ID A0A1C1CCS2_9EURO Unreviewed; 1642 AA.
AC A0A1C1CCS2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Bloom syndrome protein {ECO:0000313|EMBL:OCT46271.1};
GN ORFNames=CLCR_01028 {ECO:0000313|EMBL:OCT46271.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT46271.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OCT46271.1}.
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DR EMBL; LGRB01000016; OCT46271.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1CCS2; -.
DR STRING; 86049.A0A1C1CCS2; -.
DR VEuPathDB; FungiDB:CLCR_01028; -.
DR VEuPathDB; FungiDB:G647_09251; -.
DR eggNOG; KOG0351; Eukaryota.
DR Proteomes; UP000094526; Unassembled WGS sequence.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000094526}.
FT DOMAIN 754..935
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 959..1108
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 62..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1501
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1642 AA; 181760 MW; 41A98359B96949B6 CRC64;
MTKNNLSTCL AWLLQHPHSF GNLDHLSAIV DTPAASYDEA TATEPDNEMA RLQLAPQTNH
RPKLHSQLNN VPNPLPTPTP SRPSEEPKPR STRPKQTLAT PSAARQNATL RTPGTASGNL
GFSDGVLDID EIDLTGDVTT SSFGEFGPPL RLWREDSASR VEPLPKKNGK KRKSDEYESD
LPSPRPSRKT TKVLQNATTM VSPLHARQPE GLERHTQEEV NLTQTTIRQQ PPPLSEAEDE
FSDFSVNDFE GTQDQPAIKP DDAQHSQTLR RTNVIPDSDD DDDVVEEDVP FAPKVESDPT
SPNPYLLGHT HGRGDVVGDV KHVQEAFRSP RRSQPPKSSQ SPRKPASATL THTATSTQEP
MFKSSAASTN SSENLTAEQK DLVANFASNG QEQLQSLLQR LERSKKAVDD KIMDEICEDG
GASTESKERL RAIGDKIASA ARLRDEFDTL AKLRKQREQM VVQRNKLSNS GHSVNPDDPA
DVLMSLCSKI FQAKRDIDAR EVSVFRLLDQ IGVPTAGRMT ARANDFSDRI LSPRSIVSEQ
NVLVASTQKA PQSTSKQLKD EDRQGLSHLS TQSVRQTPAP NRFDTPVVSV KSPYRGPSPQ
YTSKRPAFVE QGRPLQSTLR TAHSAVSGHA FAYNEPESSG RGFSRTMASP TRNYSFEEDD
FEDDLDDEEM YQAVEEFEQH LSSRTADPSE IPGRAALAEV SDNIRKISPK KKPSSQQPSS
SHALMQHPWS KDVASALKRK FHLHGFRHNQ LEAINATLAG KDTFVLMPTG GGKSLCYQLP
AVIKSGRTRG VTVVVSPLLS LMQDQVDHLQ KLQIQAHLIN GNSTPEARNW VRQALQDPNP
EEVLQLLYVT PEMLGKSQAM VSAFEALYRR KRLARIVIDE AHCVSQWGHD FRPDYKSLGE
VRKRFQEVPV MALTATATEN VKIDVMHNLG MKDAEVLTQS FNRPNLTYEV RPKGKNIEVL
QSIADTIKSS YRGQAGVVYC LSRANCEKVA QDLSDKFQIE AQHYHAGMPS EERIDIQKRW
QAGEFKVIVA TIAFGMGIDK SDVRFVMHHS MPKSLEGYYQ ETGRAGRDGK RSGCYLYYGY
RDSMLLKQMI KNGDGSDEQK ERQYQLLRNM VQFCENRSDC RRVQVLGYFN EHFNRADCEN
GCDNCNSTST FETQDFSEHA RAAISIVREI HRSKVTVLHC VDIYRGSRNK KITQLEHNTL
AEYGKGAHLV RGDVERLFHR LISEKALTEY NKVNKAGFST QYIKPGPAAR DFEAGRRSLK
IQVLASPHEK ARTSAPPPQK SRQNGQGTGV RAAGDYYPTS TNVSSPLQPR TDRKLPRPVE
DPNSDDEDFI VHTSEMEGED VPSDKDEDAF GDDIALDHSG TRKKKLGPPI TSDTSMSLNS
IHQHILDHFI EDARAHIKRI SIAKCLRQVP VTESTLRLIG VEFPQDATQL QRISGMNDEI
FQLFGPVLLR LIKSAFNNYE AMMRAQEGRP DDPNHQTVIE IADDDASGPE SETDLDMDDV
DETENSHYFS VPEEDGKSSG RALPASFSEN KSRKTAAKKA PSRSRSVSWN RRGSRGWQRG
GSGGGGGGGG GGSSSGNSSS RARTSAAQGK KASGAVAKKG KSNSSARSST SSAGLSRFVH
KNNKTGPSQR SAGGSKISMM PT
//
