ID V9KIB1_CALMI Unreviewed; 626 AA.
AC V9KIB1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Myxovirus resistance 1 {ECO:0000313|EMBL:AFO97636.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO97636.1};
RN [1] {ECO:0000313|EMBL:AFO97636.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Heart {ECO:0000313|EMBL:AFO97636.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
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DR EMBL; JW865119; AFO97636.1; -; mRNA.
DR AlphaFoldDB; V9KIB1; -.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 1.20.120.1240; Dynamin, middle domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR019762; Dynamin_GTPase_CS.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR000375; Dynamin_stalk.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR003130; GED.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF237; INTERFERON-INDUCED GTP-BINDING PROTEIN MX; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 2: Evidence at transcript level;
KW GTP-binding {ECO:0000256|RuleBase:RU003932};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003932}.
FT DOMAIN 31..304
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 539..626
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 514..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 626 AA; 71997 MW; 566FA54EA1CFE64E CRC64;
MDVALYSHYE EEVRPCIDLI DHLRSLGLEK DLSLPAIAVI GDQSSGKSSV LEALSGVSLP
RGTGIVTRCP LELKLKNVKE KDVWTGFITY NNHRQELTDP SEVEQEIRIA QDIIAGKGVG
ISHELISLQI EASNVPDLTL IDLPGIARVA VGKQPLNIGD QIKQLIKSFI EKQETINLVV
VPCNVDIATT EALKMAQEVD PSGERTVGIL TKPDLVDKGT EKTVVEIIQN QVVELKKGYI
VVKCRGQQDI NEKLTLRRAL EKEKVFFEEH QHFRFLIDEG KASIPCLAKR LTSELVDHIK
KWLPKFEKEL SDRIYAITQE LKYYGEGVPD TENEKITFLI QKINTFGQHV VSLALGEEPE
TFIQKERCYS KVRKEFQQWK VYLNHALHQF QCDLKNNVCA YERMYRGREL PGFTNYKTFE
AIIKQQVCRL EQPAMLKLKN ITEIVHESFM AIALHNFNGV PNLLKASKMK MEELKKKQER
HAVSQLRIQF KLEDIVYSQD SNYSDNLELK ATEEYREQTP DQNSLTSKMS TSKSKEESIQ
EMSTHVDTYY KIMSDRLADQ VPLIIRYYMM QEFASNLQVQ MLELLQNRQQ IEEYLEEEKT
IAEKRRTLKN KLDRLSKAQV HLLDLA
//
