ID V8P2D7_OPHHA Unreviewed; 1071 AA.
AC V8P2D7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Zinc finger protein {ECO:0000313|EMBL:ETE67972.1};
DE Flags: Fragment;
GN Name=ZNF639 {ECO:0000313|EMBL:ETE67972.1};
GN ORFNames=L345_06233 {ECO:0000313|EMBL:ETE67972.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE67972.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE67972.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE67972.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE67972.1}.
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DR EMBL; AZIM01001133; ETE67972.1; -; Genomic_DNA.
DR AlphaFoldDB; V8P2D7; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008053; P:mitochondrial fusion; IEA:InterPro.
DR CDD; cd09912; DLP_2; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR006884; Fzo/mitofusin_HR2.
DR InterPro; IPR027094; Mitofusin_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR10465:SF2; MITOFUSIN-1; 1.
DR PANTHER; PTHR10465; TRANSMEMBRANE GTPASE FZO1; 1.
DR Pfam; PF00350; Dynamin_N; 2.
DR Pfam; PF04799; Fzo_mitofusin; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR SUPFAM; SSF111479; Fzo-like conserved region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 239..266
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 295..322
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 410..437
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 438..466
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 88..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1011..1055
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE67972.1"
SQ SEQUENCE 1071 AA; 122388 MW; DB5D6749739C9415 CRC64;
MNEHPKKRKR KTLHPSRYSV HAFVFFSVLD SSGIPKYIDN SGIFSDHCYS VCSMKQLDTK
VPDNRGRFHN TAPSIDTDED GSHVYAGTSQ WSGNQSNVPG THLMDPKKKD KNNNNGIFKD
SCESPVFSDS VTDEEKPLDI QTVEISTTEV QAVEVHDIET QTVSPEKLEA EEAEEIPVES
CKGLDKNLPS NVAIPPKWPL LRANSSGLYK CERCTFNSKY FSDLKQHVVL KHKTCPEGNI
CRVCKENFSS KKVLIEHLKI HEEDPYVCKY CDYKTVMFEN LSQHIADTHF SDHLYWCEQC
DVQFSSSSEL YLHFQEHSCD ELYLCQFCEH ETSDPEDLHS HVVNEHAGRL IELSDSYNSR
QPQGHYSLVN KISFDKCKNF FVCQVCGFRS RLHTNVNRHV AIEHTKIFPH VCDDCGKGFS
GMLEYCKHLN SHLTEGIYLC QYCEYSTGQI GDLRSHLDFR HSAELPHKCT DCLMRFETHK
NPQLECIATT DELKKIQAYK NKLAVIGEVL ARRHMKVAFF GRTSSGKSSV INAMLWDKVL
PSGIGHTTNC FLSTVNQLAH ALHMDKDLEA GCLVHVFWPK TKCALLRDDL VLVDSPGTDV
TTELDTWIDK FCLDADVFVL VANSESTLMN TVRKQHMERC LTFLVDELRV VDRSEAQNRI
FFVSAKEVLS ARKHKAQGMP EGGGAIAEGF QTRFQEFQHF EKIFEECISQ SAVKTKFEQH
TIRAKQILET VKNIMDNINV AAAHQRVGSP TVSLSLCPPE ADGCFSPASR VHSMEEREDQ
KDRLDFVRNQ LNLLTAEVKK KIKDVTEEVA NKVSSAMTDE ICRLSVLVDE FISDFHPSPQ
VLKLYKNELS KHLEEGLGRN LADRCSSEVN SSMHQSQQEI IENLQSLLPS EVQNKLHLLI
PCRQFDLSYD LNCNTLCSDF QEDITFRFSL GWTALVWRTV GWKVISLSLS MYGMLYLYEK
LTWTTKAKER AFKQQFVNYA TEKLQQIINL TSSNCSHQVQ QEMATTFARL CQQVDITETK
LEKEIEQLSQ KITQLEKIQN TSKHLRKKAV CLEDEFDCFS KDFLQKKKSG I
//
