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Conserved domains on  [gi|1958761072|ref|XP_038960650|]
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calmodulin-regulated spectrin-associated protein 1 isoform X5 [Rattus norvegicus]

Protein Classification

calponin homology domain-containing protein; fimbrin/plastin family actin filament-binding protein( domain architecture ID 13777712)

calponin homology (CH) domain-containing protein may bind actin filament (F-actin) or serve a regulatory function| fimbrin/plastin family actin filament-binding protein similar to Saccharomyces cerevisiae fimbrin, which binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity

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 ...
 1336-1464 1.77e-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: 1.77e-75
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072  1336 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGT 1415
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1958761072  1416 GPKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1464
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 119-202 2.01e-39

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


:

Pssm-ID: 432229  Cd Length: 85  Bit Score: 141.28  E-value: 2.01e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072  119 HLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHL-NKCFYLTLED 197
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 1958761072  198 MLYAP 202
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 751-809 4.99e-22

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: 90.44  E-value: 4.99e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958761072  751 PSRHSKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 809
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU super family cl38471
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1149-1226 4.10e-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: 59.68  E-value: 4.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1149 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVE---LKRDEARRKAEEDRL-------RKEEEKARRELIKQEYL 1218
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 1958761072 1219 RRKQQQAL 1226
Cdd:pfam15346  131 KREQQKIL 138
PTZ00121 super family cl31754
MAEBL; Provisional
 1059-1231 8.49e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 8.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1059 KDANIVSEQMNFKEGLDTSVQEAELSSSaitgkEHTPMEEPLRSKASLIEVDLSDLKAPDEDGEVVGHESSLElgGESDQ 1138
Cdd:PTZ00121  1616 EEAKIKAEELKKAEEEKKKVEQLKKKEA-----EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEK 1688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1139 KPGVGFFFKDEQKAEDELAKKRAAfllKQQRKAEEARARKQQLEAEVE-LKR--DEARRKAEEDRLRKEEEKARRELIKQ 1215
Cdd:PTZ00121  1689 KAAEALKKEAEEAKKAEELKKKEA---EEKKKAEELKKAEEENKIKAEeAKKeaEEDKKKAEEAKKDEEEKKKIAHLKKE 1765

                          170       180
                   ....*....|....*....|
gi 1958761072 1216 EYLR----RKQQQALEEQGL 1231
Cdd:PTZ00121  1766 EEKKaeeiRKEKEAVIEEEL 1785
 
Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1336-1464 1.77e-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: 1.77e-75
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072  1336 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGT 1415
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1958761072  1416 GPKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1464
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1337-1455 2.20e-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: 242.57  E-value: 2.20e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1337 PKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGTG 1416
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958761072 1417 PKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTI 1455
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 119-202 2.01e-39

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 141.28  E-value: 2.01e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072  119 HLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHL-NKCFYLTLED 197
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 1958761072  198 MLYAP 202
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 751-809 4.99e-22

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: 90.44  E-value: 4.99e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958761072  751 PSRHSKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 809
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1149-1226 4.10e-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: 59.68  E-value: 4.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1149 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVE---LKRDEARRKAEEDRL-------RKEEEKARRELIKQEYL 1218
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 1958761072 1219 RRKQQQAL 1226
Cdd:pfam15346  131 KREQQKIL 138
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1149-1224 6.47e-07

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: 53.31  E-value: 6.47e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958761072 1149 EQKAEDELAKKRAAFLLKQQRKAEearaRKQQLEAEVELKRDE-ARRKAEEDRLRKEEEKARReliKQEYLRRKQQQ 1224
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAE----AKAKAEAEAERKAKEeAAKQAEEEAKAKAAAEAKK---KAEEAKKKAEA 177
PTZ00121 PTZ00121
MAEBL; Provisional
 1148-1229 7.73e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 7.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1148 DEQKAEDELAKKRAAFLLK---QQRKAEEARARKQQLEAEvELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQQ 1224
Cdd:PTZ00121  1486 DEAKKKAEEAKKKADEAKKaaeAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEK 1563


                   ....*
gi 1958761072 1225 ALEEQ 1229
Cdd:PTZ00121  1564 KKAEE 1568
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1151-1228 1.93e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 48.72  E-value: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1151 KAEDELAKKRAAFLLKQQRK-------AEEARARKQQ-LEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQ 1222
Cdd:COG2268    241 EAEAELAKKKAEERREAETAraeaeaaYEIAEANAEReVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA 320


                   ....*.
gi 1958761072 1223 QQALEE 1228
Cdd:COG2268    321 AEAEAE 326
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1158-1228 8.59e-05

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: 43.97  E-value: 8.59e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958761072 1158 KKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE--DRLRKEEEKARRELIK--QEYLRRKQQQALEE 1228
Cdd:cd06503     29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiiEEARKEAEKIKEEILAeaKEEAERILEQAKAE 103
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1145-1228 6.77e-04

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: 41.42  E-value: 6.77e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072  1145 FFKDEQKAEDELAKKRAAFLlkqQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQ 1224
Cdd:smart00935   15 AGKAAQKQLEKEFKKRQAEL---EKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91


                    ....
gi 1958761072  1225 ALEE 1228
Cdd:smart00935   92 ELQK 95
PTZ00121 PTZ00121
MAEBL; Provisional
 1059-1231 8.49e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 8.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1059 KDANIVSEQMNFKEGLDTSVQEAELSSSaitgkEHTPMEEPLRSKASLIEVDLSDLKAPDEDGEVVGHESSLElgGESDQ 1138
Cdd:PTZ00121  1616 EEAKIKAEELKKAEEEKKKVEQLKKKEA-----EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEK 1688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1139 KPGVGFFFKDEQKAEDELAKKRAAfllKQQRKAEEARARKQQLEAEVE-LKR--DEARRKAEEDRLRKEEEKARRELIKQ 1215
Cdd:PTZ00121  1689 KAAEALKKEAEEAKKAEELKKKEA---EEKKKAEELKKAEEENKIKAEeAKKeaEEDKKKAEEAKKDEEEKKKIAHLKKE 1765

                          170       180
                   ....*....|....*....|
gi 1958761072 1216 EYLR----RKQQQALEEQGL 1231
Cdd:PTZ00121  1766 EEKKaeeiRKEKEAVIEEEL 1785
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1059-1229 1.36e-03

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 42.85  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1059 KDANIVSEQMNFKEglDTSVQEAelsssaITGKEHTPMEEPLRSKAsliEVDLSDLKAPDEDGEV-----VGHESSLELG 1133
Cdd:NF040676   192 KEEVKVQEVVKPKE--EPKVQEI------VKPKEEVKVQEEVKPKE---EEKVQEIVKPKEEAKVqeevkVKEEAKVQEI 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1134 GESDQKPGVGFFFK--DEQKAEDELAKKRAAFLLKQQRKAEEARARkQQLEAEVELKRDEARRKAEEDRLR-----KEEE 1206
Cdd:NF040676   261 AKAKEEAKAQEIAKakEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQ-EIAKAKEEAKAREIAKAKEEEKAReiakaKEEA 339

                          170       180
                   ....*....|....*....|....
gi 1958761072 1207 KARR-ELIKQEYLRRKQQQALEEQ 1229
Cdd:NF040676   340 KAREiAKAKEEAKAREIAKAKEEE 363
 
Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1336-1464 1.77e-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: 1.77e-75
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072  1336 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGT 1415
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 1958761072  1416 GPKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1464
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1337-1455 2.20e-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: 242.57  E-value: 2.20e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1337 PKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGTG 1416
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958761072 1417 PKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTI 1455
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 119-202 2.01e-39

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 141.28  E-value: 2.01e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072  119 HLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHL-NKCFYLTLED 197
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 1958761072  198 MLYAP 202
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 751-809 4.99e-22

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: 90.44  E-value: 4.99e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958761072  751 PSRHSKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 809
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1149-1226 4.10e-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: 59.68  E-value: 4.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1149 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVE---LKRDEARRKAEEDRL-------RKEEEKARRELIKQEYL 1218
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 1958761072 1219 RRKQQQAL 1226
Cdd:pfam15346  131 KREQQKIL 138
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 1157-1231 1.55e-07

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: 53.12  E-value: 1.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1157 AKKRAAFLLKQQRKA---------EEARARKQQLEAEV---ELKRDEARRKAEEDRLRKEEEKARREliKQEYLRRKQQQ 1224
Cdd:pfam09756    5 AKKRAKLELKEAKRQqreaeeeerEEREKLEEKREEEYkerEEREEEAEKEKEEEERKQEEEQERKE--QEEYEKLKSQF 82


                   ....*..
gi 1958761072 1225 ALEEQGL 1231
Cdd:pfam09756   83 VVEEEGT 89
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1147-1227 3.67e-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: 54.57  E-value: 3.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKK-RAAFLLKQQRKAEEARARKQQLEAEVELKRDEARR-----KAEEDRLRKEEEKARRELikQEYLRR 1220
Cdd:pfam15709  361 RRLQQEQLERAEKmREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKqrlqlQAAQERARQQQEEFRRKL--QELQRK 438


                   ....*..
gi 1958761072 1221 KQQQALE 1227
Cdd:pfam15709  439 KQQEEAE 445
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1149-1224 6.47e-07

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: 53.31  E-value: 6.47e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958761072 1149 EQKAEDELAKKRAAFLLKQQRKAEearaRKQQLEAEVELKRDE-ARRKAEEDRLRKEEEKARReliKQEYLRRKQQQ 1224
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAE----AKAKAEAEAERKAKEeAAKQAEEEAKAKAAAEAKK---KAEEAKKKAEA 177
PTZ00121 PTZ00121
MAEBL; Provisional
 1148-1229 7.73e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 7.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1148 DEQKAEDELAKKRAAFLLK---QQRKAEEARARKQQLEAEvELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQQ 1224
Cdd:PTZ00121  1486 DEAKKKAEEAKKKADEAKKaaeAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEK 1563


                   ....*
gi 1958761072 1225 ALEEQ 1229
Cdd:PTZ00121  1564 KKAEE 1568
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1150-1227 1.67e-05

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: 48.69  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1150 QKAEDELAKKRAAFLLKQ-----QRKAEEARARKQQLEAevELKRDEARRKAEEDRLRKEE--EKARRELIKQEYLRRKQ 1222
Cdd:TIGR02794  126 AKQAAEAKAKAEAEAERKakeeaAKQAEEEAKAKAAAEA--KKKAEEAKKKAEAEAKAKAEaeAKAKAEEAKAKAEAAKA 203


                   ....*
gi 1958761072 1223 QQALE 1227
Cdd:TIGR02794  204 KAAAE 208
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1151-1228 1.93e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 48.72  E-value: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1151 KAEDELAKKRAAFLLKQQRK-------AEEARARKQQ-LEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQ 1222
Cdd:COG2268    241 EAEAELAKKKAEERREAETAraeaeaaYEIAEANAEReVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA 320


                   ....*.
gi 1958761072 1223 QQALEE 1228
Cdd:COG2268    321 AEAEAE 326
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1149-1229 2.00e-05

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: 48.38  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1149 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEE-EKARRELIKQEYLRRKQQQALE 1227
Cdd:pfam13868  146 EKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErDELRAKLYQEEQERKERQKERE 225


                   ..
gi 1958761072 1228 EQ 1229
Cdd:pfam13868  226 EA 227
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1166-1229 4.07e-05

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: 45.42  E-value: 4.07e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958761072 1166 KQQRKAEEARARKQQL---EAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALEEQ 1229
Cdd:pfam05672   33 ERLEKEEEERLRKEELrrrAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERL 99
PRK12704 PRK12704
phosphodiesterase; Provisional
 1141-1229 4.91e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.85  E-value: 4.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1141 GVGFFF---KDEQKAEDelAKKRAAFLLKQQRKA-------------EEARARKQQLEAEV-----ELKRDEARRKAEED 1199
Cdd:PRK12704    19 VIGYFVrkkIAEAKIKE--AEEEAKRILEEAKKEaeaikkealleakEEIHKLRNEFEKELrerrnELQKLEKRLLQKEE 96

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958761072 1200 RLRKEEE---KARRELIKQEYLRRKQQQALEEQ 1229
Cdd:PRK12704    97 NLDRKLElleKREEELEKKEKELEQKQQELEKK 129
PTZ00121 PTZ00121
MAEBL; Provisional
 1148-1228 5.01e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 5.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1148 DEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDrlRKEEEKARRELIKQEYLRRKQQQALE 1227
Cdd:PTZ00121  1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEA--KKAEEDKNMALRKAEEAKKAEEARIE 1595


                   .
gi 1958761072 1228 E 1228
Cdd:PTZ00121  1596 E 1596
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 ...
 1147-1228 5.17e-05

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: 44.61  E-value: 5.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVelkRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1226
Cdd:pfam00430   36 ADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENA---KKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRAL 112


                   ..
gi 1958761072 1227 EE 1228
Cdd:pfam00430  113 AE 114
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1147-1229 5.96e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 47.17  E-value: 5.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAafllKQQRKAEEARARKQQL---------EAEVELKRDEARRKAEEDRLRKE------EEKARRE 1211
Cdd:COG2268    203 IAEAEAERETEIAIA----QANREAEEAELEQEREietariaeaEAELAKKKAEERREAETARAEAEaayeiaEANAERE 278

                           90
                   ....*....|....*....
gi 1958761072 1212 LIKQ-EYLRRKQQQALEEQ 1229
Cdd:COG2268    279 VQRQlEIAEREREIELQEK 297
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1148-1228 6.85e-05

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: 44.66  E-value: 6.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1148 DEQKAEDELAKKRAAFLLKqqRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELI----KQEYLRRKQQ 1223
Cdd:pfam15346    4 ESKLLEEETARRVEEAVAK--RVEEELEKRKDEIEAEVERRVEEARKIMEKQVLEELEREREAELEeerrKEEEERKKRE 81


                   ....*
gi 1958761072 1224 QaLEE 1228
Cdd:pfam15346   82 E-LER 85
PTZ00121 PTZ00121
MAEBL; Provisional
 1148-1229 7.08e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 7.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1148 DEQKAEDELAKKRAAFLlkqQRKAEEARARKQQLEAEVELKRDE---ARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQ 1224
Cdd:PTZ00121  1318 DEAKKKAEEAKKKADAA---KKKAEEAKKAAEAAKAEAEAAADEaeaAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394


                   ....*
gi 1958761072 1225 ALEEQ 1229
Cdd:PTZ00121  1395 EAKKK 1399
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1158-1228 8.59e-05

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: 43.97  E-value: 8.59e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958761072 1158 KKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE--DRLRKEEEKARRELIK--QEYLRRKQQQALEE 1228
Cdd:cd06503     29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiiEEARKEAEKIKEEILAeaKEEAERILEQAKAE 103
PTZ00121 PTZ00121
MAEBL; Provisional
 1135-1225 1.19e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1135 ESDQKPGVGFFFKDEQKAEDELAKKRAafllKQQRKAEEARARkqqleAEVELKRDEARRKAEEDRLRKEEEKARRELIK 1214
Cdd:PTZ00121  1401 EEDKKKADELKKAAAAKKKADEAKKKA----EEKKKADEAKKK-----AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471

                           90
                   ....*....|.
gi 1958761072 1215 QEYLRRKQQQA 1225
Cdd:PTZ00121  1472 ADEAKKKAEEA 1482
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1147-1229 1.20e-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: 45.99  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAflLKQQRKAEEARAR--KQQLEAEVELKRDEARRKAEEDRLRKEEEKARreliKQEYLRRKQQQ 1224
Cdd:TIGR02794   64 KKEQERQKKLEQQAEE--AEKQRAAEQARQKelEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA----KQAAEAKAKAE 137


                   ....*
gi 1958761072 1225 ALEEQ 1229
Cdd:TIGR02794  138 AEAER 142
PTZ00121 PTZ00121
MAEBL; Provisional
 1147-1225 1.37e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAFLLKQ---QRKAEEARARKQQLE--AEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRK 1221
Cdd:PTZ00121  1373 KEEAKKKADAAKKKAEEKKKAdeaKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452


                   ....
gi 1958761072 1222 QQQA 1225
Cdd:PTZ00121  1453 AEEA 1456
PTZ00121 PTZ00121
MAEBL; Provisional
 1147-1225 1.44e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAafllKQQRKAEEARARKQqleaEVELKRDEARRKAEE----DRLRKEEEKARRELIKQEYLRRKQ 1222
Cdd:PTZ00121  1465 KAEEAKKADEAKKKA----EEAKKADEAKKKAE----EAKKKADEAKKAAEAkkkaDEAKKAEEAKKADEAKKAEEAKKA 1536


                   ...
gi 1958761072 1223 QQA 1225
Cdd:PTZ00121  1537 DEA 1539
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
 1146-1226 1.50e-04

pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.


Pssm-ID: 461396 [Multi-domain]  Cd Length: 130  Bit Score: 43.05  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1146 FKDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDRLRKEEEKArrELIKQEYLRRKQQQA 1225
Cdd:pfam04696   21 FKKEESKQKEKEERRAEIEKRLEEKAKQEKEELEERKRE-EREELFEERRAEQIELRALEEKL--ELKELMETWHENLKA 97


                   .
gi 1958761072 1226 L 1226
Cdd:pfam04696   98 L 98
PTZ00121 PTZ00121
MAEBL; Provisional
 1148-1229 1.76e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 1.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1148 DEQKAEDELAKKraafllKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALE 1227
Cdd:PTZ00121  1339 EEAKKAAEAAKA------EAEAAADEAEAAEEKAEAA-EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411


                   ..
gi 1958761072 1228 EQ 1229
Cdd:PTZ00121  1412 KA 1413
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 1148-1229 1.85e-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: 43.52  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1148 DEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKE----EEKARRELIKQEYLRRKQQ 1223
Cdd:pfam11600   12 EKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEkerrEKKEKDEKEKAEKLRLKEE 91


                   ....*.
gi 1958761072 1224 QALEEQ 1229
Cdd:pfam11600   92 KRKEKQ 97
PTZ00121 PTZ00121
MAEBL; Provisional
 1147-1229 1.99e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1226
Cdd:PTZ00121  1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334


                   ...
gi 1958761072 1227 EEQ 1229
Cdd:PTZ00121  1335 KKK 1337
PTZ00121 PTZ00121
MAEBL; Provisional
 1148-1225 2.10e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1148 DEQKAEDELAKKRAafllKQQRKAEEARARKQQLEAEVELKR--DEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQA 1225
Cdd:PTZ00121  1394 DEAKKKAEEDKKKA----DELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1149-1225 2.32e-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: 43.11  E-value: 2.32e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958761072 1149 EQKAEDELAKKRAAfllKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQA 1225
Cdd:pfam05672   41 ERLRKEELRRRAEE---ERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEA 114
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1146-1216 2.86e-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: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1146 FKDEQKAEDELAKKRAAFLLKQ-QRKAEEARARKQQLEAEVE--------LKRDEARRKAEEDRLRKEEEKARRELIKQE 1216
Cdd:pfam13868  255 EAEREEEEFERMLRKQAEDEEIeQEEAEKRRMKRLEHRRELEkqieereeQRAAEREEELEEGERLREEEAERRERIEEE 334
PTZ00121 PTZ00121
MAEBL; Provisional
 1147-1229 3.20e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 3.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAafllKQQRKAEEARARKQQL---EAEVELKRDEARRKAEEDRLRKEEEKAR--------RELIKQ 1215
Cdd:PTZ00121  1608 KAEEAKKAEEAKIKA----EELKKAEEEKKKVEQLkkkEAEEKKKAEELKKAEEENKIKAAEEAKKaeedkkkaEEAKKA 1683

                           90
                   ....*....|....
gi 1958761072 1216 EYLRRKQQQALEEQ 1229
Cdd:PTZ00121  1684 EEDEKKAAEALKKE 1697
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
 1150-1211 3.33e-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: 40.62  E-value: 3.33e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958761072 1150 QKAEDEL----AKKRAafLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRE 1211
Cdd:cd22265      9 QEYEEEIskleAERRA--LEEEENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKEDEELARKL 72
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1150-1229 3.38e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 3.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1150 QKAEDELAKKRAAfLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE-DRLRKEEEKARRELIKQE----YLRRKQQQ 1224
Cdd:COG1196    235 RELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELELElEEAQAEEYELLAELARLEqdiaRLEERRRE 313


                   ....*
gi 1958761072 1225 ALEEQ 1229
Cdd:COG1196    314 LEERL 318
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1153-1231 3.50e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 3.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1153 EDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRK------AEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1226
Cdd:COG4913    289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggDRLEQLEREIERLERELEERERRRARLEALL 368


                   ....*
gi 1958761072 1227 EEQGL 1231
Cdd:COG4913    369 AALGL 373
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1166-1229 4.28e-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: 44.14  E-value: 4.28e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958761072 1166 KQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQ-EYLRRKQQQALEEQ 1229
Cdd:pfam13868   32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQiEEREQKRQEEYEEK 96
PTZ00121 PTZ00121
MAEBL; Provisional
 1147-1229 4.59e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 4.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1226
Cdd:PTZ00121  1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423


                   ...
gi 1958761072 1227 EEQ 1229
Cdd:PTZ00121  1424 KKK 1426
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1147-1229 4.87e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.65  E-value: 4.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAflLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRElikQEYLRRKQQQAL 1226
Cdd:COG3064     48 EAKRQAEEEAREAKAE--AEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAA---EKAAAAAEKEKA 122


                   ...
gi 1958761072 1227 EEQ 1229
Cdd:COG3064    123 EEA 125
PTZ00121 PTZ00121
MAEBL; Provisional
 1147-1225 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 1958761072 1147 KDEQKAEDELAKKRAAFLLKQQ----RKAEEARarkqQLEAEVELKRDEARRKAEEDR-----LRKEEEKARReliKQEY 1217
Cdd:PTZ00121  1621 KAEELKKAEEEKKKVEQLKKKEaeekKKAEELK----KAEEENKIKAAEEAKKAEEDKkkaeeAKKAEEDEKK---AAEA 1693


                   ....*...
gi 1958761072 1218 LRRKQQQA 1225
Cdd:PTZ00121  1694 LKKEAEEA 1701
PTZ00121 PTZ00121
MAEBL; Provisional
 1147-1225 5.21e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 5.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAFLLKQQ---RKAEEAR-ARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQ 1222
Cdd:PTZ00121  1439 KAEEAKKADEAKKKAEEAKKAEeakKKAEEAKkADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518


                   ...
gi 1958761072 1223 QQA 1225
Cdd:PTZ00121  1519 EEA 1521
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1150-1229 5.45e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.26  E-value: 5.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1150 QKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQQALEEQ 1229
Cdd:COG3064     83 EKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEA-KRKAEEERKAAEAEAAAKAEAEAARAAA 161
PTZ00121 PTZ00121
MAEBL; Provisional
 1148-1227 5.91e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 5.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1148 DEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDR---LRKEE-----EKARRELIKQEYLR 1219
Cdd:PTZ00121  1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE-EKKKAEEAKKAEEDKnmaLRKAEeakkaEEARIEEVMKLYEE 1603


                   ....*...
gi 1958761072 1220 RKQQQALE 1227
Cdd:PTZ00121  1604 EKKMKAEE 1611
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1145-1228 6.77e-04

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: 41.42  E-value: 6.77e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072  1145 FFKDEQKAEDELAKKRAAFLlkqQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQ 1224
Cdd:smart00935   15 AGKAAQKQLEKEFKKRQAEL---EKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91


                    ....
gi 1958761072  1225 ALEE 1228
Cdd:smart00935   92 ELQK 95
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1158-1228 6.91e-04

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 41.70  E-value: 6.91e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958761072 1158 KKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE--DRLRKEEEKARRELIKQ--EYLRRKQQQALEE 1228
Cdd:COG0711     30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEiiAEARKEAEAIAEEAKAEaeAEAERIIAQAEAE 104
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1147-1229 6.91e-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: 43.75  E-value: 6.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEA----RRKAEEDRLRKEEEKARRElIKQEYlRRKQ 1222
Cdd:pfam13868  218 KERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFermlRKQAEDEEIEQEEAEKRRM-KRLEH-RREL 295


                   ....*..
gi 1958761072 1223 QQALEEQ 1229
Cdd:pfam13868  296 EKQIEER 302
PTZ00121 PTZ00121
MAEBL; Provisional
 1147-1225 7.42e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 7.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAFLLKQ---QRKAEEAR-ARKQQLEAEVELKRDEARRKAEE----DRLRKEEEKARR---ELIKQ 1215
Cdd:PTZ00121  1426 KAEEKKKADEAKKKAEEAKKAdeaKKKAEEAKkAEEAKKKAEEAKKADEAKKKAEEakkaDEAKKKAEEAKKkadEAKKA 1505

                           90
                   ....*....|
gi 1958761072 1216 EYLRRKQQQA 1225
Cdd:PTZ00121  1506 AEAKKKADEA 1515
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1149-1230 8.29e-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: 8.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1149 EQKAEDELAKKRAAFLLKQ-----QRKAEEARAR-----KQQLEAEVELKRDEARRKAEEDRLRKEEE---KARRELIKQ 1215
Cdd:TIGR02794  141 ERKAKEEAAKQAEEEAKAKaaaeaKKKAEEAKKKaeaeaKAKAEAEAKAKAEEAKAKAEAAKAKAAAEaaaKAEAEAAAA 220

                           90
                   ....*....|....*
gi 1958761072 1216 EYLRRKQQQALEEQG 1230
Cdd:TIGR02794  221 AAAEAERKADEAELG 235
PTZ00121 PTZ00121
MAEBL; Provisional
 1059-1231 8.49e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 8.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1059 KDANIVSEQMNFKEGLDTSVQEAELSSSaitgkEHTPMEEPLRSKASLIEVDLSDLKAPDEDGEVVGHESSLElgGESDQ 1138
Cdd:PTZ00121  1616 EEAKIKAEELKKAEEEKKKVEQLKKKEA-----EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEK 1688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1139 KPGVGFFFKDEQKAEDELAKKRAAfllKQQRKAEEARARKQQLEAEVE-LKR--DEARRKAEEDRLRKEEEKARRELIKQ 1215
Cdd:PTZ00121  1689 KAAEALKKEAEEAKKAEELKKKEA---EEKKKAEELKKAEEENKIKAEeAKKeaEEDKKKAEEAKKDEEEKKKIAHLKKE 1765

                          170       180
                   ....*....|....*....|
gi 1958761072 1216 EYLR----RKQQQALEEQGL 1231
Cdd:PTZ00121  1766 EEKKaeeiRKEKEAVIEEEL 1785
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1149-1231 9.56e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 9.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1149 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARR-----KAEEDRLRKEEEKARRELIKQEYLRRKQQ 1223
Cdd:COG1196    217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELaeleaELEELRLELEELELELEEAQAEEYELLAE 296


                   ....*...
gi 1958761072 1224 QALEEQGL 1231
Cdd:COG1196    297 LARLEQDI 304
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1148-1229 9.80e-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: 42.98  E-value: 9.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1148 DEQKAEDELAKKRAA--FLLKQQRKAEEARARKQQLEAEVELKRDE-ARRKAEEDRLRKEEE---KARRELIKQEyLRRK 1221
Cdd:pfam13868  114 DQAEAEEKLEKQRQLreEIDEFNEEQAEWKELEKEEEREEDERILEyLKEKAEREEEREAEReeiEEEKEREIAR-LRAQ 192


                   ....*...
gi 1958761072 1222 QQQALEEQ 1229
Cdd:pfam13868  193 QEKAQDEK 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1147-1229 9.81e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 9.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAfLLKQQRKAEEARARKQQLEAEVE-----LKRDEARRKAEEDRLrKEEEKARRELIKQEYLRRK 1221
Cdd:COG1196    260 AELAELEAELEELRLE-LEELELELEEAQAEEYELLAELArleqdIARLEERRRELEERL-EELEEELAELEEELEELEE 337


                   ....*...
gi 1958761072 1222 QQQALEEQ 1229
Cdd:COG1196    338 ELEELEEE 345
PTZ00121 PTZ00121
MAEBL; Provisional
 1147-1229 1.07e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAFLLKQQRKAEEAR-ARKQQLEAEVELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQQA 1225
Cdd:PTZ00121  1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKkAEEARIEEVMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEEEKKKVEQ 1637


                   ....
gi 1958761072 1226 LEEQ 1229
Cdd:PTZ00121  1638 LKKK 1641
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 ...
 1158-1228 1.13e-03

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: 40.76  E-value: 1.13e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958761072 1158 KKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE--DRLRKEEEKARRELIKQ--EYLRRKQQQALEE 1228
Cdd:pfam00430   29 DKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEiiENAKKRAEKLKEEIVAAaeAEAERIIEQAAAE 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1147-1231 1.15e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAfLLKQQRKAEEARARKQQLEAEVELKRdEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1226
Cdd:COG1196    246 AELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRRELEERLEELEE 323


                   ....*
gi 1958761072 1227 EEQGL 1231
Cdd:COG1196    324 ELAEL 328
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 1147-1212 1.22e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 40.29  E-value: 1.22e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958761072 1147 KDEQKAEDELAKKRAAFLLKQQRKAEEAR---ARKQQLEAE-------VELKRDEARRKAEE-DRLRKEEEKARREL 1212
Cdd:pfam20492   44 RQAEEEAERLEQKRQEAEEEKERLEESAEmeaEEKEQLEAElaeaqeeIARLEEEVERKEEEaRRLQEELEEAREEE 120
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 1148-1228 1.25e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1148 DEQKAEDELAKkraafLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEdrLRKEEEKARRELiKQEYlrrkqQQALE 1227
Cdd:PRK00409   514 DKEKLNELIAS-----LEELERELEQKAEEAEALLKEAEKLKEELEEKKEK--LQEEEDKLLEEA-EKEA-----QQAIK 580


                   .
gi 1958761072 1228 E 1228
Cdd:PRK00409   581 E 581
PTZ00121 PTZ00121
MAEBL; Provisional
 1147-1229 1.35e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAafllKQQRKAEEARARKQqleaEVELKRDEARRKAEEDR-----LRKEEEKARRELIKQEYLRRK 1221
Cdd:PTZ00121  1297 KAEEKKKADEAKKKA----EEAKKADEAKKKAE----EAKKKADAAKKKAEEAKkaaeaAKAEAEAAADEAEAAEEKAEA 1368


                   ....*...
gi 1958761072 1222 QQQALEEQ 1229
Cdd:PTZ00121  1369 AEKKKEEA 1376
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1059-1229 1.36e-03

cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.


Pssm-ID: 468642 [Multi-domain]  Cd Length: 476  Bit Score: 42.85  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1059 KDANIVSEQMNFKEglDTSVQEAelsssaITGKEHTPMEEPLRSKAsliEVDLSDLKAPDEDGEV-----VGHESSLELG 1133
Cdd:NF040676   192 KEEVKVQEVVKPKE--EPKVQEI------VKPKEEVKVQEEVKPKE---EEKVQEIVKPKEEAKVqeevkVKEEAKVQEI 260

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1134 GESDQKPGVGFFFK--DEQKAEDELAKKRAAFLLKQQRKAEEARARkQQLEAEVELKRDEARRKAEEDRLR-----KEEE 1206
Cdd:NF040676   261 AKAKEEAKAQEIAKakEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQ-EIAKAKEEAKAREIAKAKEEEKAReiakaKEEA 339

                          170       180
                   ....*....|....*....|....
gi 1958761072 1207 KARR-ELIKQEYLRRKQQQALEEQ 1229
Cdd:NF040676   340 KAREiAKAKEEAKAREIAKAKEEE 363
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1147-1229 1.40e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAfLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEdrlRKEEEKARRELIKQEYLRRKQQQAL 1226
Cdd:COG1196    316 ERLEELEEELAELEEE-LEELEEELEELEEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEAEEELEELAEELLEA 391


                   ...
gi 1958761072 1227 EEQ 1229
Cdd:COG1196    392 LRA 394
PRK11637 PRK11637
AmiB activator; Provisional
 1149-1225 1.45e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 42.76  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1149 EQKAEDELAKKRAAFLL----KQQRKAEEAR-ARKQQLEA-EVELKRDEAR---RKAEEDRLR------KEEEKAR--RE 1211
Cdd:PRK11637   184 AQKAELEEKQSQQKTLLyeqqAQQQKLEQARnERKKTLTGlESSLQKDQQQlseLRANESRLRdsiaraEREAKARaeRE 263

                           90
                   ....*....|....
gi 1958761072 1212 LIKQEYLRRKQQQA 1225
Cdd:PRK11637   264 AREAARVRDKQKQA 277
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1149-1225 1.52e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.87  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1149 EQKAEDELAKKRAAfllKQQRKAEEARARKQ---QLEAEVELKR-DEARRKAEEDRLRKEEEKARReliKQEYLRRKQQQ 1224
Cdd:PRK09510   115 EQKKQAEEAAKQAA---LKQKQAEEAAAKAAaaaKAKAEAEAKRaAAAAKKAAAEAKKKAEAEAAK---KAAAEAKKKAE 188


                   .
gi 1958761072 1225 A 1225
Cdd:PRK09510   189 A 189
eIF3_subunit pfam08597
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of ...
 1147-1208 1.56e-03

Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of the eukaryotic translation initiation factor 3 (eIF3). In yeast it is called Hcr1. The Saccharomyces cerevisiae protein Swiss:Q05775 has been shown to be required for processing of 20S pre-rRNA and binds to 18S rRNA and eIF3 subunits Rpg1p and Prt1p.


Pssm-ID: 462530  Cd Length: 239  Bit Score: 41.90  E-value: 1.56e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958761072 1147 KDEQKAEDELAKKRAA-FLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKA 1208
Cdd:pfam08597   45 EEKEKAAKAAAAKAKKkKKSKKQKIAEKEAERKAEEEAEEEEELTPEDEAARKLRLRKAEEES 107
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1147-1229 1.58e-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: 42.60  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVE---LKRDEARRKAEEDRLRKEEEKARRELIKQEYL----- 1218
Cdd:pfam13868   58 EEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLqerEQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdefne 137

                           90
                   ....*....|....
gi 1958761072 1219 ---RRKQQQALEEQ 1229
Cdd:pfam13868  138 eqaEWKELEKEEER 151
PTZ00121 PTZ00121
MAEBL; Provisional
 1150-1219 1.60e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.60e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1150 QKAEDeLAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRlRKEEEKARRELIKQEYLR 1219
Cdd:PTZ00121  1194 RKAED-ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK-KAEEERNNEEIRKFEEAR 1261
PTZ00121 PTZ00121
MAEBL; Provisional
 1148-1220 2.09e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.09e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958761072 1148 DEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRR 1220
Cdd:PTZ00121  1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR-KAEDAKRVEIARKAEDARK 1165
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1147-1229 2.11e-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: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAFLLKQQRKAEEARAR-----KQQLEAEVELKRdeaRRKAEEDRLRKEEEKARRELIKQEYL--R 1219
Cdd:pfam13868   39 KEEERRLDEMMEEERERALEEEEEKEEERKEerkryRQELEEQIEERE---QKRQEEYEEKLQEREQMDEIVERIQEedQ 115

                           90
                   ....*....|
gi 1958761072 1220 RKQQQALEEQ 1229
Cdd:pfam13868  116 AEAEEKLEKQ 125
PTZ00121 PTZ00121
MAEBL; Provisional
 1135-1225 2.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1135 ESDQKPGVGFFFKDEQKAEdELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDR----LRKEEEKARR 1210
Cdd:PTZ00121  1149 EDAKRVEIARKAEDARKAE-EARKAEDAKKAEAARKAEEVRKAEELRKAE-DARKAEAARKAEEERkaeeARKAEDAKKA 1226

                           90
                   ....*....|....*.
gi 1958761072 1211 ELIKQ-EYLRRKQQQA 1225
Cdd:PTZ00121  1227 EAVKKaEEAKKDAEEA 1242
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1150-1215 2.35e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 40.16  E-value: 2.35e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958761072 1150 QKAEDELAKKRAAFLLKQQRKAEEARARKQQL--EAEVELKRDEARRKAE-EDRLRKEEEKARRELIKQ 1215
Cdd:COG0711     51 EAALAEYEEKLAEARAEAAEIIAEARKEAEAIaeEAKAEAEAEAERIIAQaEAEIEQERAKALAELRAE 119
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 1144-1210 2.42e-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: 41.78  E-value: 2.42e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958761072 1144 FFFKDEQKA------EDELAKKRAAfllKQQRKAEEARARKQQLEAEvelKRDEARRKAEEDRLRKEEEKARR 1210
Cdd:pfam07946  252 AKLRPEALKkakktrEEEIEKIKKA---AEEERAEEAQEKKEEAKKK---EREEKLAKLSPEEQRKYEEKERK 318
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1147-1229 2.43e-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: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKR-AAFLLKQQRKAEEARARKQQL-----EAEVELKRDEARRKAEEDRLRKEEE--KARRELIKQEYL 1218
Cdd:pfam13868  171 REAEREEIEEEKEReIARLRAQQEKAQDEKAERDELraklyQEEQERKERQKEREEAEKKARQRQElqQAREEQIELKER 250

                           90
                   ....*....|.
gi 1958761072 1219 RRKQQQALEEQ 1229
Cdd:pfam13868  251 RLAEEAEREEE 261
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 1150-1221 2.49e-03

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: 41.51  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1150 QKA--EDELAKKRAAFLLKQQR---------------KAEEAR---ARKQQLEAEVELKRDEARRKAE-EDRLRKEEEKA 1208
Cdd:pfam12037  101 QRAqyQDELARKRYQDQLEAQRrrneellrkqeesvaKQEAMRiqaQRRQTEEHEAELRRETERAKAEaEAEARAKEERE 180

                           90
                   ....*....|...
gi 1958761072 1209 RRELIKqEYLRRK 1221
Cdd:pfam12037  181 NEDLNL-EQLREK 192
PTZ00121 PTZ00121
MAEBL; Provisional
 1147-1225 2.60e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELA----KKRAAFLLKQQ--RKAEEARARKQQLEAEVELKR--DEARRKAEEDRLRKEEEKARRELIKQEYL 1218
Cdd:PTZ00121  1350 AEAEAAADEAEaaeeKAEAAEKKKEEakKKADAAKKKAEEKKKADEAKKkaEEDKKKADELKKAAAAKKKADEAKKKAEE 1429


                   ....*..
gi 1958761072 1219 RRKQQQA 1225
Cdd:PTZ00121  1430 KKKADEA 1436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1148-1231 2.64e-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: 42.35  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1148 DEQKAEDELAKKRAAfLLKQQRKAEEARA----RKQQLEA---EVELKRDEARRKAEEDRLRKEEEKARRELIKQEyLRR 1220
Cdd:TIGR02168  863 ELEELIEELESELEA-LLNERASLEEALAllrsELEELSEelrELESKRSELRRELEELREKLAQLELRLEGLEVR-IDN 940

                           90
                   ....*....|.
gi 1958761072 1221 KQQQALEEQGL 1231
Cdd:TIGR02168  941 LQERLSEEYSL 951
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
 1145-1229 2.86e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 39.60  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1145 FFKDEQKAEDElakkRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKA---------EEDRLRKEE---------- 1205
Cdd:PRK07353    26 FYKPVGKVVEE----REDYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAqaviaeaeaEADKLAAEAlaeaqaeaqa 101

                           90       100
                   ....*....|....*....|....*.
gi 1958761072 1206 --EKARRELIKQeylRRKQQQALEEQ 1229
Cdd:PRK07353   102 skEKARREIEQQ---KQAALAQLEQQ 124
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1149-1229 3.02e-03

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 41.95  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1149 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALEE 1228
Cdd:COG3064     32 EQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAE 111


                   .
gi 1958761072 1229 Q 1229
Cdd:COG3064    112 K 112
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 1147-1229 3.17e-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: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEE-EKARRELIKQEYLRRKQQQA 1225
Cdd:pfam13863   19 REEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEkEKEIKKLTAQIEELKSEISK 98


                   ....
gi 1958761072 1226 LEEQ 1229
Cdd:pfam13863   99 LEEK 102
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1149-1229 4.23e-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: 4.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1149 EQKAEDELAKK--RAAFLLKQQRKAEEARARKQQLEAEVELKRdEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1226
Cdd:pfam05672   49 RRRAEEERARReeEARRLEEERRREEEERQRKAEEEAEEREQR-EQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQ 127


                   ...
gi 1958761072 1227 EEQ 1229
Cdd:pfam05672  128 EEQ 130
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1147-1229 4.66e-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: 41.06  E-value: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDEL----------AKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDR------LRKEEEKARR 1210
Cdd:pfam13868  197 QDEKAERDELraklyqeeqeRKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEeefermLRKQAEDEEI 276

                           90       100
                   ....*....|....*....|..
gi 1958761072 1211 ELIKQEYLRRKQQQ---ALEEQ 1229
Cdd:pfam13868  277 EQEEAEKRRMKRLEhrrELEKQ 298
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1166-1228 4.89e-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: 4.89e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958761072 1166 KQQRKAEEARARKQQLEAEV----ELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALEE 1228
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEIsrmrELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
1168-1230 5.20e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 5.20e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958761072 1168 QRKAEEARARKQQLEAEVELKRDEARRKAEED-----------RLRKEEEKARREL--IKQEYLRRKQQQALEEQG 1230
Cdd:COG2433    433 EAELEEKDERIERLERELSEARSEERREIRKDreisrldreieRLERELEEERERIeeLKRKLERLKELWKLEHSG 508
PTZ00121 PTZ00121
MAEBL; Provisional
 1148-1223 5.36e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 5.36e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958761072 1148 DEQKAEDELAKKraafllKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQ 1223
Cdd:PTZ00121  1275 EEARKADELKKA------EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
PTZ00121 PTZ00121
MAEBL; Provisional
 1147-1223 5.79e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 5.79e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958761072 1147 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQ 1223
Cdd:PTZ00121  1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE-DAKRVEIARKAEDAR-KAEEARKAEDAKKAEAARKAEE 1186
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1149-1215 6.39e-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: 38.57  E-value: 6.39e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958761072 1149 EQKAEDEL--AKKRAAFLLKQQRKaeEARARKQQLEAEVELKRDEARRKAEEDrLRKEEEKARRELIKQ 1215
Cdd:cd06503     53 LAEYEEKLaeARAEAQEIIEEARK--EAEKIKEEILAEAKEEAERILEQAKAE-IEQEKEKALAELRKE 118
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1153-1227 6.93e-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: 40.88  E-value: 6.93e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958761072 1153 EDELAKKRAAFLLKQQRKAEEARARKQQlEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALE 1227
Cdd:pfam17380  519 EKEMEERQKAIYEEERRREAEEERRKQQ-EMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1150-1229 6.98e-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: 6.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1150 QKAEDELAKKRAAFLLKQQRkAEEARARKQQLEAEVEL---KRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1226
Cdd:COG1196    270 EELRLELEELELELEEAQAE-EYELLAELARLEQDIARleeRRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                   ...
gi 1958761072 1227 EEQ 1229
Cdd:COG1196    349 AEE 351
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1164-1228 7.26e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.25  E-value: 7.26e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958761072 1164 LLKQQRKAEEARARKQQLEAEVELKRDEARRKAE--EDRLRKEEEKARRELIKQEYLRRKQQQALEE 1228
Cdd:cd16269    193 LTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQklEDQERSYEEHLRQLKEKMEEERENLLKEQER 259
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1147-1229 7.87e-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: 40.88  E-value: 7.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQ-KAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQA 1225
Cdd:pfam17380  390 KNERvRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQE 469


                   ....
gi 1958761072 1226 LEEQ 1229
Cdd:pfam17380  470 EERK 473
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
1150-1229 8.81e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.42  E-value: 8.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1150 QKAEDELAKkraAFLLKQQRKAEEARARKQQLEAeveLKRDEARRKAEEDRLRK--EEEKARRELIKQEYLRRKQQQALE 1227
Cdd:COG1842     79 EKGREDLAR---EALERKAELEAQAEALEAQLAQ---LEEQVEKLKEALRQLESklEELKAKKDTLKARAKAAKAQEKVN 152


                   ..
gi 1958761072 1228 EQ 1229
Cdd:COG1842    153 EA 154
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 1172-1229 9.05e-03

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 39.16  E-value: 9.05e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958761072 1172 EEARARKQQLEAEVELKRDEARRKAEED---RLRKEEEKARRElIKQEYLRRKQQQALEEQ 1229
Cdd:COG1390     13 EEAEAEAEEILEEAEEEAEKILEEAEEEaeeIKEEILEKAERE-AEREKRRIISSAELEAR 72
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 1147-1229 9.88e-03

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 37.93  E-value: 9.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1147 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQqleaeveLKRDEARRKAEEDRL----RKEEEKARRELIKQEyLRRKQ 1222
Cdd:pfam12474   38 IEKLEQRQTQELRRLPKRIRAEQKKRLKMFRES-------LKQEKKELKQEVEKLpkfqRKEAKRQRKEELELE-QKHEE 109


                   ....*..
gi 1958761072 1223 QQALEEQ 1229
Cdd:pfam12474  110 LEFLQAQ 116
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1148-1230 9.88e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.24  E-value: 9.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761072 1148 DEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVE---LKRDEARRKAEEdrlrkEEEKARRELIKQEYLR----- 1219
Cdd:COG2268    269 EIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEadvRKPAEAEKQAAE-----AEAEAEAEAIRAKGLAeaegk 343

                           90
                   ....*....|.
gi 1958761072 1220 RKQQQALEEQG 1230
Cdd:COG2268    344 RALAEAWNKLG 354
 
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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