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Conserved domains on  [gi|186659512|ref|NP_056262|]
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calmodulin-regulated spectrin-associated protein 1 isoform 1 [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 ...
 1463-1591 2.01e-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: 246.12  E-value: 2.01e-75
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512   1463 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYYPDTEEIYKLTGT 1542
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 186659512   1543 GPKNITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1591
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 229-312 4.66e-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: 4.66e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512   229 HLSARQSPYFPLLEDLMRDGSDGAALLAVIHYYCPEQMKLDDICLKEVTSMADSLYNIRLLREFSNEYL-NKCFYLTLED 307
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 186659512   308 MLYAP 312
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 863-921 2.08e-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: 88.90  E-value: 2.08e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 186659512   863 PSQHGKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 921
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU super family cl38471
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1276-1353 7.90e-10

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: 58.91  E-value: 7.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1276 EQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVE---LKRDEARRKAEEDRV-------RKEEEKARRELIKQEYL 1345
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 186659512  1346 RRKQQQIL 1353
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 ...
 1463-1591 2.01e-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: 246.12  E-value: 2.01e-75
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512   1463 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYYPDTEEIYKLTGT 1542
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 186659512   1543 GPKNITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1591
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1464-1582 7.61e-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: 241.03  E-value: 7.61e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1464 PKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYYPDTEEIYKLTGTG 1543
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 186659512  1544 PKNITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTI 1582
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 229-312 4.66e-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: 4.66e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512   229 HLSARQSPYFPLLEDLMRDGSDGAALLAVIHYYCPEQMKLDDICLKEVTSMADSLYNIRLLREFSNEYL-NKCFYLTLED 307
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 186659512   308 MLYAP 312
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 863-921 2.08e-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: 88.90  E-value: 2.08e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 186659512   863 PSQHGKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 921
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1276-1353 7.90e-10

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: 58.91  E-value: 7.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1276 EQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVE---LKRDEARRKAEEDRV-------RKEEEKARRELIKQEYL 1345
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 186659512  1346 RRKQQQIL 1353
Cdd:pfam15346  131 KREQQKIL 138
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1276-1351 3.52e-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: 3.52e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186659512  1276 EQKAEDELAKKRAAFLLKQQRKAEearvRKQQLEAEVELKRDE-ARRKAEEDRVRKEEEKARReliKQEYLRRKQQQ 1351
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAE----AKAKAEAEAERKAKEeAAKQAEEEAKAKAAAEAKK---KAEEAKKKAEA 177
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1356 1.83e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1275 DEQKAEDELAKKRAAFLLK---QQRKAEEARVRKQQLEAEvELKRDEARRKAEEDRvRKEEEKARRELIKQEYLRRKQQQ 1351
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKaaeAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEK 1563


                  ....*
gi 186659512 1352 ILEEQ 1356
Cdd:PTZ00121 1564 KKAEE 1568
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1274-1352 2.30e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 45.63  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1274 KDEQKAEDELAKKRAafllKQQRKAEEARVRKQ---------QLEAEVELKRDEARRKAEEDRVRKE------EEKARRE 1338
Cdd:COG2268   203 IAEAEAERETEIAIA----QANREAEEAELEQEreietariaEAEAELAKKKAEERREAETARAEAEaayeiaEANAERE 278

                          90
                  ....*....|....
gi 186659512 1339 LIKQEYLRRKQQQI 1352
Cdd:COG2268   279 VQRQLEIAEREREI 292
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
 1277-1338 5.05e-04

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: 40.23  E-value: 5.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186659512 1277 QKAEDEL----AKKRAafLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRE 1338
Cdd:cd22265     9 QEYEEEIskleAERRA--LEEEENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKEDEELARKL 72
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1272-1355 3.82e-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: 3.82e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512   1272 FFKDEQKAEDELAKKRAAFLlkqQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQ 1351
Cdd:smart00935   15 AGKAAQKQLEKEFKKRQAEL---EKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91


                    ....
gi 186659512   1352 ILEE 1355
Cdd:smart00935   92 ELQK 95
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 249-327 8.68e-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: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  249 SDGAALLAVIHYYCPEQMKLDDIclKEVTSMADSLYNIRLLREFSNEYLNKCFyLTLEDmlyaplVLKPN---VMVFIAE 325
Cdd:cd21218    41 KDGEVYALLLHSLAPELCDKELV--LEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPED------IVSGNprlNLAFVAT 111


                  ..
gi 186659512  326 LF 327
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 ...
 1463-1591 2.01e-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: 246.12  E-value: 2.01e-75
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512   1463 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYYPDTEEIYKLTGT 1542
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 186659512   1543 GPKNITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1591
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1464-1582 7.61e-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: 241.03  E-value: 7.61e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1464 PKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYYPDTEEIYKLTGTG 1543
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 186659512  1544 PKNITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTI 1582
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 229-312 4.66e-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: 4.66e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512   229 HLSARQSPYFPLLEDLMRDGSDGAALLAVIHYYCPEQMKLDDICLKEVTSMADSLYNIRLLREFSNEYL-NKCFYLTLED 307
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 186659512   308 MLYAP 312
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 863-921 2.08e-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: 88.90  E-value: 2.08e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 186659512   863 PSQHGKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 921
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1276-1353 7.90e-10

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: 58.91  E-value: 7.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1276 EQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVE---LKRDEARRKAEEDRV-------RKEEEKARRELIKQEYL 1345
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 186659512  1346 RRKQQQIL 1353
Cdd:pfam15346  131 KREQQKIL 138
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 1284-1358 5.61e-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: 54.66  E-value: 5.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1284 AKKRAAFLLKQQRKA---------EEARVRKQQLEAEV---ELKRDEARRKAEEDRVRKEEEKARREliKQEYLRRKQQQ 1351
Cdd:pfam09756    5 AKKRAKLELKEAKRQqreaeeeerEEREKLEEKREEEYkerEEREEEAEKEKEEEERKQEEEQERKE--QEEYEKLKSQF 82


                   ....*..
gi 186659512  1352 ILEEQGL 1358
Cdd:pfam09756   83 VVEEEGT 89
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1274-1354 2.89e-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: 54.96  E-value: 2.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1274 KDEQKAEDELAKK-RAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARR-----KAEEDRVRKEEEKARRELikQEYLRR 1347
Cdd:pfam15709  361 RRLQQEQLERAEKmREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKqrlqlQAAQERARQQQEEFRRKL--QELQRK 438


                   ....*..
gi 186659512  1348 KQQQILE 1354
Cdd:pfam15709  439 KQQEEAE 445
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1276-1351 3.52e-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: 3.52e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186659512  1276 EQKAEDELAKKRAAFLLKQQRKAEearvRKQQLEAEVELKRDE-ARRKAEEDRVRKEEEKARReliKQEYLRRKQQQ 1351
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAE----AKAKAEAEAERKAKEeAAKQAEEEAKAKAAAEAKK---KAEEAKKKAEA 177
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1356 1.83e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1275 DEQKAEDELAKKRAAFLLK---QQRKAEEARVRKQQLEAEvELKRDEARRKAEEDRvRKEEEKARRELIKQEYLRRKQQQ 1351
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKaaeAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEK 1563


                  ....*
gi 186659512 1352 ILEEQ 1356
Cdd:PTZ00121 1564 KKAEE 1568
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1355 1.07e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1275 DEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEvELKRDEARRKAEEdrVRKEEEKARRELIKQEYLRRKQQQILE 1354
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEE--AKKAEEDKNMALRKAEEAKKAEEARIE 1595


                  .
gi 186659512 1355 E 1355
Cdd:PTZ00121 1596 E 1596
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1293-1356 1.26e-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: 43.88  E-value: 1.26e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186659512  1293 KQQRKAEEARVRKQQL---EAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQILEEQ 1356
Cdd:pfam05672   33 ERLEKEEEERLRKEELrrrAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERL 99
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1275-1355 1.81e-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: 43.50  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1275 DEQKAEDELAKKRAAFLLKqqRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELI----KQEYLRRKQQ 1350
Cdd:pfam15346    4 ESKLLEEETARRVEEAVAK--RVEEELEKRKDEIEAEVERRVEEARKIMEKQVLEELEREREAELEeerrKEEEERKKRE 81


                   ....*...
gi 186659512  1351 Q---ILEE 1355
Cdd:pfam15346   82 ElerILEE 89
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1276-1356 1.94e-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: 45.68  E-value: 1.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1276 EQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEE-EKARRELIKQEYLRRKQQQILE 1354
Cdd:pfam13868  146 EKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErDELRAKLYQEEQERKERQKERE 225


                   ..
gi 186659512  1355 EQ 1356
Cdd:pfam13868  226 EA 227
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1274-1352 2.30e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 45.63  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1274 KDEQKAEDELAKKRAafllKQQRKAEEARVRKQ---------QLEAEVELKRDEARRKAEEDRVRKE------EEKARRE 1338
Cdd:COG2268   203 IAEAEAERETEIAIA----QANREAEEAELEQEreietariaEAEAELAKKKAEERREAETARAEAEaayeiaEANAERE 278

                          90
                  ....*....|....
gi 186659512 1339 LIKQEYLRRKQQQI 1352
Cdd:COG2268   279 VQRQLEIAEREREI 292
PTZ00121 PTZ00121
MAEBL; Provisional
 1274-1352 3.12e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 3.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186659512 1274 KDEQKAEDELAKKRAAfllKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEdrVRKEEEKARRELIKQEYLRRKQQQI 1352
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAE---EAKKKADEAKKAAEAKKKADEAKKAEEAKKADE--AKKAEEAKKADEAKKAEEKKKADEL 1551
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1277-1354 3.28e-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: 3.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1277 QKAEDELAKKRAAFLLKQ-----QRKAEEARVRKQQLEAevELKRDEARRKAEEDRVRKEE--EKARRELIKQEYLRRKQ 1349
Cdd:TIGR02794  126 AKQAAEAKAKAEAEAERKakeeaAKQAEEEAKAKAAAEA--KKKAEEAKKKAEAEAKAKAEaeAKAKAEEAKAKAEAAKA 203


                   ....*
gi 186659512  1350 QQILE 1354
Cdd:TIGR02794  204 KAAAE 208
PRK12704 PRK12704
phosphodiesterase; Provisional
 1268-1356 3.39e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.15  E-value: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1268 GVGFFF---KDEQKAEDelAKKRAAFLLKQQRKA-------------EEARVRKQQLEAEV-----ELKRDEARRKAEED 1326
Cdd:PRK12704   19 VIGYFVrkkIAEAKIKE--AEEEAKRILEEAKKEaeaikkealleakEEIHKLRNEFEKELrerrnELQKLEKRLLQKEE 96

                          90       100       110
                  ....*....|....*....|....*....|...
gi 186659512 1327 RVRKEEE---KARRELIKQEYLRRKQQQILEEQ 1356
Cdd:PRK12704   97 NLDRKLElleKREEELEKKEKELEQKQQELEKK 129
Caldesmon pfam02029
Caldesmon;
1259-1352 3.75e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 44.86  E-value: 3.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1259 LVSEGDQKPGVGFFFKDEQKAEDELAKKRAAFLLKQQRKAEEA----RVRKQQLEAEVEL-----KRDEARRKAEEDRVR 1329
Cdd:pfam02029  220 KVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESeefeKLRQKQQEAELELeelkkKREERRKLLEEEEQR 299

                           90       100
                   ....*....|....*....|...
gi 186659512  1330 KEEEKARRELIKQEYLRRKQQQI 1352
Cdd:pfam02029  300 RKQEEAERKLREEEEKRRMKEEI 322
PTZ00121 PTZ00121
MAEBL; Provisional
 1274-1351 4.26e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 4.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1274 KDEQKAEDELAKKRAAFLLKQ---QRKAEEARVRKQQLE--AEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRK 1348
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKAdeaKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452


                  ...
gi 186659512 1349 QQQ 1351
Cdd:PTZ00121 1453 AEE 1455
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 1280-1348 4.65e-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: 43.82  E-value: 4.65e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186659512  1280 EDELAKKRAAFLLKQQRKAEEARVRKQQleaEVELKRDEARRKAEedrvRKEEEKARRELiKQEYLRRK 1348
Cdd:pfam12037  106 QDELARKRYQDQLEAQRRRNEELLRKQE---ESVAKQEAMRIQAQ----RRQTEEHEAEL-RRETERAK 166
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1356 4.95e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1275 DEQKAEDELAKKRAAFLlkqQRKAEEARVRKQQLEAEVELKRDE---ARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQ 1351
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAA---KKKAEEAKKAAEAAKAEAEAAADEaeaAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394


                  ....*
gi 186659512 1352 ILEEQ 1356
Cdd:PTZ00121 1395 EAKKK 1399
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
 1277-1338 5.05e-04

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: 40.23  E-value: 5.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186659512 1277 QKAEDEL----AKKRAafLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRE 1338
Cdd:cd22265     9 QEYEEEIskleAERRA--LEEEENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKEDEELARKL 72
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1293-1355 5.15e-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: 44.73  E-value: 5.15e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186659512  1293 KQQRKAEEARVRKQQLEAEV----ELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQILEE 1355
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEIsrmrELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
PTZ00121 PTZ00121
MAEBL; Provisional
 1261-1351 5.25e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1261 SEGDQKPGVGFFFKDEQKAEDELAKKRAafllKQQRKAEEARVRkqqleAEVELKRDEARRKAEEDRVRKEEEKARRELI 1340
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKA----EEKKKADEAKKK-----AEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470

                          90
                  ....*....|.
gi 186659512 1341 KQEYLRRKQQQ 1351
Cdd:PTZ00121 1471 KADEAKKKAEE 1481
PTZ00121 PTZ00121
MAEBL; Provisional
 1274-1351 5.39e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 5.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1274 KDEQKAEDELAKKRAafllKQQRKAEEARVRKQQL---EAEVELKRDEARRKAEEDRVRKEEE--KARRELIKQEYLRRK 1348
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKA----EELKKAEEEKKKVEQLkkkEAEEKKKAEELKKAEEENKIKAAEEakKAEEDKKKAEEAKKA 1683


                  ...
gi 186659512 1349 QQQ 1351
Cdd:PTZ00121 1684 EED 1686
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 1275-1356 5.82e-04

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: 42.37  E-value: 5.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1275 DEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKE----EEKARRELIKQEYLRRKQQ 1350
Cdd:pfam11600   12 EKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEkerrEKKEKDEKEKAEKLRLKEE 91


                   ....*.
gi 186659512  1351 QILEEQ 1356
Cdd:pfam11600   92 KRKEKQ 97
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1356 6.16e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 6.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1275 DEQKAEDELAKKRAafllKQQRKAEEAR----VRKQQLEaEVELKRDEARRKAEEDRVRKEEEK-----ARRELIKQEYL 1345
Cdd:PTZ00121 1699 EEAKKAEELKKKEA----EEKKKAEELKkaeeENKIKAE-EAKKEAEEDKKKAEEAKKDEEEKKkiahlKKEEEKKAEEI 1773

                          90
                  ....*....|.
gi 186659512 1346 RRKQQQILEEQ 1356
Cdd:PTZ00121 1774 RKEKEAVIEEE 1784
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1351 6.54e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 6.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186659512 1275 DEQKAEDELAKKRAafllKQQRKAEEARVRKQQLEAEVELKR--DEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQ 1351
Cdd:PTZ00121 1394 DEAKKKAEEDKKKA----DELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1352 7.17e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 7.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186659512 1275 DEQKAEDELAKKraafllKQQRKAEEARVRKQQLEAEvELKRDEARRKAEEDRVRKEEEKARRELIKQ-EYLRRKQQQI 1352
Cdd:PTZ00121 1339 EEAKKAAEAAKA------EAEAAADEAEAAEEKAEAA-EKKKEEAKKKADAAKKKAEEKKKADEAKKKaEEDKKKADEL 1410
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 ...
 1274-1355 8.08e-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: 41.14  E-value: 8.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1274 KDEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVelkRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQIL 1353
Cdd:pfam00430   36 ADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENA---KKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRAL 112


                   ..
gi 186659512  1354 EE 1355
Cdd:pfam00430  113 AE 114
PTZ00121 PTZ00121
MAEBL; Provisional
 1274-1356 9.79e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 9.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1274 KDEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQIL 1353
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423


                  ...
gi 186659512 1354 EEQ 1356
Cdd:PTZ00121 1424 KKK 1426
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1274-1356 9.90e-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: 9.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1274 KDEQKAEDELAKK--RAAFLLKQQRKAEEARVR--KQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQeylRRKQ 1349
Cdd:TIGR02794   60 KPAAKKEQERQKKleQQAEEAEKQRAAEQARQKelEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEA---KAKA 136


                   ....*..
gi 186659512  1350 QQILEEQ 1356
Cdd:TIGR02794  137 EAEAERK 143
PTZ00121 PTZ00121
MAEBL; Provisional
 1278-1351 1.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186659512 1278 KAEDELAKKRAafllKQQRKAEEARVRKQQL-EAEVELKRDEARRKAEEDRVRKEEEKARRE---LIKQEYLRRKQQQ 1351
Cdd:PTZ00121 1599 KLYEEEKKMKA----EEAKKAEEAKIKAEELkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEeenKIKAAEEAKKAEE 1672
PTZ00121 PTZ00121
MAEBL; Provisional
 1274-1356 1.27e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1274 KDEQKAEDELAKKRAAFLLK--QQRKAEEA-RVRKQQL---------EAEVELKRDEARRKAEEDRVRKEEEKARRELIK 1341
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKaeELKKAEEEnKIKAAEEakkaeedkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708

                          90
                  ....*....|....*..
gi 186659512 1342 Q--EYLRRKQQQILEEQ 1356
Cdd:PTZ00121 1709 KkeAEEKKKAEELKKAE 1725
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1273-1355 1.31e-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: 42.98  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1273 FKDEQKAEDELAKKRAAFLLKQQRKAEEARVRK---------QQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQE 1343
Cdd:pfam13868  255 EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKrlehrreleKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEE 334

                           90
                   ....*....|..
gi 186659512  1344 ylrrkQQQILEE 1355
Cdd:pfam13868  335 -----RQKKLKE 341
PTZ00121 PTZ00121
MAEBL; Provisional
 1274-1356 1.31e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1274 KDEQKAEDELAKKRAAFLLKQQRKAEEAR-VRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQI 1352
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638


                  ....
gi 186659512 1353 LEEQ 1356
Cdd:PTZ00121 1639 KKKE 1642
PTZ00121 PTZ00121
MAEBL; Provisional
 1274-1356 1.31e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1274 KDEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEvELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQIL 1353
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334


                  ...
gi 186659512 1354 EEQ 1356
Cdd:PTZ00121 1335 KKK 1337
PTZ00121 PTZ00121
MAEBL; Provisional
 1274-1351 1.53e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186659512 1274 KDEQKAEDELAKKRAafllKQQRKAEEARVRkqqleAEVELKRDEARRKAEEDRVRKEE-EKARRELIKQEYLRRKQQQ 1351
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKA----EEAKKADEAKKK-----AEEAKKADEAKKKAEEAKKKADEaKKAAEAKKKADEAKKAEEA 1521
PTZ00121 PTZ00121
MAEBL; Provisional
 1274-1352 1.56e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1274 KDEQKAEDELAKKRAAFLLKQQ----RKAEEarVRKQqlEAEVELKRDEARRKAEEDR-----VRKEEE---KARRELIK 1341
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEaeekKKAEE--LKKA--EEENKIKAAEEAKKAEEDKkkaeeAKKAEEdekKAAEALKK 1696

                          90
                  ....*....|.
gi 186659512 1342 QEYLRRKQQQI 1352
Cdd:PTZ00121 1697 EAEEAKKAEEL 1707
PTZ00121 PTZ00121
MAEBL; Provisional
 1257-1356 1.76e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1257 ADLVSEGDQKPGVGFFFKDEQKAEDELAKKRAafllKQQRKAEEARVRKQqleaEVELKRDEARRKAEEDR-----VRKE 1331
Cdd:PTZ00121 1280 ADELKKAEEKKKADEAKKAEEKKKADEAKKKA----EEAKKADEAKKKAE----EAKKKADAAKKKAEEAKkaaeaAKAE 1351

                          90       100
                  ....*....|....*....|....*
gi 186659512 1332 EEKARRELIKQEYLRRKQQQILEEQ 1356
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEA 1376
PTZ00121 PTZ00121
MAEBL; Provisional
 1274-1351 1.90e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186659512 1274 KDEQKAEDELAKKRAafllKQQRKAEEARVRkqqleAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQ 1351
Cdd:PTZ00121 1426 KAEEKKKADEAKKKA----EEAKKADEAKKK-----AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
PTZ00121 PTZ00121
MAEBL; Provisional
 1277-1356 1.99e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1277 QKAEDeLAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRvRKEEEKARRELIKQEYLR-----RKQQQ 1351
Cdd:PTZ00121 1194 RKAED-ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK-KAEEERNNEEIRKFEEARmahfaRRQAA 1271


                  ....*
gi 186659512 1352 ILEEQ 1356
Cdd:PTZ00121 1272 IKAEE 1276
PTZ00121 PTZ00121
MAEBL; Provisional
 1274-1356 2.07e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1274 KDEQKAEDELAKK-RAAFLLKQQRKAEEARVRK----QQLEAEVELKRDEARRKAEEDRvRKEEekarrELIKQEYLRRK 1348
Cdd:PTZ00121 1685 EDEKKAAEALKKEaEEAKKAEELKKKEAEEKKKaeelKKAEEENKIKAEEAKKEAEEDK-KKAE-----EAKKDEEEKKK 1758


                  ....*...
gi 186659512 1349 QQQILEEQ 1356
Cdd:PTZ00121 1759 IAHLKKEE 1766
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 1274-1355 2.18e-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: 39.47  E-value: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1274 KDEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEE-----EKARREL--IKQEylR 1346
Cdd:pfam13863   19 REEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEkekeiKKLTAQIeeLKSE--I 96


                   ....*....
gi 186659512  1347 RKQQQILEE 1355
Cdd:pfam13863   97 SKLEEKLEE 105
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1285-1356 2.32e-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: 39.73  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1285 KKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEE--DRVRKEEEKARRELIKQ------EYLRRKQQQILEEQ 1356
Cdd:cd06503    29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiiEEARKEAEKIKEEILAEakeeaeRILEQAKAEIEQEK 108
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1276-1356 2.99e-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: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1276 EQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRK------EEEKARRELIKQEYLRRKQ 1349
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEElrleleELELELEEAQAEEYELLAE 296


                  ....*..
gi 186659512 1350 QQILEEQ 1356
Cdd:COG1196   297 LARLEQD 303
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1275-1356 3.05e-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: 41.83  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1275 DEQKAEDELAKKRAA--FLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEY---LRRKQ 1349
Cdd:pfam13868  114 DQAEAEEKLEKQRQLreEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREiarLRAQQ 193


                   ....*..
gi 186659512  1350 QQILEEQ 1356
Cdd:pfam13868  194 EKAQDEK 200
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1347 3.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 3.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186659512 1275 DEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRvRKEEEKARRELIKQEYLRR 1347
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR-KAEDAKRVEIARKAEDARK 1165
PTZ00121 PTZ00121
MAEBL; Provisional
 1274-1352 3.40e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1274 KDEQKAEDELAKKRAafllKQQRKAEEARVRKQQLEAEVELKRD-EARRKAEEDRVRKEEEKAR-RELIKQEYLRRKQQQ 1351
Cdd:PTZ00121 1439 KAEEAKKADEAKKKA----EEAKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKaDEAKKAAEAKKKADE 1514


                  .
gi 186659512 1352 I 1352
Cdd:PTZ00121 1515 A 1515
PTZ00121 PTZ00121
MAEBL; Provisional
 1261-1351 3.80e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1261 SEGDQKPGVGFFFKDEQKAEdELAKKRAAFLLKQQRKAEEARvRKQQLEAEVELKRDEARRKAEEDR----VRKEEEKAR 1336
Cdd:PTZ00121 1148 AEDAKRVEIARKAEDARKAE-EARKAEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAARKAEEERkaeeARKAEDAKK 1225

                          90
                  ....*....|....*.
gi 186659512 1337 RELIKQ-EYLRRKQQQ 1351
Cdd:PTZ00121 1226 AEAVKKaEEAKKDAEE 1241
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1272-1355 3.82e-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: 3.82e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512   1272 FFKDEQKAEDELAKKRAAFLlkqQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQ 1351
Cdd:smart00935   15 AGKAAQKQLEKEFKKRQAEL---EKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91


                    ....
gi 186659512   1352 ILEE 1355
Cdd:smart00935   92 ELQK 95
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1277-1336 3.83e-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: 3.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1277 QKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKAR 1336
Cdd:COG3064    83 EKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERK 142
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1274-1351 4.05e-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: 42.03  E-value: 4.05e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186659512  1274 KDEQ-KAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQ 1351
Cdd:pfam17380  390 KNERvRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ 468
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1276-1350 4.86e-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: 4.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1276 EQKAEDELAKKRAAfllKQQRKAEEARVR-----KQQLEAEVELKRDEARRKAEEDRVRKEEE---KARRELIKQEYLRR 1347
Cdd:TIGR02794  149 AKQAEEEAKAKAAA---EAKKKAEEAKKKaeaeaKAKAEAEAKAKAEEAKAKAEAAKAKAAAEaaaKAEAEAAAAAAAEA 225


                   ...
gi 186659512  1348 KQQ 1350
Cdd:TIGR02794  226 ERK 228
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1276-1350 5.96e-03

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: 39.25  E-value: 5.96e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186659512  1276 EQKAEDELAKKRAAfllKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQ 1350
Cdd:pfam05672   41 ERLRKEELRRRAEE---ERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKARE 112
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1277-1356 7.03e-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: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1277 QKAEDELAKKRAAfLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEE-DRVRKEEEKARRELIKQE----YLRRKQQQ 1351
Cdd:COG1196   235 RELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELELElEEAQAEEYELLAELARLEqdiaRLEERRRE 313


                  ....*
gi 186659512 1352 ILEEQ 1356
Cdd:COG1196   314 LEERL 318
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1276-1355 7.27e-03

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: 38.87  E-value: 7.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1276 EQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEED--RVRKEEEKaRRELIKQEYLRRKQQqiL 1353
Cdd:pfam05672   63 ARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEaeRQRQEREK-IMQQEEQERLERKKR--I 139


                   ..
gi 186659512  1354 EE 1355
Cdd:pfam05672  140 EE 141
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1274-1338 7.53e-03

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.79  E-value: 7.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186659512 1274 KDEQKAEDELAKKRAAflLKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRE 1338
Cdd:COG3064    48 EAKRQAEEEAREAKAE--AEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAA 110
PTZ00121 PTZ00121
MAEBL; Provisional
 1274-1352 7.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512 1274 KDEQKAEDELA----KKRAAFLLKQQ--RKAEEARVRKQQLEAEVELKR--DEARRKAEEDRVRKEEEKARRELIKQEYL 1345
Cdd:PTZ00121 1350 AEAEAAADEAEaaeeKAEAAEKKKEEakKKADAAKKKAEEKKKADEAKKkaEEDKKKADELKKAAAAKKKADEAKKKAEE 1429


                  ....*..
gi 186659512 1346 RRKQQQI 1352
Cdd:PTZ00121 1430 KKKADEA 1436
PTZ00121 PTZ00121
MAEBL; Provisional
 1275-1350 7.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 7.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186659512 1275 DEQKAEDELAKKraafllKQQRKAEEARVRKQQLEAEVELKRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQ 1350
Cdd:PTZ00121 1275 EEARKADELKKA------EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
PTZ00121 PTZ00121
MAEBL; Provisional
 1274-1350 8.44e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 8.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186659512 1274 KDEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEvELKRDEARRKAEEDRvRKEEEKARRELIKQEYLRRKQQ 1350
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE-DAKRVEIARKAEDAR-KAEEARKAEDAKKAEAARKAEE 1186
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1275-1358 8.53e-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: 8.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1275 DEQKAEDELAKKRAAfLLKQQRKAEE----ARVRKQQLEA---EVELKRDEARRKAEEDRVRKEEEKARRELIKQEyLRR 1347
Cdd:TIGR02168  863 ELEELIEELESELEA-LLNERASLEEalalLRSELEELSEelrELESKRSELRRELEELREKLAQLELRLEGLEVR-IDN 940

                           90
                   ....*....|.
gi 186659512  1348 KQQQILEEQGL 1358
Cdd:TIGR02168  941 LQERLSEEYSL 951
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 249-327 8.68e-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: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  249 SDGAALLAVIHYYCPEQMKLDDIclKEVTSMADSLYNIRLLREFSNEYLNKCFyLTLEDmlyaplVLKPN---VMVFIAE 325
Cdd:cd21218    41 KDGEVYALLLHSLAPELCDKELV--LEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPED------IVSGNprlNLAFVAT 111


                  ..
gi 186659512  326 LF 327
Cdd:cd21218   112 LF 113
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1274-1356 8.90e-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: 40.29  E-value: 8.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186659512  1274 KDEQKAEDELAKKRAAFLLKQQRKAEEARVRKQQLEAEVElkRDEARRKAEEDRVRKEEEKARRELIKQEYLRRKQQQIL 1353
Cdd:pfam13868  218 KERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAE--REEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRREL 295


                   ...
gi 186659512  1354 EEQ 1356
Cdd:pfam13868  296 EKQ 298
 
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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