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Conserved domains on  [gi|767956384|ref|XP_011516576|]
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calmodulin-regulated spectrin-associated protein 1 isoform X5 [Homo sapiens]

Protein Classification

CAMSAP_CH and CAMSAP_CKK domain-containing protein( domain architecture ID 13777712)

protein containing domains CAMSAP_CH, CAMSAP_CC1, UDM1_RNF168, and CAMSAP_CKK

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1264-1392 3.00e-75

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.


:

Pssm-ID: 198119  Cd Length: 129  Bit Score: 245.35  E-value: 3.00e-75
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384   1264 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYYPDTEEIYKLTGT 1343
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 767956384   1344 GPKNITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1392
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 30-113 4.36e-39

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


:

Pssm-ID: 432229  Cd Length: 85  Bit Score: 140.13  E-value: 4.36e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384    30 HLSARQSPYFPLLEDLMRDGSDGAALLAVIHYYCPEQMKLDDICLKEVTSMADSLYNIRLLREFSNEYL-NKCFYLTLED 108
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 767956384   109 MLYAP 113
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 664-722 3.53e-21

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.


:

Pssm-ID: 465344 [Multi-domain]  Cd Length: 59  Bit Score: 88.13  E-value: 3.53e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767956384   664 PSQHGKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 722
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU super family cl38471
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1077-1154 1.87e-09

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.


The actual alignment was detected with superfamily member pfam15346:

Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 57.75  E-value: 1.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1077 EQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVE---LKRDEARRKAEEDRV-------RKEEEKARRELIKQEYL 1146
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 767956384  1147 RRKQQQIL 1154
Cdd:pfam15346  131 KREQQKIL 138
 
Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1264-1392 3.00e-75

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.


Pssm-ID: 198119  Cd Length: 129  Bit Score: 245.35  E-value: 3.00e-75
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384   1264 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYYPDTEEIYKLTGT 1343
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 767956384   1344 GPKNITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1392
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1265-1383 8.72e-74

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.


Pssm-ID: 462558  Cd Length: 119  Bit Score: 240.64  E-value: 8.72e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1265 PKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYYPDTEEIYKLTGTG 1344
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 767956384  1345 PKNITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTI 1383
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 30-113 4.36e-39

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 140.13  E-value: 4.36e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384    30 HLSARQSPYFPLLEDLMRDGSDGAALLAVIHYYCPEQMKLDDICLKEVTSMADSLYNIRLLREFSNEYL-NKCFYLTLED 108
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 767956384   109 MLYAP 113
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 664-722 3.53e-21

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.


Pssm-ID: 465344 [Multi-domain]  Cd Length: 59  Bit Score: 88.13  E-value: 3.53e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767956384   664 PSQHGKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 722
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1077-1154 1.87e-09

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.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 57.75  E-value: 1.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1077 EQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVE---LKRDEARRKAEEDRV-------RKEEEKARRELIKQEYL 1146
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 767956384  1147 RRKQQQIL 1154
Cdd:pfam15346  131 KREQQKIL 138
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1077-1152 2.93e-06

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]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 51.00  E-value: 2.93e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767956384  1077 EQKAEDELAKKRAAFLLKQQRKAEearvRKQQLEAEVELKRDE-ARRKAEEDRVRKEEEKARReliKQEYLRRKQQQ 1152
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAE----AKAKAEAEAERKAKEeAAKQAEEEAKAKAAAEAKK---KAEEAKKKAEA 177
PTZ00121 PTZ00121
MAEBL; Provisional
 1076-1157 2.90e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1076 DEQKAEDELAKKRAAFLLK---QQRKAEEARVRKQQLEAEvELKRDEARRKAEEDRvRKEEEKARRELIKQEYLRRKQQQ 1152
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKaaeAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEK 1563


                  ....*
gi 767956384 1153 ILEEQ 1157
Cdd:PTZ00121 1564 KKAEE 1568
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1075-1157 1.57e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.02  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1075 KDEQKAEDELAKKRAafllKQQRKAEEARVRKQ---------QLEAEVELKRDEARRKAEEDRVRKE------EEKARRE 1139
Cdd:COG2268   203 IAEAEAERETEIAIA----QANREAEEAELEQEreietariaEAEAELAKKKAEERREAETARAEAEaayeiaEANAERE 278

                          90
                  ....*....|....*....
gi 767956384 1140 LIKQEYLRRKQQQI-LEEQ 1157
Cdd:COG2268   279 VQRQLEIAEREREIeLQEK 297
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
 1078-1139 1.04e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; RING finger protein 168 (RNF168) is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. Together with RNF8, RNF168 functions 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. This model corresponds to the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) domain of RNF168, which 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.


Pssm-ID: 409018 [Multi-domain]  Cd Length: 73  Bit Score: 39.07  E-value: 1.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767956384 1078 QKAEDEL----AKKRAafLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRE 1139
Cdd:cd22265     9 QEYEEEIskleAERRA--LEEEENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKEDEELARKL 72
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1073-1156 2.67e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 39.49  E-value: 2.67e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384   1073 FFKDEQKAEDELAKKRAAFLlkqQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQ 1152
Cdd:smart00935   15 AGKAAQKQLEKEFKKRQAEL---EKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91


                    ....
gi 767956384   1153 ILEE 1156
Cdd:smart00935   92 ELQK 95
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 50-128 7.57e-03

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.


Pssm-ID: 409067  Cd Length: 114  Bit Score: 37.66  E-value: 7.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384   50 SDGAALLAVIHYYCPEQMKLDDIclKEVTSMADSLYNIRLLREFSNEYLNKCFyLTLEDmlyaplVLKPN---VMVFIAE 126
Cdd:cd21218    41 KDGEVYALLLHSLAPELCDKELV--LEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPED------IVSGNprlNLAFVAT 111


                  ..
gi 767956384  127 LF 128
Cdd:cd21218   112 LF 113
 
Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1264-1392 3.00e-75

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.


Pssm-ID: 198119  Cd Length: 129  Bit Score: 245.35  E-value: 3.00e-75
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384   1264 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYYPDTEEIYKLTGT 1343
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 767956384   1344 GPKNITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1392
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1265-1383 8.72e-74

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.


Pssm-ID: 462558  Cd Length: 119  Bit Score: 240.64  E-value: 8.72e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1265 PKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYYPDTEEIYKLTGTG 1344
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 767956384  1345 PKNITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTI 1383
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 30-113 4.36e-39

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 140.13  E-value: 4.36e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384    30 HLSARQSPYFPLLEDLMRDGSDGAALLAVIHYYCPEQMKLDDICLKEVTSMADSLYNIRLLREFSNEYL-NKCFYLTLED 108
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 767956384   109 MLYAP 113
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 664-722 3.53e-21

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.


Pssm-ID: 465344 [Multi-domain]  Cd Length: 59  Bit Score: 88.13  E-value: 3.53e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 767956384   664 PSQHGKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 722
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1077-1154 1.87e-09

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.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 57.75  E-value: 1.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1077 EQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVE---LKRDEARRKAEEDRV-------RKEEEKARRELIKQEYL 1146
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 767956384  1147 RRKQQQIL 1154
Cdd:pfam15346  131 KREQQKIL 138
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 1085-1159 9.60e-08

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


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 53.51  E-value: 9.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1085 AKKRAAFLLKQQRKA---------EEARVRKQQLEAEV---ELKRDEARRKAEEDRVRKEEEKARREliKQEYLRRKQQQ 1152
Cdd:pfam09756    5 AKKRAKLELKEAKRQqreaeeeerEEREKLEEKREEEYkerEEREEEAEKEKEEEERKQEEEQERKE--QEEYEKLKSQF 82


                   ....*..
gi 767956384  1153 ILEEQGL 1159
Cdd:pfam09756   83 VVEEEGT 89
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1075-1155 7.37e-07

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.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 53.42  E-value: 7.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1075 KDEQKAEDELAKK-RAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARR-----KAEEDRVRKEEEKARRELikQEYLRR 1148
Cdd:pfam15709  361 RRLQQEQLERAEKmREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKqrlqlQAAQERARQQQEEFRRKL--QELQRK 438


                   ....*..
gi 767956384  1149 KQQQILE 1155
Cdd:pfam15709  439 KQQEEAE 445
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1077-1152 2.93e-06

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]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 51.00  E-value: 2.93e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767956384  1077 EQKAEDELAKKRAAFLLKQQRKAEearvRKQQLEAEVELKRDE-ARRKAEEDRVRKEEEKARReliKQEYLRRKQQQ 1152
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAE----AKAKAEAEAERKAKEeAAKQAEEEAKAKAAAEAKK---KAEEAKKKAEA 177
PTZ00121 PTZ00121
MAEBL; Provisional
 1076-1157 2.90e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1076 DEQKAEDELAKKRAAFLLK---QQRKAEEARVRKQQLEAEvELKRDEARRKAEEDRvRKEEEKARRELIKQEYLRRKQQQ 1152
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKaaeAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEK 1563


                  ....*
gi 767956384 1153 ILEEQ 1157
Cdd:PTZ00121 1564 KKAEE 1568
PTZ00121 PTZ00121
MAEBL; Provisional
 1076-1156 1.50e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1076 DEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEvELKRDEARRKAEEdrVRKEEEKARRELIKQEYLRRKQQQILE 1155
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEE--AKKAEEDKNMALRKAEEAKKAEEARIE 1595


                  .
gi 767956384 1156 E 1156
Cdd:PTZ00121 1596 E 1596
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1075-1157 1.57e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.02  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1075 KDEQKAEDELAKKRAafllKQQRKAEEARVRKQ---------QLEAEVELKRDEARRKAEEDRVRKE------EEKARRE 1139
Cdd:COG2268   203 IAEAEAERETEIAIA----QANREAEEAELEQEreietariaEAEAELAKKKAEERREAETARAEAEaayeiaEANAERE 278

                          90
                  ....*....|....*....
gi 767956384 1140 LIKQEYLRRKQQQI-LEEQ 1157
Cdd:COG2268   279 VQRQLEIAEREREIeLQEK 297
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1077-1157 2.37e-04

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.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.91  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1077 EQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEE-EKARRELIKQEYLRRKQQQILE 1155
Cdd:pfam13868  146 EKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErDELRAKLYQEEQERKERQKERE 225


                   ..
gi 767956384  1156 EQ 1157
Cdd:pfam13868  226 EA 227
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1094-1157 2.64e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 42.72  E-value: 2.64e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767956384  1094 KQQRKAEEARVRKQQL---EAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQILEEQ 1157
Cdd:pfam05672   33 ERLEKEEEERLRKEELrrrAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERL 99
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1078-1155 2.80e-04

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]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.84  E-value: 2.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1078 QKAEDELAKKRAAFLLKQ-----QRKAEEARVRKQQLEAevELKRDEARRKAEEDRVRKEE--EKARRELIKQEYLRRKQ 1150
Cdd:TIGR02794  126 AKQAAEAKAKAEAEAERKakeeaAKQAEEEAKAKAAAEA--KKKAEEAKKKAEAEAKAKAEaeAKAKAEEAKAKAEAAKA 203


                   ....*
gi 767956384  1151 QQILE 1155
Cdd:TIGR02794  204 KAAAE 208
PRK12704 PRK12704
phosphodiesterase; Provisional
 1069-1157 2.85e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.15  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1069 GVGFFF---KDEQKAEDelAKKRAAFLLKQQRKA-------------EEARVRKQQLEAEV-----ELKRDEARRKAEED 1127
Cdd:PRK12704   19 VIGYFVrkkIAEAKIKE--AEEEAKRILEEAKKEaeaikkealleakEEIHKLRNEFEKELrerrnELQKLEKRLLQKEE 96

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767956384 1128 RVRKEEE---KARRELIKQEYLRRKQQQILEEQ 1157
Cdd:PRK12704   97 NLDRKLElleKREEELEKKEKELEQKQQELEKK 129
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1076-1156 3.31e-04

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.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 42.73  E-value: 3.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1076 DEQKAEDELAKKRAAFLLKqqRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELI----KQEYLRRKQQ 1151
Cdd:pfam15346    4 ESKLLEEETARRVEEAVAK--RVEEELEKRKDEIEAEVERRVEEARKIMEKQVLEELEREREAELEeerrKEEEERKKRE 81


                   ....*...
gi 767956384  1152 Q---ILEE 1156
Cdd:pfam15346   82 ElerILEE 89
PTZ00121 PTZ00121
MAEBL; Provisional
 1075-1153 4.48e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 4.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767956384 1075 KDEQKAEDELAKKRAAfllKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEdrVRKEEEKARRELIKQEYLRRKQQQI 1153
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAE---EAKKKADEAKKAAEAKKKADEAKKAEEAKKADE--AKKAEEAKKADEAKKAEEKKKADEL 1551
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 1081-1149 5.07e-04

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.


Pssm-ID: 463442 [Multi-domain]  Cd Length: 264  Bit Score: 43.43  E-value: 5.07e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767956384  1081 EDELAKKRAAFLLKQQRKAEEARVRKQQleaEVELKRDEARRKAEedrvRKEEEKARRELiKQEYLRRK 1149
Cdd:pfam12037  106 QDELARKRYQDQLEAQRRRNEELLRKQE---ESVAKQEAMRIQAQ----RRQTEEHEAEL-RRETERAK 166
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 1075-1156 5.27e-04

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 41.53  E-value: 5.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1075 KDEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVelkRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQIL 1154
Cdd:pfam00430   36 ADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENA---KKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRAL 112


                   ..
gi 767956384  1155 EE 1156
Cdd:pfam00430  113 AE 114
PTZ00121 PTZ00121
MAEBL; Provisional
 1075-1152 6.33e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 6.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1075 KDEQKAEDELAKKRAAFLLKQ---QRKAEEARVRKQQLE--AEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRK 1149
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKAdeaKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452


                  ...
gi 767956384 1150 QQQ 1152
Cdd:PTZ00121 1453 AEE 1455
PTZ00121 PTZ00121
MAEBL; Provisional
 1076-1157 6.95e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 6.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1076 DEQKAEDELAKKRAAFLlkqQRKAEEARVRKQQLEAEVELKRDE---ARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQ 1152
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAA---KKKAEEAKKAAEAAKAEAEAAADEaeaAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394


                  ....*
gi 767956384 1153 ILEEQ 1157
Cdd:PTZ00121 1395 EAKKK 1399
Caldesmon pfam02029
Caldesmon;
1060-1153 7.04e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 44.09  E-value: 7.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1060 LVSEGDQKPGVGFFFKDEQKAEDELAKKRAAFLLKQQRKAEEA----RVRKQQLEAEVEL-----KRDEARRKAEEDRVR 1130
Cdd:pfam02029  220 KVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESeefeKLRQKQQEAELELeelkkKREERRKLLEEEEQR 299

                           90       100
                   ....*....|....*....|...
gi 767956384  1131 KEEEKARRELIKQEYLRRKQQQI 1153
Cdd:pfam02029  300 RKQEEAERKLREEEEKRRMKEEI 322
PTZ00121 PTZ00121
MAEBL; Provisional
 1062-1152 7.82e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 7.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1062 SEGDQKPGVGFFFKDEQKAEDELAKKRAafllKQQRKAEEARVRkqqleAEVELKRDEARRKAEEDRVRKEEEKARRELI 1141
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKA----EEKKKADEAKKK-----AEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470

                          90
                  ....*....|.
gi 767956384 1142 KQEYLRRKQQQ 1152
Cdd:PTZ00121 1471 KADEAKKKAEE 1481
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1075-1157 8.18e-04

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]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.30  E-value: 8.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1075 KDEQKAEDELAKK--RAAFLLKQQRKAEEARVR--KQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQeylRRKQ 1150
Cdd:TIGR02794   60 KPAAKKEQERQKKleQQAEEAEKQRAAEQARQKelEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEA---KAKA 136


                   ....*..
gi 767956384  1151 QQILEEQ 1157
Cdd:TIGR02794  137 EAEAERK 143
PTZ00121 PTZ00121
MAEBL; Provisional
 1075-1152 8.22e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 8.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1075 KDEQKAEDELAKKRAafllKQQRKAEEARVRKQQL---EAEVELKRDEARRKAEEDRVRKEEE--KARRELIKQEYLRRK 1149
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKA----EELKKAEEEKKKVEQLkkkEAEEKKKAEELKKAEEENKIKAAEEakKAEEDKKKAEEAKKA 1683


                  ...
gi 767956384 1150 QQQ 1152
Cdd:PTZ00121 1684 EED 1686
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1094-1156 8.53e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.96  E-value: 8.53e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767956384  1094 KQQRKAEEARVRKQQLEAEV----ELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQILEE 1156
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEIsrmrELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
PTZ00121 PTZ00121
MAEBL; Provisional
 1076-1152 9.90e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 9.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767956384 1076 DEQKAEDELAKKRAafllKQQRKAEEARVRKQQLEAEVELKR--DEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQ 1152
Cdd:PTZ00121 1394 DEAKKKAEEDKKKA----DELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
PTZ00121 PTZ00121
MAEBL; Provisional
 1076-1157 9.98e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 9.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1076 DEQKAEDELAKKRAafllKQQRKAEEAR----VRKQQLEaEVELKRDEARRKAEEDRVRKEEEK-----ARRELIKQEYL 1146
Cdd:PTZ00121 1699 EEAKKAEELKKKEA----EEKKKAEELKkaeeENKIKAE-EAKKEAEEDKKKAEEAKKDEEEKKkiahlKKEEEKKAEEI 1773

                          90
                  ....*....|.
gi 767956384 1147 RRKQQQILEEQ 1157
Cdd:PTZ00121 1774 RKEKEAVIEEE 1784
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
 1078-1139 1.04e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; RING finger protein 168 (RNF168) is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. Together with RNF8, RNF168 functions 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. This model corresponds to the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) domain of RNF168, which 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.


Pssm-ID: 409018 [Multi-domain]  Cd Length: 73  Bit Score: 39.07  E-value: 1.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767956384 1078 QKAEDEL----AKKRAafLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRE 1139
Cdd:cd22265     9 QEYEEEIskleAERRA--LEEEENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKEDEELARKL 72
PTZ00121 PTZ00121
MAEBL; Provisional
 1076-1153 1.05e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767956384 1076 DEQKAEDELAKKraafllKQQRKAEEARVRKQQLEAEvELKRDEARRKAEEDRVRKEEEKARRELIKQ-EYLRRKQQQI 1153
Cdd:PTZ00121 1339 EEAKKAAEAAKA------EAEAAADEAEAAEEKAEAA-EKKKEEAKKKADAAKKKAEEKKKADEAKKKaEEDKKKADEL 1410
PTZ00121 PTZ00121
MAEBL; Provisional
 1075-1157 1.21e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1075 KDEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQIL 1154
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423


                  ...
gi 767956384 1155 EEQ 1157
Cdd:PTZ00121 1424 KKK 1426
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 1076-1157 1.54e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 40.83  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1076 DEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKE----EEKARRELIKQEYLRRKQQ 1151
Cdd:pfam11600   12 EKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEkerrEKKEKDEKEKAEKLRLKEE 91


                   ....*.
gi 767956384  1152 QILEEQ 1157
Cdd:pfam11600   92 KRKEKQ 97
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1086-1157 1.60e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 40.11  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1086 KKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEE--DRVRKEEEKARRELIKQ------EYLRRKQQQILEEQ 1157
Cdd:cd06503    29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiiEEARKEAEKIKEEILAEakeeaeRILEQAKAEIEQEK 108
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1074-1156 1.65e-03

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.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1074 FKDEQKAEDELAKKRAAFLLKQQRKAEEARVRK---------QQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQE 1144
Cdd:pfam13868  255 EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKrlehrreleKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEE 334

                           90
                   ....*....|..
gi 767956384  1145 ylrrkQQQILEE 1156
Cdd:pfam13868  335 -----RQKKLKE 341
PTZ00121 PTZ00121
MAEBL; Provisional
 1075-1157 1.65e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1075 KDEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEvELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQIL 1154
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334


                  ...
gi 767956384 1155 EEQ 1157
Cdd:PTZ00121 1335 KKK 1337
PTZ00121 PTZ00121
MAEBL; Provisional
 1075-1157 1.80e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1075 KDEQKAEDELAKKRAAFLLKQQRKAEEAR-VRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQI 1153
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638


                  ....
gi 767956384 1154 LEEQ 1157
Cdd:PTZ00121 1639 KKKE 1642
PTZ00121 PTZ00121
MAEBL; Provisional
 1075-1157 2.06e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1075 KDEQKAEDELAKKRAAFLLK--QQRKAEEA-RVRKQQL---------EAEVELKRDEARRKAEEDRVRKEEEKARRELIK 1142
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKaeELKKAEEEnKIKAAEEakkaeedkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708

                          90
                  ....*....|....*..
gi 767956384 1143 Q--EYLRRKQQQILEEQ 1157
Cdd:PTZ00121 1709 KkeAEEKKKAEELKKAE 1725
PTZ00121 PTZ00121
MAEBL; Provisional
 1075-1152 2.40e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767956384 1075 KDEQKAEDELAKKRAafllKQQRKAEEARVRkqqleAEVELKRDEARRKAEEDRVRKEE-EKARRELIKQEYLRRKQQQ 1152
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKA----EEAKKADEAKKK-----AEEAKKADEAKKKAEEAKKKADEaKKAAEAKKKADEAKKAEEA 1521
PTZ00121 PTZ00121
MAEBL; Provisional
 1075-1153 2.65e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1075 KDEQKAEDELAKKRAAFLLKQQ----RKAEEarVRKQqlEAEVELKRDEARRKAEEDR-----VRKEEE---KARRELIK 1142
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEaeekKKAEE--LKKA--EEENKIKAAEEAKKAEEDKkkaeeAKKAEEdekKAAEALKK 1696

                          90
                  ....*....|.
gi 767956384 1143 QEYLRRKQQQI 1153
Cdd:PTZ00121 1697 EAEEAKKAEEL 1707
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1073-1156 2.67e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 39.49  E-value: 2.67e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384   1073 FFKDEQKAEDELAKKRAAFLlkqQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQ 1152
Cdd:smart00935   15 AGKAAQKQLEKEFKKRQAEL---EKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91


                    ....
gi 767956384   1153 ILEE 1156
Cdd:smart00935   92 ELQK 95
PTZ00121 PTZ00121
MAEBL; Provisional
 1058-1157 2.74e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1058 ADLVSEGDQKPGVGFFFKDEQKAEDELAKKRAafllKQQRKAEEARVRKQqleaEVELKRDEARRKAEEDR-----VRKE 1132
Cdd:PTZ00121 1280 ADELKKAEEKKKADEAKKAEEKKKADEAKKKA----EEAKKADEAKKKAE----EAKKKADAAKKKAEEAKkaaeaAKAE 1351

                          90       100
                  ....*....|....*....|....*
gi 767956384 1133 EEKARRELIKQEYLRRKQQQILEEQ 1157
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEA 1376
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 1075-1156 2.76e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 39.09  E-value: 2.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1075 KDEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEE-----EKARREL--IKQEylR 1147
Cdd:pfam13863   19 REEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEkekeiKKLTAQIeeLKSE--I 96


                   ....*....
gi 767956384  1148 RKQQQILEE 1156
Cdd:pfam13863   97 SKLEEKLEE 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1077-1157 2.79e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1077 EQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRK------EEEKARRELIKQEYLRRKQ 1150
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEElrleleELELELEEAQAEEYELLAE 296


                  ....*..
gi 767956384 1151 QQILEEQ 1157
Cdd:COG1196   297 LARLEQD 303
PTZ00121 PTZ00121
MAEBL; Provisional
 1078-1157 2.81e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1078 QKAEDeLAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRvRKEEEKARRELIKQEYLR-----RKQQQ 1152
Cdd:PTZ00121 1194 RKAED-ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK-KAEEERNNEEIRKFEEARmahfaRRQAA 1271


                  ....*
gi 767956384 1153 ILEEQ 1157
Cdd:PTZ00121 1272 IKAEE 1276
PTZ00121 PTZ00121
MAEBL; Provisional
 1075-1152 2.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767956384 1075 KDEQKAEDELAKKRAafllKQQRKAEEARVRkqqleAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQ 1152
Cdd:PTZ00121 1426 KAEEKKKADEAKKKA----EEAKKADEAKKK-----AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
PTZ00121 PTZ00121
MAEBL; Provisional
 1075-1157 3.11e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1075 KDEQKAEDELAKK-RAAFLLKQQRKAEEARVRK----QQLEAEVELKRDEARRKAEEDRvRKEEekarrELIKQEYLRRK 1149
Cdd:PTZ00121 1685 EDEKKAAEALKKEaEEAKKAEELKKKEAEEKKKaeelKKAEEENKIKAEEAKKEAEEDK-KKAE-----EAKKDEEEKKK 1758


                  ....*...
gi 767956384 1150 QQQILEEQ 1157
Cdd:PTZ00121 1759 IAHLKKEE 1766
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1076-1157 3.52e-03

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.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 3.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1076 DEQKAEDELAKKRAA--FLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEY---LRRKQ 1150
Cdd:pfam13868  114 DQAEAEEKLEKQRQLreEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREiarLRAQQ 193


                   ....*..
gi 767956384  1151 QQILEEQ 1157
Cdd:pfam13868  194 EKAQDEK 200
PTZ00121 PTZ00121
MAEBL; Provisional
 1076-1148 4.14e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 4.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767956384 1076 DEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRvRKEEEKARRELIKQEYLRR 1148
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR-KAEDAKRVEIARKAEDARK 1165
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1077-1151 4.17e-03

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]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 4.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1077 EQKAEDELAKKRAAfllKQQRKAEEARVR-----KQQLEAEVELKRDEARRKAEEDRVRKEEE---KARRELIKQEYLRR 1148
Cdd:TIGR02794  149 AKQAEEEAKAKAAA---EAKKKAEEAKKKaeaeaKAKAEAEAKAKAEEAKAKAEAAKAKAAAEaaaKAEAEAAAAAAAEA 225


                   ...
gi 767956384  1149 KQQ 1151
Cdd:TIGR02794  226 ERK 228
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1078-1137 4.17e-03

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 41.56  E-value: 4.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1078 QKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKAR 1137
Cdd:COG3064    83 EKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERK 142
PTZ00121 PTZ00121
MAEBL; Provisional
 1062-1152 5.03e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 5.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1062 SEGDQKPGVGFFFKDEQKAEdELAKKRAAFLLKQQRKAEEARvRKQQLEAEVELKRDEARRKAEEDR----VRKEEEKAR 1137
Cdd:PTZ00121 1148 AEDAKRVEIARKAEDARKAE-EARKAEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAARKAEEERkaeeARKAEDAKK 1225

                          90
                  ....*....|....*.
gi 767956384 1138 RELIKQ-EYLRRKQQQ 1152
Cdd:PTZ00121 1226 AEAVKKaEEAKKDAEE 1241
PTZ00121 PTZ00121
MAEBL; Provisional
 1075-1153 5.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1075 KDEQKAEDELAKKRAafllKQQRKAEEARVRKQQLEAEVELKRD-EARRKAEEDRVRKEEEKAR-RELIKQEYLRRKQQQ 1152
Cdd:PTZ00121 1439 KAEEAKKADEAKKKA----EEAKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKaDEAKKAAEAKKKADE 1514


                  .
gi 767956384 1153 I 1153
Cdd:PTZ00121 1515 A 1515
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1075-1152 5.82e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.26  E-value: 5.82e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767956384  1075 KDEQ-KAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQ 1152
Cdd:pfam17380  390 KNERvRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ 468
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1078-1157 6.83e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 6.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384 1078 QKAEDELAKKRAAfLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEE-DRVRKEEEKARRELIKQEY-LRRKQQQILE 1155
Cdd:COG1196   235 RELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELELElEEAQAEEYELLAELARLEQdIARLEERRRE 313


                  ..
gi 767956384 1156 EQ 1157
Cdd:COG1196   314 LE 315
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 50-128 7.57e-03

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.


Pssm-ID: 409067  Cd Length: 114  Bit Score: 37.66  E-value: 7.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384   50 SDGAALLAVIHYYCPEQMKLDDIclKEVTSMADSLYNIRLLREFSNEYLNKCFyLTLEDmlyaplVLKPN---VMVFIAE 126
Cdd:cd21218    41 KDGEVYALLLHSLAPELCDKELV--LEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPED------IVSGNprlNLAFVAT 111


                  ..
gi 767956384  127 LF 128
Cdd:cd21218   112 LF 113
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1075-1139 7.92e-03

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.41  E-value: 7.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767956384 1075 KDEQKAEDELAKKRAAflLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRE 1139
Cdd:COG3064    48 EAKRQAEEEAREAKAE--AEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAA 110
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1077-1139 8.65e-03

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]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.21  E-value: 8.65e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767956384  1077 EQKAEDELAKKRAAfllkQQRKaeEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRE 1139
Cdd:TIGR02794   95 EQRAAAEKAAKQAE----QAAK--QAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQ 151
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1076-1159 8.78e-03

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: 40.81  E-value: 8.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767956384  1076 DEQKAEDELAKKRAAfLLKQQRKAEE----ARVRKQQLEA---EVELKRDEARRKAEEDRVRKEEEKARRELIKQEyLRR 1148
Cdd:TIGR02168  863 ELEELIEELESELEA-LLNERASLEEalalLRSELEELSEelrELESKRSELRRELEELREKLAQLELRLEGLEVR-IDN 940

                           90
                   ....*....|.
gi 767956384  1149 KQQQILEEQGL 1159
Cdd:TIGR02168  941 LQERLSEEYSL 951
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 1093-1138 9.93e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 39.86  E-value: 9.93e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767956384  1093 LKQQRKAEEARVRKQQLEAEVE---LKRDEARRKAEEDRV--------RKEEEKARR 1138
Cdd:pfam07946  262 AKKTREEEIEKIKKAAEEERAEeaqEKKEEAKKKEREEKLaklspeeqRKYEEKERK 318
 
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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