ID A0A667ZWC2_9TELE Unreviewed; 1690 AA.
AC A0A667ZWC2;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Centromere protein F-like {ECO:0000313|Ensembl:ENSMMDP00005039889.1};
GN Name=LOC115366345 {ECO:0000313|Ensembl:ENSMMDP00005039889.1};
OS Myripristis murdjan (pinecone soldierfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Holocentriformes; Holocentridae; Myripristis.
OX NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005039889.1, ECO:0000313|Proteomes:UP000472263};
RN [1] {ECO:0000313|Ensembl:ENSMMDP00005039889.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSMMDT00005040714.1; ENSMMDP00005039889.1; ENSMMDG00005018469.1.
DR GeneTree; ENSGT00730000111187; -.
DR InParanoid; A0A667ZWC2; -.
DR OrthoDB; 5402317at2759; -.
DR Proteomes; UP000472263; Unplaced.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR InterPro; IPR043513; Cenp-F.
DR InterPro; IPR018302; CenpF/LEK1_Rb-prot-bd.
DR InterPro; IPR018463; Centromere_CenpF_N.
DR PANTHER; PTHR18874:SF10; CENTROMERE PROTEIN F; 1.
DR PANTHER; PTHR18874; CMF/LEK/CENP CELL DIVISION-RELATED; 1.
DR Pfam; PF10490; CENP-F_C_Rb_bdg; 1.
DR Pfam; PF10481; CENP-F_N; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000472263}.
FT DOMAIN 1..299
FT /note="Centromere protein Cenp-F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10481"
FT DOMAIN 1633..1677
FT /note="Kinetochore protein Cenp-F/LEK1 Rb protein-binding"
FT /evidence="ECO:0000259|Pfam:PF10490"
FT REGION 128..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1543..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 983..1017
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1189..1216
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 130..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1690 AA; 189487 MW; CAF097ACDA5093A6 CRC64;
MSWAQEDWTV GLSGRVLQKV KELQVQQERL SRENRQRQLQ LDNSQAALDK QNAKYEEVRV
ELQVVQRELK GAREEVQTAV SSKERLSQEL QTKQAQVCSL EGQLDAARTH TQNLTQEVKR
LEAELEKLQN SSRSGDSSLF STPCWNMSSP WESNSIGGRR ERRLGHRGEG DSQPPHTRQQ
LQFSDAPSGS LPRQQHKSTP HRHPSNQSDS FSTPLAAFPW ERDNSRTTAR ACPPPSPQAA
SSDAISRGQV EQGDYGKAED SRRETDTRVS ELQSRVCALE EELRAEAQRL KLSQEELAQS
RKELAAKDLN LQRASDKISL AHTRMAQESE RASGAEQRLR QLQEELKCQR QNADSSRLQH
QQRTKELEKQ HQRDLLELQK EKQCLEKQQQ QEVNKLNQEL QQARTLHNAL QAQADKVSLQ
KQALDKEVET LQEKLKWTEG QLQESQRKDA QTQAKLMEAL HEAAGVAASL EQSRKRERAL
EEEGKRLTEE RAEALHLLKE LQDQKTAPTP SAPPVQVCPV GQSFSPPPCS SHHPRPSAHS
KRPSASATKD EQAREEEGEE RGAQITTTFP TDREPGEGID SEHITVFACS SSECSQRKGD
RGKSKEMERK SENETNDSMG CDSSGTEEHS SADVVLPHSS QSIAGTPTSG TVDDNTSMPS
PEKTTLLRSE QPAASEDLCK ENAALRSELQ DVREELQKRL EDLDVQRRAE AEARMRLKQL
SRKHSSQAGE REEQDRERKA ELERERAETE RLRKTLAALE AEITREREQR ERKNRGEDGA
KEKTLEDRES EMIEQNFQLK KQLAEVKAQL ALERDERERE KQEDERKRMT QAGREGKELS
IKLAELEAEL EELKSHGKNI SPVEKNLSEA NSPLTYLTLH DDEVNSNIVD LDSKPLPSPE
QHRLFCKSTN QRNMAIPQAT ADLIQEEKIG RALECSTLSH KGQTGRSVSD LDDGTLEEKL
CVSYILDQRE KGESSPSDLA KEVECLREKN AKETERANRC QAKLEALQNQ VTLQTQQLTM
AFDRQSQHIT NLLSELQEKE STVLRQGEEL QRCRQELAGL RAEREEEEKE RRGRGEEGRD
AMDETPAEQI AELKPNHEKF TNILLTTSSL TAALPVLREA GQPETRTFDV DRPPATSNSQ
NSDREALRSR TFPQGSTDTN KTQGDFVFVK ETLHTAAIYQ DTTEDQGGTA ALVTNLLALQ
EENQQLKERI KALMVLQTNS PALQDAAENQ ENSTEPGNAA TSWSEEVTTC STSVLCDIIE
GQHSKRQDGE RSGDGEREEE ESRAKEESGT VPQHQISLLQ QQVVVLQAEL QALSVENQLQ
AEELAVWRLA SQPTPALHHN LPQTDLSQSE TQDRTSAVRL TGSHQQPTDD TSHVLSEGQT
QAPALGPEGP APQGVPQSPA TVTVIREDEL LLSCSSNKLQ GRLLASRMTH KIPVPKSRQP
PKKTSVPQGY LQDFTIVDEE SDKENLESKY LKQTKTTSAQ HKEKREAELI QMYSAETGQQ
QVTRETKATP LTKVTEFHRE DPEAKPNTEV NSTCVSLETE GLGSMNNAST QTEESLNPPK
APTASELHHA YTQTEKEEQE DEELVDSPPL SPVPPSEATA VADKMLFSGS FPIPADPARL
AERIRRNRSQ LSAAFDDTEY EPYGLPEVVM KGFADIPSGP SCPYIVRRAL LGTSAVPLPQ
RDPAQSEETD
//
