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Database: UniProt
Entry: K9IMV1_DESRO
LinkDB: K9IMV1_DESRO
Original site: K9IMV1_DESRO 
ID   K9IMV1_DESRO            Unreviewed;       785 AA.
AC   K9IMV1;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
OS   Desmodus rotundus (Vampire bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC   Desmodontinae; Desmodus.
OX   NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA49048.1};
RN   [1] {ECO:0000313|EMBL:JAA49048.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland {ECO:0000313|EMBL:JAA49048.1};
RA   Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA   Ribeiro J.M.C.;
RT   "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT   and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT   Desmodus rotundus.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50
CC       subfamily. {ECO:0000256|ARBA:ARBA00006517}.
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DR   EMBL; GABZ01004477; JAA49048.1; -; mRNA.
DR   AlphaFoldDB; K9IMV1; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd17944; DEADc_DDX21_DDX50; 1.
DR   CDD; cd12936; GUCT_RHII_Gualpha_beta; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.30.70.2280; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR012562; GUCT.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   PANTHER; PTHR47963:SF8; ATP-DEPENDENT RNA HELICASE DEAD; 1.
DR   PANTHER; PTHR47963; DEAD-BOX ATP-DEPENDENT RNA HELICASE 47, MITOCHONDRIAL; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08152; GUCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:JAA49048.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          219..398
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          431..575
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..754
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        755..785
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   785 AA;  87615 MW;  B7769D50BA8DBA14 CRC64;
     MPGKLLSDTD LESNAALVKM ETPRKQNEKK ARKEKPKSNK TEKAAEEMEE AISPKAKKVK
     KKAGPSEVDM NSPKSKKEKN KEEPSQDDVI SPKIKSVKKP KEPMEKKDIS SKTKKVKKNE
     EPSEEEVGAP KPKKMKKEKE MNGEVGEKSS KLKNGFSFSG PDSNCNEAAS EESNSELEQE
     IPVEQKEGAF SNFPISEETI KLLKARGVTF LFPIQAKTFH HVYSGKDLIA QARTGTGKTF
     SFAIPLIEKL LGELQERKRG RAPQVLVLAP TRELANQVSK DFIDITKKLA VACFYGGTPY
     GGQLERMRNG IDILVGTPGR IKDHLQNGKL DLTKLKHVVL DEVDQMLDMG FADQVEEILS
     VAYKKDSEDN PQTLLFSATC PHWVFNVAKK YMKSTYEQVD LIGKKTQKTA ITVEHLAIKC
     HWTQRAAVIG DVIRVYSGFH GRTIIFCETK KEAQELSQNA SIRQDAQSLH GDIPQKQREI
     TLKGFRNGDF GVLVATNVAA RGLDIPEVDL VVQSSPPKDV ESYIHRSGRT GRAGRTGVCI
     CFYQHKEEYQ LAQVEQKAGI KFKRIGVPSA TEIIKASSKD AIRLLDSVPP TAISHFKQSA
     EKLIEEKGAV EALAAALAHI SGATSVDQRS LINSESGFVT MILKCSIEMP NISYAWKELK
     EQLGEEIDSK VKGMVFLKGK QGVCFDVRTA AVTEIQEKWH DSRRWQLSVA TEQPELEGPR
     EGYRNFRGQR EGNRGHRGQR EGNRNFRGQR EGSRNFRGQR SGGGSRNNRF QNKGQKRSFS
     KAFGQ
//
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