ID A0A3B4YP68_SERLL Unreviewed; 993 AA.
AC A0A3B4YP68;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Immunoglobulin mu DNA binding protein 2 {ECO:0000313|Ensembl:ENSSLDP00000029993.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000029993.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000029993.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B4YP68; -.
DR STRING; 1841481.ENSSLDP00000029993; -.
DR Ensembl; ENSSLDT00000030863.1; ENSSLDP00000029993.1; ENSSLDG00000023119.1.
DR GeneTree; ENSGT00930000151035; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000261360; 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:InterPro.
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 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00449}.
FT DOMAIN 718..782
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT DOMAIN 891..940
FT /note="AN1-type"
FT /evidence="ECO:0000259|PROSITE:PS51039"
FT REGION 652..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..843
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 993 AA; 109990 MW; DA70242D0BDB61BF CRC64;
MMAVEQFVSK TLELLQQERE AEIEETRLWQ ENISLKDLQN KGVCLLKLQI GSQSTGLYGR
TVVILEPRKH LGFSSLPSNS FGPGDIVGLY DTGGCTADSQ IATGIVTRVS QASISVAFDD
SKDGLSFDTD ALYILLKLAN DVTYKRMKNA LNALNRYSNG TAANLISVLF GDTKPSSQSQ
PNEVGFFNLN LDDSQREAVS FALSQRELAV IHGPPGTGKT TTVVEIILQA VKQGQKILCC
ASSNVAVDNL VERLARCKAK VLRLGHPARL LESIQKHSLD AILAQSDNAN IITDIRKDID
KAFMGMKKSH EKGERVNFRR EIGELRKELK TREATAIAQI LKSADVVLST NTGACDDGPL
KFLPAEHFDW VVIDECAQAL ESSCWIALLK ARKCILAGDY KQLPPTIKSR IAASKGLSLS
LMERLIQMYG DSVVRMLTVQ YRMNSAIMEW ASKEMYQGRL TAHSSVERHL LKDLPGVTCV
EETSTPLLLI DTAGCGLSEM EVTDEQSKGN QGEVDIVELH IKALTEAGIK AKDIAVIAPY
NLQVDLLRQK LSTRHPELEI KSVDGFQGRE KEAVVLSLVR SNRKGDVGFL AEDRRINVAV
TRARRHIAVV CDTQTVQNHA FLKSLIDHMT EFGEVRTAFE YIQDIVPQNY TRDHKDSKAN
TSASSSASTK QSVKDQARSK VKQGQKKSSG SSSKENTAGS EKYKKSPAST LTEEQQNKNR
CTEIREQVEN FLKELNQSEI QFPSSFNSHD RLLVHQIAEE LGLVHESKGE GKDRCISVSR
PLVSAPAEDS TQGEEEEEEA REEETIPNPQ SEPRSHSPLD LKSLHLERMK REQQKREENA
QRKKQQNNIP PAQTQSSKKA KGKNRTKAGA CDIAAAAAPD DDFDTLINAV KKADSVCSFV
KCKASVLTLG QLCIFCNRQY CLSHHIPEVH GCGDKAKSHA RMRISKEGVL YAGSGKKDKS
MDPNKKAYLQ RKLDSKLKDM ASQRKQKNKE KDS
//
