NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2020764001|ref|XP_040334621|]
View 

alpha-protein kinase 2 isoform X1 [Puma yagouaroundi]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Alpha_kinase_ALPK2 cd16974
Alpha-kinase domain of alpha-protein kinase 2; Alpha-protein kinase 2 (ALPK2) is also called ...
 1822-2059 3.10e-166

Alpha-kinase domain of alpha-protein kinase 2; Alpha-protein kinase 2 (ALPK2) is also called heart alpha-protein kinase (HAK). Little functional information is known about ALPK2. In a three-dimensional colonic-crypt model, it has been identified as crucial for luminal apoptosis and expression of DNA repair-related genes, possibly in the transition of normal colonic crypt to adenoma. The ALPK2 gene may also be a novel candidate gene for inherited hypertension in Dahl rats. ALPK2 contains a C-terminal alpha-kinase domain and two immunoglobulin (Ig)-like domains. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


:

Pssm-ID: 341224  Cd Length: 239  Bit Score: 508.21  E-value: 3.10e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1822 KGCEEIEFSQLIFREDFLRDSYFGDHLRGQIATEELHFGEGVHRKAFRSKVMQGLMPVFQPGHACVLKVHNAVAYGTRNN 1901
Cdd:cd16974      2 KGGEEIEFSQLMFKEDFLSDSYFGGNLHGRIATEKLHFGEGMHRKAFRSKVMCGLLPVFLPGHACVLKVHNAIAYGTKNN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1902 DELIQRNYKLAAQECYVQNTARYYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGKE 1981
Cdd:cd16974     82 DELIQKNYKLAVQECYVQNTAREYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPANNIPYATVEEELIGDFVKYSVRDGKE 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020764001 1982 INFLRRESEAGQKCCTFQHWVYQRTSGCLLVTDMQGVGMKLTDVGIATLAKGYKGFKGNCSMTFIDQFKALHQCNKYC 2059
Cdd:cd16974    162 INVLRRDSEAGQKCCTFQHWVYQKTDGNLLVTDMQGVGMKLTDVGIATCSKGYKGFKGNCSVSFIDQFKALHQCNKYC 239
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 12-105 8.06e-38

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20951:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 94  Bit Score: 137.55  E-value: 8.06e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   12 LCFLSTLLSQKVPEKSDAVLRCMISGQPKPEVTWYKNGRAIDECGIVSSYEFFQNQYIHLLHLYRCTPDDTAVYQISAKN 91
Cdd:cd20951      1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80

                           90
                   ....*....|....
gi 2020764001   92 CSGMICCSASIEVK 105
Cdd:cd20951     81 IHGEASSSASVVVE 94
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 1736-1808 4.99e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.34  E-value: 4.99e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020764001  1736 GNVKLSCQFAEiHEDSTVWWTKDSKSVAQVQRRA---DDTSAVSLAVVQAGQKDQGIYRCCIKNSYGKATAEFNLT 1808
Cdd:smart00410   10 ESVTLSCEASG-SPPPEVTWYKQGGKLLAESGRFsvsRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
 
Name Accession Description Interval E-value
Alpha_kinase_ALPK2 cd16974
Alpha-kinase domain of alpha-protein kinase 2; Alpha-protein kinase 2 (ALPK2) is also called ...
 1822-2059 3.10e-166

Alpha-kinase domain of alpha-protein kinase 2; Alpha-protein kinase 2 (ALPK2) is also called heart alpha-protein kinase (HAK). Little functional information is known about ALPK2. In a three-dimensional colonic-crypt model, it has been identified as crucial for luminal apoptosis and expression of DNA repair-related genes, possibly in the transition of normal colonic crypt to adenoma. The ALPK2 gene may also be a novel candidate gene for inherited hypertension in Dahl rats. ALPK2 contains a C-terminal alpha-kinase domain and two immunoglobulin (Ig)-like domains. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341224  Cd Length: 239  Bit Score: 508.21  E-value: 3.10e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1822 KGCEEIEFSQLIFREDFLRDSYFGDHLRGQIATEELHFGEGVHRKAFRSKVMQGLMPVFQPGHACVLKVHNAVAYGTRNN 1901
Cdd:cd16974      2 KGGEEIEFSQLMFKEDFLSDSYFGGNLHGRIATEKLHFGEGMHRKAFRSKVMCGLLPVFLPGHACVLKVHNAIAYGTKNN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1902 DELIQRNYKLAAQECYVQNTARYYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGKE 1981
Cdd:cd16974     82 DELIQKNYKLAVQECYVQNTAREYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPANNIPYATVEEELIGDFVKYSVRDGKE 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020764001 1982 INFLRRESEAGQKCCTFQHWVYQRTSGCLLVTDMQGVGMKLTDVGIATLAKGYKGFKGNCSMTFIDQFKALHQCNKYC 2059
Cdd:cd16974    162 INVLRRDSEAGQKCCTFQHWVYQKTDGNLLVTDMQGVGMKLTDVGIATCSKGYKGFKGNCSVSFIDQFKALHQCNKYC 239
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
 1839-2059 1.64e-60

Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional kinases. The family contains myosin heavy chain kinases and Elongation Factor-2 kinase and a bifunctional ion channel. This family is known as the alpha-kinase family. The structure of the kinase domain revealed unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains.


Pssm-ID: 214828  Cd Length: 198  Bit Score: 206.44  E-value: 1.64e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001  1839 LRDSYFGDHLRGQIatEELHFGEGVHRKAFRSKVMQGlmpvFQPGHACVLKVHNavaygTRNNDELIQRNYKlaaqECYV 1918
Cdd:smart00811    1 SSGKWTVSETGVKI--ELKPFAKGAMRVAFRVKDLSE----DGSGTECVAKYFK-----KEYKNTVEDRYFE----DVEM 65

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001  1919 QNTARYYAKIYAAeaqpLEGFGEVPEIIPIFLIHRPENNIPY-ATVEEELIGEFVKYSIRDGKEINFLRRESeagqKCCT 1997
Cdd:smart00811   66 QMVAKKFAEEFNQ----LKPSPKKIEFLPSYVLELPDRSIPYlFTVEPFLEGEFVKYNSNNGWVNDEARSTE----APQA 137

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020764001  1998 FQHWVYQRTSGCLLVTDMQGVGMKLTDVGIATlAKGYKGFKGNCSMTFIDQFKALHQCNKYC 2059
Cdd:smart00811  138 FSHFTYERSGGSLLVVDLQGVGDLLTDPQIHT-EDGFGFGPGNLGEEGIEKFFATHKCNSIC 198
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
 1860-2059 9.58e-52

Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional kinases. The family contains myosin heavy chain kinases and Elongation Factor-2 kinase and a bifunctional ion channel. This family is known as the alpha-kinase family. The structure of the kinase domain revealed unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains.


Pssm-ID: 460709  Cd Length: 185  Bit Score: 180.99  E-value: 9.58e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1860 GEGVHRKAFRSKVMqglmPVFQPGHACVLKVHNAVAYGTrnndeliqrNYKLAAQECYVQNTARYYAKIYAAEAQPLEGF 1939
Cdd:pfam02816    1 AEGAMRKAFKAKVD----PGDESGQNYVAKEFKKIVYGV---------ELEYYFEDAQSQALAKELAEEFNAEARALENF 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1940 GEVP-EIIPIFLI-HRPENNIPYATVEEELIGEFVKYSIRDGKEINflrRESEAGQKCCTFQHWVYQRTSGCLLVTDMQG 2017
Cdd:pfam02816   68 PPKKiEFIPPYVVeLDPANGKPYYLVEPFLEGNFVKYNSNTGFVSE---EDDELEQTMQAFSHFTYERSGGQLLVCDLQG 144

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2020764001 2018 VGMKLTDVGIATLAKGYKGFkGNCSMTFIDQFKALHQCNKYC 2059
Cdd:pfam02816  145 VGNLLTDPAIHTKDGKRFGD-TNLGEEGIASFFSTHKCNKIC 185
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 12-105 8.06e-38

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 137.55  E-value: 8.06e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   12 LCFLSTLLSQKVPEKSDAVLRCMISGQPKPEVTWYKNGRAIDECGIVSSYEFFQNQYIHLLHLYRCTPDDTAVYQISAKN 91
Cdd:cd20951      1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80

                           90
                   ....*....|....
gi 2020764001   92 CSGMICCSASIEVK 105
Cdd:cd20951     81 IHGEASSSASVVVE 94
I-set pfam07679
Immunoglobulin I-set domain;
14-104 5.23e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.82  E-value: 5.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   14 FLSTLLSQKVPEKSDAVLRCMISGQPKPEVTWYKNGRAIDECgivSSYEFFQNQYIHLLHLYRCTPDDTAVYQISAKNCS 93
Cdd:pfam07679    3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSS---DRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79

                           90
                   ....*....|.
gi 2020764001   94 GMICCSASIEV 104
Cdd:pfam07679   80 GEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 20-104 1.42e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 53.66  E-value: 1.42e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001    20 SQKVPEKSDAVLRCMISGQPKPEVTWYKNGraIDECGIVSSYEFFQNQYIHLLHLYRCTPDDTAVYQISAKNCSGMICCS 99
Cdd:smart00410    3 SVTVKEGESVTLSCEASGSPPPEVTWYKQG--GKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*
gi 2020764001   100 ASIEV 104
Cdd:smart00410   81 TTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 1736-1808 4.99e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.34  E-value: 4.99e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020764001  1736 GNVKLSCQFAEiHEDSTVWWTKDSKSVAQVQRRA---DDTSAVSLAVVQAGQKDQGIYRCCIKNSYGKATAEFNLT 1808
Cdd:smart00410   10 ESVTLSCEASG-SPPPEVTWYKQGGKLLAESGRFsvsRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
I-set pfam07679
Immunoglobulin I-set domain;
1738-1808 1.01e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 43.01  E-value: 1.01e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020764001 1738 VKLSCQFAEiHEDSTVWWTKDSKSVAQVQR---RADDTSAvSLAVVQAGQKDQGIYRCCIKNSYGKATAEFNLT 1808
Cdd:pfam07679   18 ARFTCTVTG-TPDPEVSWFKDGQPLRSSDRfkvTYEGGTY-TLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 1752-1807 2.36e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 38.72  E-value: 2.36e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2020764001 1752 TVWWTKDSKSVAQVQRRADDTSAV--SLAVVQAGQKDQGIYRCCIKNSYGKATAEFNL 1807
Cdd:cd05748     23 TVTWSKDGQPLKETGRVQIETTASstSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80
 
Name Accession Description Interval E-value
Alpha_kinase_ALPK2 cd16974
Alpha-kinase domain of alpha-protein kinase 2; Alpha-protein kinase 2 (ALPK2) is also called ...
 1822-2059 3.10e-166

Alpha-kinase domain of alpha-protein kinase 2; Alpha-protein kinase 2 (ALPK2) is also called heart alpha-protein kinase (HAK). Little functional information is known about ALPK2. In a three-dimensional colonic-crypt model, it has been identified as crucial for luminal apoptosis and expression of DNA repair-related genes, possibly in the transition of normal colonic crypt to adenoma. The ALPK2 gene may also be a novel candidate gene for inherited hypertension in Dahl rats. ALPK2 contains a C-terminal alpha-kinase domain and two immunoglobulin (Ig)-like domains. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341224  Cd Length: 239  Bit Score: 508.21  E-value: 3.10e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1822 KGCEEIEFSQLIFREDFLRDSYFGDHLRGQIATEELHFGEGVHRKAFRSKVMQGLMPVFQPGHACVLKVHNAVAYGTRNN 1901
Cdd:cd16974      2 KGGEEIEFSQLMFKEDFLSDSYFGGNLHGRIATEKLHFGEGMHRKAFRSKVMCGLLPVFLPGHACVLKVHNAIAYGTKNN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1902 DELIQRNYKLAAQECYVQNTARYYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGKE 1981
Cdd:cd16974     82 DELIQKNYKLAVQECYVQNTAREYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPANNIPYATVEEELIGDFVKYSVRDGKE 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020764001 1982 INFLRRESEAGQKCCTFQHWVYQRTSGCLLVTDMQGVGMKLTDVGIATLAKGYKGFKGNCSMTFIDQFKALHQCNKYC 2059
Cdd:cd16974    162 INVLRRDSEAGQKCCTFQHWVYQKTDGNLLVTDMQGVGMKLTDVGIATCSKGYKGFKGNCSVSFIDQFKALHQCNKYC 239
Alpha_kinase_ALPK2_3 cd16966
Alpha-kinase domain of alpha-protein kinases 2 and 3; Alpha-protein kinases 2 (ALPK2) and 3 ...
 1822-2059 2.84e-151

Alpha-kinase domain of alpha-protein kinases 2 and 3; Alpha-protein kinases 2 (ALPK2) and 3 (ALPK3) are also called heart alpha-protein kinase (HAK) and muscle alpha-protein kinase (MAK), respectively. They both contain a C-terminal alpha-kinase domain and two immunoglobulin (Ig)-like domains. Loss of function mutations in ALPK3 can cause early-onset and familial cardiomyopathy in humans. The ALPK2 gene may also be a novel candidate gene for inherited hypertension in Dahl rats. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341216  Cd Length: 239  Bit Score: 466.67  E-value: 2.84e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1822 KGCEEIEFSQLIFREDFLRDSYFGDHLRGQIATEELHFGEGVHRKAFRSKVMQGLMPVFQPGHACVLKVHNAVAYGTRNN 1901
Cdd:cd16966      2 EVGEEIEMSPLIFAKDLLDSGYWGDKLFGRIATEELHFGEGVLRKASRSKVIYGLMPIFKSGHTCIIKVHNAIAYGTRNE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1902 DELIQRNYKLAAQECYVQNTARYYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGKE 1981
Cdd:cd16966     82 DSLIQRNYKLTAQECKVQNTAREYAKIFAAEARPLEGFGEVPEIIPLFLIYRPANNIPYATVEEELIGPFVKYSIRDGKE 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020764001 1982 INFLRRESEAGQKCCTFQHWVYQRTSGCLLVTDMQGVGMKLTDVGIATLAKGYKGFKGNCSMTFIDQFKALHQCNKYC 2059
Cdd:cd16966    162 INFLRSESEAGQKCCTFQHWVYQWTNGCLLVTDLQGVGMKLTDVGIATLAKGYQGLKGNCSMTFIDQFAALHQCNKYC 239
Alpha_kinase_ALPK3 cd16973
Alpha-kinase domain of alpha-protein kinase 3; Alpha-protein kinase 3 (ALPK3) is also called ...
 1825-2059 1.35e-94

Alpha-kinase domain of alpha-protein kinase 3; Alpha-protein kinase 3 (ALPK3) is also called muscle alpha-protein kinase (MAK) or myocytic induction/differentiation originator (Midori). Its expression is restricted to fetal and adult heart and adult skeletal muscle, and is localized in the nucleus. It is thought to act as a transcriptional regulator implicated in early cardiac development. Loss of function mutations in ALPK3 can cause early-onset and familial cardiomyopathy in humans. ALPK3 contains a C-terminal alpha-kinase domain and two immunoglobulin (Ig)-like domains. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341223  Cd Length: 239  Bit Score: 305.92  E-value: 1.35e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1825 EEIEFSQLIFREDFLRDSYFGDHLRGQIATEELHFGEGVHRKAFRSKVMQGLMPVFQPGHACVLKVHNAVAYGTRNNDEL 1904
Cdd:cd16973      5 EEIEMTPMVFAKGLADSGYWGDKFFGRVMTEEAHIGEGCLRKACRAKVIYGLEPVFESGSTCIIKVRNPIAYGTKNESSL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1905 IQRNYKLAAQECYVQNTARYYAKIYAAEAQPLEGFGEVPEIIPIFLIHRPENNIPYATVEEELIGEFVKYSIRDGKEINF 1984
Cdd:cd16973     85 AERNYEITIQECKIQNMAREYCKIFAAEARAVPNFGAVLEIIPLYLIYRPANNIPYATVEEDLKGVFQKYCVLDRTGSLV 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020764001 1985 LRRESEAGQKCCTFQHWVYQRTSGCLLVTDMQGVGMKLTDVGIATLAKGYKGFKGNCSMTFIDQFKALHQCNKYC 2059
Cdd:cd16973    165 ARTKSEVEQKCCTFQHWIYQWTNGNMLVTDLEGVDWKITNVGIATKSKGYQGLKESCSPKVFEQFISHHQCNYYC 239
Alpha_kinase smart00811
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
 1839-2059 1.64e-60

Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional kinases. The family contains myosin heavy chain kinases and Elongation Factor-2 kinase and a bifunctional ion channel. This family is known as the alpha-kinase family. The structure of the kinase domain revealed unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains.


Pssm-ID: 214828  Cd Length: 198  Bit Score: 206.44  E-value: 1.64e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001  1839 LRDSYFGDHLRGQIatEELHFGEGVHRKAFRSKVMQGlmpvFQPGHACVLKVHNavaygTRNNDELIQRNYKlaaqECYV 1918
Cdd:smart00811    1 SSGKWTVSETGVKI--ELKPFAKGAMRVAFRVKDLSE----DGSGTECVAKYFK-----KEYKNTVEDRYFE----DVEM 65

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001  1919 QNTARYYAKIYAAeaqpLEGFGEVPEIIPIFLIHRPENNIPY-ATVEEELIGEFVKYSIRDGKEINFLRRESeagqKCCT 1997
Cdd:smart00811   66 QMVAKKFAEEFNQ----LKPSPKKIEFLPSYVLELPDRSIPYlFTVEPFLEGEFVKYNSNNGWVNDEARSTE----APQA 137

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020764001  1998 FQHWVYQRTSGCLLVTDMQGVGMKLTDVGIATlAKGYKGFKGNCSMTFIDQFKALHQCNKYC 2059
Cdd:smart00811  138 FSHFTYERSGGSLLVVDLQGVGDLLTDPQIHT-EDGFGFGPGNLGEEGIEKFFATHKCNSIC 198
Alpha_kinase pfam02816
Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic ...
 1860-2059 9.58e-52

Alpha-kinase family; This family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional kinases. The family contains myosin heavy chain kinases and Elongation Factor-2 kinase and a bifunctional ion channel. This family is known as the alpha-kinase family. The structure of the kinase domain revealed unexpected similarity to eukaryotic protein kinases in the catalytic core as well as to metabolic enzymes with ATP-grasp domains.


Pssm-ID: 460709  Cd Length: 185  Bit Score: 180.99  E-value: 9.58e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1860 GEGVHRKAFRSKVMqglmPVFQPGHACVLKVHNAVAYGTrnndeliqrNYKLAAQECYVQNTARYYAKIYAAEAQPLEGF 1939
Cdd:pfam02816    1 AEGAMRKAFKAKVD----PGDESGQNYVAKEFKKIVYGV---------ELEYYFEDAQSQALAKELAEEFNAEARALENF 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1940 GEVP-EIIPIFLI-HRPENNIPYATVEEELIGEFVKYSIRDGKEINflrRESEAGQKCCTFQHWVYQRTSGCLLVTDMQG 2017
Cdd:pfam02816   68 PPKKiEFIPPYVVeLDPANGKPYYLVEPFLEGNFVKYNSNTGFVSE---EDDELEQTMQAFSHFTYERSGGQLLVCDLQG 144

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2020764001 2018 VGMKLTDVGIATLAKGYKGFkGNCSMTFIDQFKALHQCNKYC 2059
Cdd:pfam02816  145 VGNLLTDPAIHTKDGKRFGD-TNLGEEGIASFFSTHKCNKIC 185
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 12-105 8.06e-38

Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin domain I1 of the titin I-band and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig I1 domain of the titin I-band is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409543 [Multi-domain]  Cd Length: 94  Bit Score: 137.55  E-value: 8.06e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   12 LCFLSTLLSQKVPEKSDAVLRCMISGQPKPEVTWYKNGRAIDECGIVSSYEFFQNQYIHLLHLYRCTPDDTAVYQISAKN 91
Cdd:cd20951      1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKNGVPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVYSAVAKN 80

                           90
                   ....*....|....
gi 2020764001   92 CSGMICCSASIEVK 105
Cdd:cd20951     81 IHGEASSSASVVVE 94
Alpha_kinase cd04515
Alpha kinase family; The alpha kinase family is a novel family of eukaryotic protein kinase ...
 1859-2059 2.26e-32

Alpha kinase family; The alpha kinase family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional serine/threonine protein kinases. The family contains myosin heavy chain kinases, elongation factor-2 kinases, and bifunctional ion channel kinases. These kinases are implicated in a large variety of cellular processes such as protein translation, Mg2+/Ca2+ homeostasis, intracellular transport, cell migration, adhesion, and proliferation. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341214  Cd Length: 213  Bit Score: 126.36  E-value: 2.26e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1859 FGEGVHRKAFRSKVmqglmpVFQPGHACVLKVhnavaygtRNNDELIQRNYKLAAQECYVQNTARYYAKIYAAEAQPLEG 1938
Cdd:cd04515     30 FAQGAMREAFKAKD------LDSKGKKYVAKR--------FKRIGDPEENLEDLFDELRMQALAQYLAKEFNARAKSKNL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1939 FGEVPEIIPIFLIHRPENNIP---YATVEEELIGEFVKYSIRDGKEINflrreSEAGQKCCTFQHWVYQRTSGCLLVTDM 2015
Cdd:cd04515     96 IAPKINFVDPFVVKLGDRDDPgkvVFLVEPFLEGKFVKYNNNNGMVND-----EDLGETAQAFSHFTYERSGGQLLVTDL 170

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2020764001 2016 QGVGMKLTDVGIATLAKGYKGfKGNCSMTFIDQFKALHQCNKYC 2059
Cdd:cd04515    171 QGVGLVLTDPQIHTVDGGGFG-LGNLGEEGIKRFFKTHKCNEIC 213
Alpha_kinase_ChaK1_TRMP7 cd16971
Alpha-kinase domain of channel kinase 1, also called transient receptor potential cation ...
 1943-2060 3.47e-13

Alpha-kinase domain of channel kinase 1, also called transient receptor potential cation channel subfamily M member 7; Channel kinase 1 (ChaK1), also called transient receptor potential cation channel subfamily M member 7 (TRMP7) or long transient receptor potential channel 7 (LTrpC7), is a fusion protein containing a transmembrane ion pore or channel and a C-terminal alpha-kinase domain, both of which are functional. It is ubiquitously expressed and is a cation-selective channel that preferentially permeates Zn2+, Mg2+, and Ca2+ ions. It is a central regulator of Mg2+ and Ca2+ homeostasis. TRPM7 plays a role in cancer proliferation, stroke, hydrogen peroxide dependent neurodegeneration, and heavy metal toxicity. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341221  Cd Length: 239  Bit Score: 71.57  E-value: 3.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1943 PEIIPIFLIHRPENNIPYAtVEEELIGEFVKYSIRDGKEI---NFLRRESEAgqkcctFQHWVYQRTSGCLLVTDMQGVG 2019
Cdd:cd16971    121 PRFLEVFLLYCHSAGQWFA-VEECMTGEFRKYNNNNGDEIiptNMLEETMLA------FSHWTYEYTRGELLVLDLQGVG 193

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2020764001 2020 MKLTDVGIATlakgyKGFKGNCSMTF---------IDQFKALHQCNKYCK 2060
Cdd:cd16971    194 ENLTDPSVIK-----AGEKRSYDMVFgpanlgedaIKNFRAKHHCNSCCR 238
Alpha_kinase_ChaK cd16965
Alpha-kinase domain of channel kinases; This group is composed of channel kinases 1 (ChaK1) ...
 1943-2060 6.62e-13

Alpha-kinase domain of channel kinases; This group is composed of channel kinases 1 (ChaK1) and 2 (ChaK2), and similar proteins. ChaK1 and ChaK2 are also called transient receptor potential cation channel subfamily M members 7 (TRMP7) and 6 (TRMP6), respectively. They are fusion proteins containing a transmembrane ion pore or channel and a C-terminal alpha-kinase domain, both of which are functional. They are both cation-selective channels that preferentially permeate Zn2+, Mg2+, and Ca2+ ions. They are central regulators of Mg2+ and Ca2+ homeostasis. TRMP7 is ubiquitously expressed while TRMP6 is highly expressed in specific tissues such as the kidney and intestine. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341215  Cd Length: 239  Bit Score: 70.75  E-value: 6.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1943 PEIIPIFLIHRPENNiPYATVEEELIGEFVKYSIRDGKEI---NFLRRESEAgqkcctFQHWVYQRTSGCLLVTDMQGVG 2019
Cdd:cd16965    121 PRFLEVFLLYCHSAG-QWLTVENNMTGEFRKYNNNNGDEIlptNTLEETMLA------FSHWTYEYTRGELLVLDLQGVG 193

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2020764001 2020 MKLTDVGIATLAKgykgfKGNCSMTF---------IDQFKALHQCNKYCK 2060
Cdd:cd16965    194 ENLTDPSVIKVED-----KSSGEMVFgpanlgedaIQNFVAKHHCNSCCR 238
I-set pfam07679
Immunoglobulin I-set domain;
14-104 5.23e-12

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 63.82  E-value: 5.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   14 FLSTLLSQKVPEKSDAVLRCMISGQPKPEVTWYKNGRAIDECgivSSYEFFQNQYIHLLHLYRCTPDDTAVYQISAKNCS 93
Cdd:pfam07679    3 FTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSS---DRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79

                           90
                   ....*....|.
gi 2020764001   94 GMICCSASIEV 104
Cdd:pfam07679   80 GEAEASAELTV 90
Alpha_kinase_MHCK_like cd16968
Alpha-kinase domain of myosin heavy chain kinase and similar domains; This group is composed ...
 1855-2059 5.30e-12

Alpha-kinase domain of myosin heavy chain kinase and similar domains; This group is composed of alpha-kinase domains of Dictyostelium discoideum myosin heavy chain kinases A-D (MHCKA, MHCKB, MHCKC, MHCKD), alpha-protein kinase 1 (AK1), and similar proteins. The myosin heavy chain kinases are involved in regulating myosin II filament assembly in Dictyostelium discoideum. They phosphorylate target threonine residues located in the carboxyl-terminal portion of the myosin II heavy chain (MHC) tail, resulting in filament disassembly. The different MHCK isoforms display different spatial regulation, indicating specific roles for each isoform in fine tuning the Dictyostelium actomyosin cytoskeleton. They all contain an alpha-kinase domain as well as WD40 repeats at the C-terminus. AK1 contains an N-terminal Arf-GAP domain and a central alpha-kinase domain. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341218  Cd Length: 202  Bit Score: 66.87  E-value: 5.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1855 EELHFGEGVHRKAFRSKVMQGLmpvfQPGHACVLKVhnavAYGTRNNDELIQRNYKLaaqecyvQNTARYYAKIYAAEAQ 1934
Cdd:cd16968     24 DPKPFAEGALREAYHLKDLSAP----GPSTLFVAKL----SKDPNESRETYFEDVEM-------QMVCKKWAEKFNAKNP 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1935 PLEgfgevPEIIPIF---LIHRPenNIPYATVEEELIGEFVKYSIRDGKEINFLRRESEAgqkcctFQHWVYQRTSGCLL 2011
Cdd:cd16968     89 PKK-----VEFLPAWvleLVDRP--PPPLCGVEPFIEGEYVKHNNNFGYVDEDERNTPQA------FSHFTYEASGHQLL 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2020764001 2012 VTDMQGVGMKLTDVGIATLAKgyKGF-KGNCSMTFIDQFKALHQCNKYC 2059
Cdd:cd16968    156 VVDIQGVGDLYTDPQIHTIDG--KGFgKGNLGQKGIEKFLETHKCNAIC 202
Alpha_kinase_ChaK2_TRPM6 cd16972
Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation ...
 1943-2060 5.54e-12

Alpha-kinase domain of channel kinase 2, also called transient receptor potential cation channel subfamily M member 6; Channel kinase 2 (ChaK2), also called transient receptor potential cation channel subfamily M member 6 (TRMP6) or melastatin-related TRP cation channel 6, is a fusion protein containing a transmembrane ion pore or channel and a C-terminal alpha-kinase domain, both of which are functional. It is highly expressed in the kidney and instestine. It is a cation-selective channel that preferentially permeates Zn2+, Mg2+, and Ca2+ ions. It is a central regulator of Mg2+ and Ca2+ homeostasis. TRPM6 is considered to be the Mg2+ entry pathway in the distal convoluted tubule of the kidney, where it functions as a gatekeeper for controlling the body's Mg2+ balance. Mutations in the TRPM6 gene cause the autosomal recessive disorder hypomagnesemia with secondary hypocalcemia, which often results in severe muscular and neurologic complications from early infancy that can lead to neurologic damage or cardiac arrest if left untreated. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341222  Cd Length: 239  Bit Score: 67.72  E-value: 5.54e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1943 PEIIPIFLIHRPENNiPYATVEEELIGEFVKYSIRDGKEINFLRRESEAgqkCCTFQHWVYQRTSGCLLVTDMQGVGMKL 2022
Cdd:cd16972    121 PRFLEVFLIYCHSAN-QWLTIEKYLTGEFRKYNNNNGDEITPTSLLEET---LLAFSHWTYEYTRGELLVLDLQGVGENL 196

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2020764001 2023 TDVG-IATLAKGYKGF---KGNCSMTFIDQFKALHQCNKYCK 2060
Cdd:cd16972    197 TDPSvIKPEDKQSRGMvfgPANLGEDAIRNFIAKHHCNSCCR 238
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 20-91 7.43e-10

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 57.19  E-value: 7.43e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020764001   20 SQKVPEKSDAVLRCMISGQPKPEVTWYKNGRAIDEcgiVSSYEFFQNQYIHLLHLYRCTPDDTAVYQISAKN 91
Cdd:pfam13927   10 SVTVREGETVTLTCEATGSPPPTITWYKNGEPISS---GSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Alpha_kinase cd17508
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
 1835-2059 1.22e-09

Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional serine/threonine protein kinases. The family contains myosin heavy chain kinases, elongation factor-2 kinases, and bifunctional ion channel kinases. These kinases are implicated in a large variety of cellular processes such as protein translation, Mg2+/Ca2+ homeostasis, intracellular transport, cell migration, adhesion, and proliferation. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341225  Cd Length: 243  Bit Score: 60.86  E-value: 1.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1835 REDFLRDSYFGDHLRGqIATEELHFGEGVHRKAFRSKVMQglmpvfqpghaCVLKVHNAVAYGTRnndeLIQRNYKLAAQ 1914
Cdd:cd17508      3 LERARIYKFLPPGAFG-IAVRKLPFGEGAERNVFRCTEIS-----------KEGGTKTATKIGPR----LVAKESRHAED 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1915 E----------CYVQNTARYYAKIYAAEAQPLEGfGEVPEI--IPIFLIHRPENNIPYAT---VEEELIGEFVKY----- 1974
Cdd:cd17508     67 EsfdikfhkkfCKTQSTAQELAERFNKRLRALPG-GPAPRVkfLPCHVYKTKDVSYRGRAwvlVEKELEGKFTKWntnag 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1975 ----SIRDGKEINFLRRESEAGQKCCT--FQHWVYQRTSGCLLVTDMQGV------GMKLTDVGIAT-LAKGY------K 2035
Cdd:cd17508    146 gvkkSIESVGEGRGESNSSRLRVDDVPqaFSHFTYEHSGGRFLVCDLQGVwnatpdGFLLTDPVIHHvSGKRHrfgatdK 225

                          250       260
                   ....*....|....*....|....
gi 2020764001 2036 GFKGncsmtfIDQFKALHQCNKYC 2059
Cdd:cd17508    226 GLEG------IRNFLRTHKCSPLC 243
Alpha_kinase_eEF2K cd16967
Alpha-kinase domain of eukaryotic elongation factor-2 kinase; Eukaryotic elongation factor-2 ...
 1859-2059 2.10e-09

Alpha-kinase domain of eukaryotic elongation factor-2 kinase; Eukaryotic elongation factor-2 kinase (eEF2K) is also called calcium/calmodulin (CaM)-dependent eEF2K. It phosphorylates eukaryotic elongation factor-2 (EEF2) at a single site, leading to its inactivation and inability to bind ribosomes, and slowing down the elongation stage of protein synthesis. It has been linked to many human diseases including cardiovascular conditions (atherosclerosis) and pulmonary arterial hypertension, as well as solid tumors and neurological disorders. eEF2K is an atypical protein kinase containing a CaM binding region, an alpha-kinase catalytic domain, and TPR-like Sel1 repeats at the C-terminus. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341217  Cd Length: 216  Bit Score: 59.65  E-value: 2.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1859 FGEGVHRKAFRSKVMQGLMPVFQPGHACvlkvhNAVAygTRNNDELIQRNYklaAQECYVQNTARYYAKIYAAEaqpleg 1938
Cdd:cd16967     36 FARGAMRECYRAKKLSNFSHNQDWKHAS-----NYVA--KRYIEPVDREVY---FEDVRLQMDAKLWGEEYNRH------ 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1939 fgEVPEIIPIF------LIHRPENniPYATVEEELIGEFVKYSIRDGkeinFLRRESE--AGQkccTFQHWVYQRTSGCL 2010
Cdd:cd16967    100 --NPPKKVDIMqmcvleFVDRPGS--PLYHLEHFIEGDYIKYNSNSG----FVRDDDIrlTPQ---AFSHFTFERSGHQL 168

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2020764001 2011 LVTDMQGVGMKLTDVGIATL-AKGYKgfKGNCSMTFIDQFKALHQCNKYC 2059
Cdd:cd16967    169 IVVDIQGVGDLYTDPQIHTAdGEGYG--DGNLGLRGMALFFHSHRCNPIC 216
Alpha_kinase_VwkA_like cd16970
Alpha-kinase domain of Dictyostelium discoideum VwkA and similar domains; Dictyostelium ...
 1960-2059 2.47e-09

Alpha-kinase domain of Dictyostelium discoideum VwkA and similar domains; Dictyostelium discoideum alpha-protein kinase VwkA is also called von Willebrand factor A alpha-kinase or vWF kinase. It influences myosin II abundance and assembly behavior as vWKA gene disruption leads to significant myosin II overassembly. VwkA also serves a critical conserved role in the periodic contractions of the contractile vacuole through its regulation of the myosin II cortical cytoskeleton. It contains a vWFa domain (named after its homology to von Willebrand factor A, a plasma glycoprotein essential for proper blood clotting) and a C-terminal alpha-kinase domain. Alpha-kinase is an atypical protein kinase catalytic domain with no detectable similarity to conventional protein serine/threonine kinases. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341220  Cd Length: 227  Bit Score: 59.66  E-value: 2.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001 1960 YATVEEELIGEFVKYSIRDGkeiNFLRRESEAGQkccTFQHWVYQRTSGCLLVTDMQGV-----GMKLTDVGI------- 2027
Cdd:cd16970    130 YYTMESFLEGEYKKFNNNVG---VVNEDEVEILQ---AFSHWTYEASKGYLMVVDLQGVrtdddGFLLTDPAIhctdvlr 203

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2020764001 2028 -ATLAKGYKGfkgncsmtfIDQFKALHQCNKYC 2059
Cdd:cd16970    204 fGRTNLGKEG---------IDKFFATHKCNQHC 227
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 20-104 1.42e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 53.66  E-value: 1.42e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001    20 SQKVPEKSDAVLRCMISGQPKPEVTWYKNGraIDECGIVSSYEFFQNQYIHLLHLYRCTPDDTAVYQISAKNCSGMICCS 99
Cdd:smart00410    3 SVTVKEGESVTLSCEASGSPPPEVTWYKQG--GKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80


                    ....*
gi 2020764001   100 ASIEV 104
Cdd:smart00410   81 TTLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 29-91 1.44e-08

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 53.10  E-value: 1.44e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020764001   29 AVLRCMISGQPKPEVTWYKNGRAIDECGIVSSYEFFQNqyiHLLHLYRCTPDDTAVYQISAKN 91
Cdd:cd00096      1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGN---GTLTISNVTLEDSGTYTCVASN 60
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 14-104 1.80e-08

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 53.79  E-value: 1.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   14 FLSTLLSQKVPEKSDAVLRCMISGQPKPEVTWYKNGRAIDECGIVSSYEffqnQYIHLLHLYRCTPDDTAVYQISAKNCS 93
Cdd:cd20976      4 FSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPLQYAADRSTCE----AGVGELHIQDVLPEDHGTYTCLAKNAA 79

                           90
                   ....*....|.
gi 2020764001   94 GMICCSASIEV 104
Cdd:cd20976     80 GQVSCSAWVTV 90
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 14-104 2.38e-08

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 53.27  E-value: 2.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   14 FLSTLLSQKVPEKSDAVLRCMISGQPKPEVTWYKNGRAIDECGIVSSYEffQNQYIHLLHLYRCTPDDTAVYQISAKNCS 93
Cdd:cd05744      3 FLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLV--RENGRHSLIIEPVTKRDAGIYTCIARNRA 80

                           90
                   ....*....|.
gi 2020764001   94 GMICCSASIEV 104
Cdd:cd05744     81 GENSFNAELVV 91
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
 17-104 2.30e-07

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 50.27  E-value: 2.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   17 TLLSQKVPEKSDAVLRCMISGQPKPEVTWYKNGRAIDECgivSSYEFFQNQ-YIHLLHLYRCTPDDTAVYQISAKNCSGM 95
Cdd:cd20973      3 TLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVES---RRFQIDQDEdGLCSLIISDVCGDDSGKYTCKAVNSLGE 79


                   ....*....
gi 2020764001   96 ICCSASIEV 104
Cdd:cd20973     80 ATCSAELTV 88
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 14-104 4.11e-07

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 49.89  E-value: 4.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   14 FLSTLLSQKVPEKSDAVLRCMISGQPKPEVTWYKNGRAIDECgivSSYEFFQNQYIHLLHLYRCTPDDTAVYQISAKNCS 93
Cdd:cd20972      4 FIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNS---PDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSV 80

                           90
                   ....*....|.
gi 2020764001   94 GMICCSASIEV 104
Cdd:cd20972     81 GSDTTSAEIFV 91
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 13-104 4.55e-07

C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating the actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin, and actin. Mutations in myotilin lead to muscle disorders. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409473  Cd Length: 92  Bit Score: 49.77  E-value: 4.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   13 CFLSTLLSQKVPEKSDAVLRCMISGQPKPEVTWYKNGRAI-----------DECGivssyeffqnqYIHLLhLYRCTPDD 81
Cdd:cd05892      2 MFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMLqyntdrislyqDNCG-----------RICLL-IQNANKKD 69

                           90       100
                   ....*....|....*....|...
gi 2020764001   82 TAVYQISAKNCSGMICCSASIEV 104
Cdd:cd05892     70 AGWYTVSAVNEAGVVSCNARLDV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 1736-1808 4.99e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.34  E-value: 4.99e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020764001  1736 GNVKLSCQFAEiHEDSTVWWTKDSKSVAQVQRRA---DDTSAVSLAVVQAGQKDQGIYRCCIKNSYGKATAEFNLT 1808
Cdd:smart00410   10 ESVTLSCEASG-SPPPEVTWYKQGGKLLAESGRFsvsRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 14-104 5.89e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 46.23  E-value: 5.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   14 FLSTLLSQKVPEK-SDAVLRCMISGQPKPEVTWYKNGRAIDECGIVSSYEFFQNQYIHLLhlyrctPDDTAVYQISAKNC 92
Cdd:cd20978      3 FIQKPEKNVVVKGgQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVEDGTLTIINVQ------PEDTGYYGCVATNE 76

                           90
                   ....*....|..
gi 2020764001   93 SGMICCSASIEV 104
Cdd:cd20978     77 IGDIYTETLLHV 88
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members ...
 29-104 6.80e-06

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); The members here are composed of the fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 409453 [Multi-domain]  Cd Length: 89  Bit Score: 46.43  E-value: 6.80e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020764001   29 AVLRCMISGQPKPEVTWYKNGRAIDECGIVSSYEFFQNQYIhllhLYRCTPDDTAVYQISAKNCSGMICCSASIEV 104
Cdd:cd05867     17 ARLDCQVEGIPTPNITWSINGAPIEGTDPDPRRHVSSGALI----LTDVQPSDTAVYQCEARNRHGNLLANAHVHV 88
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 35-105 6.91e-06

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 46.04  E-value: 6.91e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020764001   35 ISGQPKPEVTWYKNGRAIDECG--IVSSYEFFQnqyihLLHLYRCTPDDTAVYQISAKNCSGMIccSASIEVK 105
Cdd:cd05748     16 IKGRPTPTVTWSKDGQPLKETGrvQIETTASST-----SLVIKNAKRSDSGKYTLTLKNSAGEK--SATINVK 81
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
 27-104 8.02e-06

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367 [Multi-domain]  Cd Length: 89  Bit Score: 45.90  E-value: 8.02e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020764001   27 SDAVLRCMISGQPKPEVTWYKNGRAIDECGIVSSYEFFQNQYIhllhLYRCTPDDTAVYQISAKNCSGMICCSASIEV 104
Cdd:cd04978     15 ETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVDGRTLI----FSNLQPNDTAVYQCNASNVHGYLLANAFLHV 88
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 21-104 2.25e-05

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 44.83  E-value: 2.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   21 QKVPEKSDAVLRCMISGQPKPEVTWYKNGRAIDECGIVssyeffQNQYIHLLHLYRCTPDDTAVYQISAKNCSGMICCSA 100
Cdd:cd20957     11 QTVDFGRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRV------QILSEDVLVIPSVKREDKGMYQCFVRNDGDSAQATA 84


                   ....
gi 2020764001  101 SIEV 104
Cdd:cd20957     85 ELKL 88
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here ...
 26-102 5.89e-05

Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7; The members here are composed of the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines.


Pssm-ID: 409417  Cd Length: 95  Bit Score: 43.76  E-value: 5.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   26 KSDAVLRCMISGQPKPEVTWYKNGRAIDECG---IVSSYEffqnqyiHLLHLYRCTPDDTAVYQISAKNCSGMICCSASI 102
Cdd:cd05760     16 SSRVTLRCHIDGHPRPTYQWFRDGTPLSDGQgnySVSSKE-------RTLTLRSAGPDDSGLYYCCAHNAFGSVCSSQNF 88
IgI_Twitchin_like cd20949
C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, ...
 23-95 6.62e-05

C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin, and similar domains; member of the I-set IgSF domains; The members here are composed of the C-terminal immunoglobulin-like domain of the myosin-associated giant protein kinase Twitchin and similar proteins, including Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. In humans these proteins are called Titin. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The Ig-like domain of the Twitchin is a member of the I-set IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins (titin, telokin, and twitchin), the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D.


Pssm-ID: 409541 [Multi-domain]  Cd Length: 89  Bit Score: 43.47  E-value: 6.62e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020764001   23 VPEKSDAVLRCMISGQPKPEVTWYKNGRAIDEcGIVSSYEFFQNQYIHLLHlyRCTPDDTAVYQISAKNCSGM 95
Cdd:cd20949     11 VKEGQSATILCEVKGEPQPNVTWHFNGQPISA-SVADMSKYRILADGLLIN--KVTQDDTGEYTCRAYQVNSI 80
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 23-90 1.01e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 42.77  E-value: 1.01e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   23 VPEKSDAVLRCMISGQPKPEVTWYKNGRAIDecgivSSYEFFQNQyIHLLH--LYRCTPDDTAVYQISAK 90
Cdd:pfam13895   11 VTEGEPVTLTCSAPGNPPPSYTWYKDGSAIS-----SSPNFFTLS-VSAEDsgTYTCVARNGRGGKVSNP 74
I-set pfam07679
Immunoglobulin I-set domain;
1738-1808 1.01e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 43.01  E-value: 1.01e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020764001 1738 VKLSCQFAEiHEDSTVWWTKDSKSVAQVQR---RADDTSAvSLAVVQAGQKDQGIYRCCIKNSYGKATAEFNLT 1808
Cdd:pfam07679   18 ARFTCTVTG-TPDPEVSWFKDGQPLRSSDRfkvTYEGGTY-TLTISNVQPDDSGKYTCVATNSAGEAEASAELT 89
IgI_1_Palladin_C cd05893
First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig ...
 14-104 3.53e-04

First C-terminal immunoglobulin (Ig)-like domain of palladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (also known as DIP or mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409474  Cd Length: 92  Bit Score: 41.62  E-value: 3.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   14 FLSTLLSQKVPEKSDAVLRCMISGQPKPEVTWYKNGRAIDEcgiVSSYEFFQNQY--IHLLHLYRCTPDDTAVYQISAKN 91
Cdd:cd05893      3 FEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISP---KSDHYTIQRDLdgTCSLHTTASTLDDDGNYTIMAAN 79

                           90
                   ....*....|...
gi 2020764001   92 CSGMICCSASIEV 104
Cdd:cd05893     80 PQGRISCTGRLMV 92
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 25-102 4.03e-04

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 41.03  E-value: 4.03e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020764001   25 EKSDAVLRCMISGQPKPEVTWYKNGRAIdecgIVSSYefFQNQYIHLLHLYRCTPDDTAVYQISAKNCSGMICCSASI 102
Cdd:cd05723     11 ESMDIVFECEVTGKPTPTVKWVKNGDVV----IPSDY--FKIVKEHNLQVLGLVKSDEGFYQCIAENDVGNAQASAQL 82
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
 23-96 5.10e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 40.99  E-value: 5.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020764001   23 VPEKSDAVLRCMISGQPKPEVTWYKNGRAIDECGIVSSYEFFQNQYIhlLHLYRCTPDDTAVYQISAKNCSGMI 96
Cdd:cd05857     16 VPAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWS--LIMESVVPSDKGNYTCVVENEYGSI 87
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 23-110 7.34e-04

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 40.57  E-value: 7.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   23 VPEKSDAVLRCMISGQPKPEVTWYKNGRAIDEcgIVSSYEffqnqyihllhlYRCTPDDTAVYQISAKNcSGMICCSASI 102
Cdd:cd20970     14 AREGENATFMCRAEGSPEPEISWTRNGNLIIE--FNTRYI------------VRENGTTLTIRNIRRSD-MGIYLCIASN 78


                   ....*...
gi 2020764001  103 EVKCSAES 110
Cdd:cd20970     79 GVPGSVEK 86
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 14-104 1.57e-03

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 39.40  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   14 FLSTLLSQKVPEKSDAVLRCMISGQPKPEVTWYKNGRAIDECGivssyEFFQNQYIHLLHLYRCTPDDTAVYQISAKNCS 93
Cdd:cd20952      2 ILQGPQNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLGKD-----ERITTLENGSLQIKGAEKSDTGEYTCVALNLS 76

                           90
                   ....*....|.
gi 2020764001   94 GMICCSASIEV 104
Cdd:cd20952     77 GEATWSAVLDV 87
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
 31-94 1.58e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 39.50  E-value: 1.58e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020764001   31 LRCMISGQPKPEVTWYKNGRAI---DECgivsSYEFFQNQYIHLLhLYRCTPDDTAVYQISAKNCSG 94
Cdd:cd05737     21 LTCNVWGDPPPEVSWLKNDQALaflDHC----NLKVEAGRTVYFT-INGVSSEDSGKYGLVVKNKYG 82
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
 24-104 1.68e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 39.46  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   24 PEKSDAVLRCMISGQPKPEVTWYKNGRAID--ECGIVSSYEFfqnqyihLLHLYRCTPDDTAVYQISAKNCSGMICCSAS 101
Cdd:cd05856     17 PVGSSVRLKCVASGNPRPDITWLKDNKPLTppEIGENKKKKW-------TLSLKNLKPEDSGKYTCHVSNRAGEINATYK 89


                   ...
gi 2020764001  102 IEV 104
Cdd:cd05856     90 VDV 92
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 1752-1807 2.36e-03

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 38.72  E-value: 2.36e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2020764001 1752 TVWWTKDSKSVAQVQRRADDTSAV--SLAVVQAGQKDQGIYRCCIKNSYGKATAEFNL 1807
Cdd:cd05748     23 TVTWSKDGQPLKETGRVQIETTASstSLVIKNAKRSDSGKYTLTLKNSAGEKSATINV 80
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 23-104 3.19e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 38.74  E-value: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020764001   23 VPEKSDAVLRCMISGQPKPEVTWYKNGRAIDECGIVSSYEFFQNQYIhlLHLYRCTPDDTAVYQISAKNCSGMICCSASI 102
Cdd:cd05729     16 LPAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGTKVEEKGWS--LIIERAIPRDKGKYTCIVENEYGSINHTYDV 93


                   ..
gi 2020764001  103 EV 104
Cdd:cd05729     94 DV 95
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 20-95 5.06e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 38.40  E-value: 5.06e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020764001   20 SQKVPEKSDAVLRCMISGQPKPEVTWYKNGRAIDEcGIVSSYEFFQNQyiHLLHLYRCTPDDTAVYQISAKNCSGM 95
Cdd:cd05736      9 FQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINP-KLSKQLTLIANG--SELHISNVRYEDTGAYTCIAKNEGGV 81
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 1738-1803 5.25e-03

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 37.69  E-value: 5.25e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020764001 1738 VKLSCQFAEiHEDSTVWWTKDSKSV--AQVQRRADDTSAVSLAVVQAGQKDQGIYRCCIKNSYGKATA 1803
Cdd:cd00096      1 VTLTCSASG-NPPPTITWYKNGKPLppSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSAS 67
Alpha_kinase cd17509
Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of ...
 1998-2059 5.44e-03

Alpha kinase family; uncharacterized subgroup; The alpha kinase family is a novel family of eukaryotic protein kinase catalytic domains, which have no detectable similarity to conventional serine/threonine protein kinases. The family contains myosin heavy chain kinases, elongation factor-2 kinases, and bifunctional ion channel kinases. These kinases are implicated in a large variety of cellular processes such as protein translation, Mg2+/Ca2+ homeostasis, intracellular transport, cell migration, adhesion, and proliferation. The alpha-kinase family was named after the unique mode of substrate recognition by its initial members, the Dictyostelium heavy chain kinases, which targeted protein sequences that adopt an alpha-helical conformation. More recently, alpha-kinases were found to also target residues in non-helical regions.


Pssm-ID: 341226  Cd Length: 221  Bit Score: 40.41  E-value: 5.44e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020764001 1998 FQHWVYQRTSGCLLVTDMQGVGMK----LTDVGIATLAKGYKGfKGNCSMTFIDQFKALHQCNKYC 2059
Cdd:cd17509    157 LSHFSYHISGGKYLLCDLQGGVYKneyvLTDPVILSRTGREYG-VTDLGPEGIWNFFANHKCNKYC 221
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH