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Database: UniProt
Entry: A0A177D4C2_ALTAL
LinkDB: A0A177D4C2_ALTAL
Original site: A0A177D4C2_ALTAL 
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
//
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