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Q62976 (KCMA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium-activated potassium channel subunit alpha-1
Alternative name(s):
BK channel
BKCA alpha
Calcium-activated potassium channel, subfamily M subunit alpha-1
K(VCA)alpha
KCa1.1
Maxi K channel
Short name=MaxiK
Slo-alpha
Slo1
Slowpoke homolog
Short name=Slo homolog
Gene names
Name:Kcnma1
Synonyms:Kcnma
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length1209 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Potassium channel activated by both membrane depolarization or increase in cytosolic Ca2+ that mediates export of K+. It is also activated by the concentration of cytosolic Mg2+. Its activation dampens the excitatory events that elevate the cytosolic Ca2+ concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca2+, caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX).

Enzyme regulation

Ethanol and carbon monoxide-bound heme increase channel activation. Heme inhibits channel activation. Ref.6

Subunit structure

Homotetramer; which constitutes the calcium-activated potassium channel. Interacts with beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4. Interacts with gamma subunits LRRC26, LRRC38, LRRC52 and LRRC55. Beta and gamma subunits are accessory, and modulate its activity By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Isoform 7: Endoplasmic reticulum membrane; Multi-pass membrane protein. Note: Has a dominant-negative effect on other isoforms, preventing their localization to the cell membrane.

Domain

The S0 segment is essential for the modulation by the accessory beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4 By similarity.

The S4 segment, which is characterized by a series of positively charged amino acids at every third position, is part of the voltage-sensor By similarity.

The pore-forming domain (also referred as P region) is imbedded into the membrane, and forms the selectivity filter of the pore. It contains the signature sequence of potassium channels that displays selectivity to potassium By similarity.

The RCK N-terminal domain mediates the homotetramerization, thereby promoting the assembly of monomers into functional potassium channel. It includes binding sites for Ca2+ and Mg2+ By similarity.

The calcium bowl constitutes one of the Ca2+ sensors and probably acts as a Ca2+-binding site. There are however other Ca2+ sensors regions required for activation of the channel By similarity.

The heme-binding motif mediates inhibition of channel activation by heme. Carbon monoxide-bound heme leads to increased channel activation.

Post-translational modification

Phosphorylated Probable. Phosphorylation by kinases such as PKA and/or PKG. In smooth muscles, phosphorylation affects its activity By similarity.

Miscellaneous

The protein was initially thought to contain two functionally distinct parts: The core channel (from the N-terminus to the S9 segment) that mediates the channel activity, and the cytoplasmic tail (from the S9 segment to the C-terminus) that mediates the calcium sensing. The situation is however more complex, since the core channel contains binding sites for Ca2+ and Mg2+.

Sequence similarities

Belongs to the potassium channel family. Calcium-activated (TC 1.A.1.3) subfamily. KCa1.1/KCNMA1 sub-subfamily. [View classification]

Contains 1 RCK N-terminal domain.

Sequence caution

The sequence AAB51398.1 differs from that shown. Reason: Frameshift at position 1203.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MbpP026884EBI-1638146,EBI-1638296

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Note: May be partially controlled by hormonal stress. Additional isoforms seem to exist.
Isoform 1 (identifier: Q62976-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q62976-2)

Also known as: B; C; cvb1; cvb2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
     644-647: Missing.
     949-975: Missing.
Isoform 3 (identifier: Q62976-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
     644-647: Missing.
     949-975: Missing.
     1203-1209: KKEMVYR → NNRRCWWFSKRQDIHQQKRNGLQMRRIMPIPETFKSSP
Isoform 4 (identifier: Q62976-8)

Also known as: STTEX;

The sequence of this isoform differs from the canonical sequence as follows:
     703-703: L → LIYSKMSIYKRMSRACCFDCGRSERDCSCMSGRVRGNVDTLERNFPLSSVSVNDCSTSFRAF
     949-975: Missing.
Isoform 5 (identifier: Q62976-9)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     644-647: Missing.
     949-975: Missing.
     1128-1165: RYVITNPPYE...AGQSRASLSH → SNRRCWWFSK...PIPETFKSSP
     1166-1209: Missing.
Isoform 6 (identifier: Q62976-10)

Also known as: SLON-1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
     949-975: Missing.
Isoform 7 (identifier: Q62976-11)

Also known as: SV1;

The sequence of this isoform differs from the canonical sequence as follows:
     181-181: L → AFERSSLLARISIQKDGCQCVLFSSHFMPRLLM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12091209Calcium-activated potassium channel subunit alpha-1
PRO_0000054137

Regions

Topological domain1 – 8787Extracellular Potential
Transmembrane88 – 10821Helical; Name=Segment S0; Potential
Topological domain109 – 17971Cytoplasmic Potential
Transmembrane180 – 20021Helical; Name=Segment S1; Potential
Topological domain201 – 21515Extracellular Potential
Transmembrane216 – 23621Helical; Name=Segment S2; Potential
Topological domain237 – 2404Cytoplasmic Potential
Transmembrane241 – 26121Helical; Name=Segment S3; Potential
Topological domain262 – 2654Extracellular Potential
Transmembrane266 – 28621Helical; Voltage-sensor; Name=Segment S4; Potential
Topological domain287 – 30115Cytoplasmic Potential
Transmembrane302 – 32221Helical; Name=Segment S5; Potential
Topological domain323 – 33614Extracellular Potential
Intramembrane337 – 35923Pore-forming; Name=P region; Potential
Topological domain360 – 3689Extracellular Potential
Transmembrane369 – 38921Helical; Name=Segment S6; Potential
Topological domain390 – 1209820Cytoplasmic Potential
Domain416 – 559144RCK N-terminal
Region557 – 57721Segment S7
Region614 – 63421Segment S8
Region682 – 6865Heme-binding motif
Region784 – 80421Segment S9
Region1006 – 102621Segment S10
Motif353 – 3564Selectivity for potassium
Motif977 – 99923Calcium bowl
Compositional bias4 – 118Poly-Gly
Compositional bias17 – 259Poly-Gly
Compositional bias45 – 6117Poly-Ser

Sites

Metal binding4401Magnesium By similarity
Metal binding4631Magnesium By similarity
Metal binding4651Magnesium By similarity
Metal binding9861Calcium; via carbonyl oxygen By similarity
Metal binding9891Calcium; via carbonyl oxygen By similarity
Metal binding9921Calcium By similarity
Metal binding9941Calcium By similarity

Amino acid modifications

Modified residue7121Phosphoserine By similarity
Modified residue10621Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 3030Missing in isoform 2, isoform 3 and isoform 6.
VSP_009970
Alternative sequence1811L → AFERSSLLARISIQKDGCQC VLFSSHFMPRLLM in isoform 7.
VSP_009971
Alternative sequence644 – 6474Missing in isoform 2, isoform 3 and isoform 5.
VSP_009973
Alternative sequence7031L → LIYSKMSIYKRMSRACCFDC GRSERDCSCMSGRVRGNVDT LERNFPLSSVSVNDCSTSFR AF in isoform 4.
VSP_009974
Alternative sequence949 – 97527Missing in isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.
VSP_009976
Alternative sequence1128 – 116538RYVIT…ASLSH → SNRRCWWFSKRQDIHQQKRN GLQMRRIMPIPETFKSSP in isoform 5.
VSP_009978
Alternative sequence1166 – 120944Missing in isoform 5.
VSP_009979
Alternative sequence1203 – 12097KKEMVYR → NNRRCWWFSKRQDIHQQKRN GLQMRRIMPIPETFKSSP in isoform 3.
VSP_009982

Experimental info

Mutagenesis685 – 6862CH → SR: Loss of heme-induced channel inhibition as well as carbon monoxide-induced channel activation. Ref.6
Sequence conflict331Missing in AAB51398. Ref.1
Sequence conflict331Missing in AAA99161. Ref.4
Sequence conflict1321I → V in AAP82452. Ref.7
Sequence conflict1581G → V in AAC32866. Ref.5
Sequence conflict1641K → E in AAB51398. Ref.1
Sequence conflict1761L → P in AAP82451. Ref.7
Sequence conflict2051E → Q in AAC32866. Ref.5
Sequence conflict2381N → K in AAP82451. Ref.7
Sequence conflict2661N → D in AAP82451. Ref.7
Sequence conflict2791R → I in AAP82451. Ref.7
Sequence conflict2811I → V in AAP82452. Ref.7
Sequence conflict2861I → S in AAP82452. Ref.7
Sequence conflict2961S → N in AAP82450. Ref.7
Sequence conflict3381L → P in AAA99161. Ref.4
Sequence conflict3531T → A in AAP82452. Ref.7
Sequence conflict3641T → S in AAA99161. Ref.4
Sequence conflict3641T → TLGT in AAP82452. Ref.7
Sequence conflict4461N → S in AAP82451. Ref.7
Sequence conflict4501N → D in AAP82451. Ref.7
Sequence conflict4681Q → K in AAB51398. Ref.1
Sequence conflict4701S → P in AAP82452. Ref.7
Sequence conflict4791R → T in AAA99161. Ref.4
Sequence conflict5491A → S in AAC32866. Ref.5
Sequence conflict5521L → H in AAP82452. Ref.7
Sequence conflict5531A → V in AAP82454. Ref.6
Sequence conflict6001N → T in AAB51398. Ref.1
Sequence conflict6051E → G in AAA99161. Ref.4
Sequence conflict6371K → R in AAP82452. Ref.7
Sequence conflict6591I → T in AAB96356. Ref.3
Sequence conflict6601Q → R in AAB51398. Ref.1
Sequence conflict6771R → K in AAB51398. Ref.1
Sequence conflict685 – 6873CHD → YHE in AAP82452. Ref.7
Sequence conflict7341R → K in AAD34786. Ref.2
Sequence conflict7391L → S in AAP82454. Ref.6
Sequence conflict7621F → L in AAA99161. Ref.4
Sequence conflict7801A → V in AAP82454. Ref.6
Sequence conflict8061N → NRN in AAP82451. Ref.7
Sequence conflict8641I → L in AAC32866. Ref.5
Sequence conflict8851L → V in AAC32866. Ref.5
Sequence conflict9401I → T in AAP82453. Ref.6
Sequence conflict9891D → G in AAP82451. Ref.7
Sequence conflict10051P → L in AAA99161. Ref.4
Sequence conflict10121F → S in AAC32866. Ref.5
Sequence conflict10931Y → C in AAP82452. Ref.7
Sequence conflict11071L → F in AAP82451. Ref.7
Sequence conflict11731S → P in AAP82453. Ref.6
Sequence conflict11881N → S in AAP82454. Ref.6
Sequence conflict12031K → NR in AAB51398. Ref.1
Sequence conflict12031K → NR in AAD34786. Ref.2
Sequence conflict12031K → NR in AAP82454. Ref.6
Sequence conflict12031K → NR in AAP82451. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 5, 2008. Version 3.
Checksum: 14F19072DA7F22FE

FASTA1,209134,374
        10         20         30         40         50         60 
MANGGGGGGG GSSGSSGGGG GGGGGETALR MSSNIHANHL SLDASSSSSS SSSSSSSSSS 

        70         80         90        100        110        120 
SVHEPKMDAL IIPVTMEVPC DSRGQRMWWA FLASSMVTFF GGLFIILLWR TLKYLWTVCC 

       130        140        150        160        170        180 
HCGGKTKEAQ KINNGSSQAD GTLKPVDEKE EVVAAEVGWM TSVKDWAGVM ISAQTLTGRV 

       190        200        210        220        230        240 
LVVLVFALSI GALVIYFIDS SNPIESCQNF YKDFTLQIDM AFNVFFLLYF GLRFIAANDK 

       250        260        270        280        290        300 
LWFWLEVNSV VDFFTVPPVF VSVYLNRSWL GLRFLRALRL IQFSEILQFL NILKTSNSIK 

       310        320        330        340        350        360 
LVNLLSIFIS TWLTAAGFIH LVENSGDPWE NFQNNQALTY WECVYLLMVT MSTVGYGDVY 

       370        380        390        400        410        420 
AKTTLGRLFM VFFILGGLAM FASYVPEIIE LIGNRKKYGG SYSAVSGRKH IVVCGHITLE 

       430        440        450        460        470        480 
SVSNFLKDFL HKDRDDVNVE IVFLHNISPN LELEALFKRH FTQVEFYQGS VLNPHDLARV 

       490        500        510        520        530        540 
KIESADACLI LANKYCADPD AEDASNIMRV ISIKNYHPKI RIITQMLQYH NKAHLLNIPS 

       550        560        570        580        590        600 
WNWKEGDDAI CLAELKLGFI AQSCLAQGLS TMLANLFSMR SFIKIEEDTW QKYYLEGVSN 

       610        620        630        640        650        660 
EMYTEYLSSA FVGLSFPTVC ELCFVKLKLL MIAIEYKSAN RESRSRKRIL INPGNHLKIQ 

       670        680        690        700        710        720 
EGTLGFFIAS DAKEVKRAFF YCKACHDDVT DPKRIKKCGC RRLEDEQPPT LSPKKKQRNG 

       730        740        750        760        770        780 
GMRNSPNTSP KLMRHDPLLI PGNDQIDNMD SNVKKYDSTG MFHWCAPKEI EKVILTRSEA 

       790        800        810        820        830        840 
AMTVLSGHVV VCIFGDVSSA LIGLRNLVMP LRASNFHYHE LKHIVFVGSI EYLKREWETL 

       850        860        870        880        890        900 
HNFPKVSILP GTPLSRADLR AVNINLCDMC VILSANQNNI DDTSLQDKEC ILASLNIKSM 

       910        920        930        940        950        960 
QFDDSIGVLQ ANSQGFTPPG MDRSSPDNSP VHGMLRQPSI TTGVNIPIIT ELAKPGKLPL 

       970        980        990       1000       1010       1020 
VSVNQEKNSG THILMITELV NDTNVQFLDQ DDDDDPDTEL YLTQPFACGT AFAVSVLDSL 

      1030       1040       1050       1060       1070       1080 
MSATYFNDNI LTLIRTLVTG GATPELEALI AEENALRGGY STPQTLANRD RCRVAQLALL 

      1090       1100       1110       1120       1130       1140 
DGPFADLGDG GCYGDLFCKA LKTYNMLCFG IYRLRDAHLS TPSQCTKRYV ITNPPYEFEL 

      1150       1160       1170       1180       1190       1200 
VPTDLIFCLM QFDHNAGQSR ASLSHSSHSS QSSSKKSSSV HSIPSTANRP NRPKSRESRD 


KQKKEMVYR

« Hide

Isoform 2 (B) (C) (cvb1) (cvb2) [UniParc].

Checksum: 7518E011D0AED714
Show »

FASTA1,148128,684
Isoform 3 [UniParc].

Checksum: B88D1A037BE26970
Show »

FASTA1,179132,502
Isoform 4 (STTEX) [UniParc].

Checksum: 37BDFB5E50D15FAF
Show »

FASTA1,243138,388
Isoform 5 (A) [UniParc].

Checksum: 959090FF5F757293
Show »

FASTA1,134126,309
Isoform 6 (SLON-1) [UniParc].

Checksum: 9BB5D98E6BD5D293
Show »

FASTA1,152129,211
Isoform 7 (SV1) [UniParc].

Checksum: 4777BC0BFBE348FF
Show »

FASTA1,241138,029

References

[1]"Increased expression of Ca2+-sensitive K+ channels in aorta of hypertensive rats."
Liu Y., Pleyte K., Knaus H.-G., Rusch N.J.
Hypertension 30:1403-1409(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: Sprague-Dawley.
Tissue: Aortic smooth muscle.
[2]"Functional characteristics of two BKCa channel variants differentially expressed in rat brain tissues."
Ha T.S., Jeong S.Y., Cho S.-W., Jeon H.-K., Roh G.S., Choi W.S., Park C.-S.
Eur. J. Biochem. 267:910-918(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: Sprague-Dawley.
Tissue: Brain.
[3]Reimann F.
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Strain: Sprague-Dawley.
Tissue: Brain cortex.
[4]"Cloning and expression of smooth muscle specific isoforms of a rat calcium-activated potassium channel."
Lawrence K.M., Fenech C.J., Zhang H., Bolton T.B.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Strain: Wistar HsdOla.
Tissue: Myometrium.
[5]"Identification and localization of Ca(2+)-activated K+ channels in rat sciatic nerve."
Mi H., Harris-Warrick R.M., Deerinck T.J., Inman I., Ellisman M.H., Schwarz T.L.
Glia 26:166-175(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1028 (ISOFORM 6).
Strain: Sprague-Dawley.
[6]"Heme is a carbon monoxide receptor for large-conductance Ca2+-activated K+ channels."
Jaggar J.H., Li A., Parfenova H., Liu J., Umstot E.S., Dopico A.M., Leffler C.W.
Circ. Res. 97:805-812(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-1209 (ISOFORM 2), ENZYME REGULATION, MUTAGENESIS OF 685-CYS-HIS-686.
Strain: Sprague-Dawley.
Tissue: Cerebral artery.
[7]"Slo subunits cloned from freshly isolated rat cerebral artery myocytes."
Liu J., Asuncion-Chin M.T., Liu P., Dopico A.M.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-1209 (ISOFORMS 2 AND 5).
Strain: Sprague-Dawley.
Tissue: Aorta and Cerebral artery.
[8]"A novel MaxiK splice variant exhibits dominant-negative properties for surface expression."
Zarei M.M., Zhu N., Alioua A., Eghbali M., Stefani E., Toro L.
J. Biol. Chem. 276:16232-16239(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 7).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U93052 mRNA. Translation: AAB51398.1. Frameshift.
AF135265 mRNA. Translation: AAD34786.1.
U40603 mRNA. Translation: AAB96356.1.
U55995 mRNA. Translation: AAA99161.1.
AF083341 mRNA. Translation: AAC32866.1.
AY330290 mRNA. Translation: AAP82450.1.
AY330291 mRNA. Translation: AAP82451.1.
AY330292 mRNA. Translation: AAP82452.1.
AY330293 mRNA. Translation: AAP82453.2.
AY330294 mRNA. Translation: AAP82454.1.
IPIIPI00411170.
IPI00411171.
IPI00411260.
IPI00411261.
IPI00411262.
IPI00411267.
IPI00411268.
RefSeqNP_114016.1. NM_031828.1.
UniGeneRn.30616.

3D structure databases

ProteinModelPortalQ62976.
ModBaseSearch...

Protein-protein interaction databases

IntActQ62976. 42 interactions.
MINTMINT-1203282.

Protein family/group databases

TCDB1.A.1.3.2. voltage-gated ion channel (VIC) superfamily.

PTM databases

PhosphoSiteQ62976.

Proteomic databases

PaxDbQ62976.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID83731.
KEGGrno:83731.

Organism-specific databases

CTD3778.
RGD620715. Kcnma1.

Phylogenomic databases

eggNOGCOG1226.
HOVERGENHBG052222.
KOK04936.
OrthoDBEOG4QFWCD.

Gene expression databases

ArrayExpressQ62976.
GenevestigatorQ62976.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR024939. Ca-act_K_channel_Slo.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003929. K_chnl_Ca-activ_BK_asu.
IPR016040. NAD(P)-bd_dom.
IPR003148. RCK_N.
[Graphical view]
PANTHERPTHR10027:SF3. PTHR10027:SF3. 1 hit.
PfamPF03493. BK_channel_a. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02254. TrkA_N. 1 hit.
[Graphical view]
PRINTSPR01449. BKCHANNELA.
PR00169. KCHANNEL.
PROSITEPS51201. RCK_N. False negative.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL5505.
NextBio616325.

Entry information

Entry nameKCMA1_RAT
AccessionPrimary (citable) accession number: Q62976
Secondary accession number(s): O08626 expand/collapse secondary AC list , O55180, O88659, Q7TMZ7, Q7TMZ8, Q7TQ55, Q7TQ56, Q7TQ57, Q9WUI3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: February 5, 2008
Last modified: April 3, 2013
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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