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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622195365  236 PRQMPCIPPVENLLKDSTDGCALAALIHFYCPDLVKLEDICLKETMSLADSLYNLQLIQEFCQENL-NRCCHFTLEDMIY 314
Cdd:pfam11971    4 QRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLEDLLY 83

                   ..
gi 1622195365  315 AS 316
Cdd:pfam11971   84 AR 85

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622195365 1152 EDDMAMKRAALLEKRLRREKENQQRKQQLEAELEQKK---EEARVKAEEDR-------QKKEDEKARREFIKQEYLRRKQ 1221
Cdd:pfam15346   55 LEELEREREAELEEERRKEEEERKKREELERILEENNrkiEEAQRKEAEERlamleeqRRMKEERQRREKEEEEREKREQ 134

                   ....
gi 1622195365 1222 LKLM 1225
Cdd:pfam15346  135 QKIL 138

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 1622195365  1359 GPKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKNKILEEMEKSEANNFLILFRDSGCQFRSLYTYCPEMEEINKLAGI 1438
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1622195365  1439 GPKSITLKMIEGLYKYNSDRKQFSHIPAKTMSASVDAITIHSHLWQTKR 1487
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
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622195365  729 DPTQLLASEMVQLRMKLEEKRRAIEAQKKKVEAAFTRHRQRMGRTAFLTVVKK 781
Cdd:pfam17095    7 SASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59

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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622195365 1158 KRAALLEKRLRREKEnqqRKQQLEAELEQK-KEEARVKAEEDRQKKEDEKARRefiKQEYLRRKQ 1221
Cdd:TIGR02794  117 KQKQAEEAKAKQAAE---AKAKAEAEAERKaKEEAAKQAEEEAKAKAAAEAKK---KAEEAKKKA 175

cell envelope integrity inner membrane protein TolA; Provisional

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622195365 1146 KDDQKGEDDMAMKRAALLEKRLRREKE----NQQRKQQLE----AELEQKK-EEARVKAEEDRQKKEDEKARR 1209
Cdd:PRK09510    83 KKEQQQAEELQQKQAAEQERLKQLEKErlaaQEQKKQAEEaakqAALKQKQaEEAAAKAAAAAKAKAEAEAKR 155

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
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622195365   243 PPVENLLKDSTDGCALAALIHFYCPDLVKleDICLKETMSLADSLYNLQLIQEFCQENLNRCCHFTLEDMI 313
Cdd:smart00033   17 PPVTNFSSDLKDGVALCALLNSLSPGLVD--KKKVAASLSRFKKIENINLALSFAEKLGGKVVLFEPEDLV 85

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622195365 1167 LRREKENQQRKQQLEAELEQKKEEaRVKAEEDRQKKEDEKARREFIKQEYLRR 1219
Cdd:cd22249      7 IREEYEAQLKKLEEERRKEREEEE-KASEELIRKLQEEEERQRKREREEQLKQ 58

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 1622195365  1359 GPKLYKEPSAKSNKHIIQNALAHCCLAGKVNEGQKNKILEEMEKSEANNFLILFRDSGCQFRSLYTYCPEMEEINKLAGI 1438
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1622195365  1439 GPKSITLKMIEGLYKYNSDRKQFSHIPAKTMSASVDAITIHSHLWQTKR 1487
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
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622195365  729 DPTQLLASEMVQLRMKLEEKRRAIEAQKKKVEAAFTRHRQRMGRTAFLTVVKK 781
Cdd:pfam17095    7 SASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59

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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622195365 1158 KRAALLEKRLRREKEnqqRKQQLEAELEQK-KEEARVKAEEDRQKKEDEKARRefiKQEYLRRKQ 1221
Cdd:TIGR02794  117 KQKQAEEAKAKQAAE---AKAKAEAEAERKaKEEAAKQAEEEAKAKAAAEAKK---KAEEAKKKA 175

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622195365 1152 EDDMAMKRAALLEKRLRREKENQQRKQQLEAELEQKKEEARvKAEEDRQKKEDEKARREFIKQEYLRRKQLKLMEDMD-- 1229
Cdd:pfam17380  519 EKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMR-KATEERSRLEAMEREREMMRQIVESEKARAEYEATTpi 597

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1622195365 1230 TVIKP--RPASCKQKKPRPKS-VHRDIMESPKTPVRAPAGSRP 1269
Cdd:pfam17380  598 TTIKPiyRPRISEYQPPDVEShMIRFTTQSPEWATPSPATWNP 640

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622195365 1164 EKRLRREKENQQRKQQLEAELEQ--------------------KKEEARVKAEEDRQKKEDEKARREfiKQEYLRRKQ 1221
Cdd:pfam09756    5 AKKRAKLELKEAKRQQREAEEEEreerekleekreeeykereeREEEAEKEKEEEERKQEEEQERKE--QEEYEKLKS 80

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622195365 1147 DDQKGEDDMAMKRAAllEKRLRREKENQQRKQQLEAELEQKKEEARVKAEEDRQKKEDEKARRE 1210
Cdd:COG3064     40 EEERLAELEAKRQAE--EEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAA 101

MAEBL; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622195365 1011 AEEDKTIDSAKEGCSVKEGglEELPVVEKAIDNEEKTKevgglQVEKKEDNKGKLLESSVSEILSQTVTETVI-VTPNVD 1089
Cdd:PTZ00121  1530 AEEAKKADEAKKAEEKKKA--DELKKAEELKKAEEKKK-----AEEAKKAEEDKNMALRKAEEAKKAEEARIEeVMKLYE 1602

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622195365 1090 SSVEFNADTSKNSSLIEVPLSVLKPLDgevlEEANDGEAGMDNYDEEQKMCcgfffKDDQKGEDDMAMKRAALLEK---- 1165
Cdd:PTZ00121  1603 EEKKMKAEEAKKAEEAKIKAEELKKAE----EEKKKVEQLKKKEAEEKKKA-----EELKKAEEENKIKAAEEAKKaeed 1673

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622195365 1166 -----RLRREKENQQRKqqleAELEQKKEEARVKAEEDRQKKEDEKARREFIKQEYLRRK----QLKLMEDMD 1229
Cdd:PTZ00121  1674 kkkaeEAKKAEEDEKKA----AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKikaeEAKKEAEED 1742

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622195365 1156 AMKRA--ALLEKRLRREKENQQRKQQLEAELEQKKEEARVKAEEDRQKKEDEKARrefiKQEYLRRKQLKLMEDM 1228
Cdd:COG2825     40 EGKAAqkKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSEEERQKKERELQK----KQQELQRKQQEAQQDL 110

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622195365 1159 RAALLEKRLRREKENQQR------KQQLEAELEQKKEEARVKAEEDRQKKEDE---KARREFIKQEY 1216
Cdd:pfam09756   21 REAEEEEREEREKLEEKReeeykeREEREEEAEKEKEEEERKQEEEQERKEQEeyeKLKSQFVVEEE 87

second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622195365  244 PVENLLKDSTDGCALAALIHFYCPDLVKLEDICLKETMS 282
Cdd:cd21224     19 KVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQT 57

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 1622195365 1121 EEANDGEAGMDNYDEEQKmccgfffkddQKGEDDMAMKRAALLEKRLRREKENQ---QRKQQLEAELEQKKEEARVKAEE 1197
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAK----------AKQAAEAKAKAEAEAERKAKEEAAKQaeeEAKAKAAAEAKKKAEEAKKKAEA 177

                           90       100
                   ....*....|....*....|
gi 1622195365 1198 DRQKKED--EKARREFIKQE 1215
Cdd:TIGR02794  178 EAKAKAEaeAKAKAEEAKAK 197

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622195365 1158 KRAALLE--KRLRREKENQQR-KQQLEAELEQKKEEARvKAEEDRQKKEDEKAR 1208
Cdd:pfam20492   56 KRQEAEEekERLEESAEMEAEeKEQLEAELAEAQEEIA-RLEEEVERKEEEARR 108

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622195365 1157 MKRAALLEKRlRREKENQQRKQQLEAELEQKKEEARVKAEedRQKKEDEKARREfikQEYLRRKQLKL 1224
Cdd:pfam15709  374 MREELELEQQ-RRFEEIRLRKQRLEEERQRQEEEERKQRL--QLQAAQERARQQ---QEEFRRKLQEL 435

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622195365 1167 LRREKENQQRKQQLEAELEQKKEEaRVKAEEDRQKKEDEKARREFIKQEYLRR 1219
Cdd:cd22249      7 IREEYEAQLKKLEEERRKEREEEE-KASEELIRKLQEEEERQRKREREEQLKQ 58

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622195365 1168 RREKENQQRKQQLEAELEQKKEEARVKAE---EDRQKKEDEKARREFIKQEYLRRKQLKLMED 1227
Cdd:pfam17380  450 RVRLEEQERQQQVERLRQQEEERKRKKLElekEKRDRKRAEEQRRKILEKELEERKQAMIEEE 512

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622195365 1149 QKGEDDMAMKRAALLEKRLRREKENQQRKQQLEAELE---QKKEEARVKAEEDRQKKEDEKARREfiKQEYLRRKQLKL 1224
Cdd:pfam15709  383 QRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQErarQQQEEFRRKLQELQRKKQQEEAERA--EAEKQRQKELEM 459

Programmed cell death protein 7;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622195365 1164 EKRLRREKENQQRKQQLEAELEQKKE-EARVKAEEDRQKKEDEKARREfikqeylrrKQLKLMEDM 1228
Cdd:pfam16021   76 KKRLRRKRRKEERKEEKKEEQERRAErEAKIDKWRRKQIQEVEEKKRE---------RELKLAADA 132

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622195365  243 PPVENLLKDSTDGCALAALIHFYCPDLVKLEDiclKETMSLADSLYNLQLIQEFCQE-NLNRCCHFTLEDMI 313
Cdd:cd00014     18 VSITDLFESLRDGVLLCKLINKLSPGSIPKIN---KKPKSPFKKRENINLFLNACKKlGLPELDLFEPEDLY 86

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622195365 1159 RAA-LLEKRLRR-EKENQQRKQQLEAELEQKKEEARVKAEEDRQKKEDEKARREFIKQ--EYLRRKQLKLMEDM 1228
Cdd:pfam13868   24 RDAqIAEKKRIKaEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQieEREQKRQEEYEEKL 97

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.

                           10        20        30        40        50        60
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gi 1622195365  243 PPVENLLKDSTDGCALAALIHFYCPDLVKLEDICLKETmslaDSLYNLQLIQEFCQENLN 302
Cdd:pfam00307   22 VRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEF----DKLENINLALDVAEKKLG 77