Identifying　protein　fold　is　an　important　issue　in　protein　structure　research.　Based　on　the　classification　of　SCOP1.65,　17　Globin-like　proteins　from　four　homology　families　(　＜　25%　sequence　identity)　are　selected　from　Astral　1.65.　The　sequence　alignment　result,　from　structure　alignment　tool　MUSTANG　combined　with　manual　inspection,　has　been　used　to　generate　a　profile　HMM　of　Globin-like　fold.　In　a　fold　identify　test　on　68　057　sequences　of　Astral-1.65,　the　model　identified.　1　097　Globin-like　proteins　rightly,　only　4　proteins　of　this　fold　are　not　correctly　distinguished.　The　sensitivity　and　specificity　of　the　profile　HMM　reach　to　99.64%　and　100%,　respectively.　Compared　with　Pfam　and　SUPERFAMILY　which　construct　HMM　based　on　merely　sequence　alignment,　the　model　number　is　reduced　from　about　100　to　1,　while　keeping　the　sensitivity　at　the　same　level.　The　result　shows　that,　for　those　proteins　with　same　fold　type　but　low　sequence　identity,　a　unified　HMM　could　be　constructed　by　introducing　structure　alignment　to　fold　identify　with　high　accuracy.