DEXQc_SHPRH; 1.
DR CDD; cd16568; RING-HC_ScPSH1-like; 1.
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; PF13923; zf-C3HC4_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 Helicase {ECO:0000313|EMBL:OAG13819.1};
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:UP000077248};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 345..549
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1146..1184
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1255..1407
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 49..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1521 AA; 170040 MW; 5A1734221B2EBFE7 CRC64;
MSSLEGSAEL LRATAFSVAD VRSPGGPSSL PAQDASSCIR TIQDLFAAPT ALKEEEPSPK
RRKSRNGNAI PVRPQADSNE KNSVVLANVS IDLNMPTPSQ DSLSITYTPA ISQEPVNLEL
ESCRRDHTGD TLQMKLWNAV NETGVDLVAT TPSPFIDSVI PHLRNASALA TSLQGKRHKP
VSRAAFCRCQ LHPPTHGRTQ YKLVVEIRWT LNISVVEDPD IRGHYMNADL KLLSKYMSDA
APRGDKSWTL SDFYDSVHVP PANTEISPLI KQGLIDTKLL PFQERTVDWL LRREGVAFSS
SGLLEPFVNT SPPVSFRQTQ DVAGVPCYVS QLRGTIVTNL DAAKDDTLQS LRGGILAEEM
GLGKTVELIA LISHHKRDIL DGNIYDTYTG AQVRPSGATL IITPPSILEQ WLSEIHAHAP
DLKVCHYKGL PSQSAPKKDH ATATVDYLMQ HDVVVTTYQV LSKEIHHAVP PPDRSSRRPK
RQDRRHSPLV GISWWRVCLD EAQMVESGVS QAAQVARIIP RCNAWAVSGT PLRKDVQDLR
GLLIFLRCDA FANNKAAWTR LDKVSFKGIF NEIAVRNTKA RVRDDLQIPP QKRVVITVPF
TTIEEQHYNE MMRQMCDACW LTPGGQPKEE GRDETHPEVV ERMREWLIRL RQTCLHANVG
RKNKKALGAK NGALRTVHEV LEVMIEQNDT KWKAEAREMV LCLIKMGHIQ AYAGNFANRA
KSSLEYYDKA RTEAQSYIAI CRAELLAEQQ KLGRVSTGGL HGADEDEDID GDNMGRIPVL
RKSLRSFLEL EHAAQFFTAT AWHQIKENPQ LTEPDSDDWR EKDKLETDYY EAARVIRREL
LKESKGRAQQ QMAKVDSRKP FHQIPTIADL PDLGGIEARK ILDTMDNLSD YLNEQAQLIQ
TWRAKIVDIL LTRLVDDDDD KETTGEEYDD SLKAQDELYV YIMALRTLVA DRNAAINGLQ
DNLVEHELKA AEKQALKGDE DSDRGHAPQL LLEVINTRRG LQAKLQAGSL KGVVSSIRSL
ITALQWRANS GDARASSELG ILQKQNAKVQ AVVTEQAKAI TELEKEQEMY RGTMNQRLEY
YRQFQHISDT VAKYKEELDN TFDSREFDKA NQLRERKKDL ANGFKTKCTY LKHLRTENQN
EAAAECIICR DDIEIGVLTA CGHKYCKECI NQWWQVHRSC PTCKQKLSGS DFKDITFKQI
AIRAKEETTT PASPTQASTP DFSSTTSIYS DISDSTMKEI KMIDLEGSYG TKIDMIARHL
IWIRNNDPGA KSIVFSQFGD FLEVLRDALK KWKIGASNIT DKDGIRKFKA DASIECLLLD
AKTDSSGLTL VNATYVFLCE PLINPAIELQ AISRVHRIGQ QRPTTVFMYL ISDTVEEAIY
EISVARRLEH ISNNTLSKLP TQSGSTTPAL KEQTLDAANS AELQNAPFKQ LMRKKGEGEI
VKEDDLWHCL FGNHKKRTQA VLEREVGREL RAQAAEARIA GEGTVGSSGA SVAADVDMAG
GDLVETLPIV GGSSRDGVTR F
//