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Conserved domains on  [gi|2038291192|ref|XP_041430107|]
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calmodulin-regulated spectrin-associated protein 1 isoform X1 [Xenopus laevis]

Protein Classification

calponin homology domain-containing protein( domain architecture ID 13777712)

calponin homology (CH) domain-containing protein may bind actin filament (F-actin) or serve a regulatory function

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 ...
 1448-1576 1.80e-72

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: 237.64  E-value: 1.80e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192  1448 GPKLYKEPSSKSNKPLIHNAISHCCLAGKVNEAIKNSTLDELEKCDSNHYIILFRDAGCQFRALYSYYPETEEICKLTGT 1527
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 2038291192  1528 GPKNITKKMIDKLYKYSSDRKQFTVIPAKTMSASVDALTIHNHLWQAKR 1576
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 241-324 3.87e-37

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


:

Pssm-ID: 432229  Cd Length: 85  Bit Score: 134.73  E-value: 3.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192  241 HPSSRHLPYFPILEDLTKDISDGAALLAVIHFYCPEQMKLDDICLKEVTSMGDSVYNIQLLKEFSNEYL-NKCFYLTLED 319
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 2038291192  320 MLYTP 324
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 857-915 1.02e-21

Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on calmodulin-regulated spectrin-associated proteins in eukaryotes that binds spectrin. CAMSAPs are vertebrate microtubule-binding proteins, representatives of a family of cytoskeletal proteins that arose in animals. This conserved CC1 region binds to both spectrin and Ca2+/calmodulin in vitro, although the binding of Ca2+/calmodulin inhibited the binding of spectrin. CC1 appears to be a functional region of CAMSAP1 that links spectrin-binding to neurite outgrowth.


:

Pssm-ID: 465344 [Multi-domain]  Cd Length: 59  Bit Score: 89.67  E-value: 1.02e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291192  857 PGRQNRDHANVLASELVQLHMQLEEKRRVIEAQKKKMESLSARQRLKLGKAAFLHVVKK 915
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU super family cl38471
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1259-1336 3.62e-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: 60.06  E-value: 3.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1259 EQKAEDELAKKRAAFLMKQQRKAEEARLRKQQLEAEVEQ---KRDDARRKAEEDRI-------RKDEEKARRELIKQEYL 1328
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEEnnrKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 2038291192 1329 RRKQEQIL 1336
Cdd:pfam15346  131 KREQQKIL 138
PTZ00121 super family cl31754
MAEBL; Provisional
 1169-1339 7.86e-06

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 7.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1169 LSTSKDANIISEQMHREVISSSRVAGVSTSESsgkENVPVDERHKSSLIEVDLSDLKEPDEGEEESDHPEKTKDIISDDQ 1248
Cdd:PTZ00121  1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA---EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1249 KSGVGFFFKDEQKAEDELAKKRAAflmKQQRKAEEARLRKQQLEAEVEQ---KRDDARRKAEEDRIRKDEEK-----ARR 1320
Cdd:PTZ00121  1689 KAAEALKKEAEEAKKAEELKKKEA---EEKKKAEELKKAEEENKIKAEEakkEAEEDKKKAEEAKKDEEEKKkiahlKKE 1765

                          170
                   ....*....|....*....
gi 2038291192 1321 ELIKQEYLRRKQEQILEEQ 1339
Cdd:PTZ00121  1766 EEKKAEEIRKEKEAVIEEE 1784
 
Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1448-1576 1.80e-72

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: 237.64  E-value: 1.80e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192  1448 GPKLYKEPSSKSNKPLIHNAISHCCLAGKVNEAIKNSTLDELEKCDSNHYIILFRDAGCQFRALYSYYPETEEICKLTGT 1527
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 2038291192  1528 GPKNITKKMIDKLYKYSSDRKQFTVIPAKTMSASVDALTIHNHLWQAKR 1576
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1449-1567 2.30e-70

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: 231.01  E-value: 2.30e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1449 PKLYKEPSSKSNKPLIHNAISHCCLAGKVNEAIKNSTLDELEKCDSNHYIILFRDAGCQFRALYSYYPETEEICKLTGTG 1528
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2038291192 1529 PKNITKKMIDKLYKYSSDRKQFTVIPAKTMSASVDALTI 1567
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 241-324 3.87e-37

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 134.73  E-value: 3.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192  241 HPSSRHLPYFPILEDLTKDISDGAALLAVIHFYCPEQMKLDDICLKEVTSMGDSVYNIQLLKEFSNEYL-NKCFYLTLED 319
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 2038291192  320 MLYTP 324
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 857-915 1.02e-21

Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on calmodulin-regulated spectrin-associated proteins in eukaryotes that binds spectrin. CAMSAPs are vertebrate microtubule-binding proteins, representatives of a family of cytoskeletal proteins that arose in animals. This conserved CC1 region binds to both spectrin and Ca2+/calmodulin in vitro, although the binding of Ca2+/calmodulin inhibited the binding of spectrin. CC1 appears to be a functional region of CAMSAP1 that links spectrin-binding to neurite outgrowth.


Pssm-ID: 465344 [Multi-domain]  Cd Length: 59  Bit Score: 89.67  E-value: 1.02e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291192  857 PGRQNRDHANVLASELVQLHMQLEEKRRVIEAQKKKMESLSARQRLKLGKAAFLHVVKK 915
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1259-1336 3.62e-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: 60.06  E-value: 3.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1259 EQKAEDELAKKRAAFLMKQQRKAEEARLRKQQLEAEVEQ---KRDDARRKAEEDRI-------RKDEEKARRELIKQEYL 1328
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEEnnrKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 2038291192 1329 RRKQEQIL 1336
Cdd:pfam15346  131 KREQQKIL 138
PTZ00121 PTZ00121
MAEBL; Provisional
 1169-1339 7.86e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 7.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1169 LSTSKDANIISEQMHREVISSSRVAGVSTSESsgkENVPVDERHKSSLIEVDLSDLKEPDEGEEESDHPEKTKDIISDDQ 1248
Cdd:PTZ00121  1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA---EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1249 KSGVGFFFKDEQKAEDELAKKRAAflmKQQRKAEEARLRKQQLEAEVEQ---KRDDARRKAEEDRIRKDEEK-----ARR 1320
Cdd:PTZ00121  1689 KAAEALKKEAEEAKKAEELKKKEA---EEKKKAEELKKAEEENKIKAEEakkEAEEDKKKAEEAKKDEEEKKkiahlKKE 1765

                          170
                   ....*....|....*....
gi 2038291192 1321 ELIKQEYLRRKQEQILEEQ 1339
Cdd:PTZ00121  1766 EEKKAEEIRKEKEAVIEEE 1784
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1218-1326 3.62e-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: 47.92  E-value: 3.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1218 EVDLSDLKEPDEGEEESDHPEKTKDIISDDQKSGVgfffKDEQKAEDELAKKRAAFLMKQ-----QRKAEEARLRKQQLE 1292
Cdd:TIGR02794   88 QARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE----EAKAKQAAEAKAKAEAEAERKakeeaAKQAEEEAKAKAAAE 163

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2038291192 1293 AevEQKRDDARRKAEEDRIRKDE--EKARRELIKQE 1326
Cdd:TIGR02794  164 A--KKKAEEAKKKAEAEAKAKAEaeAKAKAEEAKAK 197
PTZ00121 PTZ00121
MAEBL; Provisional
 1209-1335 7.69e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 7.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1209 DERHKSSLIEVDLSDLKEPDEGEEESDHPEKTKDII---SDDQKSGVGFFFKDEQKAEDELA----KKRAAFLMKQQRKA 1281
Cdd:PTZ00121  1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAkkkAEEAKKAAEAAKAEAEAAADEAEaaeeKAEAAEKKKEEAKK 1378

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038291192 1282 EEARLRKQqleAEVEQKRDDARRKAEEDRIRKDE-EKARRELIKQEYLRRKQEQI 1335
Cdd:PTZ00121  1379 KADAAKKK---AEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEK 1430
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1257-1339 8.38e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.79  E-value: 8.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1257 KDEQKAEDELAKKRAaflmKQQRKAEEARLRKQ---------QLEAEVEQKRDDARRKAEEDRIRKD------EEKARRE 1321
Cdd:COG2268    203 IAEAEAERETEIAIA----QANREAEEAELEQEreietariaEAEAELAKKKAEERREAETARAEAEaayeiaEANAERE 278

                           90
                   ....*....|....*....
gi 2038291192 1322 LIKQEYLRRKQEQI-LEEQ 1339
Cdd:COG2268    279 VQRQLEIAEREREIeLQEK 297
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
 1260-1321 1.79e-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: 41.39  E-value: 1.79e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291192 1260 QKAEDEL----AKKRAafLMKQQRKAEEARLRKQQLEAEVEQKRDDARRKAEEDRIRKDEEKARRE 1321
Cdd:cd22265      9 QEYEEEIskleAERRA--LEEEENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKEDEELARKL 72
Caldesmon pfam02029
Caldesmon;
1023-1335 2.00e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 46.01  E-value: 2.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1023 QAIMKISQQQEMLMKAPSMAVPPlpsssqDHKLKPSVQFVEPISPPGMPIVRKTTRFGQGRNARSLRVTEQKLAKEKmqs 1102
Cdd:pfam02029   17 EERRRQKEEEEPSGQVTESVEPN------EHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQK--- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1103 sSRVITPTNSIETVPHLKSVQPLKSPSVPTEESPVEvvPEQGSASQDKPTTGGFRLHNDNSQRTFVLSTSKDANIISEQM 1182
Cdd:pfam02029   88 -EFDPTIADEKESVAERKENNEEEENSSWEKEEKRD--SRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSE 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1183 HREVISSSRVAGVSTSESSGKENVPVDERHKSSLIEVDLSDLKEPDEGEEE-SDHPEKTKDIISDDQKSgvgffFKDEQK 1261
Cdd:pfam02029  165 EAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEvTKLKVTTKRRQGGLSQS-----QEREEE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1262 AEDELAKKRAAFLMKQQRKAEEA----RLRKQQLEAEVE-----QKRDDARRKAEEDRIRKDEEKARRELIKQEYLRRKQ 1332
Cdd:pfam02029  240 AEVFLEAEQKLEELRRRRQEKESeefeKLRQKQQEAELEleelkKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMK 319


                   ...
gi 2038291192 1333 EQI 1335
Cdd:pfam02029  320 EEI 322
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 253-339 6.13e-03

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409067  Cd Length: 114  Bit Score: 38.05  E-value: 6.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192  253 LEDLTKDISDGAALLAVIHFYCPEQMKLDDIclKEVTSMGDSVYNIQLLKEFSNEYLNKCFyLTLEDmlytplVLKPN-- 330
Cdd:cd21218     33 VTNFSSDLKDGEVYALLLHSLAPELCDKELV--LEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPED------IVSGNpr 103

                           90
                   ....*....|
gi 2038291192  331 -IMVFIAELF 339
Cdd:cd21218    104 lNLAFVATLF 113
 
Name Accession Description Interval E-value
CAMSAP_CKK smart01051
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1448-1576 1.80e-72

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: 237.64  E-value: 1.80e-72
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192  1448 GPKLYKEPSSKSNKPLIHNAISHCCLAGKVNEAIKNSTLDELEKCDSNHYIILFRDAGCQFRALYSYYPETEEICKLTGT 1527
Cdd:smart01051    1 GPKLYKEPSAKSNRFIIHNALSHCCLAGKVNEPQKNKILEEMEKSEANHFLILFRDAKCQFRALYTLNPETEELVKLYGN 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 2038291192  1528 GPKNITKKMIDKLYKYSSDRKQFTVIPAKTMSASVDALTIHNHLWQAKR 1576
Cdd:smart01051   81 GPRVITSKMVESLYKYDSSRKQFTQIPSKTLSVSVDAFTIKNHLWQTKK 129
CAMSAP_CKK pfam08683
Microtubule-binding calmodulin-regulated spectrin-associated; This is the C-terminal domain of ...
 1449-1567 2.30e-70

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: 231.01  E-value: 2.30e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1449 PKLYKEPSSKSNKPLIHNAISHCCLAGKVNEAIKNSTLDELEKCDSNHYIILFRDAGCQFRALYSYYPETEEICKLTGTG 1528
Cdd:pfam08683    1 PKLFKKPSAKSNKKIIHNALSHCCLAGKVNEDQKNKILEELEKSESKHFLILFRDSGCQFRALYSYNPETEELVKLHGIG 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2038291192 1529 PKNITKKMIDKLYKYSSDRKQFTVIPAKTMSASVDALTI 1567
Cdd:pfam08683   81 PRVVTPKMIEKFYKYNSGRKQFTEIPTKTLSVSIDAFTI 119
CAMSAP_CH pfam11971
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
 241-324 3.87e-37

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


Pssm-ID: 432229  Cd Length: 85  Bit Score: 134.73  E-value: 3.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192  241 HPSSRHLPYFPILEDLTKDISDGAALLAVIHFYCPEQMKLDDICLKEVTSMGDSVYNIQLLKEFSNEYL-NKCFYLTLED 319
Cdd:pfam11971    1 PLSQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESMSLADSLYNIQLLQEFCQRHLgNRCCHLTLED 80


                   ....*
gi 2038291192  320 MLYTP 324
Cdd:pfam11971   81 LLYAR 85
CAMSAP_CC1 pfam17095
Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on ...
 857-915 1.02e-21

Spectrin-binding region of Ca2+-Calmodulin; CAMSAP_CC1 is the conserved region on calmodulin-regulated spectrin-associated proteins in eukaryotes that binds spectrin. CAMSAPs are vertebrate microtubule-binding proteins, representatives of a family of cytoskeletal proteins that arose in animals. This conserved CC1 region binds to both spectrin and Ca2+/calmodulin in vitro, although the binding of Ca2+/calmodulin inhibited the binding of spectrin. CC1 appears to be a functional region of CAMSAP1 that links spectrin-binding to neurite outgrowth.


Pssm-ID: 465344 [Multi-domain]  Cd Length: 59  Bit Score: 89.67  E-value: 1.02e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291192  857 PGRQNRDHANVLASELVQLHMQLEEKRRVIEAQKKKMESLSARQRLKLGKAAFLHVVKK 915
Cdd:pfam17095    1 PGDDSPSASPELASELSQLRLKLEEKRRAIEQQKKRMEAAFARQRQKLGKAAFLQVVKK 59
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1259-1336 3.62e-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: 60.06  E-value: 3.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1259 EQKAEDELAKKRAAFLMKQQRKAEEARLRKQQLEAEVEQ---KRDDARRKAEEDRI-------RKDEEKARRELIKQEYL 1328
Cdd:pfam15346   51 EKQVLEELEREREAELEEERRKEEEERKKREELERILEEnnrKIEEAQRKEAEERLamleeqrRMKEERQRREKEEEERE 130


                   ....*...
gi 2038291192 1329 RRKQEQIL 1336
Cdd:pfam15346  131 KREQQKIL 138
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1257-1337 3.67e-07

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 54.57  E-value: 3.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1257 KDEQKAEDELAKK-RAAFLMKQQRKAEEARLRKQQLEAEVEQKRDDARR-----KAEEDRIRKDEEKARRELikQEYLRR 1330
Cdd:pfam15709  361 RRLQQEQLERAEKmREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKqrlqlQAAQERARQQQEEFRRKL--QELQRK 438


                   ....*..
gi 2038291192 1331 KQEQILE 1337
Cdd:pfam15709  439 KQQEEAE 445
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 1267-1341 4.53e-06

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: 48.88  E-value: 4.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1267 AKKRAAFLMKQQRKA-----EEARLRKQQLEAEVEQKRDDARR-------KAEEDRIRKDEEKARREliKQEYLRRKQEQ 1334
Cdd:pfam09756    5 AKKRAKLELKEAKRQqreaeEEEREEREKLEEKREEEYKEREEreeeaekEKEEEERKQEEEQERKE--QEEYEKLKSQF 82


                   ....*..
gi 2038291192 1335 ILEEQGL 1341
Cdd:pfam09756   83 VVEEEGT 89
PTZ00121 PTZ00121
MAEBL; Provisional
 1169-1339 7.86e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 7.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1169 LSTSKDANIISEQMHREVISSSRVAGVSTSESsgkENVPVDERHKSSLIEVDLSDLKEPDEGEEESDHPEKTKDIISDDQ 1248
Cdd:PTZ00121  1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA---EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1249 KSGVGFFFKDEQKAEDELAKKRAAflmKQQRKAEEARLRKQQLEAEVEQ---KRDDARRKAEEDRIRKDEEK-----ARR 1320
Cdd:PTZ00121  1689 KAAEALKKEAEEAKKAEELKKKEA---EEKKKAEELKKAEEENKIKAEEakkEAEEDKKKAEEAKKDEEEKKkiahlKKE 1765

                          170
                   ....*....|....*....
gi 2038291192 1321 ELIKQEYLRRKQEQILEEQ 1339
Cdd:PTZ00121  1766 EEKKAEEIRKEKEAVIEEE 1784
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1218-1326 3.62e-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: 47.92  E-value: 3.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1218 EVDLSDLKEPDEGEEESDHPEKTKDIISDDQKSGVgfffKDEQKAEDELAKKRAAFLMKQ-----QRKAEEARLRKQQLE 1292
Cdd:TIGR02794   88 QARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE----EAKAKQAAEAKAKAEAEAERKakeeaAKQAEEEAKAKAAAE 163

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2038291192 1293 AevEQKRDDARRKAEEDRIRKDE--EKARRELIKQE 1326
Cdd:TIGR02794  164 A--KKKAEEAKKKAEAEAKAKAEaeAKAKAEEAKAK 197
PTZ00121 PTZ00121
MAEBL; Provisional
 1182-1333 3.79e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 3.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1182 MHREVISSSRVAGVSTSESSGKENVPVDERHKSSLIEVDLSDLKEPDEGEEESDhpekTKDIISDDQKSGVGfffKDEQK 1261
Cdd:PTZ00121  1042 LKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEE----AFGKAEEAKKTETG---KAEEA 1114

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291192 1262 AEDELAKKRA--AFLMKQQRKAEEARLRKQQLEAEvEQKRDDARRKAEEDR---IRKDEEKARR--ELIKQEYLRRKQE 1333
Cdd:PTZ00121  1115 RKAEEAKKKAedARKAEEARKAEDARKAEEARKAE-DAKRVEIARKAEDARkaeEARKAEDAKKaeAARKAEEVRKAEE 1192
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1257-1339 6.90e-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: 46.84  E-value: 6.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1257 KDEQKAEDELAKKRAAFLMKQQRKAEEARLRKQQLEAEVEQKRDDA----RRKAEEDRIRKdEEKARRELIKQEYlRRKQ 1332
Cdd:pfam13868  218 KERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFermlRKQAEDEEIEQ-EEAEKRRMKRLEH-RREL 295


                   ....*..
gi 2038291192 1333 EQILEEQ 1339
Cdd:pfam13868  296 EKQIEER 302
PTZ00121 PTZ00121
MAEBL; Provisional
 1209-1335 7.69e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 7.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1209 DERHKSSLIEVDLSDLKEPDEGEEESDHPEKTKDII---SDDQKSGVGFFFKDEQKAEDELA----KKRAAFLMKQQRKA 1281
Cdd:PTZ00121  1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAkkkAEEAKKAAEAAKAEAEAAADEAEaaeeKAEAAEKKKEEAKK 1378

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2038291192 1282 EEARLRKQqleAEVEQKRDDARRKAEEDRIRKDE-EKARRELIKQEYLRRKQEQI 1335
Cdd:PTZ00121  1379 KADAAKKK---AEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEK 1430
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1257-1339 8.38e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 46.79  E-value: 8.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1257 KDEQKAEDELAKKRAaflmKQQRKAEEARLRKQ---------QLEAEVEQKRDDARRKAEEDRIRKD------EEKARRE 1321
Cdd:COG2268    203 IAEAEAERETEIAIA----QANREAEEAELEQEreietariaEAEAELAKKKAEERREAETARAEAEaayeiaEANAERE 278

                           90
                   ....*....|....*....
gi 2038291192 1322 LIKQEYLRRKQEQI-LEEQ 1339
Cdd:COG2268    279 VQRQLEIAEREREIeLQEK 297
PTZ00121 PTZ00121
MAEBL; Provisional
 1232-1334 1.19e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1232 EESDHPEKTKDIISDDQKSGVGFFFKDEQKAEDELAKKRAaflmKQQRKAEEARLRkqqleAEVEQKRDDARRKAEEDRI 1311
Cdd:PTZ00121  1388 EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA----EEKKKADEAKKK-----AEEAKKADEAKKKAEEAKK 1458

                           90       100
                   ....*....|....*....|...
gi 2038291192 1312 RKDEEKARRELIKQEYLRRKQEQ 1334
Cdd:PTZ00121  1459 AEEAKKKAEEAKKADEAKKKAEE 1481
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1256-1338 1.23e-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: 46.07  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1256 FKDEQKAEDELAKKRAAFLMKQ-QRKAEEARLRKQQLEAEVEQKRDDARRKAEEDRIRKDEEKAR---RELIKQEYLRRK 1331
Cdd:pfam13868  255 EAEREEEEFERMLRKQAEDEEIeQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERlreEEAERRERIEEE 334


                   ....*..
gi 2038291192 1332 QEQILEE 1338
Cdd:pfam13868  335 RQKKLKE 341
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1259-1333 1.25e-04

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 43.88  E-value: 1.25e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038291192 1259 EQKAEDELAKKRAAflmKQQRKAEEARLRKQQLEAEVEQKRDDARRKAEEDRIRKDEEKARRELIKQEYLRRKQE 1333
Cdd:pfam05672   41 ERLRKEELRRRAEE---ERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKARE 112
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
 1260-1321 1.79e-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: 41.39  E-value: 1.79e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291192 1260 QKAEDEL----AKKRAafLMKQQRKAEEARLRKQQLEAEVEQKRDDARRKAEEDRIRKDEEKARRE 1321
Cdd:cd22265      9 QEYEEEIskleAERRA--LEEEENRASEEYIQKLLAEEEEEEKLAEERRRAEEEQLKEDEELARKL 72
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1257-1339 1.79e-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: 45.61  E-value: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1257 KDEQKAEDELAKKRAAflMKQQRKAEEARLR--KQQLEAEVEQKRDDARRKAEEDRIRKDEEKARRELIKQeylRRKQEQ 1334
Cdd:TIGR02794   64 KKEQERQKKLEQQAEE--AEKQRAAEQARQKelEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEA---KAKAEA 138


                   ....*
gi 2038291192 1335 ILEEQ 1339
Cdd:TIGR02794  139 EAERK 143
Caldesmon pfam02029
Caldesmon;
1023-1335 2.00e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 46.01  E-value: 2.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1023 QAIMKISQQQEMLMKAPSMAVPPlpsssqDHKLKPSVQFVEPISPPGMPIVRKTTRFGQGRNARSLRVTEQKLAKEKmqs 1102
Cdd:pfam02029   17 EERRRQKEEEEPSGQVTESVEPN------EHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQK--- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1103 sSRVITPTNSIETVPHLKSVQPLKSPSVPTEESPVEvvPEQGSASQDKPTTGGFRLHNDNSQRTFVLSTSKDANIISEQM 1182
Cdd:pfam02029   88 -EFDPTIADEKESVAERKENNEEEENSSWEKEEKRD--SRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSE 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1183 HREVISSSRVAGVSTSESSGKENVPVDERHKSSLIEVDLSDLKEPDEGEEE-SDHPEKTKDIISDDQKSgvgffFKDEQK 1261
Cdd:pfam02029  165 EAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEvTKLKVTTKRRQGGLSQS-----QEREEE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1262 AEDELAKKRAAFLMKQQRKAEEA----RLRKQQLEAEVE-----QKRDDARRKAEEDRIRKDEEKARRELIKQEYLRRKQ 1332
Cdd:pfam02029  240 AEVFLEAEQKLEELRRRRQEKESeefeKLRQKQQEAELEleelkKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMK 319


                   ...
gi 2038291192 1333 EQI 1335
Cdd:pfam02029  320 EEI 322
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1276-1339 2.02e-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: 2.02e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038291192 1276 KQQRKAEEARLRKQQL---EAEVEQKRDDARRKAEEDRIRKDEEKAR--RELIKQEYLRRKQEQILEEQ 1339
Cdd:pfam05672   33 ERLEKEEEERLRKEELrrrAEEERARREEEARRLEEERRREEEERQRkaEEEAEEREQREQEEQERLQK 101
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1260-1343 2.42e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 45.42  E-value: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1260 QKAEDELAKKRAAFLMKQQRKAEEARLRKQQLEAEVEQKRDDARRKAEEDRiRKDEEKARRELIKQEYLRRKQEQILEEQ 1339
Cdd:COG3064     83 EKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEA-KRKAEEERKAAEAEAAAKAEAEAARAAA 161


                   ....
gi 2038291192 1340 GLGR 1343
Cdd:COG3064    162 AAAA 165
PTZ00121 PTZ00121
MAEBL; Provisional
 1209-1335 2.98e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1209 DERHKSSLIEVDLSDLKEPDEGEEESDHPEKTKDII--SDDQKSGVGFFFKDEQKAEDELAKKRAaflmKQQRKAEEARL 1286
Cdd:PTZ00121  1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKkkAEEAKKAEEAKKKAEEAKKADEAKKKA----EEAKKADEAKK 1490

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2038291192 1287 RKQqleaEVEQKRDDARRKAEE----DRIRKDEEKARRELIKQEYLRRKQEQI 1335
Cdd:PTZ00121  1491 KAE----EAKKKADEAKKAAEAkkkaDEAKKAEEAKKADEAKKAEEAKKADEA 1539
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1259-1334 3.57e-04

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.84  E-value: 3.57e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038291192 1259 EQKAEDELAKKRAAflmkQQRKaeEARLRKQQLEAEVEQKRDDARRKAEEDRIRKDEEKARReliKQEYLRRKQEQ 1334
Cdd:TIGR02794   95 EQRAAAEKAAKQAE----QAAK--QAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK---QAEEEAKAKAA 161
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
 1276-1333 4.28e-04

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 43.12  E-value: 4.28e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038291192 1276 KQQRKAEEARLRKQQLEAEVEQKrddaRRKAEEDRIRKDEEKARR----ELIKQEYLRRKQE 1333
Cdd:pfam15927    1 ARLREEEEERLRAEEEEAERLEE----ERREEEEEERLAAEQDRRaeelEELKHLLEERKEA 58
PRK12704 PRK12704
phosphodiesterase; Provisional
 1251-1339 4.38e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 4.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1251 GVGFFF---KDEQKAEDelAKKRAAFLMKQQRKaeEARLRKQQLEAEVEQKRDDARRKAEEDRIRKDEEKARRE---LIK 1324
Cdd:PRK12704    19 VIGYFVrkkIAEAKIKE--AEEEAKRILEEAKK--EAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEkrlLQK 94

                           90
                   ....*....|....*
gi 2038291192 1325 QEYLRRKQEQILEEQ 1339
Cdd:PRK12704    95 EENLDRKLELLEKRE 109
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1259-1339 5.02e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.14  E-value: 5.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1259 EQKAEDELAKKRAAFLMKQQRKAEEARLRKQQLEAEVEQKRDDARRKAEEDRIRKDE-EKARRELIKQEYLRRKQEQILE 1337
Cdd:pfam13868  146 EKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErDELRAKLYQEEQERKERQKERE 225


                   ..
gi 2038291192 1338 EQ 1339
Cdd:pfam13868  226 EA 227
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1268-1338 6.46e-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: 41.27  E-value: 6.46e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038291192 1268 KKRAAFLMKQQRKAEEARLRKQQLEAEVEQKRDDARRKAEE--DRIRKDEEKARRELIKQeyLRRKQEQILEE 1338
Cdd:cd06503     29 DEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiiEEARKEAEKIKEEILAE--AKEEAERILEQ 99
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
 1256-1336 6.96e-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: 41.12  E-value: 6.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1256 FKDEQKAEDELAKKRAAFLMKQQrkaEEARLRKQQLEAEVEQKRDD--ARRKAEEDRIRKDEEKArrELIKQEYLRRKQE 1333
Cdd:pfam04696   21 FKKEESKQKEKEERRAEIEKRLE---EKAKQEKEELEERKREEREElfEERRAEQIELRALEEKL--ELKELMETWHENL 95


                   ...
gi 2038291192 1334 QIL 1336
Cdd:pfam04696   96 KAL 98
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1261-1339 7.28e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 7.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1261 KAEDELAKKRAAFLMKQQRKAEEARLRKQQLEAE-----VEQKRDDARRKA----EEDRIRKDEEKARRELIKQEYLRRK 1331
Cdd:pfam17380  426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQqqverLRQQEEERKRKKleleKEKRDRKRAEEQRRKILEKELEERK 505


                   ....*...
gi 2038291192 1332 QEQILEEQ 1339
Cdd:pfam17380  506 QAMIEEER 513
PTZ00121 PTZ00121
MAEBL; Provisional
 1209-1334 9.45e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 9.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1209 DERHKSSLIEVDLSDLKEPDEGEEESDHPEKTKDIISDDQKSGVGFFFKDEQKAEDELAKKRAAFLMKQQ----RKAEEA 1284
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEaeekKKAEEL 1652

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038291192 1285 R-------LRKQQL--EAEVEQKRDDARRKAEEDRIRKDEEKARR--ELIKQEYLRRKQEQ 1334
Cdd:PTZ00121  1653 KkaeeenkIKAAEEakKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeEAKKAEELKKKEAE 1713
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 1258-1339 1.09e-03

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


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 41.60  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1258 DEQKAEDELAKKRAAFLMKQQRKAEEARLRKQQLEAEVEQKRDDARRKAEEDRIRKD----EEKARRELIKQEYLRRKQE 1333
Cdd:pfam11600   12 EKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEkerrEKKEKDEKEKAEKLRLKEE 91


                   ....*.
gi 2038291192 1334 QILEEQ 1339
Cdd:pfam11600   92 KRKEKQ 97
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1259-1339 1.10e-03

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.49  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1259 EQKAEDELAKKRAAFLMKQQRKAEEARLRK-------QQLEAEVEQKRDDARRKAEEDRiRKDEEKARRELIKQEYLRRK 1331
Cdd:COG3064     32 EQKAKEEAEEERLAELEAKRQAEEEAREAKaeaeqraAELAAEAAKKLAEAEKAAAEAE-KKAAAEKAKAAKEAEAAAAA 110


                   ....*...
gi 2038291192 1332 QEQILEEQ 1339
Cdd:COG3064    111 EKAAAAAE 118
PTZ00121 PTZ00121
MAEBL; Provisional
 1229-1334 1.17e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1229 EGEEESDHPEKTKDIISDDQKSgvgfffKDEQKAEDELAKKRAaflmKQQRKAEEARLRkqqleAEVEQKRDDARRKAEE 1308
Cdd:PTZ00121  1351 EAEAAADEAEAAEEKAEAAEKK------KEEAKKKADAAKKKA----EEKKKADEAKKK-----AEEDKKKADELKKAAA 1415

                           90       100
                   ....*....|....*....|....*..
gi 2038291192 1309 DRIRKDEEKARRELIKQ-EYLRRKQEQ 1334
Cdd:PTZ00121  1416 AKKKADEAKKKAEEKKKaDEAKKKAEE 1442
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1259-1339 1.27e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.98  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1259 EQKAEDELAKKRAAFLMKQQRKAEEARLRKQQLEAEVEQKRDDARRKAEEDRIRKDEEKARRELIKQEYLRRKQEQILEE 1338
Cdd:pfam13868   46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125


                   .
gi 2038291192 1339 Q 1339
Cdd:pfam13868  126 R 126
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1257-1339 1.42e-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: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1257 KDEQKAEDELAKKRAAFLM--KQQRKAEEARLRKQQLEAEVEQKRDDARRKAEEDRIRKDEE--KARRELIKQEYLRRKQ 1332
Cdd:pfam13868  175 REEIEEEKEREIARLRAQQekAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQElqQAREEQIELKERRLAE 254


                   ....*..
gi 2038291192 1333 EQILEEQ 1339
Cdd:pfam13868  255 EAEREEE 261
PTZ00121 PTZ00121
MAEBL; Provisional
 1209-1338 1.59e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1209 DERHKSSLIEVDLSDLKEPDEGEEESDHPEKTKDII---SDDQKSGVGFFFKDEQKAEDELAKKRAAFLMKQQRKAEEAR 1285
Cdd:PTZ00121  1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAkkaAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2038291192 1286 LRKQQLEAEvEQKRDDARRKAEEDriRKDEEKARRELIKQEYLRRKQEQILEE 1338
Cdd:PTZ00121  1547 KADELKKAE-ELKKAEEKKKAEEA--KKAEEDKNMALRKAEEAKKAEEARIEE 1596
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1259-1332 2.00e-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: 42.14  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1259 EQKAEDELAKKRAAflmKQQRKAEEARLR-----KQQLEAEVEQKRDDARRKAEEDRIRKDEE---KARRELIKQEYLRR 1330
Cdd:TIGR02794  149 AKQAEEEAKAKAAA---EAKKKAEEAKKKaeaeaKAKAEAEAKAKAEEAKAKAEAAKAKAAAEaaaKAEAEAAAAAAAEA 225


                   ..
gi 2038291192 1331 KQ 1332
Cdd:TIGR02794  226 ER 227
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1209-1326 2.41e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1209 DERHKSSLIEVDLSDLK-EPDEGEEESDHPEKTKDIISDDQKSgvgfffKDEQKAEDELAKKRAAFLMKQQRKAEEARLR 1287
Cdd:PRK02224   472 EDRERVEELEAELEDLEeEVEEVEERLERAEDLVEAEDRIERL------EERREDLEELIAERRETIEEKRERAEELRER 545

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2038291192 1288 KQQLEAEVEQKRDDARRK---AEEDRIRKDEEKARRELIKQE 1326
Cdd:PRK02224   546 AAELEAEAEEKREAAAEAeeeAEEAREEVAELNSKLAELKER 587
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1258-1339 2.56e-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: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1258 DEQKAEDELAKKRAA--FLMKQQRKAEEAR-LRKQQLEAEVEQKRDDARRKAEEDRIRKDEE---KARRELIKQEyLRRK 1331
Cdd:pfam13868  114 DQAEAEEKLEKQRQLreEIDEFNEEQAEWKeLEKEEEREEDERILEYLKEKAEREEEREAEReeiEEEKEREIAR-LRAQ 192


                   ....*...
gi 2038291192 1332 QEQILEEQ 1339
Cdd:pfam13868  193 QEKAQDEK 200
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1257-1339 2.72e-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: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1257 KDEQKAEDELAKKRAAF---LMKQ--------QRKAEEARLRKQQLEAEVEQKRDDARRKAEEDRIRKDEEKARRELIKQ 1325
Cdd:pfam13868   58 EEEEEKEEERKEERKRYrqeLEEQieereqkrQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNE 137

                           90
                   ....*....|....
gi 2038291192 1326 EYLRRKQEQILEEQ 1339
Cdd:pfam13868  138 EQAEWKELEKEEER 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1257-1341 2.79e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1257 KDEQKAEDELAKKRAAfLMKQQRKAEEARLRKQQLEAEVEQKRDDARRkAEEDRIRKDEEKARRELIKQEYLRRKQEQIL 1336
Cdd:COG1196    246 AELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAEEYE-LLAELARLEQDIARLEERRRELEERLEELEE 323


                   ....*
gi 2038291192 1337 EEQGL 1341
Cdd:COG1196    324 ELAEL 328
PTZ00121 PTZ00121
MAEBL; Provisional
 1209-1335 2.99e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1209 DERHKSSLIEVDLSDLKEPDEGEEESDHPEKTKDII---SDDQKSGVGFFFKDEQKAEDELAKKRAaflmKQQRKAEEAR 1285
Cdd:PTZ00121  1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkkaAAAKKKADEAKKKAEEKKKADEAKKKA----EEAKKADEAK 1450

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2038291192 1286 LRKQQL-EAEVEQKRDDARRKAEEDRIRKDEEKARRELIKQ-EYLRRKQEQI 1335
Cdd:PTZ00121  1451 KKAEEAkKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKaEEAKKKADEA 1502
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1229-1337 3.19e-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: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1229 EGEEESDHPEKTKDIISDDQKSGVGFFFKDEQK---AEDELAKKRAAFLMKQQRKAEEARLRKQQleaEVEQKR--DDAR 1303
Cdd:pfam17380  482 EKRDRKRAEEQRRKILEKELEERKQAMIEEERKrklLEKEMEERQKAIYEEERRREAEEERRKQQ---EMEERRriQEQM 558

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2038291192 1304 RKAEEDRIRKDEEKARRELIKQEYLRRKQEQILE 1337
Cdd:pfam17380  559 RKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1225-1318 4.92e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.33  E-value: 4.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1225 KEPDEGEEESDHPEKTKDIISDDQKSgvgfffkDEQKAEDELAKKRAAflmKQQRKAEEARLRKQ---QLEAEVEQKR-D 1300
Cdd:PRK09510    88 QAEELQQKQAAEQERLKQLEKERLAA-------QEQKKQAEEAAKQAA---LKQKQAEEAAAKAAaaaKAKAEAEAKRaA 157

                           90
                   ....*....|....*...
gi 2038291192 1301 DARRKAEEDRIRKDEEKA 1318
Cdd:PRK09510   158 AAAKKAAAEAKKKAEAEA 175
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1258-1339 5.09e-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: 5.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1258 DEQKAEdelaKKRaaflMKQQRKAEEARLRKQqleAEVEQKRDDARRKAEEDRIRKDEEKARRELIKQEYLRRKQEQILE 1337
Cdd:pfam13868   25 DAQIAE----KKR----IKAEEKEEERRLDEM---MEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEY 93


                   ..
gi 2038291192 1338 EQ 1339
Cdd:pfam13868   94 EE 95
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 1260-1334 5.34e-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: 40.74  E-value: 5.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038291192 1260 QKA--EDELAKKRAAFLMKQQRKAEEARLRKQQleaEVEQKRDDARRKAEedriRKDEEKARRELiKQEYLRRKQEQ 1334
Cdd:pfam12037  101 QRAqyQDELARKRYQDQLEAQRRRNEELLRKQE---ESVAKQEAMRIQAQ----RRQTEEHEAEL-RRETERAKAEA 169
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 ...
 1257-1326 5.60e-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: 38.83  E-value: 5.60e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038291192 1257 KDEQKAEDELAKKRAAFLMKQQRKAEEARLRKQQL----EAEVEQKRDDARRKAEEDrIRKDEEKARRELIKQE 1326
Cdd:pfam00430   36 ADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIienaKKRAEKLKEEIVAAAEAE-AERIIEQAAAEIEQEK 108
PTZ00121 PTZ00121
MAEBL; Provisional
 1260-1339 5.67e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 5.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1260 QKAEDeLAKKRAAFLMKQQRKAEEARLRKQQLEAEVEQKRDDARRKAEEDR----IRKDEEKARRELIKQEYLRRKQEQI 1335
Cdd:PTZ00121  1194 RKAED-ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkaeeERNNEEIRKFEEARMAHFARRQAAI 1272


                   ....
gi 2038291192 1336 LEEQ 1339
Cdd:PTZ00121  1273 KAEE 1276
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 253-339 6.13e-03

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409067  Cd Length: 114  Bit Score: 38.05  E-value: 6.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192  253 LEDLTKDISDGAALLAVIHFYCPEQMKLDDIclKEVTSMGDSVYNIQLLKEFSNEYLNKCFyLTLEDmlytplVLKPN-- 330
Cdd:cd21218     33 VTNFSSDLKDGEVYALLLHSLAPELCDKELV--LEVLSEEDLEKRAEKVLQAAEKLGCKYF-LTPED------IVSGNpr 103

                           90
                   ....*....|
gi 2038291192  331 -IMVFIAELF 339
Cdd:cd21218    104 lNLAFVATLF 113
PTZ00121 PTZ00121
MAEBL; Provisional
 1164-1334 6.33e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 6.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1164 QRTFVLSTSKDANIISEQMHREVISSSRVAGVSTSESSGKENvpvDERHKSslievdlsdlKEPDEGEEESDHPEKTKDI 1243
Cdd:PTZ00121  1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE---EAKIKA----------EELKKAEEEKKKVEQLKKK 1641

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1244 ISDDQKSGvgfffkDEQKAEDELAKKRAAFLMKQ----QRKAEEARL-------RKQQLEAEVEQKR--DDARRKAEEDR 1310
Cdd:PTZ00121  1642 EAEEKKKA------EELKKAEEENKIKAAEEAKKaeedKKKAEEAKKaeedekkAAEALKKEAEEAKkaEELKKKEAEEK 1715

                          170       180
                   ....*....|....*....|....*.
gi 2038291192 1311 IRKDEEKARREL--IKQEYLRRKQEQ 1334
Cdd:PTZ00121  1716 KKAEELKKAEEEnkIKAEEAKKEAEE 1741
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 1262-1338 6.79e-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: 38.32  E-value: 6.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1262 AEDELAKKRAAFLMK-QQRKAEEARLRKQQLE------------AEVEQKRDDARRKAEEDRIRKDE-----EKARREL- 1322
Cdd:pfam13863   11 VQLALDAKREEIERLeELLKQREEELEKKEQElkedlikfdkflKENDAKRRRALKKAEEETKLKKEkekeiKKLTAQIe 90

                           90
                   ....*....|....*..
gi 2038291192 1323 -IKQEylRRKQEQILEE 1338
Cdd:pfam13863   91 eLKSE--ISKLEEKLEE 105
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 1173-1339 6.86e-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: 41.09  E-value: 6.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1173 KDANIISEQMHREVISSSRVAGVST----SESSGKENVPVDERHKSSLIEVDLSDLKEPDEGEEESDHPEKTKDIISDDQ 1248
Cdd:pfam15709  241 RNLEVAAELSGPDVINSKETEDASErgafSSDSVVEDPWLSSKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDP 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1249 KSGVGFFFKDEQKAEDELAKKRAAFLM-----KQQRKAEEARLRKQQLEA--------EVEQkrddaRRKAEEDRIRK-- 1313
Cdd:pfam15709  321 SKALLEKREQEKASRDRLRAERAEMRRleverKRREQEEQRRLQQEQLERaekmreelELEQ-----QRRFEEIRLRKqr 395

                          170       180
                   ....*....|....*....|....*..
gi 2038291192 1314 -DEEKARREliKQEYLRRKQEQILEEQ 1339
Cdd:pfam15709  396 lEEERQRQE--EEERKQRLQLQAAQER 420
PTZ00121 PTZ00121
MAEBL; Provisional
 1257-1334 8.29e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 8.29e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038291192 1257 KDEQKAEDELAKKRAaflmKQQRKAEEARLRKQqleaEVEQKRDDARRKAEEDRiRKDEEKARRELIKQEYLRRKQEQ 1334
Cdd:PTZ00121  1297 KAEEKKKADEAKKKA----EEAKKADEAKKKAE----EAKKKADAAKKKAEEAK-KAAEAAKAEAEAAADEAEAAEEK 1365
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1259-1339 8.67e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 8.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1259 EQKAEDELAKKRAAFLMKQQRKAEEARLRKQQLEAEVEQKRDDARRKAEEDRIRK------DEEKARRELIKQEYLRRKQ 1332
Cdd:COG1196    217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEElrleleELELELEEAQAEEYELLAE 296


                   ....*..
gi 2038291192 1333 EQILEEQ 1339
Cdd:COG1196    297 LARLEQD 303
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1257-1334 8.73e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 8.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1257 KDEQKAEDEL----------AKKRAAFLMKQQRKAEEARLRKQQLEAEVEQKRDDARRKAEEDR------IRKDEEKARR 1320
Cdd:pfam13868  197 QDEKAERDELraklyqeeqeRKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEeefermLRKQAEDEEI 276

                           90
                   ....*....|....
gi 2038291192 1321 ELIKQEYLRRKQEQ 1334
Cdd:pfam13868  277 EQEEAEKRRMKRLE 290
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1268-1338 9.03e-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: 38.62  E-value: 9.03e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038291192 1268 KKRAAFLMKQQRKAEEARLRKQQLEAEVEQKRDDARRKAEE--DRIRKDEEKARRELIKQeyLRRKQEQILEE 1338
Cdd:COG0711     30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEiiAEARKEAEAIAEEAKAE--AEAEAERIIAQ 100
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1257-1339 9.15e-03

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.41  E-value: 9.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1257 KDEQKAEDELAKKRAAflMKQQRKAEEARLRKQQLEAEVEQKRDDARRKAEEDRIRKDEEKARRElikQEYLRRKQEQIL 1336
Cdd:COG3064     48 EAKRQAEEEAREAKAE--AEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAA---EKAAAAAEKEKA 122


                   ...
gi 2038291192 1337 EEQ 1339
Cdd:COG3064    123 EEA 125
PTZ00121 PTZ00121
MAEBL; Provisional
 1260-1340 9.64e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 9.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1260 QKAEDELAKKRAAFlmkqQRKAEEARLRKQQLEAEVEQKRD-DARRKAEEDRIRKDEEKARRElikqEYLRRKQEQILEE 1338
Cdd:PTZ00121  1681 KKAEEDEKKAAEAL----KKEAEEAKKAEELKKKEAEEKKKaEELKKAEEENKIKAEEAKKEA----EEDKKKAEEAKKD 1752


                   ..
gi 2038291192 1339 QG 1340
Cdd:PTZ00121  1753 EE 1754
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 1259-1338 9.70e-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: 9.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038291192 1259 EQKAEDElAKKRAAFLMKQQRKAEEARLR--KQQLEAEVEQKRDDARRKAEEDRIRKdEEKARRELiKQEYLRRKQEqIL 1336
Cdd:COG1390      8 IEEILEE-AEAEAEEILEEAEEEAEKILEeaEEEAEEIKEEILEKAEREAEREKRRI-ISSAELEA-RKELLEAKEE-LI 83


                   ..
gi 2038291192 1337 EE 1338
Cdd:COG1390     84 EE 85
 
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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