Summary
Structures and Sequence Alignment
The best structural homolog that predicted by 1. PB was
E9Q1U1
(Coiled-coil domain-containing protein 171) with a FATCAT P-Value: 1.51e-09 and RMSD of 17.39 angstrom. The sequence alignment identity is 87.0%.
Structural alignment shown in left. Query protein Q6TFL3 colored as red in alignment, homolog E9Q1U1 colored as blue.
Query protein Q6TFL3 is also shown in right top, homolog E9Q1U1 showed in right bottom. They are colored based on secondary structures.
Q6TFL3 MNLNTSSN-T-GDTQRLKIASLDVKQILKNETELD-ITDNLRKKLHWAKKEKLEITTKHNAELASYESQIAKLRSEVEKGEALRQSLEYDLAVARKEAGL 97 E9Q1U1 MSLNTSSNATPGDTQRLKNASLDVKQMLKNETESDIIAD-LRKKLHRAKKEKLEMTTKHNAELSSYESQIARLRSEVEKGEALRQRLEYDLAVARKEAGL 99 Q6TFL3 GRRAAEERLAEAHRIQEKLCAQNSELQAKTNETEKAFQTSQQKWKEECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKTLQEALEKHQREKNEMESH 197 E9Q1U1 GRRAAEERLAEAQRIQERLCAQNSELQGKANEIEKTFQISQEKWREECRRFEHDLEERDNIIQNCNQEYESLMQEKTRLQKTLQEILEKHEQEKTELESR 199 Q6TFL3 IRETALEEFRLQEEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETEHMDCSDLLRRQTSELEFSTQREERLRKEFEATTLRVRKLEENIEAERAAHLES 297 E9Q1U1 VRETALGEFRLQTEEWEAERRELQLIVQEQDSAVQSMQKKVEQLEAEHMDCSDLLRRQTSELEFSTQREERLRKEFEATTLRVRKLEENIEAERAAHLES 299 Q6TFL3 KFNSEIIQLRIRDLEGALQVEKASQAEAVADLEIIKNEFKEVESAYEREKHNAQESFAKLNLLEKEYFSKNKKLNEDIEEQKKVIIDLSKRLQYNEKSCS 397 E9Q1U1 KFNSEIIQLRIRDLEGALQVEKASQAEAVADLEMIKNEFKEVESAYEREKQNTQESCAKLNLLEREYFSQNKKLNEEIEDQKKVIIDLSKRLQYNEKSCG 399 Q6TFL3 ELQEELVMAKKHQAFLVETCENNVKELESILDSFTVSGQWTSGIHKDKDKPPSFSVVLERLRRTLTDYQNKLEDASNEEKACNELDSTKQKIDSHTKNIK 497 E9Q1U1 ELQEELVMAKKHQAFLVETCENNVRELESILGSFSVSAQWTSGVHKDKDKPPSFSVVLETLRRTLTDYQNKLEDASNEEKTSNELDSTKQKIETHIKNTK 499 Q6TFL3 ELQDKLADVNKELSHLHTKCADREALISTLKVELQNVLHCWEKEKAQAAQSESELQKLSQAFHKDAEEKLTFLHTLYQHLVAGCVLIKQPEGMLDKFSWS 597 E9Q1U1 ELQDKLTEVHKELSHLRAKCADREALITSLKVELQNVLHCWEKEKACAAQCESELQKLSQAFQKDSEEKLTFLHTLYQHLVAGCVLIKQPEGMLDKFSWS 599 Q6TFL3 ELCAVLQENVDALIADLNRANEKIRHLEYICKNKSDTMRELQQTQEDTFTKVAEQIKAQESCWHRQKKELELQYSELFLEVQKRAQKFQEIAEKNMEKLN 697 E9Q1U1 ELCAVLQENVDALIADLNRANEKISHLEYICKNKSDTMRELQQTQEDTFNKVAEQIKAQESCWQKQKKELEFQYSELLLEVQRRAQKFQEIAEKNSEKLN 699 Q6TFL3 HIEKSHEQLVLENSHFKKLLSQTQREQMSLLAACALMAGALYPLYSRSCALSTQRDFLQEQVNTFELFKLEIRTLAQALSTVEEKKQEEAKMKKKTFKGL 797 E9Q1U1 RIETSHEQLVRENSHFKTTLSRTQREQTCLLAACALMAGALCPLYSRSCALSTQRDFLQEQVNSLELFKLEIRTLAQALSAVDEKKQEEAKTKKKTFKGL 799 Q6TFL3 IRIFRKGVIAVLAANRLKILGQSCASLFTWMESFKEGIGMLVCTGEPQDKHKFPKHQKEQLRCLQALSWLTSSDLLAAIISSMAELQDVIGKADPNSRIC 897 E9Q1U1 VRVFRKGVIAILAANRLKLLGQSCAFLFTWMESCKEGIGMLVCTGEPKDKRQFPKHQREQLRCLQALAWLTSSDLLGTVISSMTELQEVISKTDPNSRIC 899 Q6TFL3 GHLLIGAAKNSFAKLMDKISLVMECIPLHSSRSITYVEKDSLVQRLAHGLHKVNTLALKYGLRGHVPITKSTASLQKQILGFTQRLHAAEVERRSLRLEV 997 E9Q1U1 GHLLIGAAKNSFAKLMDKLSSAMASIPLHSSRSITYVEKDSLVQRLARGLHKVNTLALKYGLCSHIPIMKSTAALQKQIFGFTQRLHAAEVERRSLRLEV 999 Q6TFL3 TEFKRSVNEMKKELDKAQGLQMQLNEFKQSKLITHEKFESACEELNNALLREEQAQMLLNEQAQQLQELNYKLELHSSEEADKNQTLGEAVKSLSEAKME 1097 E9Q1U1 TEYKRTVHEMKKELDKSQSLQTQLNEFKHSKLITHEKFESACEELNNALLREQQAQMLLNEQAQQLQELNYRLELHSSEEADKNQTLGEAVKSLSEAKME 1099 Q6TFL3 LRRKDQSLRQLNRHLTQLEQDKRRLEENIHDAESALRMAAKDKECVANHMRAVENTLHKVRDQISLSWSAASRNDFTLQLPKLHLETFAMEGLKGGPEVV 1197 E9Q1U1 LRRKDQSLRQLNRHLTQLEQDKRRLEENIRDAESALRMAAKDKECVANHMRTIENMLHKVRDQISLSRTAATRNDFTLQLPKLHLETFAMEGLQGGPEVV 1199 Q6TFL3 ACQAMIKSFMDVYQLASTRIMTLEKEMTSHRSHIAALKSELHTACLRENASLQSIGSRDHSNLSIPSRAPLPADTTGIGDFLPLKAELDTTYTFLKETFI 1297 E9Q1U1 ACQAMIKSFMDVYQLASARISTLEKEMTSHRSHIATLKSELHTACLRENESLQSMGSRDHSNLSVPSRAAAPMDT--VGDLLPLQAELDTTYTFLKETFV 1297 Q6TFL3 NTVPHALTSSHSSP-V-TMSANANRPTQIGL 1326 E9Q1U1 NTAPHSL-SSQSSPGVPT---NAKRPSQIGL 1324
Go Annotations
1. PB indicates the go terms that are found by both PROST and BLAST.2. P indicates the go terms that are found by only PROST.
3. B indicates the go terms that are only annotated by BLAST.
Source | GO | Description |
---|---|---|
2. P | GO:0005869 | dynactin complex |
2. P | GO:0030286 | dynein complex |
2. P | GO:0051010 | microtubule plus-end binding |
2. P | GO:0031116 | positive regulation of microtubule polymerization |
2. P | GO:0005876 | spindle microtubule |
2. P | GO:0005874 | microtubule |
2. P | GO:0005814 | centriole |
2. P | GO:0007098 | centrosome cycle |
2. P | GO:0031023 | microtubule organizing center organization |
2. P | GO:0005819 | spindle |
2. P | GO:0045665 | negative regulation of neuron differentiation |
2. P | GO:0034452 | dynactin binding |
2. P | GO:0000931 | gamma-tubulin large complex |
2. P | GO:0000922 | spindle pole |
2. P | GO:0090316 | positive regulation of intracellular protein transport |
2. P | GO:0000132 | establishment of mitotic spindle orientation |
2. P | GO:0048814 | regulation of dendrite morphogenesis |
2. P | GO:0031122 | cytoplasmic microtubule organization |
2. P | GO:0034451 | centriolar satellite |
2. P | GO:0045931 | positive regulation of mitotic cell cycle |
2. P | GO:0070840 | dynein complex binding |
2. P | GO:0033365 | protein localization to organelle |
2. P | GO:0005875 | microtubule associated complex |
2. P | GO:0000086 | G2/M transition of mitotic cell cycle |
2. P | GO:0005813 | centrosome |
2. P | GO:0043015 | gamma-tubulin binding |
2. P | GO:0035371 | microtubule plus-end |
2. P | GO:0001578 | microtubule bundle formation |
2. P | GO:0070507 | regulation of microtubule cytoskeleton organization |
2. P | GO:0000242 | pericentriolar material |
2. P | GO:0007099 | centriole replication |
2. P | GO:0045736 | negative regulation of cyclin-dependent protein serine/threonine kinase activity |
2. P | GO:0051286 | cell tip |
2. P | GO:0022008 | neurogenesis |
2. P | GO:0008017 | microtubule binding |
2. P | GO:0007020 | microtubule nucleation |
2. P | GO:0060236 | regulation of mitotic spindle organization |
2. P | GO:0015631 | tubulin binding |
2. P | GO:0072393 | microtubule anchoring at microtubule organizing center |
2. P | GO:0099738 | cell cortex region |
2. P | GO:0046600 | negative regulation of centriole replication |
2. P | GO:0000776 | kinetochore |
2. P | GO:0008093 | cytoskeletal anchor activity |
2. P | GO:0000743 | nuclear migration involved in conjugation with cellular fusion |
2. P | GO:0097431 | mitotic spindle pole |
2. P | GO:0005938 | cell cortex |
2. P | GO:0090266 | regulation of mitotic cell cycle spindle assembly checkpoint |
2. P | GO:0007097 | nuclear migration |
Homologs
1. PB indicates the homologs that are found by both PROST and BLAST.
2. P indicates homologs that are only found by PROST.
3. B indicates homologs that are only found by BLAST.
Source | Homolog | Description | FATCAT p-val | PROST Evalue | BLAST Evalue |
---|---|---|---|---|---|
1. PB | Q6TFL3 | Coiled-coil domain-containing protein 171 | 0 | 1.13e-149 | 0.0 |
1. PB | E9Q1U1 | Coiled-coil domain-containing protein 171 | 1.51e-09 | 5.38e-82 | 0.0 |
2. P | Q6PHN1 | Coiled-coil domain-containing protein 57 | 6.10e-04 | 1.84e-04 | NA |
2. P | P33420 | Protein NIP100 | 2.56e-04 | 5.80e-04 | NA |
2. P | Q6PCJ1 | Dynactin subunit 1 | 2.06e-05 | 6.68e-03 | NA |
2. P | V6CJ04 | Protein bicaudal D homolog | 8.96e-06 | 1.94e-04 | NA |
2. P | Q8K389 | CDK5 regulatory subunit-associated protein 2 | 3.08e-01 | 1.07e-03 | NA |
2. P | P35458 | Dynactin subunit 1 | NA | 7.58e-03 | NA |