ID A0A2D0PYT9_ICTPU Unreviewed; 1743 AA.
AC A0A2D0PYT9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Kinesin-like protein KIF26B isoform X2 {ECO:0000313|RefSeq:XP_017311197.2};
GN Name=kif26bb {ECO:0000313|RefSeq:XP_017311197.2};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017311197.2};
RN [1] {ECO:0000313|RefSeq:XP_017311197.2}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017311197.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR RefSeq; XP_017311197.2; XM_017455708.3.
DR AlphaFoldDB; A0A2D0PYT9; -.
DR KEGG; ipu:108257734; -.
DR OrthoDB; 4195897at2759; -.
DR Proteomes; UP000221080; Chromosome 25.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21608:SF8; KINESIN-LIKE PROTEIN KIF26B; 1.
DR PANTHER; PTHR21608; UNCHARACTERIZED; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 318..659
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 38..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1452..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1639..1660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1692..1743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1743 AA; 191771 MW; AB69D2C2770825A8 CRC64;
MGSSEIARKQ RYLAQMTGTK SLSQAQFSAV CVPRAERLSP EGAGASGASG DSKSLTTKSE
RPVTPDVARF CEECVARVLV LQEQALRVLK DGHFSPRDPK LSILLYESLR VPAWIGLAGC
CDVCFTHLSQ LKREAIHMLL KQNRTIWPNS PPAGVSPGYD ALGSHTLPRA ISARSPSPNK
RQKFSNPRTE SWVREHSRFE TLWCANNETS PFADTVSQDG MKKKKDDEAT VLCRFSGPLT
FNTSKVAAML PAGTSAAFSF IVRAVQKLHL TSRRKKQCSD NDCYPTNFCG LLQKDPPPVP
LNLLQTHSKS RELPEMAKVR VMLRLNPILT ADMSQSHALK VDLHKKQVTV LDTVTQNTQR
SASGTTFTPK TFTFDATFGP ESSQAKVCEK SLYEVLQSVV AGADGCILCF GQTKVGTSYT
MIGCDDGTPN LGIIPCAISW LFKLINKKKD KTWANISVSV SAVEVCGETE VIKDLLSGFE
AGDHTHKPNV YLQEDPVCGI QLYNNRVVSA PTAERAACLL DTALASRNKG IAGCRGTFHH
HCHMFYTLHV CQKHIESSPT SGMYVEQSKL SLIDLGSCTR ERSKNNTEVC LLDLGNVIMA
KINGHKHVPN KGSKLAMLMQ DSLGNVNCHT TIVAHVSTSH EDLSETLCTI QIVSRIRRLQ
RIRKQTCNSP GSRSLGKEKK ANDSSKLRAF RYAGLLEHTF SLPHLFDDPG DYSESDKSCD
TVFCVDPKGV LHDNKGVRGN QEFVPIIPSL QRNKADLKSS FSIKHSDIIQ SNQNSKEMKK
PPAQQNSSTP DLECFKCNTF AELQNRLECI DESEMVGLHS CKIQPANAIV KSEPLSSKVV
KIPAEKPEIQ QFQCKKQANN QEQGQPTQRD AFMKDIKEIP CEYSGQDKIT QNILPCSPRF
RMSSSSMQCE QVTESQSLTK TMDTTPSVPF PVEGLSSDKS TLPLKIRIPP VGKSSSSPFS
ALGTPVSFPI TRCEVIPQFP IENQGEKATI TVTVQQPLDL NGHDELIYSV VKEVEVNSPV
NKGKSAKIAN IAELDSLKNL PLGSQPVKII GSVGKEQTAA DSVSEVQALS TIGKPSSDLS
AGKTISMGQN HAVNLKTDNN PSPLDVRSKE SQSKTVTEVA KTDFGSTSQY EVSRFGEYAF
EMAAEQECVK RKCNQSSGQL CCEFKDKISP TNQTKLEDFP MKPEENLVSS YSTYDTSSPT
RAWLGTDKQH ACKDSLYPCT SWKNETSYNP KATLEKKNSV AKPSLVEWAK YSKSMPSVPR
SDNSSPKINR KHVQPTMTQT NSENQLKTAR PKSPIDESTK LFSAKLEQLT NRSRSLSRSH
VECVAVQPFE QSNAVFIQGS SRSMEGNCTP PRVNRHLEKQ NCQDLGSKGH LEGQYALGHA
KNTACPGLLT VSEADILTLS QANHSLRRVP RFFPLYDVDE RDTTQPCKYS QPNMSSINKV
LSSPAVHTLS GTAPNICVSP KSNRRSINRS SSLTSDGFSR KQISWSSQSL SRKQVKASIS
SKYPSKILNG RVEFLRASED SLSSSSQGSS DIDDLEESKR KMKLLNQTLS SPYSRITAPR
KPNSCSGHAS DNTSVLSGEL PPAMYKTALL YHRNSMVSSG YESLKRDSET TYSSTSIHDS
ISDQSCFYST LKDARISKKR NNTVSHQRHP SQDTLSSLRR SVSGSKIHWV DRGTTDAYEI
KVYEIDSVDS LQRRGKAGNK CQAEIPGAST TKDCRDEGQV QHPKERAGTS QTASDGGSRE
MDP
//