NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|212659289|ref|NP_001023517|]
View 

LIM zinc-binding domain-containing protein [Caenorhabditis elegans]

Protein Classification

LIM domain-containing protein( domain architecture ID 10174924)

LIM (LIN-11, Isl1 and MEC-3) domain-containing protein; LIM is a small protein-protein interaction domain containing two zinc fingers; similar to Dictyostelium discoideum LimD that binds to F-actin and may modulate the chemotactic response during early development and contribute to the maintenance of the strength of the actin cytoskeleton

CATH:  2.10.110.10
Gene Ontology:  GO:0046872|GO:0005515
PubMed:  15520811|10704826|7954790|9594664|8506279
SCOP:  4003634

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LIM_Mical_like cd09358
The LIM domain of Mical (molecule interacting with CasL) like family; The LIM domain of Mical ...
 192-244 1.01e-13

The LIM domain of Mical (molecule interacting with CasL) like family; The LIM domain of Mical (molecule interacting with CasL) like family: Known members of this family includes LIM domain containing proteins; Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2) and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth and mobility. Eplin has also found to be tumor suppressor. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs.. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


:

Pssm-ID: 188744 [Multi-domain]  Cd Length: 53  Bit Score: 66.14  E-value: 1.01e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 212659289 192 CCICDKVVYPVEKVLANKNLYHIQCFKCCKCAKKLTPTNFNSHEGKLLCKVHM 244
Cdd:cd09358    1 CAVCGKTVYPMERLVADGKLFHKSCFRCSHCNKTLRLGNYASLEGKLYCKPHF 53
PTZ00121 super family cl31754
MAEBL; Provisional
 263-754 1.28e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  263 EDEHAASDEEEFAVSSKPKQLQGVVKSGGGGVHDELAQLKSlREKKGDFESSCKEVDNVEKKTQIEKDLLAAGKVKANaE 342
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA-EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-E 1389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  343 KFISGAALENSDDESESADRDPNIIRGSKKAEKVELNFENV---GDIKNKWKEGNVETAEAKEAAERKELEALKGGVSVK 419
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  420 DRFKERGDNDEQV--VERSWNKDELSTSAAAEARKSFMAGSAYDAANPVEKTvKDLDDLKFGQLKGFKDKFEKGEEGVEV 497
Cdd:PTZ00121 1470 KKADEAKKKAEEAkkADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA-KKADEAKKAEEAKKADEAKKAEEKKKA 1548

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  498 QktQVDLGEGVQLGNIKATFEKGNAVDESEMTAEERAELKKREIEA---EFQRYKLARKSAKAQEEVVGEEEANKGYnpl 574
Cdd:PTZ00121 1549 D--ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArieEVMKLYEEEKKMKAEEAKKAEEAKIKAE--- 1623

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  575 dvEVKMAGKAREKFRQIDASGASPVL-PQQSKKSTEPSKWDKKDDKPVAEVINRRNTDEQEPEEEEDDAfdVKNLMNKFK 653
Cdd:PTZ00121 1624 --ELKKAEEEKKKVEQLKKKEAEEKKkAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA--AEALKKEAE 1699

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  654 NIGDSGNQKTQNTEHRAELEALKCAAKDFKAKFENAGEADADAAVVEAK-RQQMEEEFEAMKREREEAQKRLEEERLAEA 732
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEaKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779

                         490       500
                  ....*....|....*....|..
gi 212659289  733 SASQGNEARDEDVAIKAEHASK 754
Cdd:PTZ00121 1780 VIEEELDEEDEKRRMEVDKKIK 1801
 
Name Accession Description Interval E-value
LIM_Mical_like cd09358
The LIM domain of Mical (molecule interacting with CasL) like family; The LIM domain of Mical ...
 192-244 1.01e-13

The LIM domain of Mical (molecule interacting with CasL) like family; The LIM domain of Mical (molecule interacting with CasL) like family: Known members of this family includes LIM domain containing proteins; Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2) and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth and mobility. Eplin has also found to be tumor suppressor. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs.. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188744 [Multi-domain]  Cd Length: 53  Bit Score: 66.14  E-value: 1.01e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 212659289 192 CCICDKVVYPVEKVLANKNLYHIQCFKCCKCAKKLTPTNFNSHEGKLLCKVHM 244
Cdd:cd09358    1 CAVCGKTVYPMERLVADGKLFHKSCFRCSHCNKTLRLGNYASLEGKLYCKPHF 53
PTZ00121 PTZ00121
MAEBL; Provisional
 263-754 1.28e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  263 EDEHAASDEEEFAVSSKPKQLQGVVKSGGGGVHDELAQLKSlREKKGDFESSCKEVDNVEKKTQIEKDLLAAGKVKANaE 342
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA-EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-E 1389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  343 KFISGAALENSDDESESADRDPNIIRGSKKAEKVELNFENV---GDIKNKWKEGNVETAEAKEAAERKELEALKGGVSVK 419
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  420 DRFKERGDNDEQV--VERSWNKDELSTSAAAEARKSFMAGSAYDAANPVEKTvKDLDDLKFGQLKGFKDKFEKGEEGVEV 497
Cdd:PTZ00121 1470 KKADEAKKKAEEAkkADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA-KKADEAKKAEEAKKADEAKKAEEKKKA 1548

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  498 QktQVDLGEGVQLGNIKATFEKGNAVDESEMTAEERAELKKREIEA---EFQRYKLARKSAKAQEEVVGEEEANKGYnpl 574
Cdd:PTZ00121 1549 D--ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArieEVMKLYEEEKKMKAEEAKKAEEAKIKAE--- 1623

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  575 dvEVKMAGKAREKFRQIDASGASPVL-PQQSKKSTEPSKWDKKDDKPVAEVINRRNTDEQEPEEEEDDAfdVKNLMNKFK 653
Cdd:PTZ00121 1624 --ELKKAEEEKKKVEQLKKKEAEEKKkAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA--AEALKKEAE 1699

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  654 NIGDSGNQKTQNTEHRAELEALKCAAKDFKAKFENAGEADADAAVVEAK-RQQMEEEFEAMKREREEAQKRLEEERLAEA 732
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEaKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779

                         490       500
                  ....*....|....*....|..
gi 212659289  733 SASQGNEARDEDVAIKAEHASK 754
Cdd:PTZ00121 1780 VIEEELDEEDEKRRMEVDKKIK 1801
 
Name Accession Description Interval E-value
LIM_Mical_like cd09358
The LIM domain of Mical (molecule interacting with CasL) like family; The LIM domain of Mical ...
 192-244 1.01e-13

The LIM domain of Mical (molecule interacting with CasL) like family; The LIM domain of Mical (molecule interacting with CasL) like family: Known members of this family includes LIM domain containing proteins; Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2) and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth and mobility. Eplin has also found to be tumor suppressor. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs.. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188744 [Multi-domain]  Cd Length: 53  Bit Score: 66.14  E-value: 1.01e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 212659289 192 CCICDKVVYPVEKVLANKNLYHIQCFKCCKCAKKLTPTNFNSHEGKLLCKVHM 244
Cdd:cd09358    1 CAVCGKTVYPMERLVADGKLFHKSCFRCSHCNKTLRLGNYASLEGKLYCKPHF 53
LIM2_SF3 cd09441
The second Lim domain of pollen specific protein SF3; The second Lim domain of pollen specific ...
 192-248 5.59e-09

The second Lim domain of pollen specific protein SF3; The second Lim domain of pollen specific protein SF3: SF3 is a Lim protein that is found exclusively in mature plant pollen grains. It contains two LIM domains. The exact function of SF3 is unknown. It may be a transcription factor required for the expression of late pollen genes. It is possible that SF3 protein is involved in controlling pollen-specific processes such as male gamete maturation, pollen tube formation, or even fertilization. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188825 [Multi-domain]  Cd Length: 61  Bit Score: 52.86  E-value: 5.59e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 212659289 192 CCICDKVVYPVEKVLANKNLYHIQCFKCCKCAKKLTPTNFNSHEGKLLCKVHMLEVF 248
Cdd:cd09441    1 CVACGKTVYPIEKVTVEGTSYHKSCFKCSHGGCTISPSNYAAHEGRLYCKHHHSQLF 57
LIM_Mical_like_2 cd09445
This domain belongs to the LIM domain family which are found on Mical (molecule interacting ...
 192-243 3.22e-08

This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL) like proteins; The LIM domain on proteins of unknown function: This domain belongs to the LIM domain family which are found on Mical (molecule interacting with CasL)-like proteins. Known members of the Mical-like family includes single LIM domain containing proteins, Mical (molecule interacting with CasL), pollen specific protein SF3, Eplin, xin actin-binding repeat-containing protein 2 (XIRP2), and Ltd-1. The members of this family function mainly at the cytoskeleton and focal adhesions. They interact with transcription factors or other signaling molecules to play roles in muscle development, neuronal differentiation, cell growth, and mobility. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188829 [Multi-domain]  Cd Length: 53  Bit Score: 50.54  E-value: 3.22e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 212659289 192 CCICDKVVYPVEKVLANKNLYHIQCFKCCKCAKKLTPTNFNSHEGKLLCKVH 243
Cdd:cd09445    1 CRSCGKPVYKMEEIIAEKHIYHKNCFRCKDCNKQLKVDNYQSHEGNLYCKVH 52
LIM1_SF3 cd09440
The first Lim domain of pollen specific protein SF3; The first Lim domain of pollen specific ...
 192-248 1.74e-06

The first Lim domain of pollen specific protein SF3; The first Lim domain of pollen specific protein SF3: SF3 is a Lim protein that is found exclusively in mature plant pollen grains. It contains two LIM domains. The exact function of SF3 is unknown. It may be a transcription factor required for the expression of late pollen genes. It is possible that SF3 protein is involved in controlling pollen-specific processes such as male gamete maturation, pollen tube formation, or even fertilization. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188824 [Multi-domain]  Cd Length: 63  Bit Score: 45.92  E-value: 1.74e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 212659289 192 CCICDKVVYPVEKVLANKNLYHIQCFKCCKCAKKLTPTNFNSHEGKLLCKVHMLEVF 248
Cdd:cd09440    5 CKACDKTVYLVDQLSADGVVYHKSCFRCSHCKGTLKLSNYSSMEGVLYCKPHFEQLF 61
LIM_Eplin_alpha_beta cd09485
The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin); The Lim domain of Epithelial ...
 192-243 8.56e-06

The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin); The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin): Epithelial Protein Lost in Neoplasm is a cytoskeleton-associated tumor suppressor whose expression inversely correlates with cell growth, motility, invasion and cancer mortality. Eplin interacts and stabilizes F-actin filaments and stress fibers, which correlates with its ability to suppress anchorage independent growth. In epithelial cells, Eplin is required for formation of the F-actin adhesion belt by binding to the E-cadherin-catenin complex through alpha-catenin. Eplin is expressed in two isoforms, a longer Eplin-beta and a shorter Eplin-alpha. Eplin-alpha mRNA is detected in various tissues and cell lines, but is absent or down regulated in cancer cells. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188869 [Multi-domain]  Cd Length: 53  Bit Score: 43.71  E-value: 8.56e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 212659289 192 CCICDKVVYPVEKVLANKNLYHIQCFKCCKCAKKLTPTNFNSHEGKLLCKVH 243
Cdd:cd09485    1 CVSCQKTVYPLERLVANQQIYHNSCFRCSYCNTKLSLGTYASLHGNIYCKPH 52
LIM_Eplin_like cd09442
The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin) like proteins; The Lim domain of ...
 192-243 2.55e-04

The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin) like proteins; The Lim domain of Epithelial Protein Lost in Neoplasm (Eplin) like proteins: This family contains Epithelial Protein Lost in Neoplasm in Neoplasm (Eplin), xin actin-binding repeat-containing protein 2 (XIRP2) and a group of protein with unknown function. The members of this family all contain a single LIM domain. Epithelial Protein Lost in Neoplasm is a cytoskeleton-associated tumor suppressor whose expression inversely correlates with cell growth, motility, invasion and cancer mortality. Eplin interacts and stabilizes F-actin filaments and stress fibers, which correlates with its ability to suppress anchorage independent growth. In epithelial cells, Eplin is required for formation of the F-actin adhesion belt by binding to the E-cadherin-catenin complex through alpha-catenin. Eplin is expressed in two isoforms, a longer Eplin-beta and a shorter Eplin-alpha. Eplin-alpha mRNA is detected in various tissues and cell lines, but is absent or down regulated in cancer cells. Xirp2 contains a LIM domain and Xin re peats for binding to and stabilising F-actin. Xirp2 is expressed in muscles and is significantly induced in the heart in response to systemic administration of angiotensin II. Xirp2 is an important effector of the Ang II signaling pathway in the heart. The expression of Xirp2 is activated by myocyte enhancer factor (MEF)2A, whose transcriptional activity is stimulated by angiotersin II. Thus, Xirp2 plays important pathological roles in the angiotensin II induced hypertension. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188826 [Multi-domain]  Cd Length: 53  Bit Score: 39.39  E-value: 2.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 212659289 192 CCICDKVVYPVEKVLANKNLYHIQCFKCCKCAKKLTPTNFNSHEGKLLCKVH 243
Cdd:cd09442    1 CTVCQKRVYPMERLIADKQNFHKSCFRCEHCNSKLSLGNYASLHGRIYCKPH 52
PTZ00121 PTZ00121
MAEBL; Provisional
 263-754 1.28e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  263 EDEHAASDEEEFAVSSKPKQLQGVVKSGGGGVHDELAQLKSlREKKGDFESSCKEVDNVEKKTQIEKDLLAAGKVKANaE 342
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA-EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-E 1389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  343 KFISGAALENSDDESESADRDPNIIRGSKKAEKVELNFENV---GDIKNKWKEGNVETAEAKEAAERKELEALKGGVSVK 419
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  420 DRFKERGDNDEQV--VERSWNKDELSTSAAAEARKSFMAGSAYDAANPVEKTvKDLDDLKFGQLKGFKDKFEKGEEGVEV 497
Cdd:PTZ00121 1470 KKADEAKKKAEEAkkADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA-KKADEAKKAEEAKKADEAKKAEEKKKA 1548

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  498 QktQVDLGEGVQLGNIKATFEKGNAVDESEMTAEERAELKKREIEA---EFQRYKLARKSAKAQEEVVGEEEANKGYnpl 574
Cdd:PTZ00121 1549 D--ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArieEVMKLYEEEKKMKAEEAKKAEEAKIKAE--- 1623

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  575 dvEVKMAGKAREKFRQIDASGASPVL-PQQSKKSTEPSKWDKKDDKPVAEVINRRNTDEQEPEEEEDDAfdVKNLMNKFK 653
Cdd:PTZ00121 1624 --ELKKAEEEKKKVEQLKKKEAEEKKkAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA--AEALKKEAE 1699

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  654 NIGDSGNQKTQNTEHRAELEALKCAAKDFKAKFENAGEADADAAVVEAK-RQQMEEEFEAMKREREEAQKRLEEERLAEA 732
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEaKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779

                         490       500
                  ....*....|....*....|..
gi 212659289  733 SASQGNEARDEDVAIKAEHASK 754
Cdd:PTZ00121 1780 VIEEELDEEDEKRRMEVDKKIK 1801
LIM_Eplin_like_1 cd09486
a LIM domain subfamily on a group of proteins with unknown function; This model represents a ...
 192-243 3.59e-03

a LIM domain subfamily on a group of proteins with unknown function; This model represents a LIM domain subfamily of Eplin-like family. This family shows highest homology to the LIM domains on Eplin and XIRP2 protein families. Epithelial Protein Lost in Neoplasm is a cytoskeleton-associated tumor suppressor whose expression inversely correlates with cell growth, motility, invasion and cancer mortality. Xirp2 is expressed in muscles and is an important effector of the Ang II signaling pathway in the heart. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188870 [Multi-domain]  Cd Length: 53  Bit Score: 36.10  E-value: 3.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 212659289 192 CCICDKVVYPVEKVLANKNLYHIQCFKCCKCAKKLTPTNFNSHEGKLLCKVH 243
Cdd:cd09486    1 CSSCQKTVYPMERLVADKLVFHNSCFCCKHCNAKLSLGSYAALHGEFYCKPH 52
PTZ00121 PTZ00121
MAEBL; Provisional
 518-754 5.77e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 5.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  518 EKGNAVDESEMTAEERA---ELKKREIEAEFQRYKLARKSAKAQEEV-VGEEEANKGYNPLDVEVKMAGKAREKFRQIDA 593
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKkadEAKKKAEEAKKKADAAKKKAEEAKKAAeAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  594 SGASPVLPQQSKKSTEPSKWDKKDDKPVAEVINRRNTDEQEPEEEEDDAFDVKNlmnkfknigdSGNQKTQNTEHRAELE 673
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK----------ADEAKKKAEEAKKADE 1448

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  674 ALKCAAKDFKAKFENAGEADADAAVVEAKRQQMEEEFEAMKREREEAQKRLEEERLAEASASQGNEARDEDVAIKAEHAS 753
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528


                  .
gi 212659289  754 K 754
Cdd:PTZ00121 1529 K 1529
LIM_Ltd-1 cd09443
The LIM domain of LIM and transglutaminase domains protein (Ltd-1); The LIM domain of LIM and ...
 192-243 7.45e-03

The LIM domain of LIM and transglutaminase domains protein (Ltd-1); The LIM domain of LIM and transglutaminase domains protein (Ltd-1): This family includes mouse Ky protein and Caenorhabditis elegans Ltd-1 protein. The members of this family consists a N-terminal Lim domain and a C-terminal transglutaminase domain. The mouse Ky protein has putative function in muscle development. The mouse with ky mutant exhibits combined posterior and lateral curvature of the spine. The Ltd-1 gene in C. elegans is expressed in developing hypodermal cells from the twofold stage embryo through adulthood. These data define the ltd-1 gene as a novel marker for C. elegans epithelial cell development. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188827 [Multi-domain]  Cd Length: 55  Bit Score: 35.47  E-value: 7.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 212659289 192 CCICDKVVYPVEKVLANKNLYHIQCFKCCKCAKKLT--PTNFNSHEGKLLCKVH 243
Cdd:cd09443    1 CPRCGKTAYPAESVDKDGTFYHKGCFKCRECGTRLSlkTFTFVQGDGEVYCARH 54
PTZ00121 PTZ00121
MAEBL; Provisional
 370-778 8.52e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 8.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  370 SKKAEKVElNFENVGDIKNKWKEGNVETAEAKEAAERKELEALKGGVSVKDRFKERGDNDEQVVERSWNKDELSTSAAAE 449
Cdd:PTZ00121 1242 AKKAEEER-NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  450 ARKSFMAGSAYDAANPVEKTVKDLDDLKFGQLKGFKDKFEKGEEGVEVQKTQVDlGEGVQLGNIKATFEKGNAVDESEMT 529
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE-EAKKKADAAKKKAEEKKKADEAKKK 1399

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  530 AEERAElKKREIEAEFQRYKLARKSAKAQEEVVGEEEANKGYNpldvEVKMAGKAREKFRQIDASGASPVLPQQSKKSTE 609
Cdd:PTZ00121 1400 AEEDKK-KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE----EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  610 PSKwdKKDDKPVAEVINRRNTDEQEPEEEEDDAFDVKNLMNKFKNIGDS--GNQKTQNTEHRAELEALKCAAKDFKAKFE 687
Cdd:PTZ00121 1475 AKK--KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAkkADEAKKAEEAKKADEAKKAEEKKKADELK 1552

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212659289  688 NAGEADADAAVVEAKRQQMEEEFEAMKREREEAQKRLEEERLAEASASQGNEA--------RDEDVAIKAEHASKMAAKW 759
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmkaeeakKAEEAKIKAEELKKAEEEK 1632

                         410
                  ....*....|....*....
gi 212659289  760 EKIQQKEAKKAEKGKMPEK 778
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEE 1651
LIM_TLP_like cd09401
The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like ...
 192-242 9.39e-03

The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like proteins: This family includes the LIM domains of TLP and CRIP (Cysteine-Rich Intestinal Protein). TLP is the distant member of the CRP family of proteins. TLP has two isomers (TLP-A and TLP-B) and sharing approximately 30% with each of the three other CRPs. Like CRP1, CRP2 and CRP3/MLP, TLP has two LIM domains, connected by a flexible linker region. Unlike the CRPs, TLP lacks the nuclear targeting signal (K/R-K/R-Y-G-P-K) and is localized solely in the cytoplasm. TLP is specifically expressed in the thymus in a subset of cortical epithelial cells. TLP has a role in development of normal thymus and in controlling the development and differentiation of thymic epithelial cells. CRIP is a short LIM protein with only one LIM domain. CRIP gene is developmentally regulated and can be induced by glucocorticoid hormones during the first three postnatal weeks. The domain shows close sequence homology to LIM domain of thymus LIM protein. However, unlike the TLP proteins which have two LIM domains, the members of this family have only one LIM domain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188785 [Multi-domain]  Cd Length: 53  Bit Score: 35.01  E-value: 9.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 212659289 192 CCICDKVVYPVEKVLANKNLYHIQCFKCCKCAKKLTPTNFNSHEGKLLCKV 242
Cdd:cd09401    1 CPKCGKPVYFAEKKTSLGRDWHKPCLRCEKCKKTLTPGQHSEHEGKPYCNK 51
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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