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PR00186

Identifier
HEMERYTHRIN  [View Relations]  [View Alignment]  
Accession
PR00186
No. of Motifs
4
Creation Date
04-JAN-1994  (UPDATE 07-JUN-1999)
Title
Hemerythrin signature
Database References

PROSITE; PS00550 HEMERYTHRINS
BLOCKS; BL00550
INTERPRO; IPR002063
PDB; 1HMD
SCOP; 1HMD
CATH; 1HMD
Literature References
1. TAKAGI, T. AND COX, J.A.
Primary structure of myohemerythrin from the annelid Nereis diversicolor.
FEBS LETT. 285(1) 25-27 (1991).
 
2. STENKAMP, R.E., SIEKER, L.C., JENSEN, L.H., MCCALLUM, J.D. AND
SANDERSLOEHR, J.
Active-site structures of deoxyhemerythrin and oxyhemerythrin.
PROC.NATL.ACAD.SCI.U.S.A. 82(3) 713-716 (1985).
 
3. BAERT, J.L., BRITEL, M., SAUTIERE, P. AND MALECHA, J.
Ovohemerythrin, a major 14kDa yolk protein distinct from vitellogenin in
leech.
EUR.J.BIOCHEMISTRY 209(2) 563-569 (1992).

Documentation
Marine invertebrates possess 2 different types of oxygen-binding protein:
porphyrin-containing pigments, such as haemoglobin; and hemerythrin,
found in the vascular system and coelemic fluid, or in muscles (myohem-
erythrin) [1]. The active centre of both proteins is a binuclear iron
complex, bound directly to the protein via 7 amino acid side chains [2], 
5 His, 1 Glu and 1 Asp [1]. Hemerythrins comprise left-twisted 4-alpha-
helical bundles, which provide a hydrophobic pocket where dioxygen binds
as a peroxo species, interacting with adjacent aliphatic side chains via
van der Waals forces [2]. The leech yolk protein, ovohemerythrin, is 
another family member, possibly playing a role in the detoxification 
of free iron after a blood meal [3].
 
HEMERYTHRIN is a 4-element fingerprint that provides a signature for the
hemerythrins. The fingerprint was derived from an initial alignment of 6
sequences: motif 1 is drawn from a well-conserved N-terminal region; and
motifs 2, 3 and 4 include parts of helices 1, 3 and 4, which contain the
Asp, Tyr and 4 His residues involved in binding the binuclear iron cluster
- motif 4 includes the region encoded by PROSITE pattern HEMERYTHRINS
(PS00550). Two iterations on OWL22.1 were required to reach convergence,
at which point a true set comprising 20 sequences was identified. Eight
partial matches were also found, all of which are hemerythrin fragments
from crystallographic studies.
 
An update on SPTR37_9f identified a true set of 10 sequences.
Summary Information
10 codes involving  4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
410101010
30000
20000
1234
True Positives
HEM1_PHAGO    HEMM_NERDI    HEMM_THEZO    HEMT_LINUN    
HEMT_PHAGO HEMT_SIPCU HEMT_THEDY HEMT_THEZO
HEMU_LINUN MP2_NERDI
Sequence Titles
HEM1_PHAGO  MYOHEMERYTHRIN ISOFORM 1 (MHR 1) - PHASCOLOPSIS GOULDII (GOLFINGIA GOULDII). 
HEMM_NERDI MYOHEMERYTHRIN (MHR) - NEREIS DIVERSICOLOR (SANDWORM) (HEDISTE DIVERSICOLOR).
HEMM_THEZO MYOHEMERYTHRIN (MHR) - THEMISTE ZOSTERICOLA.
HEMT_LINUN HEMERYTHRIN ALPHA CHAIN - LINGULA UNGUIS.
HEMT_PHAGO HEMERYTHRIN - PHASCOLOPSIS GOULDII (GOLFINGIA GOULDII).
HEMT_SIPCU HEMERYTHRIN - SIPHONOSOMA CUMANENSE.
HEMT_THEDY HEMERYTHRIN - THEMISTE DYSCRITUM.
HEMT_THEZO HEMERYTHRIN - THEMISTE ZOSTERICOLA.
HEMU_LINUN HEMERYTHRIN BETA CHAIN - LINGULA UNGUIS.
MP2_NERDI NON-METALLOTHIONEIN CADMIUM-BINDING PROTEIN (CD-BP) (MP II) - NEREIS DIVERSICOLOR (SANDWORM) (HEDISTE DIVERSICOLOR).
Scan History
OWL22_1    2  100  NSINGLE    
OWL26_0 1 100 NSINGLE
SPTR37_9f 2 12 NSINGLE
Initial Motifs
Motif 1  width=14
Element Seqn Id St Int Rpt
VPDPFIWDASFKTF HEMT_SIPCU 4 4 -
VPEPFAWNESFATS HEMT_LINUN 3 3 -
IPDPYCWDISFRTF NRL_1HMDA 4 4 -
IPVPYAWTPDFKTT HEMU_LINUN 3 3 -
IPEPYVWDESFRVF HEM1_PHAGO 4 4 -
VPEPFKWDESFQVF HEMM_NERDI 4 4 -

Motif 2 width=15
Element Seqn Id St Int Rpt
YKNIDLEHRTLFNGL HEMT_LINUN 17 0 -
YTIIDDEHKTLFNGI NRL_1HMDA 18 0 -
YDNLDDEHKGLFKGV HEM1_PHAGO 18 0 -
YDKLDEEHKQIFNAI HEMM_NERDI 18 0 -
YDDLDNQHKQLFQAI HEMT_SIPCU 18 0 -
YENIDSEHRTLFNGL HEMU_LINUN 17 0 -

Motif 3 width=12
Element Seqn Id St Int Rpt
HKKAHDDFIHKL NRL_1HMDA 73 40 -
HKQMHKDFLAKL HEM1_PHAGO 74 41 -
HKKKHEDFLAVI HEMM_NERDI 75 42 -
HKAAHEEFLGKV HEMT_SIPCU 73 40 -
HRGIHEGFLEKM HEMT_LINUN 72 40 -
HTDIHNGFMDTM HEMU_LINUN 72 40 -

Motif 4 width=17
Element Seqn Id St Int Rpt
EWLVNHIPTEDFKYKGK HEMT_LINUN 100 16 -
EWLANHIPTEDFKYKGK HEMU_LINUN 100 16 -
DWLVQHIKTTDFKYKGK HEM1_PHAGO 102 16 -
NWLVNHIKTIDFKYRGK NRL_1HMDA 96 11 -
DWLVNHIKGTDFTYKGK HEMM_NERDI 103 16 -
DWLTQHIKTIDFKYKGK HEMT_SIPCU 96 11 -
Final Motifs
Motif 1  width=14
Element Seqn Id St Int Rpt
IPDPYVWDPSFRTF HEMT_PHAGO 4 4 -
IPDPYGWDPSFRTF HEMT_THEZO 4 4 -
IPEPYVWDESFRVF HEMM_THEZO 4 4 -
IPEPYKWDESFQVF MP2_NERDI 4 4 -
IPDPYCWDISFRTF HEMT_THEDY 4 4 -
IPEPYVWDESFRVF HEM1_PHAGO 4 4 -
VPEPFKWDESFQVF HEMM_NERDI 4 4 -
VPDPFIWDASFKTF HEMT_SIPCU 4 4 -
VPEPFAWNESFATS HEMT_LINUN 3 3 -
IPVPYAWTPDFKTT HEMU_LINUN 3 3 -

Motif 2 width=15
Element Seqn Id St Int Rpt
YSIIDDEHKTLFNGI HEMT_PHAGO 18 0 -
YSIIDDEHKTLFNGI HEMT_THEZO 18 0 -
YEQLDEEHKKIFKGI HEMM_THEZO 18 0 -
YEKLDEEHKQIFNAI MP2_NERDI 18 0 -
YTIVDDEHKTLFNGI HEMT_THEDY 18 0 -
YDNLDDEHKGLFKGV HEM1_PHAGO 18 0 -
YDKLDEEHKQIFNAI HEMM_NERDI 18 0 -
YDDLDNQHKQLFQAI HEMT_SIPCU 18 0 -
YKNIDLEHRTLFNGL HEMT_LINUN 17 0 -
YENIDSEHRTLFNGL HEMU_LINUN 17 0 -

Motif 3 width=12
Element Seqn Id St Int Rpt
HKKEHEGFIHAL HEMT_PHAGO 73 40 -
HKKAHEEFIRAL HEMT_THEZO 73 40 -
HKKMHKDFLEKI HEMM_THEZO 73 40 -
HKKKHEDFLAVI MP2_NERDI 74 41 -
HKKAHDDFIHKL HEMT_THEDY 73 40 -
HKQMHKDFLAKL HEM1_PHAGO 74 41 -
HKKKHEDFLAVI HEMM_NERDI 75 42 -
HKAAHEEFLGKV HEMT_SIPCU 73 40 -
HRGIHEGFLEKM HEMT_LINUN 72 40 -
HTDIHNGFMDTM HEMU_LINUN 72 40 -

Motif 4 width=17
Element Seqn Id St Int Rpt
SWLVNHIKTIDFKYKGK HEMT_PHAGO 96 11 -
SWLVNHIKTIDFKYKGK HEMT_THEZO 96 11 -
EWLVNHIKGTDFKYKGK HEMM_THEZO 101 16 -
EWLVNHIKGTDFGYKGK MP2_NERDI 102 16 -
NWLVNHIKTIDFKYRGK HEMT_THEDY 96 11 -
DWLVQHIKTTDFKYKGK HEM1_PHAGO 102 16 -
DWLVNHIKGTDFTYKGK HEMM_NERDI 103 16 -
DWLTQHIKTIDFKYKGK HEMT_SIPCU 96 11 -
EWLVNHIPTEDFKYKGK HEMT_LINUN 100 16 -
EWLANHIPTEDFKYKGK HEMU_LINUN 100 16 -