ID A0A2Y9JNN2_ENHLU Unreviewed; 1027 AA.
AC A0A2Y9JNN2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=DNA-binding protein SMUBP-2 isoform X1 {ECO:0000313|RefSeq:XP_022362236.1};
GN Name=LOC111149444 {ECO:0000313|RefSeq:XP_022362236.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022362236.1};
RN [1] {ECO:0000313|RefSeq:XP_022362236.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022362236.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:ARBA00000600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913}.
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DR RefSeq; XP_022362236.1; XM_022506528.1.
DR AlphaFoldDB; A0A2Y9JNN2; -.
DR STRING; 391180.A0A2Y9JNN2; -.
DR KEGG; elk:111149444; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18044; DEXXQc_SMUBP2; 1.
DR CDD; cd02641; R3H_Smubp-2_like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 2.40.30.270; -; 1.
DR Gene3D; 4.10.1110.10; AN1-like Zinc finger; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR034072; R3H_Smubp-2.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR004483; SMUBP-2/Hcs1-like.
DR InterPro; IPR048761; SMUBP-2_HCS1_1B.
DR InterPro; IPR000058; Znf_AN1.
DR NCBIfam; TIGR00376; IGHMBP2 family helicase; 1.
DR PANTHER; PTHR43788:SF19; DNA-BINDING PROTEIN SMUBP-2; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF21138; SMUBP-2_HCS1_1B; 1.
DR Pfam; PF01428; zf-AN1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00393; R3H; 1.
DR SMART; SM00154; ZnF_AN1; 1.
DR SUPFAM; SSF118310; AN1-like Zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF82708; R3H domain; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS51039; ZF_AN1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA-binding {ECO:0000313|RefSeq:XP_022362236.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
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:UP000248482};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00449}.
FT DOMAIN 722..785
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT DOMAIN 925..974
FT /note="AN1-type"
FT /evidence="ECO:0000259|PROSITE:PS51039"
FT REGION 648..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..812
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1027 AA; 111689 MW; BE21E8149E1505CF CRC64;
MASAAVESFV TKQLDLLELE RDAEVEERRS WQENISPKEL QSRGVCLLKL QVSSQRTGLY
GRLLVTLEPR RCVAAAVLPS NSFTSGDIVG LYDEGSQLAT GILTRITQRS VTVAFDESHD
FRLSLDREQT YRLLKLANDV TYKRLKKALI TLKKYHSGPA CSLIDVLFGG SAPSPASEIQ
PLPFCNPCLD ASQKEAVSFA LSQKELAIIH GPPGTGKTTT VVEIILQAVR QGLKVLCCAP
SNVAVDNLVE RLAHSKQKIV RLGHPARLLD SIQQHSLDAV LARSDSAQIV ADIRKDIDQA
FAKNRQTQEK REKSGVWSEI KLLRKELKER EEAAVLESLR SAAVVLATNT GASSDGPLRL
LPDGHFDMLV IDECAQALEA SCWIPLLKAR RCVLAGDHKQ LPPTTVSHKA ALAGLSRSLM
ERLADELGAQ VVRTLTVQYR MHQAIMRWAS DALYSGQLTA HPAVAGHLLR DLPGVAATEE
TSVPLLLVDT AGCGLFELEE EDDQSKGNPG EVRLASLHIQ ALVDAGVQAS DIAVITPYNL
QVDLLRQSLA HRYPELEIKS VDGFQGREKE AVVLSFVRSN RKGDVGFLAE DRRVNVAVTR
ARRHVAVVCD SRTVSNHTFL KTLLGHFIEH GEVRTAFEYL DDIVPENYSH ESSQGHSQAG
AKPHSSAVSA RKPPGGRPRD RTQETRAAAG LQWKRTGGRP SGPEVPSQPS LNGGSPEGMA
TRDRAEHFRA KIAEFVASEK TQLEFPASLN SHDRMWVHQI AEEHGLRHDS SGEGKKRFIT
VSKRAWPAPP APPAPPAPPA PPAPPPPAGA SSHTPVGPMA PGPTQNEPPA GGQSSQDTLN
LKALHLERLQ RAKSKQERPT TDGAATDGAT KDRAARDGAA TDGQQASRSG LRTLPEKKKK
KEAKGNTAMD LPGKEDFEAL VAAAIKADNT CGLAKCTASV ATLGQLCLHC GRRFCLSHHL
PEIHGCGERA RAHARQRISR EGVLYAGSGT KDRSLDPAKR AQLQRRLDKK LDELSGQRKS
KRKEKEK
//
