Ontology highlight
ABSTRACT:
SUBMITTER: Dixon B
PROVIDER: S-EPMC51936 | biostudies-other | 1991 Jul
REPOSITORIES: biostudies-other
Dixon B B Walker B B Kimmins W W Pohajdak B B
Proceedings of the National Academy of Sciences of the United States of America 19910701 13
A cDNA clone encoding a 333-amino acid hemoglobin was isolated from the nematode Pseudoterranova decipiens. The protein contains an 18-amino acid hydrophobic signal sequence and has a calculated mass of 37.6 kDa in the mature form. The predicted protein reveals an internal duplication of a 154-amino acid domain (51% identity). Both domains have significant sequence homology to other primitive hemoglobins, in agreement with a duplication event. Hydrophobicity plots reveal identical strongly hydro ...[more]