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Database: UniProt
Entry: V9K9Z6_CALMI
LinkDB: V9K9Z6_CALMI
Original site: V9K9Z6_CALMI 
ID   V9K9Z6_CALMI            Unreviewed;      1373 AA.
AC   V9K9Z6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Kinesin family member 16B {ECO:0000313|EMBL:AFO94454.1};
DE   Flags: Fragment;
OS   Callorhinchus milii (Ghost shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX   NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO94454.1};
RN   [1] {ECO:0000313|EMBL:AFO94454.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:AFO94454.1};
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).
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DR   EMBL; JW861937; AFO94454.1; -; mRNA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR47117:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 1.
DR   PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50195; PX; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          1262..1373
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          655..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1159..1181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          165..419
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          455..482
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          516..589
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          615..645
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          679..923
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          959..986
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1020..1093
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1119..1149
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        657..671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1161..1175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFO94454.1"
FT   NON_TER         1373
FT                   /evidence="ECO:0000313|EMBL:AFO94454.1"
SQ   SEQUENCE   1373 AA;  162409 MW;  D4FC9884D603C5E2 CRC64;
     EETLALRKEG IGVVLDSELP HLIGIDDDLL STGIILYHLK EGKTYVGRDD ATTEQDIVLH
     GLDLESDHCI FENLNNTVML IPLNDAQCSV NGIQIKEASH LNQGAVILLG RTNMFRFNHP
     KEAAKLREKR KSGLLSTFSL SMTDLSKSCE NLSAIMLYNP GLEFERQQRE ELEKLENKRR
     LIAEMEEKQQ SEKMELERMQ QEVESQRKET EIVKLRIRKQ EESLKRRNLD IEGRLNDLRA
     EKEKFEEERQ REQQEIELQK KKQEEEIHSR VQKELQKLQE LHEQEKARKL EILRELEKLK
     KEKDEHSMKL ELEKRRLEEQ AKDQQNLVAR LGEQLREKVE MIQLLKQDDV HMIEDEKNVL
     EEIREVLLKA KEARPDGDED HEDVQRAKQK YMDLKRRQLE ELEATEEKAI HQKDFLEREI
     FIEHEVLDQL RHTQEEPMNT MKEDAENRAL DSMELHEAAE RVKLVEQRLQ NKERQLLFLT
     KNHLPSVSEE KQRTADVLVR GLPALDVALY QTEKEIEEKG EQLAQYRASS DQLQQLQQTY
     EFTANVARQE EKVRMIEKEI IESREKQQRE ALEQAVAKIE KRHSALQRHS VVDLEIEEQK
     RKLATLNICE EADLRDSLET EQKALEQDRE RLEQEIQQLK QKICENDVAL RECGTAEEKS
     SYTSSPASPK RSPSIMGPIA DERRLIAEME EKQQSEKMEL ERMQQEVESQ RKETEIVKLR
     IRKQEESLKR RNLDIEGRLN DLRAEKEKFE EERQREQQEI ELQKKKQEEE IHSRVQKELQ
     KLQELHEQEK ARKLEILREL EKLKKEKDEH SMKLELEKRR LEEQAKDQQN LVARLGEQLR
     EKVEMIQLLK QDDVHMIEDE KNVLEEIREV LLKAKEARPD GDEDHEDVQR AKQKYMDLKR
     RQLEELEATE EKAIHQKDFL EREIFIEHEV LDQLRHTQEE PMNTMKEDAE NRALDSMELH
     EAAERVKLVE QRLQNKERQL LFLTKNHLPS VSEEKQRTAD VLVRGLPALD VALYQTEKEI
     EEKGEQLAQY RASSDQLQQL QQTYEFTANV ARQEEKVRMI EKEIIESREK QQREALEQAV
     AKIEKRHSAL QRHSVVDLEI EEQKRKLATL NICEEADLRD SLETEQKALE QDRERLEQEI
     QQLKQKICEN DVALRECGTA EEKSSYTSSP ASPKRSPSIM GPIADERLNA YIEEEVQRRL
     AEKEKIQTKY ETHSTNDAFD LSSSMDISQE NGSLHNGQIQ RKLKYERLVY RPLGNDPDSL
     KDPIKISIPR YVLRGQGKDE HYEFEVKITI LEETWAVFRR YSRFRELHRT MKMKYPEIGG
     LEFPPKKLFG NRDERVIAER RSHLESYLRK FLTLILKSPT SPISLNTEGF NLS
//
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