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Conserved domains on  [gi|564339711|ref|XP_006233737|]
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calmodulin-regulated spectrin-associated protein 1 isoform X1 [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 ...
 1456-1584 8.35e-76

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: 246.89  E-value: 8.35e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711   1456 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGT 1535
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 564339711   1536 GPKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1584
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 239-322 2.26e-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: 2.26e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711   239 HLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHL-NKCFYLTLED 317
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 564339711   318 MLYAP 322
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 871-929 3.35e-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: 91.21  E-value: 3.35e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564339711   871 PSRHSKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 929
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU super family cl38471
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1269-1346 2.78e-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: 60.45  E-value: 2.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1269 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVE---LKRDEARRKAEEDRL-------RKEEEKARRELIKQEYL 1338
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 564339711  1339 RRKQQQAL 1346
Cdd:pfam15346  131 KREQQKIL 138
PTZ00121 super family cl31754
MAEBL; Provisional
 1179-1351 6.67e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 6.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1179 KDANIVSEQMNFKEGLDTSVQEAELSSSaitgkEHTPMEEPLRSKASLIEVDLSDLKAPDEDGEVVGHESSLElgGESDQ 1258
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEA-----EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEK 1688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1259 KPGVGFFFKDEQKAEDELAKKRAAfllKQQRKAEEARARKQQLEAEVE-LKR--DEARRKAEEDRLRKEEEKARRELIKQ 1335
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEA---EEKKKAEELKKAEEENKIKAEeAKKeaEEDKKKAEEAKKDEEEKKKIAHLKKE 1765

                         170       180
                  ....*....|....*....|
gi 564339711 1336 EYLR----RKQQQALEEQGL 1351
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 ...
 1456-1584 8.35e-76

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: 246.89  E-value: 8.35e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711   1456 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGT 1535
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 564339711   1536 GPKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1584
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1457-1575 1.50e-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: 242.95  E-value: 1.50e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1457 PKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGTG 1536
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 564339711  1537 PKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTI 1575
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 239-322 2.26e-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: 2.26e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711   239 HLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHL-NKCFYLTLED 317
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 564339711   318 MLYAP 322
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 871-929 3.35e-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: 91.21  E-value: 3.35e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564339711   871 PSRHSKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 929
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1269-1346 2.78e-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: 60.45  E-value: 2.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1269 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVE---LKRDEARRKAEEDRL-------RKEEEKARRELIKQEYL 1338
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 564339711  1339 RRKQQQAL 1346
Cdd:pfam15346  131 KREQQKIL 138
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1269-1344 8.07e-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: 52.93  E-value: 8.07e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339711  1269 EQKAEDELAKKRAAFLLKQQRKAEearaRKQQLEAEVELKRDE-ARRKAEEDRLRKEEEKARReliKQEYLRRKQQQ 1344
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAE----AKAKAEAEAERKAKEeAAKQAEEEAKAKAAAEAKK---KAEEAKKKAEA 177
PTZ00121 PTZ00121
MAEBL; Provisional
 1268-1349 6.51e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 6.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1268 DEQKAEDELAKKRAAFLLK---QQRKAEEARARKQQLEAEvELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQQ 1344
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKaaeAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEK 1563


                  ....*
gi 564339711 1345 ALEEQ 1349
Cdd:PTZ00121 1564 KKAEE 1568
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1271-1348 2.44e-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: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1271 KAEDELAKKRAAFLLKQQRK-------AEEARARKQQ-LEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQ 1342
Cdd:COG2268   241 EAEAELAKKKAEERREAETAraeaeaaYEIAEANAEReVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA 320


                  ....*.
gi 564339711 1343 QQALEE 1348
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 ...
 1278-1348 1.13e-04

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: 43.58  E-value: 1.13e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339711 1278 KKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE--DRLRKEEEKARRELIK--QEYLRRKQQQALEE 1348
Cdd:cd06503    29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiiEEARKEAEKIKEEILAeaKEEAERILEQAKAE 103
PTZ00121 PTZ00121
MAEBL; Provisional
 1179-1351 6.67e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 6.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1179 KDANIVSEQMNFKEGLDTSVQEAELSSSaitgkEHTPMEEPLRSKASLIEVDLSDLKAPDEDGEVVGHESSLElgGESDQ 1258
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEA-----EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEK 1688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1259 KPGVGFFFKDEQKAEDELAKKRAAfllKQQRKAEEARARKQQLEAEVE-LKR--DEARRKAEEDRLRKEEEKARRELIKQ 1335
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEA---EEKKKAEELKKAEEENKIKAEeAKKeaEEDKKKAEEAKKDEEEKKKIAHLKKE 1765

                         170       180
                  ....*....|....*....|
gi 564339711 1336 EYLR----RKQQQALEEQGL 1351
Cdd:PTZ00121 1766 EEKKaeeiRKEKEAVIEEEL 1785
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1265-1348 8.01e-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: 8.01e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711   1265 FFKDEQKAEDELAKKRAAFLlkqQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQ 1344
Cdd:smart00935   15 AGKAAQKQLEKEFKKRQAEL---EKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91


                    ....
gi 564339711   1345 ALEE 1348
Cdd:smart00935   92 ELQK 95
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1179-1349 9.19e-04

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: 43.62  E-value: 9.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1179 KDANIVSEQMNFKEglDTSVQEAelsssaITGKEHTPMEEPLRSKAsliEVDLSDLKAPDEDGEV-----VGHESSLELG 1253
Cdd:NF040676  192 KEEVKVQEVVKPKE--EPKVQEI------VKPKEEVKVQEEVKPKE---EEKVQEIVKPKEEAKVqeevkVKEEAKVQEI 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1254 GESDQKPGVGFFF--KDEQKAEDELAKKRAAFLLKQQRKAEEARARkQQLEAEVELKRDEARRKAEEDRLR-----KEEE 1326
Cdd:NF040676  261 AKAKEEAKAQEIAkaKEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQ-EIAKAKEEAKAREIAKAKEEEKAReiakaKEEA 339

                         170       180
                  ....*....|....*....|....
gi 564339711 1327 KARR-ELIKQEYLRRKQQQALEEQ 1349
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 ...
 1456-1584 8.35e-76

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: 246.89  E-value: 8.35e-76
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711   1456 GPKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGT 1535
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 564339711   1536 GPKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKR 1584
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1457-1575 1.50e-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: 242.95  E-value: 1.50e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1457 PKLFKEPSSKSNKPIIHNAISHCCLAGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYQPDTEEIYKLTGTG 1536
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 564339711  1537 PKSITKKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTI 1575
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 239-322 2.26e-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: 2.26e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711   239 HLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHL-NKCFYLTLED 317
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 564339711   318 MLYAP 322
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 871-929 3.35e-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: 91.21  E-value: 3.35e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564339711   871 PSRHSKDPASLLASELVQLHMQLEEKRRAIEAQKKKMEALSARQRLKLGKAAFLHVVKK 929
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1269-1346 2.78e-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: 60.45  E-value: 2.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1269 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVE---LKRDEARRKAEEDRL-------RKEEEKARRELIKQEYL 1338
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEennRKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 564339711  1339 RRKQQQAL 1346
Cdd:pfam15346  131 KREQQKIL 138
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 1277-1351 1.24e-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: 53.51  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1277 AKKRAAFLLKQQRKA---------EEARARKQQLEAEV---ELKRDEARRKAEEDRLRKEEEKARREliKQEYLRRKQQQ 1344
Cdd:pfam09756    5 AKKRAKLELKEAKRQqreaeeeerEEREKLEEKREEEYkerEEREEEAEKEKEEEERKQEEEQERKE--QEEYEKLKSQF 82


                   ....*..
gi 564339711  1345 ALEEQGL 1351
Cdd:pfam09756   83 VVEEEGT 89
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1267-1347 2.22e-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: 55.34  E-value: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1267 KDEQKAEDELAKK-RAAFLLKQQRKAEEARARKQQLEAEVELKRDEARR-----KAEEDRLRKEEEKARRELikQEYLRR 1340
Cdd:pfam15709  361 RRLQQEQLERAEKmREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKqrlqlQAAQERARQQQEEFRRKL--QELQRK 438


                   ....*..
gi 564339711  1341 KQQQALE 1347
Cdd:pfam15709  439 KQQEEAE 445
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1269-1344 8.07e-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: 52.93  E-value: 8.07e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339711  1269 EQKAEDELAKKRAAFLLKQQRKAEearaRKQQLEAEVELKRDE-ARRKAEEDRLRKEEEKARReliKQEYLRRKQQQ 1344
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAE----AKAKAEAEAERKAKEeAAKQAEEEAKAKAAAEAKK---KAEEAKKKAEA 177
PTZ00121 PTZ00121
MAEBL; Provisional
 1268-1349 6.51e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 6.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1268 DEQKAEDELAKKRAAFLLK---QQRKAEEARARKQQLEAEvELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQQ 1344
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKaaeAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEK 1563


                  ....*
gi 564339711 1345 ALEEQ 1349
Cdd:PTZ00121 1564 KKAEE 1568
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1269-1349 2.02e-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: 48.76  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1269 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEE-EKARRELIKQEYLRRKQQQALE 1347
Cdd:pfam13868  146 EKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErDELRAKLYQEEQERKERQKERE 225


                   ..
gi 564339711  1348 EQ 1349
Cdd:pfam13868  226 EA 227
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1270-1347 2.04e-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: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1270 QKAEDELAKKRAAFLLKQ-----QRKAEEARARKQQLEAevELKRDEARRKAEEDRLRKEE--EKARRELIKQEYLRRKQ 1342
Cdd:TIGR02794  126 AKQAAEAKAKAEAEAERKakeeaAKQAEEEAKAKAAAEA--KKKAEEAKKKAEAEAKAKAEaeAKAKAEEAKAKAEAAKA 203


                   ....*
gi 564339711  1343 QQALE 1347
Cdd:TIGR02794  204 KAAAE 208
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1271-1348 2.44e-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: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1271 KAEDELAKKRAAFLLKQQRK-------AEEARARKQQ-LEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQ 1342
Cdd:COG2268   241 EAEAELAKKKAEERREAETAraeaeaaYEIAEANAEReVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA 320


                  ....*.
gi 564339711 1343 QQALEE 1348
Cdd:COG2268   321 AEAEAE 326
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1286-1349 3.14e-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: 45.80  E-value: 3.14e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339711  1286 KQQRKAEEARARKQQL---EAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALEEQ 1349
Cdd:pfam05672   33 ERLEKEEEERLRKEELrrrAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERL 99
PTZ00121 PTZ00121
MAEBL; Provisional
 1268-1348 4.05e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1268 DEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDrlRKEEEKARRELIKQEYLRRKQQQALE 1347
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEA--KKAEEDKNMALRKAEEAKKAEEARIE 1595


                  .
gi 564339711 1348 E 1348
Cdd:PTZ00121 1596 E 1596
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1268-1348 4.99e-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: 45.04  E-value: 4.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1268 DEQKAEDELAKKRAAFLLKqqRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELI----KQEYLRRKQQ 1343
Cdd:pfam15346    4 ESKLLEEETARRVEEAVAK--RVEEELEKRKDEIEAEVERRVEEARKIMEKQVLEELEREREAELEeerrKEEEERKKRE 81


                   ....*
gi 564339711  1344 QaLEE 1348
Cdd:pfam15346   82 E-LER 85
PRK12704 PRK12704
phosphodiesterase; Provisional
 1261-1349 5.69e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.85  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1261 GVGFFF---KDEQKAEDelAKKRAAFLLKQQRKA-------------EEARARKQQLEAEV-----ELKRDEARRKAEED 1319
Cdd:PRK12704   19 VIGYFVrkkIAEAKIKE--AEEEAKRILEEAKKEaeaikkealleakEEIHKLRNEFEKELrerrnELQKLEKRLLQKEE 96

                          90       100       110
                  ....*....|....*....|....*....|...
gi 564339711 1320 RLRKEEE---KARRELIKQEYLRRKQQQALEEQ 1349
Cdd:PRK12704   97 NLDRKLElleKREEELEKKEKELEQKQQELEKK 129
PTZ00121 PTZ00121
MAEBL; Provisional
 1268-1349 5.76e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 5.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1268 DEQKAEDELAKKRAAFLlkqQRKAEEARARKQQLEAEVELKRDE---ARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQ 1344
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAA---KKKAEEAKKAAEAAKAEAEAAADEaeaAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394


                  ....*
gi 564339711 1345 ALEEQ 1349
Cdd:PTZ00121 1395 EAKKK 1399
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 ...
 1267-1348 7.42e-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: 44.23  E-value: 7.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1267 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVelkRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1346
Cdd:pfam00430   36 ADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENA---KKRAEKLKEEIVAAAEAEAERIIEQAAAEIEQEKDRAL 112


                   ..
gi 564339711  1347 EE 1348
Cdd:pfam00430  113 AE 114
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1267-1349 7.60e-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: 7.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAafllKQQRKAEEARARKQ---------QLEAEVELKRDEARRKAEEDRLRKE------EEKARRE 1331
Cdd:COG2268   203 IAEAEAERETEIAIA----QANREAEEAELEQEreietariaEAEAELAKKKAEERREAETARAEAEaayeiaEANAERE 278

                          90
                  ....*....|....*....
gi 564339711 1332 LIKQ-EYLRRKQQQALEEQ 1349
Cdd:COG2268   279 VQRQlEIAEREREIELQEK 297
PTZ00121 PTZ00121
MAEBL; Provisional
 1255-1345 1.01e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1255 ESDQKPGVGFFFKDEQKAEDELAKKRAafllKQQRKAEEARARkqqleAEVELKRDEARRKAEEDRLRKEEEKARRELIK 1334
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKA----EEKKKADEAKKK-----AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471

                          90
                  ....*....|.
gi 564339711 1335 QEYLRRKQQQA 1345
Cdd:PTZ00121 1472 ADEAKKKAEEA 1482
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 1268-1349 1.07e-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: 44.29  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1268 DEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKE----EEKARRELIKQEYLRRKQQ 1343
Cdd:pfam11600   12 EKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEkerrEKKEKDEKEKAEKLRLKEE 91


                   ....*.
gi 564339711  1344 QALEEQ 1349
Cdd:pfam11600   92 KRKEKQ 97
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1278-1348 1.13e-04

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: 43.58  E-value: 1.13e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339711 1278 KKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE--DRLRKEEEKARRELIK--QEYLRRKQQQALEE 1348
Cdd:cd06503    29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiiEEARKEAEKIKEEILAeaKEEAERILEQAKAE 103
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
 1266-1346 1.19e-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: 43.43  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1266 FKDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDRLRKEEEKArrELIKQEYLRRKQQQA 1345
Cdd:pfam04696   21 FKKEESKQKEKEERRAEIEKRLEEKAKQEKEELEERKRE-EREELFEERRAEQIELRALEEKL--ELKELMETWHENLKA 97


                   .
gi 564339711  1346 L 1346
Cdd:pfam04696   98 L 98
PTZ00121 PTZ00121
MAEBL; Provisional
 1267-1345 1.20e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAafllKQQRKAEEARARKQqleaEVELKRDEARRKAEE----DRLRKEEEKARRELIKQEYLRRKQ 1342
Cdd:PTZ00121 1465 KAEEAKKADEAKKKA----EEAKKADEAKKKAE----EAKKKADEAKKAAEAkkkaDEAKKAEEAKKADEAKKAEEAKKA 1536


                  ...
gi 564339711 1343 QQA 1345
Cdd:PTZ00121 1537 DEA 1539
PTZ00121 PTZ00121
MAEBL; Provisional
 1267-1345 1.20e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAAFLLKQ---QRKAEEARARKQQLE--AEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRK 1341
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKAdeaKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452


                  ....
gi 564339711 1342 QQQA 1345
Cdd:PTZ00121 1453 AEEA 1456
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1267-1349 1.42e-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: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1267 KDEQKAEDELAKK--RAAFLLKQQRKAEEARAR--KQQLEAEVELKRDEARRKAEEDRLRKEEEKARreliKQEYLRRKQ 1342
Cdd:TIGR02794   60 KPAAKKEQERQKKleQQAEEAEKQRAAEQARQKelEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA----KQAAEAKAK 135


                   ....*..
gi 564339711  1343 QQALEEQ 1349
Cdd:TIGR02794  136 AEAEAER 142
PTZ00121 PTZ00121
MAEBL; Provisional
 1268-1349 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 564339711 1268 DEQKAEDELAKKraafllKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALE 1347
Cdd:PTZ00121 1339 EEAKKAAEAAKA------EAEAAADEAEAAEEKAEAA-EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411


                  ..
gi 564339711 1348 EQ 1349
Cdd:PTZ00121 1412 KA 1413
PTZ00121 PTZ00121
MAEBL; Provisional
 1267-1349 1.77e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1346
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAA 1334


                  ...
gi 564339711 1347 EEQ 1349
Cdd:PTZ00121 1335 KKK 1337
PTZ00121 PTZ00121
MAEBL; Provisional
 1268-1345 1.84e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1268 DEQKAEDELAKKRAafllKQQRKAEEARARKQQLEAEVELKR--DEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQA 1345
Cdd:PTZ00121 1394 DEAKKKAEEDKKKA----DELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1269-1345 1.90e-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: 43.49  E-value: 1.90e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339711  1269 EQKAEDELAKKRAAfllKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQA 1345
Cdd:pfam05672   41 ERLRKEELRRRAEE---ERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEA 114
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
 1270-1331 2.34e-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: 41.00  E-value: 2.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339711 1270 QKAEDEL----AKKRAafLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRE 1331
Cdd:cd22265     9 QEYEEEIskleAERRA--LEEEENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKEDEELARKL 72
PTZ00121 PTZ00121
MAEBL; Provisional
 1267-1349 2.62e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAafllKQQRKAEEARARKQQL---EAEVELKRDEARRKAEEDRLRKEEEKAR--------RELIKQ 1335
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKA----EELKKAEEEKKKVEQLkkkEAEEKKKAEELKKAEEENKIKAAEEAKKaeedkkkaEEAKKA 1683

                          90
                  ....*....|....
gi 564339711 1336 EYLRRKQQQALEEQ 1349
Cdd:PTZ00121 1684 EEDEKKAAEALKKE 1697
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1266-1336 2.81e-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: 2.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1266 FKDEQKAEDELAKKRAAFLLKQ-QRKAEEARARKQQLEAEVE--------LKRDEARRKAEEDRLRKEEEKARRELIKQE 1336
Cdd:pfam13868  255 EAEREEEEFERMLRKQAEDEEIeQEEAEKRRMKRLEHRRELEkqieereeQRAAEREEELEEGERLREEEAERRERIEEE 334
PTZ00121 PTZ00121
MAEBL; Provisional
 1267-1345 4.03e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAAFLLKQQ----RKAEEARarkqQLEAEVELKRDEARRKAEEDR-----LRKEEEKARReliKQEY 1337
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEaeekKKAEELK----KAEEENKIKAAEEAKKAEEDKkkaeeAKKAEEDEKK---AAEA 1693


                  ....*...
gi 564339711 1338 LRRKQQQA 1345
Cdd:PTZ00121 1694 LKKEAEEA 1701
PTZ00121 PTZ00121
MAEBL; Provisional
 1267-1349 4.03e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1346
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423


                  ...
gi 564339711 1347 EEQ 1349
Cdd:PTZ00121 1424 KKK 1426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1270-1349 4.08e-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: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1270 QKAEDELAKKRAAfLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE-DRLRKEEEKARRELI---KQEYLRRKQQQA 1345
Cdd:COG1196   235 RELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELELElEEAQAEEYELLAELArleQDIARLEERRRE 313


                  ....
gi 564339711 1346 LEEQ 1349
Cdd:COG1196   314 LEER 317
PTZ00121 PTZ00121
MAEBL; Provisional
 1267-1345 4.16e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAAFLLKQQ---RKAEEAR-ARKQQLEAEVELKRDEARRKAEE-----DRLRK-EEEKARRELIKQE 1336
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEeakKKAEEAKkADEAKKKAEEAKKADEAKKKAEEakkkaDEAKKaAEAKKKADEAKKA 1518


                  ....*....
gi 564339711 1337 YLRRKQQQA 1345
Cdd:PTZ00121 1519 EEAKKADEA 1527
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1273-1351 4.30e-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: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1273 EDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRK------AEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1346
Cdd:COG4913   289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggDRLEQLEREIERLERELEERERRRARLEALL 368


                  ....*
gi 564339711 1347 EEQGL 1351
Cdd:COG4913   369 AALGL 373
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1286-1349 4.43e-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: 44.52  E-value: 4.43e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339711  1286 KQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQ-EYLRRKQQQALEEQ 1349
Cdd:pfam13868   32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQiEEREQKRQEEYEEK 96
PTZ00121 PTZ00121
MAEBL; Provisional
 1268-1347 4.77e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 4.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1268 DEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDR---LRKEE-----EKARRELIKQEYLR 1339
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE-EKKKAEEAKKAEEDKnmaLRKAEeakkaEEARIEEVMKLYEE 1603


                  ....*...
gi 564339711 1340 RKQQQALE 1347
Cdd:PTZ00121 1604 EKKMKAEE 1611
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1267-1349 5.50e-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: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAAflLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRElikQEYLRRKQQQAL 1346
Cdd:COG3064    48 EAKRQAEEEAREAKAE--AEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAA---EKAAAAAEKEKA 122


                  ...
gi 564339711 1347 EEQ 1349
Cdd:COG3064   123 EEA 125
PTZ00121 PTZ00121
MAEBL; Provisional
 1267-1345 6.03e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAAFLLKQ---QRKAEEAR-ARKQQLEAEVELKRDEARRKAEE----DRLRKEEEKARR---ELIKQ 1335
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEEAKKAdeaKKKAEEAKkAEEAKKKAEEAKKADEAKKKAEEakkaDEAKKKAEEAKKkadEAKKA 1505

                          90
                  ....*....|
gi 564339711 1336 EYLRRKQQQA 1345
Cdd:PTZ00121 1506 AEAKKKADEA 1515
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1270-1349 6.10e-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: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1270 QKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQQALEEQ 1349
Cdd:COG3064    83 EKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEA-KRKAEEERKAAEAEAAAKAEAEAARAAA 161
PTZ00121 PTZ00121
MAEBL; Provisional
 1179-1351 6.67e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 6.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1179 KDANIVSEQMNFKEGLDTSVQEAELSSSaitgkEHTPMEEPLRSKASLIEVDLSDLKAPDEDGEVVGHESSLElgGESDQ 1258
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEA-----EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEK 1688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1259 KPGVGFFFKDEQKAEDELAKKRAAfllKQQRKAEEARARKQQLEAEVE-LKR--DEARRKAEEDRLRKEEEKARRELIKQ 1335
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEA---EEKKKAEELKKAEEENKIKAEeAKKeaEEDKKKAEEAKKDEEEKKKIAHLKKE 1765

                         170       180
                  ....*....|....*....|
gi 564339711 1336 EYLR----RKQQQALEEQGL 1351
Cdd:PTZ00121 1766 EEKKaeeiRKEKEAVIEEEL 1785
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1267-1349 7.22e-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: 7.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1267 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEA----RRKAEEDRLRKEEEKARRElIKQEYlRRKQ 1342
Cdd:pfam13868  218 KERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFermlRKQAEDEEIEQEEAEKRRM-KRLEH-RREL 295


                   ....*..
gi 564339711  1343 QQALEEQ 1349
Cdd:pfam13868  296 EKQIEER 302
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1265-1348 8.01e-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: 8.01e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711   1265 FFKDEQKAEDELAKKRAAFLlkqQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQ 1344
Cdd:smart00935   15 AGKAAQKQLEKEFKKRQAEL---EKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91


                    ....
gi 564339711   1345 ALEE 1348
Cdd:smart00935   92 ELQK 95
wall_bind_EntB NF040676
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ...
 1179-1349 9.19e-04

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: 43.62  E-value: 9.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1179 KDANIVSEQMNFKEglDTSVQEAelsssaITGKEHTPMEEPLRSKAsliEVDLSDLKAPDEDGEV-----VGHESSLELG 1253
Cdd:NF040676  192 KEEVKVQEVVKPKE--EPKVQEI------VKPKEEVKVQEEVKPKE---EEKVQEIVKPKEEAKVqeevkVKEEAKVQEI 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1254 GESDQKPGVGFFF--KDEQKAEDELAKKRAAFLLKQQRKAEEARARkQQLEAEVELKRDEARRKAEEDRLR-----KEEE 1326
Cdd:NF040676  261 AKAKEEAKAQEIAkaKEEAKAQEIAKAKEEAKAQEIAKAKEEEKAQ-EIAKAKEEAKAREIAKAKEEEKAReiakaKEEA 339

                         170       180
                  ....*....|....*....|....
gi 564339711 1327 KARR-ELIKQEYLRRKQQQALEEQ 1349
Cdd:NF040676  340 KAREiAKAKEEAKAREIAKAKEEE 363
PTZ00121 PTZ00121
MAEBL; Provisional
 1267-1349 9.34e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 9.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAAFLLKQQRKAEEAR-ARKQQLEAEVELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQQA 1345
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKkAEEARIEEVMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEEEKKKVEQ 1637


                  ....
gi 564339711 1346 LEEQ 1349
Cdd:PTZ00121 1638 LKKK 1641
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 1267-1332 9.72e-04

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: 40.67  E-value: 9.72e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339711  1267 KDEQKAEDELAKKRAAFLLKQQRKAEEAR---ARKQQLEAE-------VELKRDEARRKAEE-DRLRKEEEKARREL 1332
Cdd:pfam20492   44 RQAEEEAERLEQKRQEAEEEKERLEESAEmeaEEKEQLEAElaeaqeeIARLEEEVERKEEEaRRLQEELEEAREEE 120
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1278-1348 9.89e-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: 41.31  E-value: 9.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339711 1278 KKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE--DRLRKEEEKARRELIKQ--EYLRRKQQQALEE 1348
Cdd:COG0711    30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEiiAEARKEAEAIAEEAKAEaeAEAERIIAQAEAE 104
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1269-1350 1.02e-03

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.30  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1269 EQKAEDELAKKRAAFLLKQ-----QRKAEEARAR-----KQQLEAEVELKRDEARRKAEEDRLRKEEE---KARRELIKQ 1335
Cdd:TIGR02794  141 ERKAKEEAAKQAEEEAKAKaaaeaKKKAEEAKKKaeaeaKAKAEAEAKAKAEEAKAKAEAAKAKAAAEaaaKAEAEAAAA 220

                           90
                   ....*....|....*
gi 564339711  1336 EYLRRKQQQALEEQG 1350
Cdd:TIGR02794  221 AAAEAERKADEAELG 235
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1268-1349 1.02e-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: 43.37  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1268 DEQKAEDELAKKRAA--FLLKQQRKAEEARARKQQLEAEVELKRDE-ARRKAEEDRLRKEEE---KARRELIKQEyLRRK 1341
Cdd:pfam13868  114 DQAEAEEKLEKQRQLreEIDEFNEEQAEWKELEKEEEREEDERILEyLKEKAEREEEREAEReeiEEEKEREIAR-LRAQ 192


                   ....*...
gi 564339711  1342 QQQALEEQ 1349
Cdd:pfam13868  193 QEKAQDEK 200
PTZ00121 PTZ00121
MAEBL; Provisional
 1267-1349 1.11e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAafllKQQRKAEEARARKQqleaEVELKRDEARRKAEEDR-----LRKEEEKARRELIKQEYLRRK 1341
Cdd:PTZ00121 1297 KAEEKKKADEAKKKA----EEAKKADEAKKKAE----EAKKKADAAKKKAEEAKkaaeaAKAEAEAAADEAEAAEEKAEA 1368


                  ....*...
gi 564339711 1342 QQQALEEQ 1349
Cdd:PTZ00121 1369 AEKKKEEA 1376
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1269-1351 1.11e-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: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1269 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARR-----KAEEDRLRKEEEKARRELIKQEYLRRKQQ 1343
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELaeleaELEELRLELEELELELEEAQAEEYELLAE 296


                  ....*...
gi 564339711 1344 QALEEQGL 1351
Cdd:COG1196   297 LARLEQDI 304
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1267-1349 1.13e-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: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAAfLLKQQRKAEEARARKQQLEAEVE-----LKRDEARRKAEEDRLrKEEEKARRELIKQEYLRRK 1341
Cdd:COG1196   260 AELAELEAELEELRLE-LEELELELEEAQAEEYELLAELArleqdIARLEERRRELEERL-EELEEELAELEEELEELEE 337


                  ....*...
gi 564339711 1342 QQQALEEQ 1349
Cdd:COG1196   338 ELEELEEE 345
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 1268-1348 1.29e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1268 DEQKAEDELAKkraafLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEdrLRKEEEKARRELiKQEYlrrkqQQALE 1347
Cdd:PRK00409  514 DKEKLNELIAS-----LEELERELEQKAEEAEALLKEAEKLKEELEEKKEK--LQEEEDKLLEEA-EKEA-----QQAIK 580


                  .
gi 564339711 1348 E 1348
Cdd:PRK00409  581 E 581
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1267-1351 1.31e-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: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAAfLLKQQRKAEEARARKQQLEAEVELKRdEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1346
Cdd:COG1196   246 AELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRRELEERLEELEE 323


                  ....*
gi 564339711 1347 EEQGL 1351
Cdd:COG1196   324 ELAEL 328
PTZ00121 PTZ00121
MAEBL; Provisional
 1270-1339 1.34e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1270 QKAEDeLAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRlRKEEEKARRELIKQEYLR 1339
Cdd:PTZ00121 1194 RKAED-ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK-KAEEERNNEEIRKFEEAR 1261
eIF3_subunit pfam08597
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of ...
 1267-1328 1.38e-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: 42.28  E-value: 1.38e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339711  1267 KDEQKAEDELAKKRAA-FLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKA 1328
Cdd:pfam08597   45 EEKEKAAKAAAAKAKKkKKSKKQKIAEKEAERKAEEEAEEEEELTPEDEAARKLRLRKAEEES 107
PRK11637 PRK11637
AmiB activator; Provisional
 1269-1345 1.58e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 42.76  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1269 EQKAEDELAKKRAAFLL----KQQRKAEEAR-ARKQQLEA-EVELKRDEAR---RKAEEDRLR------KEEEKAR--RE 1331
Cdd:PRK11637  184 AQKAELEEKQSQQKTLLyeqqAQQQKLEQARnERKKTLTGlESSLQKDQQQlseLRANESRLRdsiaraEREAKARaeRE 263

                          90
                  ....*....|....
gi 564339711 1332 LIKQEYLRRKQQQA 1345
Cdd:PRK11637  264 AREAARVRDKQKQA 277
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1267-1349 1.64e-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: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1267 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVE---LKRDEARRKAEEDRLRKEEEKARRELIKQEYL----- 1338
Cdd:pfam13868   58 EEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLqerEQMDEIVERIQEEDQAEAEEKLEKQRQLREEIdefne 137

                           90
                   ....*....|....
gi 564339711  1339 ---RRKQQQALEEQ 1349
Cdd:pfam13868  138 eqaEWKELEKEEER 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1267-1349 1.65e-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: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELAKKRAAfLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEdrlRKEEEKARRELIKQEYLRRKQQQAL 1346
Cdd:COG1196   316 ERLEELEEELAELEEE-LEELEEELEELEEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEAEEELEELAEELLEA 391


                  ...
gi 564339711 1347 EEQ 1349
Cdd:COG1196   392 LRA 394
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 ...
 1278-1348 1.67e-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: 40.37  E-value: 1.67e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339711  1278 KKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEE--DRLRKEEEKARRELIKQ--EYLRRKQQQALEE 1348
Cdd:pfam00430   29 DKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEiiENAKKRAEKLKEEIVAAaeAEAERIIEQAAAE 103
PTZ00121 PTZ00121
MAEBL; Provisional
 1255-1345 1.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1255 ESDQKPGVGFFFKDEQKAEdELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDR----LRKEEEKARR 1330
Cdd:PTZ00121 1149 EDAKRVEIARKAEDARKAE-EARKAEDAKKAEAARKAEEVRKAEELRKAE-DARKAEAARKAEEERkaeeARKAEDAKKA 1226

                          90
                  ....*....|....*.
gi 564339711 1331 ELIKQ-EYLRRKQQQA 1345
Cdd:PTZ00121 1227 EAVKKaEEAKKDAEEA 1242
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1269-1345 1.82e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.49  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1269 EQKAEDELAKKRAAfllKQQRKAEEARARKQ---QLEAEVELKR-DEARRKAEEDRLRKEEEKARReliKQEYLRRKQQQ 1344
Cdd:PRK09510  115 EQKKQAEEAAKQAA---LKQKQAEEAAAKAAaaaKAKAEAEAKRaAAAAKKAAAEAKKKAEAEAAK---KAAAEAKKKAE 188


                  .
gi 564339711 1345 A 1345
Cdd:PRK09510  189 A 189
PTZ00121 PTZ00121
MAEBL; Provisional
 1268-1340 1.85e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339711 1268 DEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRR 1340
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR-KAEDAKRVEIARKAEDARK 1165
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1267-1349 2.05e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1267 KDEQKAEDELAKKRAAFLLKQQRKAEEARAR-----KQQLEAEVELKRdeaRRKAEEDRLRKEEEKARRELIKQEYL--R 1339
Cdd:pfam13868   39 KEEERRLDEMMEEERERALEEEEEKEEERKEerkryRQELEEQIEERE---QKRQEEYEEKLQEREQMDEIVERIQEedQ 115

                           90
                   ....*....|
gi 564339711  1340 RKQQQALEEQ 1349
Cdd:pfam13868  116 AEAEEKLEKQ 125
PTZ00121 PTZ00121
MAEBL; Provisional
 1267-1345 2.10e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1267 KDEQKAEDELA----KKRAAFLLKQQ--RKAEEARARKQQLEAEVELKR--DEARRKAEEDRLRKEEEKARRELIKQEYL 1338
Cdd:PTZ00121 1350 AEAEAAADEAEaaeeKAEAAEKKKEEakKKADAAKKKAEEKKKADEAKKkaEEDKKKADELKKAAAAKKKADEAKKKAEE 1429


                  ....*..
gi 564339711 1339 RRKQQQA 1345
Cdd:PTZ00121 1430 KKKADEA 1436
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 1264-1330 2.44e-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: 2.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564339711  1264 FFFKDEQKA------EDELAKKRAAfllKQQRKAEEARARKQQLEAEvelKRDEARRKAEEDRLRKEEEKARR 1330
Cdd:pfam07946  252 AKLRPEALKkakktrEEEIEKIKKA---AEEERAEEAQEKKEEAKKK---EREEKLAKLSPEEQRKYEEKERK 318
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 1270-1341 2.54e-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: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1270 QKA--EDELAKKRAAFLLKQQR---------------KAEEAR---ARKQQLEAEVELKRDEARRKAE-EDRLRKEEEKA 1328
Cdd:pfam12037  101 QRAqyQDELARKRYQDQLEAQRrrneellrkqeesvaKQEAMRiqaQRRQTEEHEAELRRETERAKAEaEAEARAKEERE 180

                           90
                   ....*....|...
gi 564339711  1329 RRELIKqEYLRRK 1341
Cdd:pfam12037  181 NEDLNL-EQLREK 192
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1267-1349 2.55e-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: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1267 KDEQKAEDELAKKR-AAFLLKQQRKAEEARARKQQL-----EAEVELKRDEARRKAEEDRLRKEEE--KARRELIKQEYL 1338
Cdd:pfam13868  171 REAEREEIEEEKEReIARLRAQQEKAQDEKAERDELraklyQEEQERKERQKEREEAEKKARQRQElqQAREEQIELKER 250

                           90
                   ....*....|.
gi 564339711  1339 RRKQQQALEEQ 1349
Cdd:pfam13868  251 RLAEEAEREEE 261
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1268-1351 2.65e-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: 42.74  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1268 DEQKAEDELAKKRAAfLLKQQRKAEEARA----RKQQLEA---EVELKRDEARRKAEEDRLRKEEEKARRELIKQEyLRR 1340
Cdd:TIGR02168  863 ELEELIEELESELEA-LLNERASLEEALAllrsELEELSEelrELESKRSELRRELEELREKLAQLELRLEGLEVR-IDN 940

                           90
                   ....*....|.
gi 564339711  1341 KQQQALEEQGL 1351
Cdd:TIGR02168  941 LQERLSEEYSL 951
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 1267-1349 2.98e-03

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 39.09  E-value: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1267 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEE-EKARRELIKQEYLRRKQQQA 1345
Cdd:pfam13863   19 REEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEkEKEIKKLTAQIEELKSEISK 98


                   ....
gi 564339711  1346 LEEQ 1349
Cdd:pfam13863   99 LEEK 102
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1270-1335 3.23e-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: 39.77  E-value: 3.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339711 1270 QKAEDELAKKRAAFLLKQQRKAEEARARKQQL--EAEVELKRDEARRKAE-EDRLRKEEEKARRELIKQ 1335
Cdd:COG0711    51 EAALAEYEEKLAEARAEAAEIIAEARKEAEAIaeEAKAEAEAEAERIIAQaEAEIEQERAKALAELRAE 119
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1269-1349 3.24e-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: 40.02  E-value: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1269 EQKAEDELAKK--RAAFLLKQQRKAEEARARKQQLEAEVELKRdEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1346
Cdd:pfam05672   49 RRRAEEERARReeEARRLEEERRREEEERQRKAEEEAEEREQR-EQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQ 127


                   ...
gi 564339711  1347 EEQ 1349
Cdd:pfam05672  128 EEQ 130
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1269-1349 3.32e-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: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1269 EQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALEE 1348
Cdd:COG3064    32 EQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAE 111


                  .
gi 564339711 1349 Q 1349
Cdd:COG3064   112 K 112
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
 1265-1349 3.51e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 39.60  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1265 FFKDEQKAEDElakkRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKA---------EEDRLRKEE---------- 1325
Cdd:PRK07353   26 FYKPVGKVVEE----REDYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAqaviaeaeaEADKLAAEAlaeaqaeaqa 101

                          90       100
                  ....*....|....*....|....*.
gi 564339711 1326 --EKARRELIKQeylRRKQQQALEEQ 1349
Cdd:PRK07353  102 skEKARREIEQQ---KQAALAQLEQQ 124
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1286-1348 3.80e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.03  E-value: 3.80e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339711  1286 KQQRKAEEARARKQQLEAEV----ELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALEE 1348
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEIsrmrELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1267-1349 4.70e-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: 4.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1267 KDEQKAEDEL----------AKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDR------LRKEEEKARR 1330
Cdd:pfam13868  197 QDEKAERDELraklyqeeqeRKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEeefermLRKQAEDEEI 276

                           90       100
                   ....*....|....*....|..
gi 564339711  1331 ELIKQEYLRRKQQQ---ALEEQ 1349
Cdd:pfam13868  277 EQEEAEKRRMKRLEhrrELEKQ 298
PTZ00121 PTZ00121
MAEBL; Provisional
 1267-1343 4.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 4.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339711 1267 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEvELKRDEARRKAEEDRlRKEEEKARRELIKQEYLRRKQQ 1343
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE-DAKRVEIARKAEDAR-KAEEARKAEDAKKAEAARKAEE 1186
PTZ00121 PTZ00121
MAEBL; Provisional
 1268-1343 4.94e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 4.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339711 1268 DEQKAEDELAKKraafllKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQ 1343
Cdd:PTZ00121 1275 EEARKADELKKA------EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1273-1347 5.24e-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: 41.65  E-value: 5.24e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564339711  1273 EDELAKKRAAFLLKQQRKAEEARARKQQlEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQALE 1347
Cdd:pfam17380  519 EKEMEERQKAIYEEERRREAEEERRKQQ-EMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
1288-1350 5.67e-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: 5.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339711 1288 QRKAEEARARKQQLEAEVELKRDEARRKAEED-----------RLRKEEEKARREL--IKQEYLRRKQQQALEEQG 1350
Cdd:COG2433   433 EAELEEKDERIERLERELSEARSEERREIRKDreisrldreieRLERELEEERERIeeLKRKLERLKELWKLEHSG 508
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1267-1349 6.06e-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: 6.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1267 KDEQ-KAEDELAKKRAAFLLKQQRKAEEARARKQQLEAEVELKRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQA 1345
Cdd:pfam17380  390 KNERvRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQE 469


                   ....
gi 564339711  1346 LEEQ 1349
Cdd:pfam17380  470 EERK 473
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 1284-1348 7.17e-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: 7.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339711 1284 LLKQQRKAEEARARKQQLEAEVELKRDEARRKAE--EDRLRKEEEKARRELIKQEYLRRKQQQALEE 1348
Cdd:cd16269   193 LTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQklEDQERSYEEHLRQLKEKMEEERENLLKEQER 259
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 1267-1349 7.18e-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: 38.70  E-value: 7.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1267 KDEQKAEDELAKKRAAFLLKQQRKAEEARARKQqleaeveLKRDEARRKAEEDRL----RKEEEKARRELIKQEyLRRKQ 1342
Cdd:pfam12474   38 IEKLEQRQTQELRRLPKRIRAEQKKRLKMFRES-------LKQEKKELKQEVEKLpkfqRKEAKRQRKEELELE-QKHEE 109


                   ....*..
gi 564339711  1343 QQALEEQ 1349
Cdd:pfam12474  110 LEFLQAQ 116
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1269-1335 8.01e-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: 38.19  E-value: 8.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339711 1269 EQKAEDEL--AKKRAAFLLKQQRKaeEARARKQQLEAEVELKRDEARRKAEEDrLRKEEEKARRELIKQ 1335
Cdd:cd06503    53 LAEYEEKLaeARAEAQEIIEEARK--EAEKIKEEILAEAKEEAERILEQAKAE-IEQEKEKALAELRKE 118
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1270-1349 8.22e-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: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711 1270 QKAEDELAKKRAAFLLKQQRkAEEARARKQQLEAEVEL---KRDEARRKAEEDRLRKEEEKARRELIKQEYLRRKQQQAL 1346
Cdd:COG1196   270 EELRLELEELELELEEAQAE-EYELLAELARLEQDIARleeRRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348


                  ...
gi 564339711 1347 EEQ 1349
Cdd:COG1196   349 AEE 351
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1255-1349 9.38e-03

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: 40.32  E-value: 9.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339711  1255 ESDQKPGVGFFFKDEQK--AEDELAKKRAafllkQQRKAEEARARKQQ----------------LEAEVELkrdEARRKA 1316
Cdd:pfam15709  315 RSEEDPSKALLEKREQEkaSRDRLRAERA-----EMRRLEVERKRREQeeqrrlqqeqleraekMREELEL---EQQRRF 386

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 564339711  1317 EEDRLRK---EEEKARREliKQEYLRRKQQQALEEQ 1349
Cdd:pfam15709  387 EEIRLRKqrlEEERQRQE--EEERKQRLQLQAAQER 420
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 1292-1349 9.84e-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: 9.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564339711 1292 EEARARKQQLEAEVELKRDEARRKAEED---RLRKEEEKARRElIKQEYLRRKQQQALEEQ 1349
Cdd:COG1390    13 EEAEAEAEEILEEAEEEAEKILEEAEEEaeeIKEEILEKAERE-AEREKRRIISSAELEAR 72
 
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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