Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552703    1399 GPKLYKQPAAKSNRGIILNAVEYCVFPGVVNREAKQKVLEKIARSEAKHFLVLFRDAGCQFRALYSYQPETDQVTKLYGT 1478
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 45552703    1479 GPSQVEEVMFDKFFKYNSGGKCFSQVHTKHLTVTIDAFTIHNSLWQGKR 1527
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129

Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on calmodulin-regulated spectrin-associated proteins in eukaryotes that binds spectrin. CAMSAPs are vertebrate microtubule-binding proteins, representatives of a family of cytoskeletal proteins that arose in animals. This conserved CC1 region binds to both spectrin and Ca2+/calmodulin in vitro, although the binding of Ca2+/calmodulin inhibited the binding of spectrin. CC1 appears to be a functional region of CAMSAP1 that links spectrin-binding to neurite outgrowth.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552703    612 DVGDDDMRSLENASKLSTIRMKLEEKRRRIEQDKRKIEMALLRHQEKedlescpdvMKWETMSNESKR 679
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQK---------LGKAAFLQVVKK 59

Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552703    1399 GPKLYKQPAAKSNRGIILNAVEYCVFPGVVNREAKQKVLEKIARSEAKHFLVLFRDAGCQFRALYSYQPETDQVTKLYGT 1478
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 45552703    1479 GPSQVEEVMFDKFFKYNSGGKCFSQVHTKHLTVTIDAFTIHNSLWQGKR 1527
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552703    189 NGSRLQTPDIPPVRDF-QDLCDGICLALLISYYCPKVVPWTSVRINYLPAVEDSIHNILLVCNFSQKHLPYTVMHMTPED 267
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLlRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLGNRCCHLTLED 80

                   ....*
gi 45552703    268 VTYMR 272
Cdd:pfam11971   81 LLYAR 85

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552703  145 ISGNNYQAPtgqsyEQALLGWISHAcaaLKKriikevdaglpddngsrlQTPDIPPVRDF-QDLCDGICLALLISYYCPK 223
Cdd:cd21218    3 LESLLYLPP-----EEILLRWVNYH---LKK------------------AGPTKKRVTNFsSDLKDGEVYALLLHSLAPE 56

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552703  224 VVPWTSVRINYLPavEDSIHNILLVCNFSQK-HLPYtvmHMTPEDVtyMRGSMKLNLvVLLTDLFN 288
Cdd:cd21218   57 LCDKELVLEVLSE--EDLEKRAEKVLQAAEKlGCKY---FLTPEDI--VSGNPRLNL-AFVATLFN 114

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552703     191 SRLQTPDIPPVRDF-QDLCDGICLALLISYYCPKVVPWtsVRINYLPAVEDSIHNILLVCNFSQKHLPYTVMhMTPEDVT 269
Cdd:smart00033    9 SLLAEYDKPPVTNFsSDLKDGVALCALLNSLSPGLVDK--KKVAASLSRFKKIENINLALSFAEKLGGKVVL-FEPEDLV 85

                            90
                    ....*....|....*
gi 45552703     270 YMRgsmKLNLVVLLT 284
Cdd:smart00033   86 EGP---KLILGVIWT 97

Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552703    1399 GPKLYKQPAAKSNRGIILNAVEYCVFPGVVNREAKQKVLEKIARSEAKHFLVLFRDAGCQFRALYSYQPETDQVTKLYGT 1478
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 45552703    1479 GPSQVEEVMFDKFFKYNSGGKCFSQVHTKHLTVTIDAFTIHNSLWQGKR 1527
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129

CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552703    189 NGSRLQTPDIPPVRDF-QDLCDGICLALLISYYCPKVVPWTSVRINYLPAVEDSIHNILLVCNFSQKHLPYTVMHMTPED 267
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLlRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLGNRCCHLTLED 80

                   ....*
gi 45552703    268 VTYMR 272
Cdd:pfam11971   81 LLYAR 85

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552703  145 ISGNNYQAPtgqsyEQALLGWISHAcaaLKKriikevdaglpddngsrlQTPDIPPVRDF-QDLCDGICLALLISYYCPK 223
Cdd:cd21218    3 LESLLYLPP-----EEILLRWVNYH---LKK------------------AGPTKKRVTNFsSDLKDGEVYALLLHSLAPE 56

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45552703  224 VVPWTSVRINYLPavEDSIHNILLVCNFSQK-HLPYtvmHMTPEDVtyMRGSMKLNLvVLLTDLFN 288
Cdd:cd21218   57 LCDKELVLEVLSE--EDLEKRAEKVLQAAEKlGCKY---FLTPEDI--VSGNPRLNL-AFVATLFN 114

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552703   1189 NQSPQQTQQPMSPT------RLQQSSNNAEAAKNKALVIGADSTNLDPESVDEME-RRKEKIMLLSLQRRQQQEEAKARK 1261
Cdd:TIGR02794   49 AQQANRIQQQKKPAakkeqeRQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAaKQAEQAAKQAEEKQKQAEEAKAKQ 128

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 45552703   1262 EIEASQkrekereKEEERARKKEEQMARRAAilEQHRLKKAIEEAERE 1309
Cdd:TIGR02794  129 AAEAKA-------KAEAEAERKAKEEAAKQA--EEEAKAKAAAEAKKK 167