Protein

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Genbank accession
AHK11233.1 [GenBank]
Protein name
hypothetical protein
RBP type
TSP
Evidence DepoScope
Probability 1,00
TF
Evidence RBPdetect2
Probability 0,43
Protein sequence
MPLYTPSLPTLQGSVNGQTIFLMDAAGNLLQSPASAFRGAGFYTGDALPTEVHPDSGNNASFIDGDFYVYTQGNSGFLYKWDQTQTAGNRWVEVGSLTGTRRHTAISLGVDTFETATTLMNDPITFAAGDTYYNFAKDKTFGPMIAGVGIDFNVENRNYFTSRAPRELTHTDNDPAKLVHTWTPAAITDIEDLAYSPQRGDTYHQEVGNTDHGGYVYTWDEDEFQARILAGDTYAQALSSGWTNIAREFKRAPRSFSETGAPTVDDEKYIDGDTYFDTTNLLIYSGYQTGLVQDNPPLTPAETNGQFLLRVWGNQLPTSLGASSIQHTNNTIALDVTYAADDLVLENRDNTPILYGPYDPLQATIQAAAPYISVMRAPVTHHGLTTPPTNVVGTISGTRVATGDYYIQTESVVRLTEGKQTIFGPCTVDYSDPALPITWDVGVNNNRPLTFFDGIGSNITNDSGFSAGDFLEVNSAIKYGPYVSGAATAALSWPFHSYTRPYRVIQLPTTESNNYTPVTTYDTENGNDVITGDFIEWEVTGTTTGKRVRIGPCNYDHATGVINWGTNRVDMSPSIMHNGPVSTGTPARNDADYCEGDYILNPAGAMYGPYSENEATDTLAWPLYRDLSINPTIVDTGNVDAGTVWRLVAINGVLKLDDGNP
Physico‐chemical
properties
protein length:661 AA
molecular weight: 71995,24790 Da
isoelectric point:4,41391
aromaticity:0,10893
hydropathy:-0,37126

Tail Spike Domain Segmentation

Segmented into three structural domains: N-terminal, central, and C-terminal.

Domain layout
AHK11233.1
1 661 aa
Domain Start End Length (AA) Confidence
N-terminal 1 155 155 0,5827
Central domain 156 354 200 0,1992
C-terminal 355 661 306 0,8875
N-terminal Central domain C-terminal

View these domains on the 3D structure via the Color by → Tail spike option in the Tertiary structure section below.

Taxonomy

Phage
Shewanella sp. phage 1/4 [NCBI] · taxon 1458859
Viruses Duplodnaviria Heunggongvirae Uroviricota Caudoviricetes
Host
Shewanella sp. [NCBI] · taxon 50422
cellular organisms Bacteria Pseudomonadati Pseudomonadota Gammaproteobacteria Alteromonadales
Host
Shewanella sp. 4 [NCBI] · taxon 1386772
Bacteria Proteobacteria Gammaproteobacteria Alteromonadales Shewanellaceae Shewanella

Coding sequence (CDS)

Genbank protein accession
AHK11233.1 [NCBI]
Genbank nucleotide accession
KJ018209 [NCBI]
CDS location
range 69586 -> 71571
strand +
CDS
ATGCCTTTATACACACCATCACTACCTACCTTGCAAGGTAGTGTTAATGGACAAACAATATTTTTAATGGATGCTGCGGGTAATCTGCTACAGTCCCCAGCCAGTGCTTTCCGTGGTGCAGGTTTTTATACAGGAGACGCACTACCTACAGAAGTACATCCAGATAGCGGCAATAACGCATCCTTTATTGACGGAGATTTTTATGTATATACTCAAGGTAACTCTGGATTCCTTTATAAATGGGATCAGACACAAACCGCAGGTAACCGTTGGGTAGAGGTAGGCTCTTTAACTGGTACCCGAAGACATACAGCGATAAGTTTGGGGGTAGATACTTTTGAAACCGCCACTACACTTATGAATGACCCAATTACTTTTGCCGCAGGTGATACATACTACAACTTTGCTAAAGATAAAACCTTTGGTCCTATGATTGCTGGTGTTGGTATTGATTTTAATGTAGAGAATAGAAACTACTTTACAAGTAGGGCACCAAGAGAATTAACACATACAGATAATGACCCAGCTAAATTAGTACATACTTGGACTCCTGCAGCCATAACGGACATAGAAGACCTAGCATACTCTCCACAAAGAGGAGATACATATCACCAAGAAGTTGGTAATACAGATCATGGTGGTTATGTATACACATGGGATGAGGATGAGTTTCAAGCAAGAATCTTAGCTGGGGATACTTATGCACAAGCATTATCATCAGGTTGGACTAATATAGCAAGAGAGTTCAAAAGAGCACCTAGATCATTCTCTGAGACAGGAGCACCCACGGTTGATGACGAAAAATACATTGACGGTGATACTTATTTTGATACAACCAACTTACTAATATACTCAGGTTACCAGACTGGTTTGGTGCAAGACAACCCACCACTGACACCTGCGGAAACAAACGGGCAGTTTCTTTTACGTGTATGGGGGAATCAGTTACCAACCTCTTTGGGTGCTTCTTCAATACAACACACAAACAACACGATAGCTTTAGATGTAACTTATGCCGCAGATGATTTAGTACTAGAGAATAGAGATAATACTCCTATACTATATGGTCCTTATGACCCACTACAAGCAACTATTCAAGCCGCCGCACCTTATATTTCTGTGATGAGAGCACCAGTAACCCACCACGGCTTGACAACACCACCCACTAATGTGGTAGGTACTATCAGTGGGACTAGGGTTGCAACAGGGGATTATTATATTCAGACGGAATCTGTTGTCCGTTTAACTGAAGGTAAGCAGACTATTTTTGGTCCTTGTACTGTAGATTACTCTGACCCTGCTTTACCGATAACTTGGGATGTTGGTGTTAATAACAACAGACCTTTGACCTTTTTTGATGGTATTGGATCTAATATAACCAATGATTCAGGTTTCTCAGCAGGAGATTTCCTTGAGGTAAATAGTGCCATAAAATATGGTCCTTATGTTTCAGGAGCAGCCACTGCTGCATTATCTTGGCCTTTTCATAGCTACACCAGACCTTATAGGGTTATACAGTTACCAACCACAGAGAGTAATAACTACACCCCTGTAACGACATATGATACAGAGAATGGTAATGATGTTATTACGGGAGACTTCATCGAGTGGGAAGTTACAGGAACAACTACAGGTAAGCGGGTAAGGATAGGTCCTTGTAATTATGACCATGCCACAGGAGTTATAAACTGGGGTACTAATAGAGTAGATATGTCTCCTTCTATCATGCACAATGGCCCTGTATCTACAGGAACCCCTGCTAGAAATGATGCAGACTATTGTGAAGGGGATTATATACTTAATCCAGCAGGTGCTATGTATGGTCCTTATAGTGAGAATGAAGCTACAGACACGTTGGCTTGGCCTTTATACAGGGATTTATCTATTAATCCTACCATTGTAGATACAGGGAATGTAGATGCTGGTACTGTTTGGAGATTAGTAGCCATCAATGGTGTTCTCAAGTTAGATGATGGCAACCCATAA

Genome Context

Tertiary structure

AHK11233.1
ESMFold structure
Source ESMFold
pLDDT 58.1
Oligomeric state monomer
Download structure