ID A0A091IDC1_CALAN Unreviewed; 970 AA.
AC A0A091IDC1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=DNA-binding protein SMUBP-2 {ECO:0000313|EMBL:KFO97745.1};
DE Flags: Fragment;
GN ORFNames=N300_10650 {ECO:0000313|EMBL:KFO97745.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO97745.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFO97745.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO97745.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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: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 EMBL; KL217671; KFO97745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091IDC1; -.
DR STRING; 9244.A0A091IDC1; -.
DR Proteomes; UP000054308; Unassembled WGS sequence.
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; 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; 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; 2.
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|EMBL:KFO97745.1};
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:UP000054308};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00449}.
FT DOMAIN 705..768
FT /note="R3H"
FT /evidence="ECO:0000259|PROSITE:PS51061"
FT DOMAIN 868..917
FT /note="AN1-type"
FT /evidence="ECO:0000259|PROSITE:PS51039"
FT REGION 284..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..799
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..970
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO97745.1"
FT NON_TER 970
FT /evidence="ECO:0000313|EMBL:KFO97745.1"
SQ SEQUENCE 970 AA; 105179 MW; 1A52D56EA6F396C4 CRC64;
RTWQQSVSLR ELQHRGLCLL HLRAAAHRTG LYGRLLVTFQ PRKHPPDTEL PYNSFGPGDI
VGLYDSAGQG DPLSSGVITG VTPRAVTVAF EESQEGLPSL DPEGSYRLLK LANDVTYNRM
RKALHTLHGY RAGPAARLID VLFFNSAPSP ASDTKPLKLY NTSLDVSQQE AVSFCLAQRE
LAIVHGPPGT GKTTTLVEII LQAVQQGLKV LCCAPSNVAV DNLVERLAAH STHSTRILRL
GHPPLLLEPI QQHSLDAILA RGDNAQIVAD IRKDIDQAFV RRAEGSSGSA NEAVPPARTP
DPEHRPYRSG RGQGLALNAA PRASRVWVGT QGGASSDGPL KLLPENHFDL VVIDECAQAL
EASCWIPLLK APRCILAGDH KQLPPTIISH KAAAEGLSLS LMERLLQRYG EQVVRMLRVQ
YRMHQDIMHW ASTELYGGRL TAHPSVAQHL LKDLPGVTST EETTIPLLLI DTAGCGLFEL
EVEDEQSKGN PGEVQLAGLH IQALVEAGVK ARDIAVVAPY NLQVDMLREH LCHRYPELEI
KSVDGFQGRE KEAVILSFVR SNRKGEVGFL AEDRRVNVAV TRARRHVAIV CDSHTVSTQP
FLQRLLGHFS QHGEVRTAFQ YLDNLVPQNY PTGGRGERGK SGAKRPKTPP GKKLNTGAPK
AGCQGKEKAP TSPETGGTGG QSVGTRGDQL SPETGGTGGQ SVGTRDVAER LKATLEAFLE
SRETQMDFPP SLSSHARMLV HLLAEERGLQ HLSTGQGRAR FISVRKKGSV EPPRAAAPSP
CQGLPLAPQP QPPCRDTPGP AEPEGSSSGK VDLKSLHLER VRREEAARKA REPGAAGQGS
SSRRKEKGKP SATSGAEEDF DALIAAAVKA DTTCGFPRCQ ASVTTLGQLC PHCKRSYCLS
HHIPEVHGCG EKAKAQARQR ISREGVLYPG SGSKDKSLDP ARRAHLQRRL DKKLSELTSQ
RKSKKKEKEK
//
