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Conserved domains on  [gi|1785413433|ref|XP_002935732|]
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coiled-coil domain-containing protein 141 [Xenopus tropicalis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 1370-1449 1.83e-09

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: 56.11  E-value: 1.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433 1370 PGFSKHLPNVTVKEGSPVTLEVEVTGYPEPAVTWCRKTAVHRTDPLSDLQKPAHHHTPIIPEVQETDAAKYIsqgsvCKA 1449
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYT-----CVA 75
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 133-357 1.89e-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: 56.30  E-value: 1.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  133 FFRMVLEFAATLDQAEDFLHSSLAQDSVESVTEILHQHQSHTKAL--LGRSLAALNKSHEltglieefksnpsiansEMI 210
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELaaHEERVEALNELGE-----------------QLI 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  211 RQARISCRKVESLLESLQDRRRQLDKQLRQKRGRLEKVLQVIQWHQQEDKVTCWLQKhIDLYLKNGQLGASLTENEELIH 290
Cdd:cd00176     68 EEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEE-KEAALASEDLGKDLESVEELLK 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785413433  291 KHSQLALDAKQWTLAIDKLKTEASRIGTLESCEENGTPEDLNERLKKLHAEFWELMDERLDVLQEAN 357
Cdd:cd00176    147 KHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 224-1011 1.85e-06

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: 52.75  E-value: 1.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  224 LESLQDRRRQLDKQLRQKRGRLEKVLQVIQWHQQEDKVTCWLQKhIDLYLKNGQLGASLTENEELIHKHSQLALDAKQWT 303
Cdd:TIGR02168  188 LDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLV-LRLEELREELEELQEELKEAEEELEELTAELQELE 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  304 LAIDKLKTEASRigtlesceengtpedLNERLKKLHAEFWELMDERLDVLQEANAFFKSVNKAFDKLGSIETNLKQWKSQ 383
Cdd:TIGR02168  267 EKLEELRLEVSE---------------LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  384 GRNLVHLTVKQREAEAEIRNCTTDPFQKGKALLSKSL-SGSAMSGIQEMIGYLQKRVDQLTVQIsapnEQALKEQQNAVT 462
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEeLESRLEELEEQLETLRSKVAQLELQI----ASLNNEIERLEA 407

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  463 PEEHL-RKVSLWLQRITADLERYSEPgwSLAECEEALSKLIELANQAKEASQYMESARKTLKEDVQMFPLGTEEFSSRTH 541
Cdd:TIGR02168  408 RLERLeDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  542 LLEEQLKDLdQSIDEKLECLNVYIAFLKASSELKPAIQS-LRKLYtsSTEEGTETDVSLALKSAeaqLQFVLTEissvqd 620
Cdd:TIGR02168  486 QLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLSGILGvLSELI--SVDEGYEAAIEAALGGR---LQAVVVE------ 553

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  621 mgqnclniikmmnrntvlnnrHAQVIERTIDNLNKEKNEITNLGLIWQQRVNQANSTKQQWRTIKDKLQSATDGLEALEK 700
Cdd:TIGR02168  554 ---------------------NLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  701 DLQPFYTLNLGNDF--QTILNAQEKLSHIKNKYQNLSAEAEYaIKISDLLTReGPRLPEKS--GKINDLAELHQKVRDSI 776
Cdd:TIGR02168  613 KLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLDGDL-VRPGGVITG-GSAKTNSSilERRREIEELEEKIEELE 690

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  777 AEYEDIFIKV----VAFYQVKTELEFLVK---------AEQKCQSEHITNDELQLSQIQDQQTHFQTLYKLVVNLGREII 843
Cdd:TIGR02168  691 EKIAELEKALaelrKELEELEEELEQLRKeleelsrqiSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  844 STIQHSKHITIPVME-LQEQIAKMERDNACWNSTVDKQEKQL-LSHLDFGTTIEDINELKESFKDLKKKFNNLkfnytkK 921
Cdd:TIGR02168  771 EEAEEELAEAEAEIEeLEAQIEQLKEELKALREALDELRAELtLLNEEAANLRERLESLERRIAATERRLEDL------E 844

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  922 AEKGRNLKVIKNQIQQVEMYAERMQALRKKVDNLGKKMPVptvtpQANGADAVQEAMGDFQKQVHDFSIVIEEYKQNLEM 1001
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-----LEEALALLRSELEELSEELRELESKRSELRRELEE 919

                          810
                   ....*....|
gi 1785413433 1002 AEDLHHIMEE 1011
Cdd:TIGR02168  920 LREKLAQLEL 929
 
Name Accession Description Interval E-value
I-set pfam07679
Immunoglobulin I-set domain;
1370-1449 1.83e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 56.11  E-value: 1.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433 1370 PGFSKHLPNVTVKEGSPVTLEVEVTGYPEPAVTWCRKTAVHRTDPLSDLQKPAHHHTPIIPEVQETDAAKYIsqgsvCKA 1449
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYT-----CVA 75
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 133-357 1.89e-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: 56.30  E-value: 1.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  133 FFRMVLEFAATLDQAEDFLHSSLAQDSVESVTEILHQHQSHTKAL--LGRSLAALNKSHEltglieefksnpsiansEMI 210
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELaaHEERVEALNELGE-----------------QLI 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  211 RQARISCRKVESLLESLQDRRRQLDKQLRQKRGRLEKVLQVIQWHQQEDKVTCWLQKhIDLYLKNGQLGASLTENEELIH 290
Cdd:cd00176     68 EEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEE-KEAALASEDLGKDLESVEELLK 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785413433  291 KHSQLALDAKQWTLAIDKLKTEASRIGTLESCEENGTPEDLNERLKKLHAEFWELMDERLDVLQEAN 357
Cdd:cd00176    147 KHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 1370-1440 2.65e-07

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: 50.11  E-value: 2.65e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785413433 1370 PGFSKHLPNVTVKEGSPVTLEVEVTGYPEPAVTWCR---KTAVHRTDPLSDLQKPAHHHTPIIPEVQETDAAKY 1440
Cdd:cd20951      1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKngvPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVY 74
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 1377-1449 1.62e-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: 47.50  E-value: 1.62e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785413433  1377 PNVTVKEGSPVTLEVEVTGYPEPAVTWCRKTAV-HRTDPLSDLQKPAHHHTPIIPEVQETDAAKYisqgsVCKA 1449
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTY-----TCAA 70
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 224-1011 1.85e-06

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: 52.75  E-value: 1.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  224 LESLQDRRRQLDKQLRQKRGRLEKVLQVIQWHQQEDKVTCWLQKhIDLYLKNGQLGASLTENEELIHKHSQLALDAKQWT 303
Cdd:TIGR02168  188 LDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLV-LRLEELREELEELQEELKEAEEELEELTAELQELE 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  304 LAIDKLKTEASRigtlesceengtpedLNERLKKLHAEFWELMDERLDVLQEANAFFKSVNKAFDKLGSIETNLKQWKSQ 383
Cdd:TIGR02168  267 EKLEELRLEVSE---------------LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  384 GRNLVHLTVKQREAEAEIRNCTTDPFQKGKALLSKSL-SGSAMSGIQEMIGYLQKRVDQLTVQIsapnEQALKEQQNAVT 462
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEeLESRLEELEEQLETLRSKVAQLELQI----ASLNNEIERLEA 407

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  463 PEEHL-RKVSLWLQRITADLERYSEPgwSLAECEEALSKLIELANQAKEASQYMESARKTLKEDVQMFPLGTEEFSSRTH 541
Cdd:TIGR02168  408 RLERLeDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  542 LLEEQLKDLdQSIDEKLECLNVYIAFLKASSELKPAIQS-LRKLYtsSTEEGTETDVSLALKSAeaqLQFVLTEissvqd 620
Cdd:TIGR02168  486 QLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLSGILGvLSELI--SVDEGYEAAIEAALGGR---LQAVVVE------ 553

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  621 mgqnclniikmmnrntvlnnrHAQVIERTIDNLNKEKNEITNLGLIWQQRVNQANSTKQQWRTIKDKLQSATDGLEALEK 700
Cdd:TIGR02168  554 ---------------------NLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  701 DLQPFYTLNLGNDF--QTILNAQEKLSHIKNKYQNLSAEAEYaIKISDLLTReGPRLPEKS--GKINDLAELHQKVRDSI 776
Cdd:TIGR02168  613 KLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLDGDL-VRPGGVITG-GSAKTNSSilERRREIEELEEKIEELE 690

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  777 AEYEDIFIKV----VAFYQVKTELEFLVK---------AEQKCQSEHITNDELQLSQIQDQQTHFQTLYKLVVNLGREII 843
Cdd:TIGR02168  691 EKIAELEKALaelrKELEELEEELEQLRKeleelsrqiSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  844 STIQHSKHITIPVME-LQEQIAKMERDNACWNSTVDKQEKQL-LSHLDFGTTIEDINELKESFKDLKKKFNNLkfnytkK 921
Cdd:TIGR02168  771 EEAEEELAEAEAEIEeLEAQIEQLKEELKALREALDELRAELtLLNEEAANLRERLESLERRIAATERRLEDL------E 844

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  922 AEKGRNLKVIKNQIQQVEMYAERMQALRKKVDNLGKKMPVptvtpQANGADAVQEAMGDFQKQVHDFSIVIEEYKQNLEM 1001
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-----LEEALALLRSELEELSEELRELESKRSELRRELEE 919

                          810
                   ....*....|
gi 1785413433 1002 AEDLHHIMEE 1011
Cdd:TIGR02168  920 LREKLAQLEL 929
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 644-805 9.13e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.08  E-value: 9.13e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433   644 QVIERTIDNLNKEKNEITnlgliwqQRVNQANSTKQQWRTIKDKLQSATDGLEALEKDLQpfytlnlgNDFQTILNAqek 723
Cdd:smart00787  147 EGLDENLEGLKEDYKLLM-------KELELLNSIKPKLRDRKDALEEELRQLKQLEDELE--------DCDPTELDR--- 208

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433   724 lshIKNKYQNLSAEAEYAIKISDLLTREgprLPEKSGKINDLAELHQKVRDSIAEYEDIF--IKVVAFYQVKTELEFLVK 801
Cdd:smart00787  209 ---AKEKLKKLLQEIMIKVKKLEELEEE---LQELESKIEDLTNKKSELNTEIAEAEKKLeqCRGFTFKEIEKLKEQLKL 282


                    ....
gi 1785413433   802 AEQK 805
Cdd:smart00787  283 LQSL 286
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
224-609 2.24e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  224 LESLQDRRRQLDKQLRQKRGRLEKVLQVIQWHQQEDKVTCWLQKHIDLYLKNGQLGASLTEN-------EELIHKHSQLA 296
Cdd:COG4717     83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELperleelEERLEELRELE 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  297 LDAKQWTLAIDKLKTEASRIGTLESCEENGTPEDLNERLKKLHAEFWELmDERLDVLQEanaffksvnkafdKLGSIETN 376
Cdd:COG4717    163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL-EEELEEAQE-------------ELEELEEE 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  377 LKQWKSQGRNLvhltvkqrEAEAEIRNCTTDPFQKGKALLSKSLSGSAMSGIQEMIGYLQKRVDQLTVQISAPNEQALKE 456
Cdd:COG4717    229 LEQLENELEAA--------ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  457 QQNAVTPEEHLRKVSLWLQRITADLERYsepGWSLAECEEALSKLIELANQAKEASQYMESARKTLKEDVQMfplgteef 536
Cdd:COG4717    301 GKEAEELQALPALEELEEEELEELLAAL---GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE-------- 369

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785413433  537 SSRTHLLEEQLKDLDQSIDEKLECLNVYIAFLKASSELKPAIQSLRKLYTSSTEEGTETDVSLALKSAEAQLQ 609
Cdd:COG4717    370 QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELE 442
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 175-529 2.68e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  175 KALLGRSLAALNKSHELTGLIEEFKSNPSIANSEMIR------QARISCRKVESLLESLQDRRRQLDKQLRQKRGRLEKV 248
Cdd:TIGR02169  663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRienrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  249 LQVIQWHQQEDKVTCWLQKHIDlylkngqlgASLTENEELIHKHsQLALDA----------KQWTLAIDKLKTEASRIgt 318
Cdd:TIGR02169  743 EEDLSSLEQEIENVKSELKELE---------ARIEELEEDLHKL-EEALNDlearlshsriPEIQAELSKLEEEVSRI-- 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  319 lesceeNGTPEDLNERLKKLHAEFWELMDERLDVLQEANAF---FKSVNKAFD----KLGSIETNLKQWKSQGRNL---- 387
Cdd:TIGR02169  811 ------EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIEnlngKKEELEEELEELEAALRDLesrl 884

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  388 VHLTVKQREAEAEIRNcttdpfqkgkallskslsgsAMSGIQEM---IGYLQKRVDQLTVQISAPNEQ------ALKEQQ 458
Cdd:TIGR02169  885 GDLKKERDELEAQLRE--------------------LERKIEELeaqIEKKRKRLSELKAKLEALEEElseiedPKGEDE 944

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785413433  459 NAVTPEEHLRKVSLWLQRITADLERYsEPGWSLA--ECEEALSKLIELanqaKEASQYMESARKTLKEDVQMF 529
Cdd:TIGR02169  945 EIPEEELSLEDVQAELQRVEEEIRAL-EPVNMLAiqEYEEVLKRLDEL----KEKRAKLEEERKAILERIEEY 1012
 
Name Accession Description Interval E-value
I-set pfam07679
Immunoglobulin I-set domain;
1370-1449 1.83e-09

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 56.11  E-value: 1.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433 1370 PGFSKHLPNVTVKEGSPVTLEVEVTGYPEPAVTWCRKTAVHRTDPLSDLQKPAHHHTPIIPEVQETDAAKYIsqgsvCKA 1449
Cdd:pfam07679    1 PKFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYT-----CVA 75
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 133-357 1.89e-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: 56.30  E-value: 1.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  133 FFRMVLEFAATLDQAEDFLHSSLAQDSVESVTEILHQHQSHTKAL--LGRSLAALNKSHEltglieefksnpsiansEMI 210
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELaaHEERVEALNELGE-----------------QLI 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  211 RQARISCRKVESLLESLQDRRRQLDKQLRQKRGRLEKVLQVIQWHQQEDKVTCWLQKhIDLYLKNGQLGASLTENEELIH 290
Cdd:cd00176     68 EEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEE-KEAALASEDLGKDLESVEELLK 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785413433  291 KHSQLALDAKQWTLAIDKLKTEASRIGTLESCEENGTPEDLNERLKKLHAEFWELMDERLDVLQEAN 357
Cdd:cd00176    147 KHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 1370-1449 2.18e-08

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 52.57  E-value: 2.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433 1370 PGFSKHLPNVTVKEGSPVTLEVEVTGYPEPAVTWCRKTAVHRTDPLSDLQKPAHHHTPIIPEVQETDAAKYIsqgsvCKA 1449
Cdd:pfam13927    2 PVITVSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYT-----CVA 76
IgI_titin_I1-like cd20951
Immunoglobulin domain I1 of the titin I-band and similar proteins; a member of the I-set of ...
 1370-1440 2.65e-07

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: 50.11  E-value: 2.65e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785413433 1370 PGFSKHLPNVTVKEGSPVTLEVEVTGYPEPAVTWCR---KTAVHRTDPLSDLQKPAHHHTPIIPEVQETDAAKY 1440
Cdd:cd20951      1 PEFIIRLQSHTVWEKSDAKLRVEVQGKPDPEVKWYKngvPIDPSSIPGKYKIESEYGVHVLHIRRVTVEDSAVY 74
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 52-249 1.22e-06

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: 50.91  E-value: 1.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433   52 EIGSNQDETQKLLQDHEMLLGKLKSLEDNVWDLLCEADKTAEENPEQGQVYDAMAVTLKDAWEALISALENRQALLKLAS 131
Cdd:cd00176     27 DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEAL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  132 A---FFRMVLEFAATLDQAEDFLHSSLAQDSVESVTEILHQHQSHTKALLGRSlaalNKSHELTGLIEEFKSNPSIANSE 208
Cdd:cd00176    107 DlqqFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE----PRLKSLNELAEELLEEGHPDADE 182

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1785413433  209 mirqariscrKVESLLESLQDRRRQLDKQLRQKRGRLEKVL 249
Cdd:cd00176    183 ----------EIEEKLEELNERWEELLELAEERQKKLEEAL 213
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 1370-1440 1.57e-06

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: 47.58  E-value: 1.57e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785413433 1370 PGFSKHLPNVTVKEGSPVTLEVEVTGYPEPAVTWCRKTAVHRTDPLSDLQKPAHHHTPIIPEVQETDAAKY 1440
Cdd:cd20972      2 PQFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRY 72
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 1377-1449 1.62e-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: 47.50  E-value: 1.62e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785413433  1377 PNVTVKEGSPVTLEVEVTGYPEPAVTWCRKTAV-HRTDPLSDLQKPAHHHTPIIPEVQETDAAKYisqgsVCKA 1449
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTY-----TCAA 70
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 224-1011 1.85e-06

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: 52.75  E-value: 1.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  224 LESLQDRRRQLDKQLRQKRGRLEKVLQVIQWHQQEDKVTCWLQKhIDLYLKNGQLGASLTENEELIHKHSQLALDAKQWT 303
Cdd:TIGR02168  188 LDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLV-LRLEELREELEELQEELKEAEEELEELTAELQELE 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  304 LAIDKLKTEASRigtlesceengtpedLNERLKKLHAEFWELMDERLDVLQEANAFFKSVNKAFDKLGSIETNLKQWKSQ 383
Cdd:TIGR02168  267 EKLEELRLEVSE---------------LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  384 GRNLVHLTVKQREAEAEIRNCTTDPFQKGKALLSKSL-SGSAMSGIQEMIGYLQKRVDQLTVQIsapnEQALKEQQNAVT 462
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEeLESRLEELEEQLETLRSKVAQLELQI----ASLNNEIERLEA 407

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  463 PEEHL-RKVSLWLQRITADLERYSEPgwSLAECEEALSKLIELANQAKEASQYMESARKTLKEDVQMFPLGTEEFSSRTH 541
Cdd:TIGR02168  408 RLERLeDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  542 LLEEQLKDLdQSIDEKLECLNVYIAFLKASSELKPAIQS-LRKLYtsSTEEGTETDVSLALKSAeaqLQFVLTEissvqd 620
Cdd:TIGR02168  486 QLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLSGILGvLSELI--SVDEGYEAAIEAALGGR---LQAVVVE------ 553

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  621 mgqnclniikmmnrntvlnnrHAQVIERTIDNLNKEKNEITNLGLIWQQRVNQANSTKQQWRTIKDKLQSATDGLEALEK 700
Cdd:TIGR02168  554 ---------------------NLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  701 DLQPFYTLNLGNDF--QTILNAQEKLSHIKNKYQNLSAEAEYaIKISDLLTReGPRLPEKS--GKINDLAELHQKVRDSI 776
Cdd:TIGR02168  613 KLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLDGDL-VRPGGVITG-GSAKTNSSilERRREIEELEEKIEELE 690

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  777 AEYEDIFIKV----VAFYQVKTELEFLVK---------AEQKCQSEHITNDELQLSQIQDQQTHFQTLYKLVVNLGREII 843
Cdd:TIGR02168  691 EKIAELEKALaelrKELEELEEELEQLRKeleelsrqiSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  844 STIQHSKHITIPVME-LQEQIAKMERDNACWNSTVDKQEKQL-LSHLDFGTTIEDINELKESFKDLKKKFNNLkfnytkK 921
Cdd:TIGR02168  771 EEAEEELAEAEAEIEeLEAQIEQLKEELKALREALDELRAELtLLNEEAANLRERLESLERRIAATERRLEDL------E 844

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  922 AEKGRNLKVIKNQIQQVEMYAERMQALRKKVDNLGKKMPVptvtpQANGADAVQEAMGDFQKQVHDFSIVIEEYKQNLEM 1001
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-----LEEALALLRSELEELSEELRELESKRSELRRELEE 919

                          810
                   ....*....|
gi 1785413433 1002 AEDLHHIMEE 1011
Cdd:TIGR02168  920 LREKLAQLEL 929
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 1370-1449 2.04e-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: 47.39  E-value: 2.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433 1370 PGFSKHLP-NVTVKEGSPVTLEVEVTGYPEPAVTWcrktaVHRTDPLSDLQKPA--HHHTPIIPEVQETDAAKYIsqgsv 1446
Cdd:cd20978      1 PKFIQKPEkNVVVKGGQDVTLPCQVTGVPQPKITW-----LHNGKPLQGPMERAtvEDGTLTIINVQPEDTGYYG----- 70


                   ...
gi 1785413433 1447 CKA 1449
Cdd:cd20978     71 CVA 73
IgI_1_Titin_Z1z2-like cd20974
First Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and ...
 1370-1441 1.71e-05

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: 45.04  E-value: 1.71e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785413433 1370 PGFSKHLPNVTVKEGSPVTLEVEVTGYPEPAVTWCRKTAVHRTDPLSDLQ--KPAHHHTPIIPEVQETDAAKYI 1441
Cdd:cd20974      1 PVFTQPLQSVVVLEGSTATFEAHVSGKPVPEVSWFRDGQVISTSTLPGVQisFSDGRAKLSIPAVTKANSGRYS 74
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 190-559 2.35e-05

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: 49.28  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  190 ELTGLIEEFKSNpsiansemIRQARISCRKVESLLESLQDRRRQLDKQLRQKRGRLEKVLQVIQWHQQEdkVTCWLQKHI 269
Cdd:TIGR02168  681 ELEEKIEELEEK--------IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE--VEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  270 DLYLKNGQLGASLTENEELIHKhSQLALDAkqwtlAIDKLKTEASRIGTLEscEENGTpedLNERLKKLHAEFWELMDER 349
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEE-AEEELAE-----AEAEIEELEAQIEQLK--EELKA---LREALDELRAELTLLNEEA 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  350 LDVLQEANaffKSVNKAFDKLGSIETNLKQWKSqgrnlvhLTVKQREAEAEIRNCTTDPFQKGKALLSKSlsgSAMSGIQ 429
Cdd:TIGR02168  820 ANLRERLE---SLERRIAATERRLEDLEEQIEE-------LSEDIESLAAEIEELEELIEELESELEALL---NERASLE 886

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  430 EMIGYLQKRVDQLTVQISAPNEQALKEQQNAVTPEEHLRKVSLWLQRITADLERYSEPGWSLA--ECEEALSKLIELANQ 507
Cdd:TIGR02168  887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYslTLEEAEALENKIEDD 966

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1785413433  508 AKEASQYMESARKTLKE--DVQMfpLGTEEFSS---RTHLLEEQLKDLDQSIdEKLE 559
Cdd:TIGR02168  967 EEEARRRLKRLENKIKElgPVNL--AAIEEYEElkeRYDFLTAQKEDLTEAK-ETLE 1020
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 1378-1406 2.49e-05

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: 44.42  E-value: 2.49e-05
                           10        20
                   ....*....|....*....|....*....
gi 1785413433 1378 NVTVKEGSPVTLEVEVTGYPEPAVTWCRK 1406
Cdd:cd20970     11 TVTAREGENATFMCRAEGSPEPEISWTRN 39
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
 1379-1440 1.43e-04

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: 41.81  E-value: 1.43e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785413433 1379 VTVKEGSPVTLEVEVTGYPEPAVTWCRKTAVHRTDPLSDLQKPAHHHTPIIPEVQETDAAKY 1440
Cdd:cd05748      2 IVVRAGESLRLDIPIKGRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKY 63
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 1387-1449 1.74e-04

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: 41.16  E-value: 1.74e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785413433 1387 VTLEVEVTGYPEPAVTWCRKTAVHRTDPLSDLQKPAHHHTPIIPEVQETDAAKYisqgsVCKA 1449
Cdd:cd00096      1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTY-----TCVA 58
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 1370-1441 4.92e-04

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: 40.56  E-value: 4.92e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785413433 1370 PGFSKHLPNVTVKEGSPVTLEVEVTGYPEPAVTWCRKT-AVHRTDPLSDLQKPAHHHTPIIPEVQETDAAKYI 1441
Cdd:cd05744      1 PHFLQAPGDLEVQEGRLCRFDCKVSGLPTPDLFWQLNGkPVRPDSAHKMLVRENGRHSLIIEPVTKRDAGIYT 73
IgI_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; member of the I-set of Ig superfamily ...
 1370-1440 7.48e-04

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: 40.14  E-value: 7.48e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785413433 1370 PGFSKHLPNVTVKEGSPVTLEVEVTGYPEPAVTWCRKTAV--HRTDPLSDLQKPAHHHTPIIPEVQETDAAKY 1440
Cdd:cd05892      1 PMFIQKPQNKKVLEGDPVRLECQISAIPPPQIFWKKNNEMlqYNTDRISLYQDNCGRICLLIQNANKKDAGWY 73
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 644-805 9.13e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.08  E-value: 9.13e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433   644 QVIERTIDNLNKEKNEITnlgliwqQRVNQANSTKQQWRTIKDKLQSATDGLEALEKDLQpfytlnlgNDFQTILNAqek 723
Cdd:smart00787  147 EGLDENLEGLKEDYKLLM-------KELELLNSIKPKLRDRKDALEEELRQLKQLEDELE--------DCDPTELDR--- 208

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433   724 lshIKNKYQNLSAEAEYAIKISDLLTREgprLPEKSGKINDLAELHQKVRDSIAEYEDIF--IKVVAFYQVKTELEFLVK 801
Cdd:smart00787  209 ---AKEKLKKLLQEIMIKVKKLEELEEE---LQELESKIEDLTNKKSELNTEIAEAEKKLeqCRGFTFKEIEKLKEQLKL 282


                    ....
gi 1785413433   802 AEQK 805
Cdd:smart00787  283 LQSL 286
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
 1370-1440 1.89e-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: 1.89e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785413433 1370 PGFSKHLPNVTVKEGSPVTLEVEVTGYPEPAVTWCRKTavhrtdplSDLQKPAHHHTP-------IIPEVQETDAAKY 1440
Cdd:cd20976      2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITWIRNA--------QPLQYAADRSTCeagvgelHIQDVLPEDHGTY 71
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
224-609 2.24e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  224 LESLQDRRRQLDKQLRQKRGRLEKVLQVIQWHQQEDKVTCWLQKHIDLYLKNGQLGASLTEN-------EELIHKHSQLA 296
Cdd:COG4717     83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELperleelEERLEELRELE 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  297 LDAKQWTLAIDKLKTEASRIGTLESCEENGTPEDLNERLKKLHAEFWELmDERLDVLQEanaffksvnkafdKLGSIETN 376
Cdd:COG4717    163 EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL-EEELEEAQE-------------ELEELEEE 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  377 LKQWKSQGRNLvhltvkqrEAEAEIRNCTTDPFQKGKALLSKSLSGSAMSGIQEMIGYLQKRVDQLTVQISAPNEQALKE 456
Cdd:COG4717    229 LEQLENELEAA--------ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  457 QQNAVTPEEHLRKVSLWLQRITADLERYsepGWSLAECEEALSKLIELANQAKEASQYMESARKTLKEDVQMfplgteef 536
Cdd:COG4717    301 GKEAEELQALPALEELEEEELEELLAAL---GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE-------- 369

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785413433  537 SSRTHLLEEQLKDLDQSIDEKLECLNVYIAFLKASSELKPAIQSLRKLYTSSTEEGTETDVSLALKSAEAQLQ 609
Cdd:COG4717    370 QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELE 442
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
 1376-1445 2.37e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395 [Multi-domain]  Cd Length: 96  Bit Score: 38.66  E-value: 2.37e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785413433 1376 LPNVTVKEGSPVTLEVEVTGYPEPAVTWCRKTAVH---RTDPLSDLQKPAHHHTP--IIPEVQETDAAKYISQGS 1445
Cdd:cd05732      8 LENQTAVELEQITLTCEAEGDPIPEITWRRATRGIsfeEGDLDGRIVVRGHARVSslTLKDVQLTDAGRYDCEAS 82
IgI_APEG-1_like cd20975
Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and ...
 1370-1413 2.60e-03

Immunoglobulin-like domain of human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin I-set (IgI) domain of the Human Aortic Preferentially Expressed Protein-1 (APEG-1) and similar proteins. APEG-1 is a novel specific smooth muscle differentiation marker predicted to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). 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 human APEG-1 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: 409567  Cd Length: 91  Bit Score: 38.61  E-value: 2.60e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1785413433 1370 PGFSKHLPNVTVKEGSPVTLEVEVTGYPEPAVTWCRKTAVHRTD 1413
Cdd:cd20975      1 PTFKVSLMDQSVREGQDVIMSIRVQGEPKPVVSWLRNRQPVRPD 44
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 175-529 2.68e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  175 KALLGRSLAALNKSHELTGLIEEFKSNPSIANSEMIR------QARISCRKVESLLESLQDRRRQLDKQLRQKRGRLEKV 248
Cdd:TIGR02169  663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRienrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  249 LQVIQWHQQEDKVTCWLQKHIDlylkngqlgASLTENEELIHKHsQLALDA----------KQWTLAIDKLKTEASRIgt 318
Cdd:TIGR02169  743 EEDLSSLEQEIENVKSELKELE---------ARIEELEEDLHKL-EEALNDlearlshsriPEIQAELSKLEEEVSRI-- 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  319 lesceeNGTPEDLNERLKKLHAEFWELMDERLDVLQEANAF---FKSVNKAFD----KLGSIETNLKQWKSQGRNL---- 387
Cdd:TIGR02169  811 ------EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIEnlngKKEELEEELEELEAALRDLesrl 884

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785413433  388 VHLTVKQREAEAEIRNcttdpfqkgkallskslsgsAMSGIQEM---IGYLQKRVDQLTVQISAPNEQ------ALKEQQ 458
Cdd:TIGR02169  885 GDLKKERDELEAQLRE--------------------LERKIEELeaqIEKKRKRLSELKAKLEALEEElseiedPKGEDE 944

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785413433  459 NAVTPEEHLRKVSLWLQRITADLERYsEPGWSLA--ECEEALSKLIELanqaKEASQYMESARKTLKEDVQMF 529
Cdd:TIGR02169  945 EIPEEELSLEDVQAELQRVEEEIRAL-EPVNMLAiqEYEEVLKRLDEL----KEKRAKLEEERKAILERIEEY 1012
 
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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