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Database: UniProt
Entry: A9UWY8_MONBE
LinkDB: A9UWY8_MONBE
Original site: A9UWY8_MONBE 
ID   A9UWY8_MONBE            Unreviewed;      1094 AA.
AC   A9UWY8;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=RanBP-type and C3HC4-type zinc finger-containing protein 1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MONBRDRAFT_24613 {ECO:0000313|EMBL:EDQ90124.1};
OS   Monosiga brevicollis (Choanoflagellate).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX   NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ90124.1, ECO:0000313|Proteomes:UP000001357};
RN   [1] {ECO:0000313|EMBL:EDQ90124.1, ECO:0000313|Proteomes:UP000001357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX   PubMed=18273011; DOI=10.1038/nature06617;
RG   JGI Sequencing;
RA   King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA   Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA   Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA   Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA   Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA   McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT   "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT   metazoans.";
RL   Nature 451:783-788(2008).
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DR   EMBL; CH991548; EDQ90124.1; -; Genomic_DNA.
DR   RefSeq; XP_001744891.1; XM_001744839.1.
DR   AlphaFoldDB; A9UWY8; -.
DR   STRING; 81824.A9UWY8; -.
DR   EnsemblProtists; EDQ90124; EDQ90124; MONBRDRAFT_24613.
DR   GeneID; 5890294; -.
DR   KEGG; mbr:MONBRDRAFT_24613; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   InParanoid; A9UWY8; -.
DR   OMA; KVEPWSN; -.
DR   Proteomes; UP000001357; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 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; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45626:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001357};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT   DOMAIN          6..35
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          440..677
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          882..920
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          909..1088
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          38..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1094 AA;  120373 MW;  5ADD96EA3FD08E78 CRC64;
     MAQPQPPEQW ACPACTLLNN VLLPRCTLCG AARPASINAK RPASSLDRLQ APSRKISRNK
     PKLSTASSQP QSPDTSAAAK GAGSGANTTA VATGAASASK NRPKSGSKAS VKAGKTGTKA
     NPTQRRGSDR FGTQRDGTPT YRALHHLYEQ GRSATEQIRA PFEHGPWPKV IGECIVQGIA
     NRSGRGLLSA GDALRFSYSL PDKRHSHHGT VTFGRDHELG TLSTQASLWL GPLLAAGAVR
     LTGTAIYLKN PEKLSFSDTI DISITIYGSP VAFLQRPDEA FAGNVATEGL EVTIITRAWQ
     ACFTNCGFID ANAHGGPALR RPSTADAATD STQADETADR DGAQDEEGEE NNDLQFICEQ
     LGLDQTLMPT LEPHACVKST LRPYQKQALW WLVSREQLSA SARDTGRERQ LHPLWQEMRF
     ASGDAFFWKQ AGGRVSVYFP HASQQARGGI LADAMGLGKT VQSLALVATQ PAPPSFIASH
     HDSAASNASS AEPLLGAPTQ RARDSLSLDE FLDARPTRRS SDGSEAASAV GNALASSNTS
     GIPGSKATLI VCPVSLLSQW EEEVHQHLEG MKVLPYHAQR STVTPALIWT EYDVVLTTYG
     VVTSEHMQHL RGQTSLLFGT HFWRIILDEG HMIRNRNTAG ARACHELSAR NRWVLTGTPI
     QNRLEDVYSL IRFLRVEPYA HFSYWRQHVQ EPFERDEDAG ISALQKILAP LLLRRTKHTK
     DETGSPIVQL PSSSVEVLML EFSSAEREFY DAIFQRSKNK FDEFQAAGKV LNNYANILEL
     LLRLRQACDH PFLTLRNMTQ EEEAAREDKR LRTQARQGVF SDIDTLVAKF MSDSRQGNAS
     LRADHVATMA EDLRYLLQRS SHGASAQQNQ ETKATEQAPP ECSVCLDTID EPVVTPCAHY
     GCRVCMENAV DNFHECPLCR KPLQRSSLFR IQAPDPDVES AATAPPNEDD RQHWLSSSKL
     KALLADLDAA TQQPDRPKVI VFSQWTSMLD LIEVFLMTLR TGGVGLNLTA ASHVILVDPW
     WSPAVEAQAI DRVHRIGQDK PVTIKRYIMR DSIEERILAL QKRKRALVHS ALTRNATERQ
     AERMSDLKLL FGQF
//
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