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Conserved domains on  [gi|767917659|ref|XP_011509293|]
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coiled-coil domain-containing protein 141 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 132-356 6.09e-08

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 54.76  E-value: 6.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659  132 EFFENALEFAIKIDQAEDFLQNTHEFESAESLKSLLQLHEHHTKELLERSlallNKSQQLTDFIEKfkcegpnvnpeLTQ 211
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHE----ERVEALNELGEQ-----------LIE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659  212 GAHSSCLKVDRLLELLQDRRRQLDKYLKQQWQELSQVLQICQWDQQENQVTCWFQKTIRNLQEQSLGSSLSDNEDRIHKQ 291
Cdd:cd00176    69 EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKH 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767917659  292 EELIIKAKEWNSAVEKLKSEALRILLSKDYVEKEHLQLSHQKLSQLQEEFGQLMVERNTWLKKAN 356
Cdd:cd00176   149 KELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 1409-1442 6.00e-07

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 pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 48.79  E-value: 6.00e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767917659  1409 PNFSRLLSNVTVMEGSPVTLEVEVTGFPEPTLTW 1442
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSW 34
235kDa-fam super family cl31124
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 904-1151 2.14e-05

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


The actual alignment was detected with superfamily member TIGR01612:

Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 49.66  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   904 DEINELKDSFKDIK------------KKFNNLKFNYTKKNEKSrnlkalkyQIQQVDMYAEKMQALKRKMEKVSNKTSDS 971
Cdd:TIGR01612  974 DKINELDKAFKDASlndyeaknneliKYFNDLKANLGKNKENM--------LYHQFDEKEKATNDIEQKIEDANKNIPNI 1045

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   972 FLNYPSDKVNVLLEVMKDLQKHVDDFDKVVTDyKKNLDLTeHFQEVIEEC-HFWYEDasatVVRVG--KYSTEC-KTKEA 1047
Cdd:TIGR01612 1046 EIAIHTSIYNIIDEIEKEIGKNIELLNKEILE-EAEINIT-NFNEIKEKLkHYNFDD----FGKEEniKYADEInKIKDD 1119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659  1048 VKILHQQFNKFIAP-------------SVPQQEERIQEATDLAQHLYGLEEGQKYIEKIVTK---HKEVLESVTELCESL 1111
Cdd:TIGR01612 1120 IKNLDQKIDHHIKAleeikkksenyidEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKidkKKNIYDEIKKLLNEI 1199

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 767917659  1112 TELE------EKLKqGDVLKMNPNLEDFHYDYIDllKEPAKNKQTI 1151
Cdd:TIGR01612 1200 AEIEkdktslEEVK-GINLSYGKNLGKLFLEKID--EEKKKSEHMI 1242
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 221-846 2.21e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   221 DRLLELLQDRRRQLDKY------------LKQQWQELSQVLQICQWDQQENQVTCWFQKTIRNLQE--------QSLGSS 280
Cdd:TIGR02168  189 DRLEDILNELERQLKSLerqaekaerykeLKAELRELELALLVLRLEELREELEELQEELKEAEEEleeltaelQELEEK 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   281 LSDNEDRIHKQEELIikakewNSAVEKLKseALRILLSKDYVEKEHLQlshQKLSQLQEEFGQLMVERNTWLKKANEFFN 360
Cdd:TIGR02168  269 LEELRLEVSELEEEI------EELQKELY--ALANEISRLEQQKQILR---ERLANLERQLEELEAQLEELESKLDELAE 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   361 SANKAFDVLGRVEAYLKLLKSEglsLAVLAVRHEELHRKIKDCTTDALQKGQTLIS---QVDSCSSQVSGIHEMMGCIKR 437
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAE---LEELEAELEELESRLEELEEQLETLRSKVAQlelQIASLNNEIERLEARLERLED 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   438 RVDHLTEQCSAHKEyALKKQQLTASVEGYLRKVEMSIQKISPVLSNAMDVGSTRSESEKILNKYLELDIQAKETSHELeA 517
Cdd:TIGR02168  415 RRERLQQEIEELLK-KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL-D 492

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   518 AAKTMMEKNEFVSDEMVSLSSKARWLAEELNLFGQSI----DYRSQV-------LQTYV-----------AFLKSSEEVE 575
Cdd:TIGR02168  493 SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdeGYEAAIeaalggrLQAVVvenlnaakkaiAFLKQNELGR 572

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   576 MQFQSLKEFYETEIPQKEQDDAKAKHC-----------SDSAEKQWQLFLKKSFITQDL--GLEFLNLIN---------- 632
Cdd:TIGR02168  573 VTFLPLDSIKGTEIQGNDREILKNIEGflgvakdlvkfDPKLRKALSYLLGGVLVVDDLdnALELAKKLRpgyrivtldg 652

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   633 --------------------MAKENEILDVKNEVYLMKNTMENQKAE-----------REELSLLRLAWQLKATESKPGK 681
Cdd:TIGR02168  653 dlvrpggvitggsaktnssiLERRREIEELEEKIEELEEKIAELEKAlaelrkeleelEEELEQLRKELEELSRQISALR 732

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   682 QQWAAFKEQLKKTSHNLKLLQEAL------MPVSALDLGGSLQFILDLRQKWNDMKPQFQQLNDEVQYIMKESEELTGRG 755
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELteleaeIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   756 APVKEKSQQLKDLIHFHQKQKERIQDYEDILYKvvQFHQVKEELGRLIKSRElEFVEQPKELGDAHDVQIHLRCSQEKQA 835
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEE--QIEELSEDIESLAAEIE-ELEELIEELESELEALLNERASLEEAL 889

                          730
                   ....*....|.
gi 767917659   836 rvdHLHRLALS 846
Cdd:TIGR02168  890 ---ALLRSELE 897
 
Name Accession Description Interval E-value
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 132-356 6.09e-08

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 54.76  E-value: 6.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659  132 EFFENALEFAIKIDQAEDFLQNTHEFESAESLKSLLQLHEHHTKELLERSlallNKSQQLTDFIEKfkcegpnvnpeLTQ 211
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHE----ERVEALNELGEQ-----------LIE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659  212 GAHSSCLKVDRLLELLQDRRRQLDKYLKQQWQELSQVLQICQWDQQENQVTCWFQKTIRNLQEQSLGSSLSDNEDRIHKQ 291
Cdd:cd00176    69 EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKH 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767917659  292 EELIIKAKEWNSAVEKLKSEALRILLSKDYVEKEHLQLSHQKLSQLQEEFGQLMVERNTWLKKAN 356
Cdd:cd00176   149 KELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
I-set pfam07679
Immunoglobulin I-set domain;
1409-1442 6.00e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 48.79  E-value: 6.00e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767917659  1409 PNFSRLLSNVTVMEGSPVTLEVEVTGFPEPTLTW 1442
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSW 34
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 904-1151 2.14e-05

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 49.66  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   904 DEINELKDSFKDIK------------KKFNNLKFNYTKKNEKSrnlkalkyQIQQVDMYAEKMQALKRKMEKVSNKTSDS 971
Cdd:TIGR01612  974 DKINELDKAFKDASlndyeaknneliKYFNDLKANLGKNKENM--------LYHQFDEKEKATNDIEQKIEDANKNIPNI 1045

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   972 FLNYPSDKVNVLLEVMKDLQKHVDDFDKVVTDyKKNLDLTeHFQEVIEEC-HFWYEDasatVVRVG--KYSTEC-KTKEA 1047
Cdd:TIGR01612 1046 EIAIHTSIYNIIDEIEKEIGKNIELLNKEILE-EAEINIT-NFNEIKEKLkHYNFDD----FGKEEniKYADEInKIKDD 1119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659  1048 VKILHQQFNKFIAP-------------SVPQQEERIQEATDLAQHLYGLEEGQKYIEKIVTK---HKEVLESVTELCESL 1111
Cdd:TIGR01612 1120 IKNLDQKIDHHIKAleeikkksenyidEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKidkKKNIYDEIKKLLNEI 1199

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 767917659  1112 TELE------EKLKqGDVLKMNPNLEDFHYDYIDllKEPAKNKQTI 1151
Cdd:TIGR01612 1200 AEIEkdktslEEVK-GINLSYGKNLGKLFLEKID--EEKKKSEHMI 1242
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 1409-1442 8.70e-05

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: 42.79  E-value: 8.70e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767917659 1409 PNFSRLLSNVTVMEGSPVTLEVEVTGFPEPTLTW 1442
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKW 34
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 221-846 2.21e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   221 DRLLELLQDRRRQLDKY------------LKQQWQELSQVLQICQWDQQENQVTCWFQKTIRNLQE--------QSLGSS 280
Cdd:TIGR02168  189 DRLEDILNELERQLKSLerqaekaerykeLKAELRELELALLVLRLEELREELEELQEELKEAEEEleeltaelQELEEK 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   281 LSDNEDRIHKQEELIikakewNSAVEKLKseALRILLSKDYVEKEHLQlshQKLSQLQEEFGQLMVERNTWLKKANEFFN 360
Cdd:TIGR02168  269 LEELRLEVSELEEEI------EELQKELY--ALANEISRLEQQKQILR---ERLANLERQLEELEAQLEELESKLDELAE 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   361 SANKAFDVLGRVEAYLKLLKSEglsLAVLAVRHEELHRKIKDCTTDALQKGQTLIS---QVDSCSSQVSGIHEMMGCIKR 437
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAE---LEELEAELEELESRLEELEEQLETLRSKVAQlelQIASLNNEIERLEARLERLED 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   438 RVDHLTEQCSAHKEyALKKQQLTASVEGYLRKVEMSIQKISPVLSNAMDVGSTRSESEKILNKYLELDIQAKETSHELeA 517
Cdd:TIGR02168  415 RRERLQQEIEELLK-KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL-D 492

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   518 AAKTMMEKNEFVSDEMVSLSSKARWLAEELNLFGQSI----DYRSQV-------LQTYV-----------AFLKSSEEVE 575
Cdd:TIGR02168  493 SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdeGYEAAIeaalggrLQAVVvenlnaakkaiAFLKQNELGR 572

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   576 MQFQSLKEFYETEIPQKEQDDAKAKHC-----------SDSAEKQWQLFLKKSFITQDL--GLEFLNLIN---------- 632
Cdd:TIGR02168  573 VTFLPLDSIKGTEIQGNDREILKNIEGflgvakdlvkfDPKLRKALSYLLGGVLVVDDLdnALELAKKLRpgyrivtldg 652

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   633 --------------------MAKENEILDVKNEVYLMKNTMENQKAE-----------REELSLLRLAWQLKATESKPGK 681
Cdd:TIGR02168  653 dlvrpggvitggsaktnssiLERRREIEELEEKIEELEEKIAELEKAlaelrkeleelEEELEQLRKELEELSRQISALR 732

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   682 QQWAAFKEQLKKTSHNLKLLQEAL------MPVSALDLGGSLQFILDLRQKWNDMKPQFQQLNDEVQYIMKESEELTGRG 755
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELteleaeIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   756 APVKEKSQQLKDLIHFHQKQKERIQDYEDILYKvvQFHQVKEELGRLIKSRElEFVEQPKELGDAHDVQIHLRCSQEKQA 835
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEE--QIEELSEDIESLAAEIE-ELEELIEELESELEALLNERASLEEAL 889

                          730
                   ....*....|.
gi 767917659   836 rvdHLHRLALS 846
Cdd:TIGR02168  890 ---ALLRSELE 897
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 120-429 9.26e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.96  E-value: 9.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   120 LERRTELLRLTSEFFENALEFAIKIDQAEDFLQNT-----HEFESAESLKSLLQLHEHHTKELLERSLALLNKSQQLTDF 194
Cdd:pfam05557   23 LEHKRARIELEKKASALKRQLDRESDRNQELQKRIrllekREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADA 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   195 IEKFKCEGPNVNpELTQGAHSSCLKVDRLLELLQDRRRQLDKYlKQQWQELSQVLQicqwdqqenqvtcwfqktirNLQE 274
Cdd:pfam05557  103 REVISCLKNELS-ELRRQIQRAELELQSTNSELEELQERLDLL-KAKASEAEQLRQ--------------------NLEK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   275 QSlgSSLSDNEDRIHKQEELIIKAKEWNSAVEKLKSEALRIllSKDYVEKEHLQLSHQKLSQLQEEFGQLMVERNTWLKK 354
Cdd:pfam05557  161 QQ--SSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARI--PELEKELERLREHNKHLNENIENKLLLKEEVEDLKRK 236

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767917659   355 ANEFFNSANKAFDV---LGRVEAYLKLLKSEGLSLAVLAVRHEELHRKIKDCttdaLQKGQTLISQVDSCSSQVSGIH 429
Cdd:pfam05557  237 LEREEKYREEAATLeleKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQL----QQREIVLKEENSSLTSSARQLE 310
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 1416-1442 1.36e-03

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: 39.41  E-value: 1.36e-03
                            10        20
                    ....*....|....*....|....*..
gi 767917659   1416 SNVTVMEGSPVTLEVEVTGFPEPTLTW 1442
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTW 28
 
Name Accession Description Interval E-value
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 132-356 6.09e-08

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 54.76  E-value: 6.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659  132 EFFENALEFAIKIDQAEDFLQNTHEFESAESLKSLLQLHEHHTKELLERSlallNKSQQLTDFIEKfkcegpnvnpeLTQ 211
Cdd:cd00176     4 QFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHE----ERVEALNELGEQ-----------LIE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659  212 GAHSSCLKVDRLLELLQDRRRQLDKYLKQQWQELSQVLQICQWDQQENQVTCWFQKTIRNLQEQSLGSSLSDNEDRIHKQ 291
Cdd:cd00176    69 EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKH 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767917659  292 EELIIKAKEWNSAVEKLKSEALRILLSKDYVEKEHLQLSHQKLSQLQEEFGQLMVERNTWLKKAN 356
Cdd:cd00176   149 KELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
I-set pfam07679
Immunoglobulin I-set domain;
1409-1442 6.00e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 48.79  E-value: 6.00e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767917659  1409 PNFSRLLSNVTVMEGSPVTLEVEVTGFPEPTLTW 1442
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSW 34
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 904-1151 2.14e-05

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 49.66  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   904 DEINELKDSFKDIK------------KKFNNLKFNYTKKNEKSrnlkalkyQIQQVDMYAEKMQALKRKMEKVSNKTSDS 971
Cdd:TIGR01612  974 DKINELDKAFKDASlndyeaknneliKYFNDLKANLGKNKENM--------LYHQFDEKEKATNDIEQKIEDANKNIPNI 1045

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   972 FLNYPSDKVNVLLEVMKDLQKHVDDFDKVVTDyKKNLDLTeHFQEVIEEC-HFWYEDasatVVRVG--KYSTEC-KTKEA 1047
Cdd:TIGR01612 1046 EIAIHTSIYNIIDEIEKEIGKNIELLNKEILE-EAEINIT-NFNEIKEKLkHYNFDD----FGKEEniKYADEInKIKDD 1119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659  1048 VKILHQQFNKFIAP-------------SVPQQEERIQEATDLAQHLYGLEEGQKYIEKIVTK---HKEVLESVTELCESL 1111
Cdd:TIGR01612 1120 IKNLDQKIDHHIKAleeikkksenyidEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTKidkKKNIYDEIKKLLNEI 1199

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 767917659  1112 TELE------EKLKqGDVLKMNPNLEDFHYDYIDllKEPAKNKQTI 1151
Cdd:TIGR01612 1200 AEIEkdktslEEVK-GINLSYGKNLGKLFLEKID--EEKKKSEHMI 1242
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 1409-1442 8.70e-05

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: 42.79  E-value: 8.70e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767917659 1409 PNFSRLLSNVTVMEGSPVTLEVEVTGFPEPTLTW 1442
Cdd:cd20951     1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKW 34
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 1416-1442 1.26e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.78  E-value: 1.26e-04
                           10        20
                   ....*....|....*....|....*..
gi 767917659  1416 SNVTVMEGSPVTLEVEVTGFPEPTLTW 1442
Cdd:pfam13927    9 SSVTVREGETVTLTCEATGSPPPTITW 35
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 221-846 2.21e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   221 DRLLELLQDRRRQLDKY------------LKQQWQELSQVLQICQWDQQENQVTCWFQKTIRNLQE--------QSLGSS 280
Cdd:TIGR02168  189 DRLEDILNELERQLKSLerqaekaerykeLKAELRELELALLVLRLEELREELEELQEELKEAEEEleeltaelQELEEK 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   281 LSDNEDRIHKQEELIikakewNSAVEKLKseALRILLSKDYVEKEHLQlshQKLSQLQEEFGQLMVERNTWLKKANEFFN 360
Cdd:TIGR02168  269 LEELRLEVSELEEEI------EELQKELY--ALANEISRLEQQKQILR---ERLANLERQLEELEAQLEELESKLDELAE 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   361 SANKAFDVLGRVEAYLKLLKSEglsLAVLAVRHEELHRKIKDCTTDALQKGQTLIS---QVDSCSSQVSGIHEMMGCIKR 437
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAE---LEELEAELEELESRLEELEEQLETLRSKVAQlelQIASLNNEIERLEARLERLED 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   438 RVDHLTEQCSAHKEyALKKQQLTASVEGYLRKVEMSIQKISPVLSNAMDVGSTRSESEKILNKYLELDIQAKETSHELeA 517
Cdd:TIGR02168  415 RRERLQQEIEELLK-KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL-D 492

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   518 AAKTMMEKNEFVSDEMVSLSSKARWLAEELNLFGQSI----DYRSQV-------LQTYV-----------AFLKSSEEVE 575
Cdd:TIGR02168  493 SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdeGYEAAIeaalggrLQAVVvenlnaakkaiAFLKQNELGR 572

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   576 MQFQSLKEFYETEIPQKEQDDAKAKHC-----------SDSAEKQWQLFLKKSFITQDL--GLEFLNLIN---------- 632
Cdd:TIGR02168  573 VTFLPLDSIKGTEIQGNDREILKNIEGflgvakdlvkfDPKLRKALSYLLGGVLVVDDLdnALELAKKLRpgyrivtldg 652

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   633 --------------------MAKENEILDVKNEVYLMKNTMENQKAE-----------REELSLLRLAWQLKATESKPGK 681
Cdd:TIGR02168  653 dlvrpggvitggsaktnssiLERRREIEELEEKIEELEEKIAELEKAlaelrkeleelEEELEQLRKELEELSRQISALR 732

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   682 QQWAAFKEQLKKTSHNLKLLQEAL------MPVSALDLGGSLQFILDLRQKWNDMKPQFQQLNDEVQYIMKESEELTGRG 755
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELteleaeIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   756 APVKEKSQQLKDLIHFHQKQKERIQDYEDILYKvvQFHQVKEELGRLIKSRElEFVEQPKELGDAHDVQIHLRCSQEKQA 835
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEE--QIEELSEDIESLAAEIE-ELEELIEELESELEALLNERASLEEAL 889

                          730
                   ....*....|.
gi 767917659   836 rvdHLHRLALS 846
Cdd:TIGR02168  890 ---ALLRSELE 897
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
 1409-1442 7.75e-04

First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the first 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: 409566 [Multi-domain]  Cd Length: 93  Bit Score: 40.03  E-value: 7.75e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767917659 1409 PNFSRLLSNVTVMEGSPVTLEVEVTGFPEPTLTW 1442
Cdd:cd20974     1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSW 34
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 120-429 9.26e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.96  E-value: 9.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   120 LERRTELLRLTSEFFENALEFAIKIDQAEDFLQNT-----HEFESAESLKSLLQLHEHHTKELLERSLALLNKSQQLTDF 194
Cdd:pfam05557   23 LEHKRARIELEKKASALKRQLDRESDRNQELQKRIrllekREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADA 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   195 IEKFKCEGPNVNpELTQGAHSSCLKVDRLLELLQDRRRQLDKYlKQQWQELSQVLQicqwdqqenqvtcwfqktirNLQE 274
Cdd:pfam05557  103 REVISCLKNELS-ELRRQIQRAELELQSTNSELEELQERLDLL-KAKASEAEQLRQ--------------------NLEK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   275 QSlgSSLSDNEDRIHKQEELIIKAKEWNSAVEKLKSEALRIllSKDYVEKEHLQLSHQKLSQLQEEFGQLMVERNTWLKK 354
Cdd:pfam05557  161 QQ--SSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARI--PELEKELERLREHNKHLNENIENKLLLKEEVEDLKRK 236

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767917659   355 ANEFFNSANKAFDV---LGRVEAYLKLLKSEGLSLAVLAVRHEELHRKIKDCttdaLQKGQTLISQVDSCSSQVSGIH 429
Cdd:pfam05557  237 LEREEKYREEAATLeleKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQL----QQREIVLKEENSSLTSSARQLE 310
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 1408-1442 1.19e-03

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: 39.49  E-value: 1.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767917659 1408 APNFSRLLSNVTVMEGSPVTLEVEVTGFPEPTLTW 1442
Cdd:cd20972     1 PPQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRW 35
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 1416-1442 1.36e-03

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: 39.41  E-value: 1.36e-03
                            10        20
                    ....*....|....*....|....*..
gi 767917659   1416 SNVTVMEGSPVTLEVEVTGFPEPTLTW 1442
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTW 28
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 1415-1442 1.64e-03

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: 39.03  E-value: 1.64e-03
                          10        20
                  ....*....|....*....|....*...
gi 767917659 1415 LSNVTVMEGSPVTLEVEVTGFPEPTLTW 1442
Cdd:cd20970     9 SFTVTAREGENATFMCRAEGSPEPEISW 36
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 259-451 2.15e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.28  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659  259 NQVTCWFQKTIRNLQEQSLGSSLSDNEDRIHKQEELIIKAKEWNSAVEKLKSEALRiLLSKDYVEKEHLQLSHQKLSQLQ 338
Cdd:cd00176    10 DELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQ-LIEEGHPDAEEIQERLEELNQRW 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659  339 EEFGQLMVERNTWLKKANEFFNSANKAFDVLGRVEAYLKLLKSEGL-----SLAVLAVRHEELHRKIKDCTTD---ALQK 410
Cdd:cd00176    89 EELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLgkdleSVEELLKKHKELEEELEAHEPRlksLNEL 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767917659  411 GQTLISQVDSCSSQVsgIHEMMGCIKRRVDHLTEQCSAHKE 451
Cdd:cd00176   169 AEELLEEGHPDADEE--IEEKLEELNERWEELLELAEERQK 207
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 1408-1442 2.60e-03

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: 38.77  E-value: 2.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767917659 1408 APNFSRLLSNVTVMEGSPVTLEVEVTGFPEPTLTW 1442
Cdd:cd20976     1 APSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITW 35
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 1409-1442 2.97e-03

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: 38.53  E-value: 2.97e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767917659 1409 PNF-SRLLSNVTVMEGSPVTLEVEVTGFPEPTLTW 1442
Cdd:cd20978     1 PKFiQKPEKNVVVKGGQDVTLPCQVTGVPQPKITW 35
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 52-238 3.71e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.51  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659   52 EIGSSQDETKKLLHDHELLLAKLKALEDRVWELLQEADKTAEENKDQSQVYDAMAETLGEAWAALVSMLERRTELLRLTS 131
Cdd:cd00176    27 DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEAL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917659  132 E---FFENALEFAIKIDQAEDFLQNTHEFESAESLKSLLQLHEHHTKELLERSlallNKSQQLTDFIEKFKCEG-PNVNP 207
Cdd:cd00176   107 DlqqFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE----PRLKSLNELAEELLEEGhPDADE 182

                         170       180       190
                  ....*....|....*....|....*....|.
gi 767917659  208 ELTQGAHSSCLKVDRLLELLQDRRRQLDKYL 238
Cdd:cd00176   183 EIEEKLEELNERWEELLELAEERQKKLEEAL 213
 
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.
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