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Conserved domains on  [gi|1622916950|ref|XP_028697424|]
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hydrocephalus-inducing protein homolog isoform X2 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Hydin_ADK pfam17213
Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to ...
2032-2230 4.20e-118

Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to adenylate kinases.


:

Pssm-ID: 465383  Cd Length: 199  Bit Score: 372.55  E-value: 4.20e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2032 AIIIHGTPLSGKSATAVSMAKYYNAACLSIDSIVLEAVSDSNNVPGIRARELCIRAAIEQSMKEGEEAAQEAAMGQNIIG 2111
Cdd:pfam17213    1 AIIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAAVVPGQPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2112 QGRLSTETLGKLTSEMTLLAPEIKPGKSVRGSVVMTKSKADSHGSGSQKQHHSHQSETPQISSSPLLPGPTHRRLSVSPS 2191
Cdd:pfam17213   81 TYRLSVEALTKHTSEGTLVGPESKISKGKRGSVVSGKGKADSHGTGSQKQHHQHQSETPQISSSPPPAGPIQRRLSVSAS 160
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1622916950 2192 VGGETGLMSCVLPDELLVQILAERIQLSDCYRGVVFDGL 2230
Cdd:pfam17213  161 VGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
514-613 1.20e-22

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


:

Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 95.42  E-value: 1.20e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950  514 EGIIEPSGVQAiQISFSSTILGNFEEEFLVNVNGSPEPVkLTIRGCVIGPTFHFNVPALHFgDVSFGFPHTLICSLNNTS 593
Cdd:pfam15780    2 VLLLAPFSRQP-FVCFGDVPVGTSAERLLTVVNPSEEPA-EVKVSKVPAPTKGFSVSPLEF-TVQPGESQTLTVTWTPTE 78
                           90       100
                   ....*....|....*....|
gi 1622916950  594 LVPMTFKLRIPGDGLGRKSI 613
Cdd:pfam15780   79 EGAVRETLQFTVNDVGKHQV 98
TPH super family cl38442
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2260-2367 7.08e-12

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.


The actual alignment was detected with superfamily member pfam13868:

Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 70.33  E-value: 7.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2260 MAQDYAAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQALRERKKREQERLAK------ 2333
Cdd:pfam13868  156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKkarqrq 235
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622916950 2334 --------EMQEKKLQQELERQKEEDELKRKVKKGKQGPIKE 2367
Cdd:pfam13868  236 elqqareeQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE 277
PTZ00121 super family cl31754
MAEBL; Provisional
2249-2619 4.18e-11

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 70.17  E-value: 4.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2249 IGSREHIYVLNMAQDYAAMKAQEKAKKEQ----EERKHKEALEKEKERlQNMDEEEYDAlteEEKLTFNQGIQQAlrERK 2324
Cdd:PTZ00121  1254 IRKFEEARMAHFARRQAAIKAEEARKADElkkaEEKKKADEAKKAEEK-KKADEAKKKA---EEAKKADEAKKKA--EEA 1327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2325 KREQERLAKEMQEKKLQQELERQKEE---DELKRKVKKGKQGPIKEEPPPKKSQASNKQVPPFTKVD-VKMETIERKISV 2400
Cdd:PTZ00121  1328 KKKADAAKKKAEEAKKAAEAAKAEAEaaaDEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADeAKKKAEEDKKKA 1407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2401 REptVSEKEELNKK----KRNMGDVSMLGLPLVQDQEDSEGDVSKdpdKQLAQRFKAYELTLKDVQNILMYWDRKQGVQL 2476
Cdd:PTZ00121  1408 DE--LKKAAAAKKKadeaKKKAEEKKKADEAKKKAEEAKKADEAK---KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2477 PPA-----GMEEAAHEPDDQRQVPSGGRRGRKDRERERLEKERTEKERLEREKA-------ERERLEKLRALEERSDWEG 2544
Cdd:PTZ00121  1483 KKAdeakkKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeakkaeEKKKADELKKAEELKKAEE 1562
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916950 2545 EGEEDHEGKKEKDLGVPFLNI----QTPDFEGLNWKQALESDKLPKGEQAQEEQTSSSKGGKQKVKEKTDQVVETQKDK 2619
Cdd:PTZ00121  1563 KKKAEEAKKAEEDKNMALRKAeeakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
Motile_Sperm super family cl44412
MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These ...
203-269 2.13e-03

MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These proteins oligomerise to form filaments. This family contains many other proteins.


The actual alignment was detected with superfamily member pfam00635:

Pssm-ID: 459882  Cd Length: 109  Bit Score: 40.81  E-value: 2.13e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916950  203 PDKLNFSTCPVKYSTQKILLVrNIGNKIAVFHIKTCRP--FSVEPAVGTLNVGESMQLEVEFEPQSVGD 269
Cdd:pfam00635    7 PDLIFFAAPGNKQGTSTLTLK-NTSDKRVAFKVKTTNPkkYRVRPNYGIIKPGESVTITITRQPFDEEP 74
 
Name Accession Description Interval E-value
Hydin_ADK pfam17213
Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to ...
2032-2230 4.20e-118

Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to adenylate kinases.


Pssm-ID: 465383  Cd Length: 199  Bit Score: 372.55  E-value: 4.20e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2032 AIIIHGTPLSGKSATAVSMAKYYNAACLSIDSIVLEAVSDSNNVPGIRARELCIRAAIEQSMKEGEEAAQEAAMGQNIIG 2111
Cdd:pfam17213    1 AIIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAAVVPGQPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2112 QGRLSTETLGKLTSEMTLLAPEIKPGKSVRGSVVMTKSKADSHGSGSQKQHHSHQSETPQISSSPLLPGPTHRRLSVSPS 2191
Cdd:pfam17213   81 TYRLSVEALTKHTSEGTLVGPESKISKGKRGSVVSGKGKADSHGTGSQKQHHQHQSETPQISSSPPPAGPIQRRLSVSAS 160
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1622916950 2192 VGGETGLMSCVLPDELLVQILAERIQLSDCYRGVVFDGL 2230
Cdd:pfam17213  161 VGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
514-613 1.20e-22

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 95.42  E-value: 1.20e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950  514 EGIIEPSGVQAiQISFSSTILGNFEEEFLVNVNGSPEPVkLTIRGCVIGPTFHFNVPALHFgDVSFGFPHTLICSLNNTS 593
Cdd:pfam15780    2 VLLLAPFSRQP-FVCFGDVPVGTSAERLLTVVNPSEEPA-EVKVSKVPAPTKGFSVSPLEF-TVQPGESQTLTVTWTPTE 78
                           90       100
                   ....*....|....*....|
gi 1622916950  594 LVPMTFKLRIPGDGLGRKSI 613
Cdd:pfam15780   79 EGAVRETLQFTVNDVGKHQV 98
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2260-2367 7.08e-12

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: 70.33  E-value: 7.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2260 MAQDYAAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQALRERKKREQERLAK------ 2333
Cdd:pfam13868  156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKkarqrq 235
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622916950 2334 --------EMQEKKLQQELERQKEEDELKRKVKKGKQGPIKE 2367
Cdd:pfam13868  236 elqqareeQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE 277
PTZ00121 PTZ00121
MAEBL; Provisional
2249-2619 4.18e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 70.17  E-value: 4.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2249 IGSREHIYVLNMAQDYAAMKAQEKAKKEQ----EERKHKEALEKEKERlQNMDEEEYDAlteEEKLTFNQGIQQAlrERK 2324
Cdd:PTZ00121  1254 IRKFEEARMAHFARRQAAIKAEEARKADElkkaEEKKKADEAKKAEEK-KKADEAKKKA---EEAKKADEAKKKA--EEA 1327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2325 KREQERLAKEMQEKKLQQELERQKEE---DELKRKVKKGKQGPIKEEPPPKKSQASNKQVPPFTKVD-VKMETIERKISV 2400
Cdd:PTZ00121  1328 KKKADAAKKKAEEAKKAAEAAKAEAEaaaDEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADeAKKKAEEDKKKA 1407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2401 REptVSEKEELNKK----KRNMGDVSMLGLPLVQDQEDSEGDVSKdpdKQLAQRFKAYELTLKDVQNILMYWDRKQGVQL 2476
Cdd:PTZ00121  1408 DE--LKKAAAAKKKadeaKKKAEEKKKADEAKKKAEEAKKADEAK---KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2477 PPA-----GMEEAAHEPDDQRQVPSGGRRGRKDRERERLEKERTEKERLEREKA-------ERERLEKLRALEERSDWEG 2544
Cdd:PTZ00121  1483 KKAdeakkKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeakkaeEKKKADELKKAEELKKAEE 1562
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916950 2545 EGEEDHEGKKEKDLGVPFLNI----QTPDFEGLNWKQALESDKLPKGEQAQEEQTSSSKGGKQKVKEKTDQVVETQKDK 2619
Cdd:PTZ00121  1563 KKKAEEAKKAEEDKNMALRKAeeakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
PTZ00121 PTZ00121
MAEBL; Provisional
2257-2463 2.80e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.47  E-value: 2.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2257 VLNMAQDYAAMKAqEKAKKEQEERKHKEALEKEKE------RLQNMDEEEYDALTEEEKLTFNQGIQQALRERKKREQER 2330
Cdd:PTZ00121  1597 VMKLYEEEKKMKA-EEAKKAEEAKIKAEELKKAEEekkkveQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2331 LAKEMQ-----EKKLQQELERQKEEDELKRKVKKGKQGPIKEEPPPKKSQASNKqvppftkvdVKMETIERKisvREPTV 2405
Cdd:PTZ00121  1676 KAEEAKkaeedEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK---------IKAEEAKKE---AEEDK 1743
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916950 2406 SEKEELNKKKRNMGDVSMLGLPLVQDQE----DSEGDVSKDPDKQLAQRFKAYELTLKDVQN 2463
Cdd:PTZ00121  1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEeirkEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2268-2538 6.17e-10

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: 65.92  E-value: 6.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQ---ALRERKKREQERLAKEMQEK--KLQQ 2342
Cdd:pfam17380  317 KLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQeeiAMEISRMRELERLQMERQQKneRVRQ 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2343 ELE---RQK-EEDELKRKVKKGKqgpiKEEPPPKKSQASNKQVppftKVDVKMETIERKIS-VREPTVSEKEELNKKKRN 2417
Cdd:pfam17380  397 ELEaarKVKiLEEERQRKIQQQK----VEMEQIRAEQEEARQR----EVRRLEEERAREMErVRLEEQERQQQVERLRQQ 468
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2418 MGDVSMLGLPLVQDQEdsegdvskdpDKQLA--QRFKAYELTLKDVQNILMYWDRKQgvQLPPAGMEE---AAHEpDDQR 2492
Cdd:pfam17380  469 EEERKRKKLELEKEKR----------DRKRAeeQRRKILEKELEERKQAMIEEERKR--KLLEKEMEErqkAIYE-EERR 535
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1622916950 2493 QVPSGGRRGRKDRERERLEKERTEK---ERLEREKAERERlEKLRALEE 2538
Cdd:pfam17380  536 REAEEERRKQQEMEERRRIQEQMRKateERSRLEAMERER-EMMRQIVE 583
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
2261-2380 7.94e-08

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: 57.93  E-value: 7.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2261 AQDYAAMKAQEK--AKKEQEERKH----KEALEK----EKERLQNMDEEEYDALT----EEEKLTFNQGIQQALRERKKR 2326
Cdd:TIGR02794   49 AQQANRIQQQKKpaAKKEQERQKKleqqAEEAEKqraaEQARQKELEQRAAAEKAakqaEQAAKQAEEKQKQAEEAKAKQ 128
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916950 2327 EQERLAKEMQ--EKKLQQELERQKEEDELKRKVKKGKQgpiKEEPPPKKSQASNKQ 2380
Cdd:TIGR02794  129 AAEAKAKAEAeaERKAKEEAAKQAEEEAKAKAAAEAKK---KAEEAKKKAEAEAKA 181
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2269-2352 8.45e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 8.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2269 AQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALtEEEKLTFNQGIQQALRERKKREQERLAKEMQEKKLQQELERQK 2348
Cdd:COG1196    342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA-EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420

                   ....
gi 1622916950 2349 EEDE 2352
Cdd:COG1196    421 EELE 424
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
2255-2359 1.05e-05

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: 48.35  E-value: 1.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950  2255 IYVLNMAQDYAAMKAQEKAKK--EQEERKHKEALEKEKERLQNMdEEEYDAltEEEKLTfnqgiqQALRERKKREQERLA 2332
Cdd:smart00935    1 IGVVDVQKILQESPAGKAAQKqlEKEFKKRQAELEKLEKELQKL-KEKLQK--DAATLS------EAAREKKEKELQKKV 71
                            90       100       110
                    ....*....|....*....|....*....|.
gi 1622916950  2333 KEMQEK--KLQQELE--RQKEEDELKRKVKK 2359
Cdd:smart00935   72 QEFQRKqqKLQQDLQkrQQEELQKILDKINK 102
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2297-2632 1.53e-05

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2297 DEEEYDALTEEEKLTFNQGIQQALRERKKREQERLAKEMQEKKLQQELERQKEEDELKRKVKKgkqgpiKEEPPPKKSQA 2376
Cdd:TIGR02169  169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKE------KEALERQKEAI 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2377 sNKQVPPFTKVdvkMETIERKISVREPTVSEKE----ELNKKKRNMGDVSMLGL-----------PLVQDQEDSEGDVSK 2441
Cdd:TIGR02169  243 -ERQLASLEEE---LEKLTEEISELEKRLEEIEqlleELNKKIKDLGEEEQLRVkekigeleaeiASLERSIAEKERELE 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2442 DPDKQLAQRFKAYELTLKDVQNIlmywDRKQG-VQLPPAGMEEaahEPDDQRQVpsggrrgRKDRERERLEKERTEKERL 2520
Cdd:TIGR02169  319 DAEERLAKLEAEIDKLLAEIEEL----EREIEeERKRRDKLTE---EYAELKEE-------LEDLRAELEEVDKEFAETR 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2521 EREKAERERLEKLRalEERSDWEGEGEEDHEGKKEKDLGVPFLNIQTPDFEGLnwKQALESDKLPKGEQ--AQEEQTSSS 2598
Cdd:TIGR02169  385 DELKDYREKLEKLK--REINELKRELDRLQEELQRLSEELADLNAAIAGIEAK--INELEEEKEDKALEikKQEWKLEQL 460
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1622916950 2599 KGGKQKVKEKTDQVVETQKD--KRRVALNRKVISGE 2632
Cdd:TIGR02169  461 AADLSKYEQELYDLKEEYDRveKELSKLQRELAEAE 496
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
2269-2642 1.94e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 50.81  E-value: 1.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2269 AQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKltfnqgiQQALRERKKREQERLAK----EMQEKKLQQEL 2344
Cdd:COG3064      1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEE-------ERLAELEAKRQAEEEAReakaEAEQRAAELAA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2345 ERQKEEDELKRKVKKGKQgPIKEEPPPKKSQASNKQVPpftkvdvkmetiERKISV--REPTVSEKEELNKKKRNmgdvs 2422
Cdd:COG3064     74 EAAKKLAEAEKAAAEAEK-KAAAEKAKAAKEAEAAAAA------------EKAAAAaeKEKAEEAKRKAEEEAKR----- 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2423 mlglplvQDQEDSEGDVSKDPDKQLAQRFKAYELTLKDVQNILMYWDRKQGVQLPPAGMEEAAHEPDDQRQVPSGGRRGR 2502
Cdd:COG3064    136 -------KAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAA 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2503 KDRERERLEKERTEKERLEREKAERERLEKLRALEERSDWEGEGEEDHEGKKEKDLGVPFLNIQTPDFEGLNWKQALESD 2582
Cdd:COG3064    209 AAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGL 288
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2583 KLPKGEQAQEEQTSSSKGGKQKVKEKTDQVVETQKDKRRVALNRKVISGEPAGTISQLSD 2642
Cdd:COG3064    289 AAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGA 348
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
2260-2362 1.07e-04

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: 47.57  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2260 MAQDYAAMKAQEKAKKEQEERkhkEALEKEKERLQNMdEEEYDALTEEEKLTFNQGIQQaLRERKKREQERLAKEmQEKK 2339
Cdd:cd16269    187 LQADQALTEKEKEIEAERAKA---EAAEQERKLLEEQ-QRELEQKLEDQERSYEEHLRQ-LKEKMEEERENLLKE-QERA 260
                           90       100
                   ....*....|....*....|....*
gi 1622916950 2340 LQQELERQKE--EDELKRKVKKGKQ 2362
Cdd:cd16269    261 LESKLKEQEAllEEGFKEQAELLQE 285
Motile_Sperm pfam00635
MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These ...
203-269 2.13e-03

MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These proteins oligomerise to form filaments. This family contains many other proteins.


Pssm-ID: 459882  Cd Length: 109  Bit Score: 40.81  E-value: 2.13e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916950  203 PDKLNFSTCPVKYSTQKILLVrNIGNKIAVFHIKTCRP--FSVEPAVGTLNVGESMQLEVEFEPQSVGD 269
Cdd:pfam00635    7 PDLIFFAAPGNKQGTSTLTLK-NTSDKRVAFKVKTTNPkkYRVRPNYGIIKPGESVTITITRQPFDEEP 74
 
Name Accession Description Interval E-value
Hydin_ADK pfam17213
Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to ...
2032-2230 4.20e-118

Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to adenylate kinases.


Pssm-ID: 465383  Cd Length: 199  Bit Score: 372.55  E-value: 4.20e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2032 AIIIHGTPLSGKSATAVSMAKYYNAACLSIDSIVLEAVSDSNNVPGIRARELCIRAAIEQSMKEGEEAAQEAAMGQNIIG 2111
Cdd:pfam17213    1 AIIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAAVVPGQPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2112 QGRLSTETLGKLTSEMTLLAPEIKPGKSVRGSVVMTKSKADSHGSGSQKQHHSHQSETPQISSSPLLPGPTHRRLSVSPS 2191
Cdd:pfam17213   81 TYRLSVEALTKHTSEGTLVGPESKISKGKRGSVVSGKGKADSHGTGSQKQHHQHQSETPQISSSPPPAGPIQRRLSVSAS 160
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1622916950 2192 VGGETGLMSCVLPDELLVQILAERIQLSDCYRGVVFDGL 2230
Cdd:pfam17213  161 VGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
514-613 1.20e-22

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 95.42  E-value: 1.20e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950  514 EGIIEPSGVQAiQISFSSTILGNFEEEFLVNVNGSPEPVkLTIRGCVIGPTFHFNVPALHFgDVSFGFPHTLICSLNNTS 593
Cdd:pfam15780    2 VLLLAPFSRQP-FVCFGDVPVGTSAERLLTVVNPSEEPA-EVKVSKVPAPTKGFSVSPLEF-TVQPGESQTLTVTWTPTE 78
                           90       100
                   ....*....|....*....|
gi 1622916950  594 LVPMTFKLRIPGDGLGRKSI 613
Cdd:pfam15780   79 EGAVRETLQFTVNDVGKHQV 98
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2260-2367 7.08e-12

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: 70.33  E-value: 7.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2260 MAQDYAAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQALRERKKREQERLAK------ 2333
Cdd:pfam13868  156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKkarqrq 235
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622916950 2334 --------EMQEKKLQQELERQKEEDELKRKVKKGKQGPIKE 2367
Cdd:pfam13868  236 elqqareeQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE 277
PTZ00121 PTZ00121
MAEBL; Provisional
2249-2619 4.18e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 70.17  E-value: 4.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2249 IGSREHIYVLNMAQDYAAMKAQEKAKKEQ----EERKHKEALEKEKERlQNMDEEEYDAlteEEKLTFNQGIQQAlrERK 2324
Cdd:PTZ00121  1254 IRKFEEARMAHFARRQAAIKAEEARKADElkkaEEKKKADEAKKAEEK-KKADEAKKKA---EEAKKADEAKKKA--EEA 1327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2325 KREQERLAKEMQEKKLQQELERQKEE---DELKRKVKKGKQGPIKEEPPPKKSQASNKQVPPFTKVD-VKMETIERKISV 2400
Cdd:PTZ00121  1328 KKKADAAKKKAEEAKKAAEAAKAEAEaaaDEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADeAKKKAEEDKKKA 1407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2401 REptVSEKEELNKK----KRNMGDVSMLGLPLVQDQEDSEGDVSKdpdKQLAQRFKAYELTLKDVQNILMYWDRKQGVQL 2476
Cdd:PTZ00121  1408 DE--LKKAAAAKKKadeaKKKAEEKKKADEAKKKAEEAKKADEAK---KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2477 PPA-----GMEEAAHEPDDQRQVPSGGRRGRKDRERERLEKERTEKERLEREKA-------ERERLEKLRALEERSDWEG 2544
Cdd:PTZ00121  1483 KKAdeakkKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeakkaeEKKKADELKKAEELKKAEE 1562
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916950 2545 EGEEDHEGKKEKDLGVPFLNI----QTPDFEGLNWKQALESDKLPKGEQAQEEQTSSSKGGKQKVKEKTDQVVETQKDK 2619
Cdd:PTZ00121  1563 KKKAEEAKKAEEDKNMALRKAeeakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
2270-2376 1.13e-10

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: 63.14  E-value: 1.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2270 QEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKltfnqgiQQALRERKKREQERLAKEMQEKKLQQELERQKE 2349
Cdd:pfam05672   32 QERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERR-------REEEERQRKAEEEAEEREQREQEEQERLQKQKE 104
                           90       100
                   ....*....|....*....|....*..
gi 1622916950 2350 EDELKRKVKKGKQGPIKEEPPPKKSQA 2376
Cdd:pfam05672  105 EAEAKAREEAERQRQEREKIMQQEEQE 131
PTZ00121 PTZ00121
MAEBL; Provisional
2265-2632 2.49e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.47  E-value: 2.49e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2265 AAMKAQEKAKKEQEERKHKEalEKEKERLQNMDEE-EYDAL-TEEEKLTFNQGIQQALRERK-----------KREQERL 2331
Cdd:PTZ00121  1333 AAKKKAEEAKKAAEAAKAEA--EAAADEAEAAEEKaEAAEKkKEEAKKKADAAKKKAEEKKKadeakkkaeedKKKADEL 1410
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2332 AKEMQEKKLQQELERQKEE----DELKRKVKKGKqgpiKEEPPPKKSQASNKQVPPFTKVDVKMETIERKISVREPTVSE 2407
Cdd:PTZ00121  1411 KKAAAAKKKADEAKKKAEEkkkaDEAKKKAEEAK----KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2408 ----KEELNKKKRNMGDVSMLGLPLVQDQEDSEGDVSKDPDKQLAQRFKAYEltLKDVQNILMYWDRKQGVQLPPA---- 2479
Cdd:PTZ00121  1487 eakkKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE--AKKAEEKKKADELKKAEELKKAeekk 1564
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2480 GMEEAAHEPDDQRQVPSGGRRGRK-------DRERERLEKERTEKERLEREKAERERLEKLRALEERSDWEGEGEEDHEG 2552
Cdd:PTZ00121  1565 KAEEAKKAEEDKNMALRKAEEAKKaeearieEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2553 KKEKDLGVpflniqtpdfeglnwKQALESDKLPKGEQAQEEQTSSSKGGKQKVKE-----KTDQVVETQKDKRRVALNRK 2627
Cdd:PTZ00121  1645 EKKKAEEL---------------KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEedekkAAEALKKEAEEAKKAEELKK 1709

                   ....*
gi 1622916950 2628 VISGE 2632
Cdd:PTZ00121  1710 KEAEE 1714
PTZ00121 PTZ00121
MAEBL; Provisional
2257-2463 2.80e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.47  E-value: 2.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2257 VLNMAQDYAAMKAqEKAKKEQEERKHKEALEKEKE------RLQNMDEEEYDALTEEEKLTFNQGIQQALRERKKREQER 2330
Cdd:PTZ00121  1597 VMKLYEEEKKMKA-EEAKKAEEAKIKAEELKKAEEekkkveQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2331 LAKEMQ-----EKKLQQELERQKEEDELKRKVKKGKQGPIKEEPPPKKSQASNKqvppftkvdVKMETIERKisvREPTV 2405
Cdd:PTZ00121  1676 KAEEAKkaeedEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK---------IKAEEAKKE---AEEDK 1743
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916950 2406 SEKEELNKKKRNMGDVSMLGLPLVQDQE----DSEGDVSKDPDKQLAQRFKAYELTLKDVQN 2463
Cdd:PTZ00121  1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEeirkEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
PTZ00121 PTZ00121
MAEBL; Provisional
2265-2684 3.76e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.09  E-value: 3.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2265 AAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDAlteEEKLTFNQGIQQALRERKKREQERLAKEM----QEKKL 2340
Cdd:PTZ00121  1382 AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA---DEAKKKAEEKKKADEAKKKAEEAKKADEAkkkaEEAKK 1458
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2341 QQELERQKEE----DELKRKV---KKGKQGPIKEEPPPKKSQASNKQVPPFTKVDVKMETIERKISVREPTVSEK---EE 2410
Cdd:PTZ00121  1459 AEEAKKKAEEakkaDEAKKKAeeaKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkaDE 1538
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2411 LNK--KKRNMGDVSML-GLPLVQDQEDSEGDVSKDPDKQLAQRfKAYEltLKDVQNILMYWDRKQGVQLPPAGMEEAAHE 2487
Cdd:PTZ00121  1539 AKKaeEKKKADELKKAeELKKAEEKKKAEEAKKAEEDKNMALR-KAEE--AKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2488 PDDQRQvpsgGRRGRKDRERERLEKERTEKERLEREKAER----ERLEKLRALEERSDWEGEGEEDHEGKKE------KD 2557
Cdd:PTZ00121  1616 EEAKIK----AEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkaEEENKIKAAEEAKKAEEDKKKAEEAKKAeedekkAA 1691
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2558 LGVPFLNIQTPDFEGLNWKQALESDKLPKGEQAQEEQTSSSKGGKQKVKEKTDQVVETQKD---KRRVALNRK------- 2627
Cdd:PTZ00121  1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeeKKKIAHLKKeeekkae 1771
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916950 2628 VISGEPAGTISQ-LSDTDLNNFNGQHSQEKFTRLNhFRWIVPANGEVTLQVHFSSDEF 2684
Cdd:PTZ00121  1772 EIRKEKEAVIEEeLDEEDEKRRMEVDKKIKDIFDN-FANIIEGGKEGNLVINDSKEME 1828
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2268-2538 6.17e-10

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: 65.92  E-value: 6.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQ---ALRERKKREQERLAKEMQEK--KLQQ 2342
Cdd:pfam17380  317 KLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQeeiAMEISRMRELERLQMERQQKneRVRQ 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2343 ELE---RQK-EEDELKRKVKKGKqgpiKEEPPPKKSQASNKQVppftKVDVKMETIERKIS-VREPTVSEKEELNKKKRN 2417
Cdd:pfam17380  397 ELEaarKVKiLEEERQRKIQQQK----VEMEQIRAEQEEARQR----EVRRLEEERAREMErVRLEEQERQQQVERLRQQ 468
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2418 MGDVSMLGLPLVQDQEdsegdvskdpDKQLA--QRFKAYELTLKDVQNILMYWDRKQgvQLPPAGMEE---AAHEpDDQR 2492
Cdd:pfam17380  469 EEERKRKKLELEKEKR----------DRKRAeeQRRKILEKELEERKQAMIEEERKR--KLLEKEMEErqkAIYE-EERR 535
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1622916950 2493 QVPSGGRRGRKDRERERLEKERTEK---ERLEREKAERERlEKLRALEE 2538
Cdd:pfam17380  536 REAEEERRKQQEMEERRRIQEQMRKateERSRLEAMERER-EMMRQIVE 583
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2258-2362 6.41e-10

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: 64.55  E-value: 6.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2258 LNMAQDYAAMKA------QEKAKKEQEERKHKEALEK--EKERLQNMD-EEEYDALTEEEKLTFNQGIQQALRERKKREQ 2328
Cdd:pfam13868   11 LNSKLLAAKCNKerdaqiAEKKRIKAEEKEEERRLDEmmEEERERALEeEEEKEEERKEERKRYRQELEEQIEEREQKRQ 90
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1622916950 2329 ERLAKEMQEKKLQQE-LERQKEEDELKRKVKKGKQ 2362
Cdd:pfam13868   91 EEYEEKLQEREQMDEiVERIQEEDQAEAEEKLEKQ 125
PTZ00121 PTZ00121
MAEBL; Provisional
2263-2661 1.87e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.78  E-value: 1.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2263 DYAAMKAQEKAKKEQ----EERKHKEALEKEKER-----LQNMDE-EEYDALTEEEKLTFNQGIQQAlrERKKREQER-- 2330
Cdd:PTZ00121  1500 DEAKKAAEAKKKADEakkaEEAKKADEAKKAEEAkkadeAKKAEEkKKADELKKAEELKKAEEKKKA--EEAKKAEEDkn 1577
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2331 -------LAKEMQEKKLQQELERQKEEDELK-RKVKKGKQGPIKEEpPPKKSQASNKQVPPFTKVDV----KMETI---E 2395
Cdd:PTZ00121  1578 malrkaeEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAeekkKAEELkkaE 1656
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2396 RKISVREPTVSEKEELNKKKRNMgdvsmlglplVQDQEDSEGDVSKDPDKQLAQRFKAYELTLKDVQNILMYWDRKQGVQ 2475
Cdd:PTZ00121  1657 EENKIKAAEEAKKAEEDKKKAEE----------AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2476 LPPAGMEEAAHEPDDQRqvpsggRRGRKDRERERLEKERTEKERLEREKAERERLEKLRALEERSDWEGEGEEDHEGKKE 2555
Cdd:PTZ00121  1727 ENKIKAEEAKKEAEEDK------KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2556 KDLGVPFLNIQTPDFEG-------------------------LNWKQALESDKLPKGEQAQEEQTSSSKGGKQK--VKEK 2608
Cdd:PTZ00121  1801 KDIFDNFANIIEGGKEGnlvindskemedsaikevadsknmqLEEADAFEKHKFNKNNENGEDGNKEADFNKEKdlKEDD 1880
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622916950 2609 TDQVVETQKDKRrvaLNRKVISGEPAGtisqlsdtdlNNFNGQHSQEKFTRLN 2661
Cdd:PTZ00121  1881 EEEIEEADEIEK---IDKDDIEREIPN----------NNMAGKNNDIIDDKLD 1920
PTZ00121 PTZ00121
MAEBL; Provisional
2266-2627 2.55e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.39  E-value: 2.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2266 AMKAQEKAKKEQEERKHKEALEKEKERlqnmdEEEYDALTEEEKLTFNQGIQQALRERKKREQERLaKEMQEKKLQQEL- 2344
Cdd:PTZ00121  1223 AKKAEAVKKAEEAKKDAEEAKKAEEER-----NNEEIRKFEEARMAHFARRQAAIKAEEARKADEL-KKAEEKKKADEAk 1296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2345 --ERQKEEDELKRKV---KKGKQGPIKEEPPPKKSQASNKQVPPFTKVDVKMETIERKISVREPTVSEKEELNKKKRnmg 2419
Cdd:PTZ00121  1297 kaEEKKKADEAKKKAeeaKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK--- 1373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2420 dvsmlglplvqDQEDSEGDVSKdpdKQLAQRFKAYELTLKDVQnilmywDRKQGVQLPPAG-----MEEAAHEPDDQRQV 2494
Cdd:PTZ00121  1374 -----------EEAKKKADAAK---KKAEEKKKADEAKKKAEE------DKKKADELKKAAaakkkADEAKKKAEEKKKA 1433
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2495 PSGGRRG---RKDRERERLEKERTEKERLEREKAERERLEKL-RALEERSDWEGEGEEDHEGKKEKDLGVPFLNIQTPDF 2570
Cdd:PTZ00121  1434 DEAKKKAeeaKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAkKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916950 2571 EGLNWKQALESDKLPKGEQAQEEQTSSSKGGKQKVKE-KTDQVVETQKDKRRVALNRK 2627
Cdd:PTZ00121  1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEEKKKAEEAKK 1571
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
2260-2359 2.87e-09

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: 58.01  E-value: 2.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2260 MAQDyAAMKAQEKAKKEQEERKhkeALEKEKERLQnmdEEEYDALTEEEKLtfnqgiqQALRERKKREQERLAKEMQEK- 2338
Cdd:pfam20492   24 KAQE-ELEESEETAEELEEERR---QAEEEAERLE---QKRQEAEEEKERL-------EESAEMEAEEKEQLEAELAEAq 89
                           90       100
                   ....*....|....*....|....*.
gi 1622916950 2339 ----KLQQELERQKEE-DELKRKVKK 2359
Cdd:pfam20492   90 eeiaRLEEEVERKEEEaRRLQEELEE 115
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
2271-2416 6.72e-09

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: 57.74  E-value: 6.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2271 EKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLtfnqgiQQALRERKKREQE--RLAKE--MQEKKLQQELER 2346
Cdd:pfam05672   10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELR------RRAEEERARREEEarRLEEErrREEEERQRKAEE 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622916950 2347 QKEEDELKRKVKKGKQGPIKEEPPPKKSQASNKQVPpftkvdvkmetiER-KISVREptvsEKEELNKKKR 2416
Cdd:pfam05672   84 EAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQ------------EReKIMQQE----EQERLERKKR 138
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
2252-2359 1.46e-08

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: 56.04  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2252 REhIYVLNMAQDyaaMKAQEKAKKEQEERKHKEALEKEKERLQNmDEEEYDALTEEEKLTFNQGIQQALRERKKREQerl 2331
Cdd:pfam13863    6 RE-MFLVQLALD---AKREEIERLEELLKQREEELEKKEQELKE-DLIKFDKFLKENDAKRRRALKKAEEETKLKKE--- 77
                           90       100
                   ....*....|....*....|....*....
gi 1622916950 2332 aKEMQEKKLQQELER-QKEEDELKRKVKK 2359
Cdd:pfam13863   78 -KEKEIKKLTAQIEElKSEISKLEEKLEE 105
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
2270-2352 1.85e-08

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: 60.74  E-value: 1.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2270 QEKAKK-----EQEERKHKEALEKEKERLqnmdEEEYDALTEEEKltfNQGIQ-QALRERKKREQE---RLAKEMQEKKL 2340
Cdd:pfam15709  368 LERAEKmreelELEQQRRFEEIRLRKQRL----EEERQRQEEEER---KQRLQlQAAQERARQQQEefrRKLQELQRKKQ 440
                           90
                   ....*....|..
gi 1622916950 2341 QQELERQKEEDE 2352
Cdd:pfam15709  441 QEEAERAEAEKQ 452
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
2266-2350 2.01e-08

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: 55.31  E-value: 2.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2266 AMKAQEKAKKEQEER-----KHKEALEkEKERLQ---NMDEEEYDALTEEekltfnqgIQQALRERKKREQERLAKEMQE 2337
Cdd:pfam20492   36 AEELEEERRQAEEEAerleqKRQEAEE-EKERLEesaEMEAEEKEQLEAE--------LAEAQEEIARLEEEVERKEEEA 106
                           90
                   ....*....|...
gi 1622916950 2338 KKLQQELERQKEE 2350
Cdd:pfam20492  107 RRLQEELEEAREE 119
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2265-2359 2.44e-08

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: 59.55  E-value: 2.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2265 AAMKAQEKAKKEQEERKhkeALEKEKERLQNMDEEEYDALTEEEKLTFNQgIQQALRERKKREQERLAKEMQEKKLQQEL 2344
Cdd:pfam13868  127 QLREEIDEFNEEQAEWK---ELEKEEEREEDERILEYLKEKAEREEEREA-EREEIEEEKEREIARLRAQQEKAQDEKAE 202
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1622916950 2345 ----------------ERQKEEDELKRKVKK 2359
Cdd:pfam13868  203 rdelraklyqeeqerkERQKEREEAEKKARQ 233
Caldesmon pfam02029
Caldesmon;
2269-2538 3.02e-08

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 59.88  E-value: 3.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2269 AQEKAKKEQEER-KHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGI----QQALRER-KKREQERlakemqEKKLQQ 2342
Cdd:pfam02029    8 ARERRRRAREERrRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGgldeEEAFLDRtAKREERR------QKRLQE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2343 ELERQKEEDElkrkvkkgkqgPIKEEPPPKKSQASNKQVPPFTKV--DVKMETIERKISVREPTVSEKEELNKKKRNmgd 2420
Cdd:pfam02029   82 ALERQKEFDP-----------TIADEKESVAERKENNEEEENSSWekEEKRDSRLGRYKEEETEIREKEYQENKWST--- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2421 vsmlGLPLVQDQEDSEGDVSKDPDKQLAQRFKAYELT-------LKDVQNILMYWDRKQGV--QLPPAGMEEAAHEPDDQ 2491
Cdd:pfam02029  148 ----EVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKdekikkeKKVKYESKVFLDQKRGHpeVKSQNGEEEVTKLKVTT 223
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916950 2492 RQVPSGGRRGRKDRERERLEKERTEK-ERLEREKAERE------------------------RLEKLRALEE 2538
Cdd:pfam02029  224 KRRQGGLSQSQEREEEAEVFLEAEQKlEELRRRRQEKEseefeklrqkqqeaeleleelkkkREERRKLLEE 295
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2265-2355 5.15e-08

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: 58.39  E-value: 5.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2265 AAMKAQEKAKKEQ---------------EERKHKEALEKEKERLQnMDeEEYDALTEEEkltfnqgiqQALRERKKREQE 2329
Cdd:pfam13868   58 EEEEEKEEERKEErkryrqeleeqieerEQKRQEEYEEKLQEREQ-MD-EIVERIQEED---------QAEAEEKLEKQR 126
                           90       100       110
                   ....*....|....*....|....*....|
gi 1622916950 2330 RLAKEM----QEKKLQQELERQKEEDELKR 2355
Cdd:pfam13868  127 QLREEIdefnEEQAEWKELEKEEEREEDER 156
Caldesmon pfam02029
Caldesmon;
2263-2539 5.80e-08

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 59.11  E-value: 5.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2263 DYAAMKAQEKAKKEQEERKHKEALEKEKE--------------RLQNMDEEEYDALTEEEKltfnqgIQQALRERKKREQ 2328
Cdd:pfam02029   60 EEEAFLDRTAKREERRQKRLQEALERQKEfdptiadekesvaeRKENNEEEENSSWEKEEK------RDSRLGRYKEEET 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2329 ERLAKEMQEKKLQQELERQKEEDElkRKVKKGKqgpiKEEPPPKKSQASNKQVPPFTKVDVKMETIERKISVREPTVSEK 2408
Cdd:pfam02029  134 EIREKEYQENKWSTEVRQAEEEGE--EEEDKSE----EAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEV 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2409 -----EELNKKKRNMGDVSMLGLPLVQDQEdSEGDVSKDPDKQLA-QRFKAYELTLKDVQNIlmywdrKQGVQLPPAGME 2482
Cdd:pfam02029  208 ksqngEEEVTKLKVTTKRRQGGLSQSQERE-EEAEVFLEAEQKLEeLRRRRQEKESEEFEKL------RQKQQEAELELE 280
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622916950 2483 EAAHEPDDQRQVPSGGRRGRKDRERERLEKERTEKERLeREKAERERLEklrALEER 2539
Cdd:pfam02029  281 ELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRM-KEEIERRRAE---AAEKR 333
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
2266-2384 6.91e-08

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: 55.46  E-value: 6.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2266 AMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDaltEEEKLtfnqgiqQALRERKKREQERLAKEMQEKKLQQELE 2345
Cdd:pfam11600   45 AKAEKERAKEEARRKKEEEKELKEKERREKKEKDEKE---KAEKL-------RLKEEKRKEKQEALEAKLEEKRKKEEEK 114
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1622916950 2346 RQKEEdelKRKVKKGK-------QGPiKEEPPPKKSQASNKQVPPF 2384
Cdd:pfam11600  115 RLKEE---EKRIKAEKaeitrflQKP-KTQQAPKTLAGSCGKFAPF 156
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
2261-2380 7.94e-08

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: 57.93  E-value: 7.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2261 AQDYAAMKAQEK--AKKEQEERKH----KEALEK----EKERLQNMDEEEYDALT----EEEKLTFNQGIQQALRERKKR 2326
Cdd:TIGR02794   49 AQQANRIQQQKKpaAKKEQERQKKleqqAEEAEKqraaEQARQKELEQRAAAEKAakqaEQAAKQAEEKQKQAEEAKAKQ 128
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916950 2327 EQERLAKEMQ--EKKLQQELERQKEEDELKRKVKKGKQgpiKEEPPPKKSQASNKQ 2380
Cdd:TIGR02794  129 AAEAKAKAEAeaERKAKEEAAKQAEEEAKAKAAAEAKK---KAEEAKKKAEAEAKA 181
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
2266-2359 1.30e-07

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 56.91  E-value: 1.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2266 AMKAQEKAKKEqeERKHKEALEKEKERLQNMDEEEyDALTEEEKLTFNQGIQQaLRERKKREQERLAKEmQEKKLQQELE 2345
Cdd:pfam02841  198 ALTAKEKAIEA--ERAKAEAAEAEQELLREKQKEE-EQMMEAQERSYQEHVKQ-LIEKMEAEREQLLAE-QERMLEHKLQ 272
                           90
                   ....*....|....*.
gi 1622916950 2346 RQKE--EDELKRKVKK 2359
Cdd:pfam02841  273 EQEEllKEGFKTEAES 288
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2267-2418 2.04e-07

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: 57.83  E-value: 2.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2267 MKAQEKAKKEQEERKHKEA--LEKEKER-LQNMDEEEYDALTEEEKLTfnqgIQQALRERKKREQER------LAKEMQE 2337
Cdd:pfam17380  419 KVEMEQIRAEQEEARQREVrrLEEERAReMERVRLEEQERQQQVERLR----QQEEERKRKKLELEKekrdrkRAEEQRR 494
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2338 KKLQQELERQKE---EDELKRKV----KKGKQGPIKEEPPPKKSQASNKQvppftkvDVKMETiERKISVREPTVSEKE- 2409
Cdd:pfam17380  495 KILEKELEERKQamiEEERKRKLlekeMEERQKAIYEEERRREAEEERRK-------QQEMEE-RRRIQEQMRKATEERs 566
                          170
                   ....*....|.
gi 1622916950 2410 --ELNKKKRNM 2418
Cdd:pfam17380  567 rlEAMEREREM 577
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
2268-2416 3.06e-07

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: 53.54  E-value: 3.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEErKHKEALEKEKERLQNmdEEEYDALTEEEKltfnqgiqqALRERKKREQERLAKEMQEKKlqqelERQ 2347
Cdd:pfam11600    1 RRSQKSVQSQEE-KEKQRLEKDKERLRR--QLKLEAEKEEKE---------RLKEEAKAEKERAKEEARRKK-----EEE 63
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916950 2348 KEEDELKRKVKKGKQGPIKEEpppkksqasnkqvppftKVDVKMETIERKISVREPTVSEKEELNKKKR 2416
Cdd:pfam11600   64 KELKEKERREKKEKDEKEKAE-----------------KLRLKEEKRKEKQEALEAKLEEKRKKEEEKR 115
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
2269-2356 4.04e-07

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: 52.74  E-value: 4.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2269 AQEKAKKEQEERKHKE--ALEKEKERLQNMDEEEYDALTEEEKltfnqgiqQALRERKKREQERLAKEMQEKKlQQELER 2346
Cdd:pfam05672   53 EEERARREEEARRLEEerRREEEERQRKAEEEAEEREQREQEE--------QERLQKQKEEAEAKAREEAERQ-RQEREK 123
                           90
                   ....*....|...
gi 1622916950 2347 --QKEEDE-LKRK 2356
Cdd:pfam05672  124 imQQEEQErLERK 136
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
2261-2376 5.74e-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: 55.24  E-value: 5.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2261 AQDYAAMKAQEKAKKEQEErKHKEALE-KEKERLQNMDEEEYDAlteeEKLTFNQGIQQALRERKKREQERLAKEMQEKK 2339
Cdd:TIGR02794   98 AAAEKAAKQAEQAAKQAEE-KQKQAEEaKAKQAAEAKAKAEAEA----ERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK 172
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1622916950 2340 LQQELERqKEEDELKRKvKKGKQGPIKEEPPPKKSQA 2376
Cdd:TIGR02794  173 KKAEAEA-KAKAEAEAK-AKAEEAKAKAEAAKAKAAA 207
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
2268-2379 6.27e-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: 55.24  E-value: 6.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEERKhKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQAlreRKKREQERLAKEMQEKKLQQELERQ 2347
Cdd:TIGR02794   98 AAAEKAAKQAEQAA-KQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEA---AKQAEEEAKAKAAAEAKKKAEEAKK 173
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1622916950 2348 KEEDELKRKV---KKGKQgpikEEPPPKKSQASNK 2379
Cdd:TIGR02794  174 KAEAEAKAKAeaeAKAKA----EEAKAKAEAAKAK 204
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
2268-2356 1.43e-06

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 54.27  E-value: 1.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALT-EEEKLTFNQGIQQALRERKKREQerlaKEMQEKKLQQELER 2346
Cdd:pfam15558   38 RRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGrEERRRADRREKQVIEKESRWREQ----AEDQENQRQEKLER 113
                           90
                   ....*....|
gi 1622916950 2347 QKEEDELKRK 2356
Cdd:pfam15558  114 ARQEAEQRKQ 123
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
2268-2416 1.79e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 54.45  E-value: 1.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEE---KLTFNQGIQQALRERKKrEQERLAKEMQEK-KLQQE 2343
Cdd:PRK00409   524 SLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEdklLEEAEKEAQQAIKEAKK-EADEIIKELRQLqKGGYA 602
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2344 LERQKEEDELKRKVKKGKQgPIKEEPPPKKSQASNKQV------PPF-TKVDV-----KMETIER----KISVR----EP 2403
Cdd:PRK00409   603 SVKAHELIEARKRLNKANE-KKEKKKKKQKEKQEELKVgdevkyLSLgQKGEVlsipdDKEAIVQagimKMKVPlsdlEK 681
                          170
                   ....*....|...
gi 1622916950 2404 TVSEKEELNKKKR 2416
Cdd:PRK00409   682 IQKPKKKKKKKPK 694
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
2251-2356 2.03e-06

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 53.50  E-value: 2.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2251 SREHIYVLNMAQDYAAMKAQEKAKKEQEERKHKEALEKEKERLQNM--DEEEYDALTEEEKLTFNQGIQQALRERKKREQ 2328
Cdd:pfam15558   84 RREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLkeKEEELQALREQNSLQLQERLEEACHKRQLKER 163
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1622916950 2329 ErLAKEMQEKKLQ---------QELERQKEEDELKRK 2356
Cdd:pfam15558  164 E-EQKKVQENNLSellnhqarkVLVDCQAKAEELLRR 199
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
2269-2356 2.82e-06

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: 50.05  E-value: 2.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2269 AQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDA-----LTEEEKLTFNQGIQQALRERKKREQERLAKEMQEKKLQQE 2343
Cdd:pfam15346    3 AESKLLEEETARRVEEAVAKRVEEELEKRKDEIEAeverrVEEARKIMEKQVLEELEREREAELEEERRKEEEERKKREE 82
                           90
                   ....*....|....*...
gi 1622916950 2344 LER-----QKEEDELKRK 2356
Cdd:pfam15346   83 LERileenNRKIEEAQRK 100
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2267-2542 4.39e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 53.44  E-value: 4.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2267 MKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKltFNQGIQQALRERKKREQERLAKEMQE-KKLQQELE 2345
Cdd:pfam02463  254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE--ELKSELLKLERRKVDDEEKLKESEKEkKKAEKELK 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2346 RQKEEDELKRKVKKgKQGPIKEEPPPKKSQASNKQVPPFTKVDVKMETIERKISVREPTVSEKEELNKKKRNMGDVSMLG 2425
Cdd:pfam02463  332 KEKEEIEELEKELK-ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLL 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2426 LPLVQDQEDSEgdvskdpdKQLAQRFKAYELTLKDVQNILMYWDRKQGVQLppagMEEAAHEPDDQRQVpsggRRGRKDR 2505
Cdd:pfam02463  411 LELARQLEDLL--------KEEKKEELEILEEEEESIELKQGKLTEEKEEL----EKQELKLLKDELEL----KKSEDLL 474
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1622916950 2506 ERERLEKERTEKERLEREKAERERLEKLRALEERSDW 2542
Cdd:pfam02463  475 KETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2259-2538 6.63e-06

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: 51.84  E-value: 6.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2259 NMAQDYAAMKAQEKAKKEQEER---------KHKEALEK---EKERLQNMDEEEYdaltEEEKLTFNQgIQQALRErkkr 2326
Cdd:pfam13868   42 ERRLDEMMEEERERALEEEEEKeeerkeerkRYRQELEEqieEREQKRQEEYEEK----LQEREQMDE-IVERIQE---- 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2327 EQERLAKEMQEKK--LQQELERQKEEDELKRKVKKGKQgpiKEEppPKKSQASNKQvppftkvdvKMETIERKISVREPT 2404
Cdd:pfam13868  113 EDQAEAEEKLEKQrqLREEIDEFNEEQAEWKELEKEEE---REE--DERILEYLKE---------KAEREEEREAEREEI 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2405 VSEKEELNKKkrnmgdvsmlglpLVQDQEDSEgdvskdpDKQLAQ---RFKAY--ELTLKdvqnilmyWDRKQgvqlppa 2479
Cdd:pfam13868  179 EEEKEREIAR-------------LRAQQEKAQ-------DEKAERdelRAKLYqeEQERK--------ERQKE------- 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916950 2480 gMEEAAHEPDDQRQVpsggRRGRKDrererlekERTEKERLEREKAERERLEKLRALEE 2538
Cdd:pfam13868  224 -REEAEKKARQRQEL----QQAREE--------QIELKERRLAEEAEREEEEFERMLRK 269
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2251-2639 6.64e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 53.05  E-value: 6.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2251 SREHIYVLNMAQDY---AAMKAQEKAKKEQE------ERKHKEALEKEKERLQNMDEEEYDALTEEEKLtfnqgiQQALR 2321
Cdd:pfam02463  131 SPEAYNFLVQGGKIeiiAMMKPERRLEIEEEaagsrlKRKKKEALKKLIEETENLAELIIDLEELKLQE------LKLKE 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2322 ERKKrEQERLAKEMQEKKLQQEL-------ERQKEEDELKRKVKKGKQGPIKEEPPPKKSQASNKQVppfTKVDVKMETI 2394
Cdd:pfam02463  205 QAKK-ALEYYQLKEKLELEEEYLlyldylkLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQV---LKENKEEEKE 280
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2395 ERKISVREPTVSEKEELNKKKRNMGDV--SMLGLPLVQDQEDSEgdvSKDPDKQLAQRFKAYELTLKDVQNILMYWDRKQ 2472
Cdd:pfam02463  281 KKLQEEELKLLAKEEEELKSELLKLERrkVDDEEKLKESEKEKK---KAEKELKKEKEEIEELEKELKELEIKREAEEEE 357
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2473 GVQLpPAGMEEAAHEPDDQRQVPSGGRRGRKDrererlEKERTEKERLEREKAERERLEKLRALEERSDwegegeedhEG 2552
Cdd:pfam02463  358 EEEL-EKLQEKLEQLEEELLAKKKLESERLSS------AAKLKEEELELKSEEEKEAQLLLELARQLED---------LL 421
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2553 KKEKDLGVPFLNIQTPDFEGLNWKQALESDKLPKGE------QAQEEQTSSSKGGKQKVKEKTDQV--VETQKDKRRVAL 2624
Cdd:pfam02463  422 KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQElkllkdELELKKSEDLLKETQLVKLQEQLEllLSRQKLEERSQK 501
                          410
                   ....*....|....*
gi 1622916950 2625 NRKVISGEPAGTISQ 2639
Cdd:pfam02463  502 ESKARSGLKVLLALI 516
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2260-2359 6.80e-06

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: 51.84  E-value: 6.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2260 MAQDYAAMKAQEK------AKKEQEERKHKEALEKEKERLQNMDEEEydalTEEEKLTFNQGIQQALRERK-KREQERLA 2332
Cdd:pfam13868  237 LQQAREEQIELKErrlaeeAEREEEEFERMLRKQAEDEEIEQEEAEK----RRMKRLEHRRELEKQIEEREeQRAAEREE 312
                           90       100
                   ....*....|....*....|....*....
gi 1622916950 2333 KEMQEKKLQQELERQKE--EDELKRKVKK 2359
Cdd:pfam13868  313 ELEEGERLREEEAERREriEEERQKKLKE 341
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
2262-2362 6.86e-06

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 50.47  E-value: 6.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2262 QDYAAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYD---------ALTEEEKLTFNQGIQQALRERKKREQERLA 2332
Cdd:pfam13904   58 ENWLAAKQRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQewlqrkarqQTKKREESHKQKAAESASKSLAKPERKVSQ 137
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1622916950 2333 KEMQE-------KKLQQELERQKEEDELKRKVKKGKQ 2362
Cdd:pfam13904  138 EEAKEvlqewerKKLEQQQRKREEEQREQLKKEEEEQ 174
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
2261-2380 7.09e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.12  E-value: 7.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2261 AQDYAAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEeydalteeekltfnqgiQQALRER-KKREQERLAKEMQEKK 2339
Cdd:PRK09510    61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAE-----------------QERLKQLeKERLAAQEQKKQAEEA 123
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1622916950 2340 LQQELERQKEEDELKRKVKKGKQgpIKEEPPPKKSQASNKQ 2380
Cdd:PRK09510   124 AKQAALKQKQAEEAAAKAAAAAK--AKAEAEAKRAAAAAKK 162
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
2259-2380 7.94e-06

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: 52.26  E-value: 7.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2259 NMAQDYAA---MKAQEKAKKEQE-ERKHKEalEKEKERLQNMDEEEYDALTEEEKLTfNQGIQQALRERKKR-EQERLAK 2333
Cdd:pfam15709  327 KREQEKASrdrLRAERAEMRRLEvERKRRE--QEEQRRLQQEQLERAEKMREELELE-QQRRFEEIRLRKQRlEEERQRQ 403
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622916950 2334 EMQEKK--LQQELERQK---EEDELKRKVKKGKQGPIKEEpppKKSQASNKQ 2380
Cdd:pfam15709  404 EEEERKqrLQLQAAQERarqQQEEFRRKLQELQRKKQQEE---AERAEAEKQ 452
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2268-2362 8.01e-06

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: 52.43  E-value: 8.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEERKHKEA-------LEKE-KERLQNMDEEEYD-ALTEEEKLTFNQGIQQALRERKKREQERLAKEMQEK 2338
Cdd:pfam17380  472 RKRKKLELEKEKRDRKRAeeqrrkiLEKElEERKQAMIEEERKrKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEER 551
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1622916950 2339 KLQQE-----------LERQKEEDELKRKVKKGKQ 2362
Cdd:pfam17380  552 RRIQEqmrkateersrLEAMEREREMMRQIVESEK 586
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2269-2352 8.45e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 8.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2269 AQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALtEEEKLTFNQGIQQALRERKKREQERLAKEMQEKKLQQELERQK 2348
Cdd:COG1196    342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA-EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420

                   ....
gi 1622916950 2349 EEDE 2352
Cdd:COG1196    421 EELE 424
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2271-2362 9.75e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 50.31  E-value: 9.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2271 EKAKKEQEERKHKEALEKEKERLQN-MDEEEYDALTEEekltfnqgIQQALRERKKREQERLAKEMQEKKLQQELERQKE 2349
Cdd:COG1579     60 EIKRLELEIEEVEARIKKYEEQLGNvRNNKEYEALQKE--------IESLKRRISDLEDEILELMERIEELEEELAELEA 131
                           90
                   ....*....|....
gi 1622916950 2350 E-DELKRKVKKGKQ 2362
Cdd:COG1579    132 ElAELEAELEEKKA 145
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
2255-2359 1.05e-05

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: 48.35  E-value: 1.05e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950  2255 IYVLNMAQDYAAMKAQEKAKK--EQEERKHKEALEKEKERLQNMdEEEYDAltEEEKLTfnqgiqQALRERKKREQERLA 2332
Cdd:smart00935    1 IGVVDVQKILQESPAGKAAQKqlEKEFKKRQAELEKLEKELQKL-KEKLQK--DAATLS------EAAREKKEKELQKKV 71
                            90       100       110
                    ....*....|....*....|....*....|.
gi 1622916950  2333 KEMQEK--KLQQELE--RQKEEDELKRKVKK 2359
Cdd:smart00935   72 QEFQRKqqKLQQDLQkrQQEELQKILDKINK 102
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2271-2415 1.28e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2271 EKAKKEQEERKHKEALEKEKERLQNMDEE-----------EYDALTEEEKLtfnQGIQQALRERKKREQERLAKEMQEKK 2339
Cdd:PRK03918   211 EISSELPELREELEKLEKEVKELEELKEEieelekeleslEGSKRKLEEKI---RELEERIEELKKEIEELEEKVKELKE 287
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916950 2340 LQQELERQKEEDELKRKVKKGKQGPIKEEpppkksqasnkqvppfTKVDVKMETIERKISVREPTVSEKEELNKKK 2415
Cdd:PRK03918   288 LKEKAEEYIKLSEFYEEYLDELREIEKRL----------------SRLEEEINGIEERIKELEEKEERLEELKKKL 347
DUF612 pfam04747
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ...
2268-2415 1.36e-05

Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.


Pssm-ID: 282585 [Multi-domain]  Cd Length: 511  Bit Score: 51.60  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEERKH---KEALEKEKERLQNmdEEEYDALTEEEKLTFnqgiqQALRERKKREQERlaKEMQEKKLQQEL 2344
Cdd:pfam04747   77 KAQKQIAKDHEAEQKvnaKKAAEKEARRAEA--EAKKRAAQEEEHKQW-----KAEQERIQKEQEK--KEADLKKLQAEK 147
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916950 2345 ERQK----EEDELKRKVKKGKQ-GPIKEEPPPKKSQASNKQVP---PFTKVDVKMETIERkisVREPTvSEKEELNKKK 2415
Cdd:pfam04747  148 KKEKavkaEKAEKAEKTKKASTpAPVEEEIVVKKVANDRSAAPapePKTPTNTPAEPAEQ---VQEIT-GKKNKKNKKK 222
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2297-2632 1.53e-05

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2297 DEEEYDALTEEEKLTFNQGIQQALRERKKREQERLAKEMQEKKLQQELERQKEEDELKRKVKKgkqgpiKEEPPPKKSQA 2376
Cdd:TIGR02169  169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKE------KEALERQKEAI 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2377 sNKQVPPFTKVdvkMETIERKISVREPTVSEKE----ELNKKKRNMGDVSMLGL-----------PLVQDQEDSEGDVSK 2441
Cdd:TIGR02169  243 -ERQLASLEEE---LEKLTEEISELEKRLEEIEqlleELNKKIKDLGEEEQLRVkekigeleaeiASLERSIAEKERELE 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2442 DPDKQLAQRFKAYELTLKDVQNIlmywDRKQG-VQLPPAGMEEaahEPDDQRQVpsggrrgRKDRERERLEKERTEKERL 2520
Cdd:TIGR02169  319 DAEERLAKLEAEIDKLLAEIEEL----EREIEeERKRRDKLTE---EYAELKEE-------LEDLRAELEEVDKEFAETR 384
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2521 EREKAERERLEKLRalEERSDWEGEGEEDHEGKKEKDLGVPFLNIQTPDFEGLnwKQALESDKLPKGEQ--AQEEQTSSS 2598
Cdd:TIGR02169  385 DELKDYREKLEKLK--REINELKRELDRLQEELQRLSEELADLNAAIAGIEAK--INELEEEKEDKALEikKQEWKLEQL 460
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1622916950 2599 KGGKQKVKEKTDQVVETQKD--KRRVALNRKVISGE 2632
Cdd:TIGR02169  461 AADLSKYEQELYDLKEEYDRveKELSKLQRELAEAE 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2259-2403 1.81e-05

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 1.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2259 NMAQDYAAMKAQEKAKKEQEE--RKHKEALEKEKERLQNmdeEEYDALTEEEKLTfnqgiqqalRERKKREQErlAKEMQ 2336
Cdd:TIGR02169  837 ELQEQRIDLKEQIKSIEKEIEnlNGKKEELEEELEELEA---ALRDLESRLGDLK---------KERDELEAQ--LRELE 902
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2337 EKKLQQELERQKEEDELKR-KVKKG-KQGPIKE-EPPPKKSQASNKQVPPFTKVDVKMETIERKISVREP 2403
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSElKAKLEaLEEELSEiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEP 972
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2265-2367 1.82e-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: 50.30  E-value: 1.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2265 AAMKAQEKAKKEQEERKHKEALEKEKERLQNM----DEEEYDALTEEEKLTFNQGIQQALRERKKREQER--LAKEMQEK 2338
Cdd:pfam13868  223 EREEAEKKARQRQELQQAREEQIELKERRLAEeaerEEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRreLEKQIEER 302
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622916950 2339 KLQQELER----------QKEEDELKRKVKKGKQGPIKE 2367
Cdd:pfam13868  303 EEQRAAEReeeleegerlREEEAERRERIEEERQKKLKE 341
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
2269-2642 1.94e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 50.81  E-value: 1.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2269 AQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKltfnqgiQQALRERKKREQERLAK----EMQEKKLQQEL 2344
Cdd:COG3064      1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEE-------ERLAELEAKRQAEEEAReakaEAEQRAAELAA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2345 ERQKEEDELKRKVKKGKQgPIKEEPPPKKSQASNKQVPpftkvdvkmetiERKISV--REPTVSEKEELNKKKRNmgdvs 2422
Cdd:COG3064     74 EAAKKLAEAEKAAAEAEK-KAAAEKAKAAKEAEAAAAA------------EKAAAAaeKEKAEEAKRKAEEEAKR----- 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2423 mlglplvQDQEDSEGDVSKDPDKQLAQRFKAYELTLKDVQNILMYWDRKQGVQLPPAGMEEAAHEPDDQRQVPSGGRRGR 2502
Cdd:COG3064    136 -------KAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAA 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2503 KDRERERLEKERTEKERLEREKAERERLEKLRALEERSDWEGEGEEDHEGKKEKDLGVPFLNIQTPDFEGLNWKQALESD 2582
Cdd:COG3064    209 AAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGL 288
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2583 KLPKGEQAQEEQTSSSKGGKQKVKEKTDQVVETQKDKRRVALNRKVISGEPAGTISQLSD 2642
Cdd:COG3064    289 AAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGA 348
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2265-2356 2.33e-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: 49.92  E-value: 2.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2265 AAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYdaltEEEKLTFNQGIQQALRERKKREQERLAKEMQEKKLQQE- 2343
Cdd:pfam13868  190 RAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREE----AEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFEr 265
                           90
                   ....*....|....
gi 1622916950 2344 -LERQKEEDELKRK 2356
Cdd:pfam13868  266 mLRKQAEDEEIEQE 279
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
2265-2494 2.58e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 50.42  E-value: 2.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2265 AAMKAQE------KAKKEQEERKHKEALEkEKERLQNMDEEEYDALTEEEKLTfnQGIQQALRERKKREQERLAKEMQEK 2338
Cdd:COG3064     35 AKEEAEEerlaelEAKRQAEEEAREAKAE-AEQRAAELAAEAAKKLAEAEKAA--AEAEKKAAAEKAKAAKEAEAAAAAE 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2339 KLQQELERQKEEDElKRKVKKGKQGPIKEEPPPKKSQASNKQVPPFTKVDVKMETIERKISVREPTVSEKEELNKKKRNM 2418
Cdd:COG3064    112 KAAAAAEKEKAEEA-KRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAV 190
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916950 2419 GDVSMLGLPLVQDQEDSEGDVSKDPDKQLAQRFKAYELTLKDVQNILMYWDRKQGVQLPPAGMEEAAHEPDDQRQV 2494
Cdd:COG3064    191 EAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAA 266
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
2270-2358 2.75e-05

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 50.04  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2270 QEKAKKEQEERKHKEALEKEKERLQNMDEEEYDAltEEEKLtfNQgiQQALRE-----RKKREQERLakEMQEKKLQQEL 2344
Cdd:pfam15558   85 REKQVIEKESRWREQAEDQENQRQEKLERARQEA--EQRKQ--CQ--EQRLKEkeeelQALREQNSL--QLQERLEEACH 156
                           90
                   ....*....|....
gi 1622916950 2345 ERQKEEDELKRKVK 2358
Cdd:pfam15558  157 KRQLKEREEQKKVQ 170
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
2255-2359 2.79e-05

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 47.91  E-value: 2.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2255 IYVLNMA---QDYAAMK-AQEKAKKEQEERKhkEALEKEKERLQNMdEEEYDA----LTEEEkltfnqgiqqalreRKKR 2326
Cdd:COG2825     26 IGVVDVQrilQESPEGKaAQKKLEKEFKKRQ--AELQKLEKELQAL-QEKLQKeaatLSEEE--------------RQKK 88
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622916950 2327 EQE--RLAKEMQEK--KLQQEL--ERQKEEDELKRKVKK 2359
Cdd:COG2825     89 ERElqKKQQELQRKqqEAQQDLqkRQQELLQPILEKIQK 127
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
2261-2353 2.99e-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: 49.84  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2261 AQDYAAMKAQEKAKKEQE-ERKHKEALEKEKERLQNMDEEEYDALTEEE---KLTFNQGIQQALRERKKREQERLAKEMQ 2336
Cdd:TIGR02794  136 AEAEAERKAKEEAAKQAEeEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEaeaKAKAEEAKAKAEAAKAKAAAEAAAKAEA 215
                           90
                   ....*....|....*..
gi 1622916950 2337 EKKLQQELERQKEEDEL 2353
Cdd:TIGR02794  216 EAAAAAAAEAERKADEA 232
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
2268-2351 3.22e-05

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 47.10  E-value: 3.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQE--KAKKEQ-EERKHKEALEKEKERLQNMDEE--------------EYDALTEEEKLTFNQGIQQALRERKKREQEr 2330
Cdd:pfam15236   53 KALEhqNAIKKQlEEKERQKKLEEERRRQEEQEEEerlrrereeeqkqfEEERRKQKEKEEAMTRKTQALLQAMQKAQE- 131
                           90       100
                   ....*....|....*....|.
gi 1622916950 2331 LAKEMQEKKLQQELErQKEED 2351
Cdd:pfam15236  132 LAQRLKQEQRIRELA-EKGHD 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2269-2356 3.40e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2269 AQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQALRERKKREQERLAKEMQEKKLQQELERQK 2348
Cdd:COG1196    259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338

                   ....*...
gi 1622916950 2349 EEDELKRK 2356
Cdd:COG1196    339 LEELEEEL 346
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
2269-2356 5.11e-05

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: 49.56  E-value: 5.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2269 AQEKAKKEQEERkHKEALEKEKERLQnmdEEEYDALTEEEKltfnqgiQQALRERKKREQERLAKEMQEKKLqqELERQK 2348
Cdd:pfam15709  417 AQERARQQQEEF-RRKLQELQRKKQQ---EEAERAEAEKQR-------QKELEMQLAEEQKRLMEMAEEERL--EYQRQK 483

                   ....*...
gi 1622916950 2349 EEDELKRK 2356
Cdd:pfam15709  484 QEAEEKAR 491
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
2261-2639 6.72e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 49.27  E-value: 6.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2261 AQDYAAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLTF---NQGIQQALRE-----RKKREQERLA 2332
Cdd:COG3064     64 AEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAaaeKEKAEEAKRKaeeeaKRKAEEERKA 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2333 KEmQEKKLQQELERQKEEDELKRKVKKGKQGPIKEEPPPKKSQASNKQVPPFTKVDVKMETIERKIsvREPTVSEKEELN 2412
Cdd:COG3064    144 AE-AEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAA--AAAADAALLALA 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2413 KKKRNMGDVSMLGLPLVQDQEDSEGDVSKDPDKQLAQRFKAYELTLKDVQNILMYWDRKQGVQLPPAGMEEAAHEPDDQR 2492
Cdd:COG3064    221 VAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDS 300
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2493 QVPSGGRRGRKDRERERLEKERTEKERLEREKAERERLEKLRALEERSDWEGEGEEDHEGKKEKDLGVPFLNIQTP---- 2568
Cdd:COG3064    301 AALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLlgkl 380
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622916950 2569 DFEGLNWKQALESDKLPKGEQAQEEQTSSSKGGKQKVKEKTDQVVETQKDKRRVALNRKVISGEPAGTISQ 2639
Cdd:COG3064    381 ADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGI 451
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
2267-2379 8.13e-05

Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and tropomyosin binding (TnT). this Pfam contains members of the TnT subunit. Troponin is a complex of three proteins, Ca2+ binding (TnC), inhibitory (TnI), and tropomyosin binding (TnT). The troponin complex regulates Ca++ induced muscle contraction. This family includes troponin T and troponin I. Troponin I binds to actin and troponin T binds to tropomyosin.


Pssm-ID: 460018 [Multi-domain]  Cd Length: 132  Bit Score: 45.63  E-value: 8.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2267 MKAQEKAKKEQEERkhkealEKEKERlqnmdeeeydALTEE-EKLTFNQGIQQALRERKKREQERLAKEMQEK--KLQQE 2343
Cdd:pfam00992   10 QKAAEELEFEQEKK------EEEKLR----------YLAERiPPLRLRGLSAEQLQELCEELHERIDKLEEERydIEEKV 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1622916950 2344 LERQKEEDELKRKV--KKGKQGpikeePPP--KKSQASNK 2379
Cdd:pfam00992   74 AKKDKEINDLKKKVndLRGKFK-----KPLlkKVRKTADA 108
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
2265-2359 9.85e-05

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 48.11  E-value: 9.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2265 AAMKAQEKAKKEQ---------EERKHkEALEKEKERlQNMDEEEYDALTEEEKLTFNQGIQQALRERKKRE-QERLAKE 2334
Cdd:pfam15558  154 ACHKRQLKEREEQkkvqennlsELLNH-QARKVLVDC-QAKAEELLRRLSLEQSLQRSQENYEQLVEERHRElREKAQKE 231
                           90       100
                   ....*....|....*....|....*
gi 1622916950 2335 mqEKKLQQELERQKEEDELKRKVKK 2359
Cdd:pfam15558  232 --EEQFQRAKWRAEEKEEERQEHKE 254
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
2263-2362 1.01e-04

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 48.60  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2263 DYAAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALteEEKLTFNqgiQQALRERKKREQERLAKEMqEKKLQQ 2342
Cdd:pfam09731  295 EIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARL--EEVRAAD---EAQLRLEFEREREEIRESY-EEKLRT 368
                           90       100
                   ....*....|....*....|..
gi 1622916950 2343 ELERQKE--EDELKRKVKKGKQ 2362
Cdd:pfam09731  369 ELERQAEahEEHLKDVLVEQEI 390
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
2260-2362 1.07e-04

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: 47.57  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2260 MAQDYAAMKAQEKAKKEQEERkhkEALEKEKERLQNMdEEEYDALTEEEKLTFNQGIQQaLRERKKREQERLAKEmQEKK 2339
Cdd:cd16269    187 LQADQALTEKEKEIEAERAKA---EAAEQERKLLEEQ-QRELEQKLEDQERSYEEHLRQ-LKEKMEEERENLLKE-QERA 260
                           90       100
                   ....*....|....*....|....*
gi 1622916950 2340 LQQELERQKE--EDELKRKVKKGKQ 2362
Cdd:cd16269    261 LESKLKEQEAllEEGFKEQAELLQE 285
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
2258-2368 1.12e-04

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 45.43  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2258 LNMAQDYAAMKAQEKAKKEQEER--KHKEALEKEKERLQnmdEEEYDALTEEEKLTFNQGIQQALR--------ERKKRE 2327
Cdd:pfam15346    5 SKLLEEETARRVEEAVAKRVEEEleKRKDEIEAEVERRV---EEARKIMEKQVLEELEREREAELEeerrkeeeERKKRE 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622916950 2328 Q-ERLAKEMQEK------KLQQE----LERQKEEDELKRKVKKGKQGPIKEE 2368
Cdd:pfam15346   82 ElERILEENNRKieeaqrKEAEErlamLEEQRRMKEERQRREKEEEEREKRE 133
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
2262-2337 1.22e-04

G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 47.22  E-value: 1.22e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916950 2262 QDYAAMKAQEKAKKEQEERKHKE--ALEKEKERLQNMDeEEYDALTEEEKLTFNQgIQQALRERKKReqERLAKEMQE 2337
Cdd:pfam15991   27 QEQEAKMEEERLRREREEREKEDrmTLEETKEQILKLE-KKLADLKEEKHQLFLQ-LKKVLHEDETR--KRQLKEQSE 100
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
2265-2349 1.98e-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: 44.21  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2265 AAMKAQEKAKKEQE-ERKHKEALEKEKERLQNMDEEEYDALTEEekltfnqgiqqalRERKKREQERLAKEMQEKKLQQE 2343
Cdd:pfam04696   24 EESKQKEKEERRAEiEKRLEEKAKQEKEELEERKREEREELFEE-------------RRAEQIELRALEEKLELKELMET 90

                   ....*.
gi 1622916950 2344 LERQKE 2349
Cdd:pfam04696   91 WHENLK 96
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
2260-2361 2.42e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.86  E-value: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2260 MAQDYAAMKAQEKAKKE--QEERKHK-------EALEKEKERLQNMDEEEYDALTEEEKLTfnQGIQQALRERKKR-EQE 2329
Cdd:pfam01576  459 LSKDVSSLESQLQDTQEllQEETRQKlnlstrlRQLEDERNSLQEQLEEEEEAKRNVERQL--STLQAQLSDMKKKlEED 536
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622916950 2330 RLAKEMQE---KKLQQELE----RQKEEDELKRKVKKGK 2361
Cdd:pfam01576  537 AGTLEALEegkKRLQRELEaltqQLEEKAAAYDKLEKTK 575
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
2256-2359 2.60e-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: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 44.10  E-value: 2.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2256 YVLNMAQDYAAmkAQEKAKKEQEERKhkEALEKEKERLQNMdeeeydalteEEKLTFNQGIQQALRERKKREQERLAKEM 2335
Cdd:pfam03938    9 KILEESPEGKA--AQAQLEKKFKKRQ--AELEAKQKELQKL----------YEELQKDGALLEEEREEKEQELQKKEQEL 74
                           90       100
                   ....*....|....*....|....*...
gi 1622916950 2336 QE--KKLQQELERQKEE--DELKRKVKK 2359
Cdd:pfam03938   75 QQlqQKAQQELQKKQQEllQPIQDKINK 102
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
2267-2380 2.77e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 46.72  E-value: 2.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2267 MKAQEKAK-KEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQALRERKKREQERLAKEMQEKKLQQELE 2345
Cdd:PRK09510   103 LKQLEKERlAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1622916950 2346 RQKE-EDELKRKVKKGKQGPIKEEPPPKKSQASNKQ 2380
Cdd:PRK09510   183 AKKKaEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKK 218
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
2270-2422 3.53e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 47.12  E-value: 3.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2270 QEKAKKEQEERKHKEA-LEKEKERLQNMDEEEYD---AL-TEEEKLTFNQGIQQALRERKKREQERLAKEMQEkkLQQEL 2344
Cdd:pfam10174  400 QKKIENLQEQLRDKDKqLAGLKERVKSLQTDSSNtdtALtTLEEALSEKERIIERLKEQREREDRERLEELES--LKKEN 477
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916950 2345 ERQKEEDELKRKVKKGKQGPIKEEPPPKKSQASNKqvppfTKVDVKMETIERKISVREPTVSEKEELNKKKRNMGDVS 2422
Cdd:pfam10174  478 KDLKEKVSALQPELTEKESSLIDLKEHASSLASSG-----LKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAV 550
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2265-2356 3.54e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 3.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2265 AAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQALRERKKR---EQERLAKEMQEKKLQ 2341
Cdd:COG1196    357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERleeELEELEEALAELEEE 436
                           90
                   ....*....|....*
gi 1622916950 2342 QELERQKEEDELKRK 2356
Cdd:COG1196    437 EEEEEEALEEAAEEE 451
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
2266-2359 3.60e-04

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: 3.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2266 AMKAQEKAKKEQE-ERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQALRERKKREQERLAKEMQEKKLQQEl 2344
Cdd:COG2268    219 ANREAEEAELEQErEIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEK- 297
                           90
                   ....*....|....*
gi 1622916950 2345 ERQKEEDELKRKVKK 2359
Cdd:COG2268    298 EAEREEAELEADVRK 312
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
2265-2371 3.62e-04

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 46.52  E-value: 3.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2265 AAMKAQEKAKKEQEERK-----HKEALEKEKERLQNMDEEeydaltEEEKLtfnqgiQQALRERK-KREQERLAKEMQEK 2338
Cdd:pfam07767  224 KIAESAATAEAREEKRKtkaqrNKEKRRKEEEREAKEEKA------LKKKL------AQLERLKEiAKEIAEKEKEREEK 291
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1622916950 2339 KLQQELERQKEEDELKrKVKKGKQGPIKEEPPP 2371
Cdd:pfam07767  292 AEARKREKRKKKKEEK-KLRPRKLGKHKVPEPD 323
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
2262-2380 3.72e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 46.34  E-value: 3.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2262 QDYAAMKAQEKAKK--EQEERKHKEALEKEKERLQNmDEEEYDALTEEEKltfnQGIQQAlreRKKREQERLAKEmqEKK 2339
Cdd:PRK09510    70 QQKSAKRAEEQRKKkeQQQAEELQQKQAAEQERLKQ-LEKERLAAQEQKK----QAEEAA---KQAALKQKQAEE--AAA 139
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1622916950 2340 LQQELERQKEEDELKRKVKKGKQGpikEEPPPKKSQASNKQ 2380
Cdd:PRK09510   140 KAAAAAKAKAEAEAKRAAAAAKKA---AAEAKKKAEAEAAK 177
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2258-2651 3.74e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 47.27  E-value: 3.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2258 LNMAQDYAAMKAQEKAKKEQEERKHKEALEKEKErlqnmDEEEYDALTEEEKltfnqgiqQALRERKKREQERLAKEMQE 2337
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEK-----EELEKQELKLLKD--------ELELKKSEDLLKETQLVKLQ 483
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2338 KKLQQELERQKEEDEL-----KRKVKKGKQGPIKEEPPPKKSQASNKQVPPFTKVdvkmETIERKISVREPTVSEKEELN 2412
Cdd:pfam02463  484 EQLELLLSRQKLEERSqkeskARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAV----ENYKVAISTAVIVEVSATADE 559
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2413 KKKRNMGDVSMLGLPLVQDQEDSEGDVSKDPDKQLAQRFKAYELTLKDVQNILMYWDRKQGVQLPPAGMEEAAHEPDDQR 2492
Cdd:pfam02463  560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKE 639
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2493 QVPSGGRRGRKDRERERLEKERTEKERLEREKAERERLEKLRALEERSDWEGEGEEDHEGKKEKdlgvpflNIQTPDFEG 2572
Cdd:pfam02463  640 SAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK-------KEQREKEEL 712
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916950 2573 LNWKQALESDKLPKGEQAQEEQTSSSKGGKQKVKEKTDQVVETQKDKRRVALNRKVISGEPAGTISQLSDTDLNNFNGQ 2651
Cdd:pfam02463  713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
2276-2356 5.54e-04

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 43.63  E-value: 5.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2276 EQEERKHKEALEKEKERLQNMDEEEYDALTEEEKltfnqgiqqaLRERKKREQERLA--KEMQEKKLQQELERQKEEDEL 2353
Cdd:pfam15236   45 EERERKRQKALEHQNAIKKQLEEKERQKKLEEER----------RRQEEQEEEERLRreREEEQKQFEEERRKQKEKEEA 114

                   ...
gi 1622916950 2354 KRK 2356
Cdd:pfam15236  115 MTR 117
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2269-2356 5.58e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 5.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2269 AQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLtfNQGIQQALRERKKREQERLAKEMQEKKLQQELERQK 2348
Cdd:COG1196    315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                   ....*...
gi 1622916950 2349 EEDELKRK 2356
Cdd:COG1196    393 RAAAELAA 400
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
2275-2356 6.29e-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: 42.60  E-value: 6.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2275 KEQEERKHKEaLEkekERLQNMdEEEY----DALTE--------EEKLTFNQgiQQALR-ERKKREQERLAKEMQEKKLQ 2341
Cdd:pfam20492    1 REEAEREKQE-LE---ERLKQY-EEETkkaqEELEEseetaeelEEERRQAE--EEAERlEQKRQEAEEEKERLEESAEM 73
                           90
                   ....*....|....*
gi 1622916950 2342 QELERQKEEDELKRK 2356
Cdd:pfam20492   74 EAEEKEQLEAELAEA 88
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
2268-2377 7.36e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 45.41  E-value: 7.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEERK-HKEALEKEKER-LQNmdEEEYDALTEEEKLtfnQGIQQALRERKKREQERLAKEMQEKKLQQE-- 2343
Cdd:pfam15558  237 RAKWRAEEKEEERQeHKEALAELADRkIQQ--ARQVAHKTVQDKA---QRARELNLEREKNHHILKLKVEKEEKCHREgi 311
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1622916950 2344 LERQKEEDELKRKVKKGKQgPIKEEpPPKKSQAS 2377
Cdd:pfam15558  312 KEAIKKKEQRSEQISREKE-ATLEE-ARKTARAS 343
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
2268-2363 7.46e-04

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 43.11  E-value: 7.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEERKHKEALEKEKERLQNMDEEEyDALTEEEkltfnqgiqqALRERKKREQeRLAKEMQEKklqqeLERQ 2347
Cdd:pfam05672   74 EEERQRKAEEEAEEREQREQEEQERLQKQKEEA-EAKAREE----------AERQRQEREK-IMQQEEQER-----LERK 136
                           90
                   ....*....|....*.
gi 1622916950 2348 KEEDELKRKVKKGKQG 2363
Cdd:pfam05672  137 KRIEEIMKRTRKSDQA 152
ALMS_motif pfam15309
ALMS motif; This domain is found at the C-terminus of Alstrom syndrome protein 1 (ALMS1), ...
2279-2357 9.52e-04

ALMS motif; This domain is found at the C-terminus of Alstrom syndrome protein 1 (ALMS1), KIAA1731 and C10orf90.


Pssm-ID: 464634  Cd Length: 131  Bit Score: 42.36  E-value: 9.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2279 ERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQ-----ALRERKKREQERlaKEMQE--KKLQQEL-ERQKEE 2350
Cdd:pfam15309   23 ERLKRLELLVEERKLQEVLQRERERLFNKPIPRTNKRQQTvplpdNLFKPRRRAISK--KEMIArsKRIYEQLpEVKKKK 100

                   ....*..
gi 1622916950 2351 DELKRKV 2357
Cdd:pfam15309  101 EEEKRKA 107
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2260-2542 9.70e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.28  E-value: 9.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2260 MAQDYAAMKAQEKAKKEQEERKhKEALEKEKERLQNMDEEeydaLTEEekltfNQGIQQALRERKKREQERLAKEMQEKK 2339
Cdd:COG4372     43 LQEELEQLREELEQAREELEQL-EEELEQARSELEQLEEE----LEEL-----NEQLQAAQAELAQAQEELESLQEEAEE 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2340 LQQELER-QKEEDELKRKVKKGKQgpikeepppkksqasnkqvppftkvdvKMETIERKISVREPTVSE-KEELNKKKRN 2417
Cdd:COG4372    113 LQEELEElQKERQDLEQQRKQLEA---------------------------QIAELQSEIAEREEELKElEEQLESLQEE 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2418 MGDVSmlglplVQDQEDSEGDVSKDPDKQL--AQRFKAYELTLKDVQNILMYWDRKQGVQLPPAGMEEAAHEPDDQRQVP 2495
Cdd:COG4372    166 LAALE------QELQALSEAEAEQALDELLkeANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1622916950 2496 SGGRRGRKDRERERLEKERTEKERLEREKAERERLEKLRALEERSDW 2542
Cdd:COG4372    240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
2275-2362 1.14e-03

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: 43.49  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2275 KEQEERKHKEALEKEKERLQNMDEEEydaltEEEkltfnqgiqqalrERKKREQERLAKEMQEKKLQQELERQKEEDELK 2354
Cdd:pfam09756    1 KKLGAKKRAKLELKEAKRQQREAEEE-----ERE-------------EREKLEEKREEEYKEREEREEEAEKEKEEEERK 62

                   ....*...
gi 1622916950 2355 RKVKKGKQ 2362
Cdd:pfam09756   63 QEEEQERK 70
Utp11 pfam03998
Utp11 protein; This protein is found to be part of a large ribonucleoprotein complex ...
2268-2363 1.14e-03

Utp11 protein; This protein is found to be part of a large ribonucleoprotein complex containing the U3 snoRNA. Depletion of the Utp proteins impedes production of the 18S rRNA, indicating that they are part of the active pre-rRNA processing complex. This large RNP complex has been termed the small subunit (SSU) processome.


Pssm-ID: 461122 [Multi-domain]  Cd Length: 241  Bit Score: 44.15  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEERKHKEALEKEKERLQNmdeeeyDALTEEEKLTFNQGIQQALRERKKRE-QERLAKEMQEKKLQQELER 2346
Cdd:pfam03998  136 EEVKNFDPAEYFDTDPELLDRRENRLKK------EQLESNSLTAATLKKLDKKKEKLYKElKARLEREKELKKAEQKLEL 209
                           90
                   ....*....|....*....
gi 1622916950 2347 QKE--EDELKRKVKKGKQG 2363
Cdd:pfam03998  210 QRAlmKKGAKKKVKGGTTK 228
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2269-2359 1.18e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.15  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2269 AQEKAKKEQEE----RKHKE--ALEKE----KERLQNMDEEEYDALTEEEKLtfnQGIQQALRERKKREQERLAKEMQEk 2338
Cdd:COG1579     71 VEARIKKYEEQlgnvRNNKEyeALQKEieslKRRISDLEDEILELMERIEEL---EEELAELEAELAELEAELEEKKAE- 146
                           90       100
                   ....*....|....*....|..
gi 1622916950 2339 kLQQELER-QKEEDELKRKVKK 2359
Cdd:COG1579    147 -LDEELAElEAELEELEAEREE 167
eIF3_subunit pfam08597
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of ...
2265-2335 1.22e-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: 43.82  E-value: 1.22e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622916950 2265 AAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLtfnqgiqqALRERKKREQE----RLAKEM 2335
Cdd:pfam08597   49 KAAKAAAAKAKKKKKSKKQKIAEKEAERKAEEEAEEEEELTPEDEA--------ARKLRLRKAEEesdlENAADL 115
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
2264-2353 1.25e-03

Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.


Pssm-ID: 399954 [Multi-domain]  Cd Length: 148  Bit Score: 42.39  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2264 YAAMKAQEKAKKEQEERKHKEAL--EKEKERLQNMDEEEYDALTEEEKLTFnqgIQQALRERKkREQERLA--KEMQEKK 2339
Cdd:pfam07321   55 YAEIQGKLVLLKELEKVKQQVALlrENEADLEKQVAEARQQLEAEREALRQ---ARQALAEAR-RAVEKFAelVRLVQAE 130
                           90
                   ....*....|....
gi 1622916950 2340 LQQELERQkEEDEL 2353
Cdd:pfam07321  131 ELRQQERQ-EEQEL 143
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
2256-2359 1.26e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 43.66  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2256 YVLNMAQDYAAMK---AQEKAKKEQEERKHKEALEKEKERlqnmdeeeydalteEEKltfnqgIQQALrerkKREQERLA 2332
Cdd:COG1842     31 AIRDMEEDLVEARqalAQVIANQKRLERQLEELEAEAEKW--------------EEK------ARLAL----EKGREDLA 86
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1622916950 2333 KEMQEKK---------LQQELERQKEE-DELKRKVKK 2359
Cdd:COG1842     87 REALERKaeleaqaeaLEAQLAQLEEQvEKLKEALRQ 123
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2268-2355 1.30e-03

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: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEERKHKEALEK----EKERLQNMDEEEYDALTEEEKLTFNQGIQQALRERKKREQERLAKEMQEKKLQQE 2343
Cdd:COG1196    282 ELEEAQAEEYELLAELARLEQdiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
                           90
                   ....*....|..
gi 1622916950 2344 LERQKEEDELKR 2355
Cdd:COG1196    362 EAEEALLEAEAE 373
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2258-2350 1.36e-03

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: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2258 LNMAQDYAAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEydALTEEEKLTFNQGIQQALRERKKREQERLAKEMQE 2337
Cdd:COG1196    283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL--AELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
                           90
                   ....*....|...
gi 1622916950 2338 KKLQQELERQKEE 2350
Cdd:COG1196    361 AEAEEALLEAEAE 373
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2262-2414 1.48e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 45.35  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2262 QDYAAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQAL-------RERKKREQERLAKE 2334
Cdd:pfam02463  764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLlieqeekIKEEELEELALELK 843
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2335 M---QEKKLQQELERQKEE-------DELKRKVKKGKQGPIKEEPPPKKSQASNKQVPPFTKVDVKMETIERKISVREPT 2404
Cdd:pfam02463  844 EeqkLEKLAEEELERLEEEitkeellQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERI 923
                          170
                   ....*....|
gi 1622916950 2405 VSEKEELNKK 2414
Cdd:pfam02463  924 KEEAEILLKY 933
Saf4_Yju2 pfam04502
Saf4/Yju2 protein; This is a family of eukaryotic proteins that includes CCDC130 and CCDC94 ...
2271-2449 1.72e-03

Saf4/Yju2 protein; This is a family of eukaryotic proteins that includes CCDC130 and CCDC94 from humans, Saf4 from fission yeasts and Yju2 from budding yeasts. Saf4 (also known as cwc16) is involved in mRNA splicing where it associates with cdc5 and the other cwf proteins as part of the spliceosome. Yju2 is a splicing factor that is associated with the Prp 19-associated complex and acts after Prp2 in promoting the first catalytic reaction of pre-mRNA splicing.


Pssm-ID: 461333 [Multi-domain]  Cd Length: 328  Bit Score: 44.27  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2271 EKAKKEQEERKHKEA------LEK-EKERLQNMD-----EEEYDALTEEEKLTFNQGIQQALR---ERKKREQERLAKE- 2334
Cdd:pfam04502  113 EEEKREEKEREEEEAndamkkLEKrTKDSKREMEalerlEELQELNQRQWKDDYDANLKLRREfreEKKEREEEEEDEEa 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2335 MQEKKLQQELERQKEEDELKRK---VKKGKQGPIKEEPPPKKSQASNKQVPPFTKVDVKMETIERKISVREPTVSEKEEL 2411
Cdd:pfam04502  193 LKEKMSLEIIKLLPEDEEDDRRaalVEFGSRPLFGDSSPPAKTESPTDSLTSEISASSKRESLKKSLGKLTRKAADPLLL 272
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1622916950 2412 N-KKKRNMGDVSMLGLPLVQDQEDSEGDVSKDPDKQLAQ 2449
Cdd:pfam04502  273 GvKRKKAATEEPSTPSSETSTESSKTSTPSSAQVSSSSP 311
RRP36 pfam06102
rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.
2283-2362 1.75e-03

rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.


Pssm-ID: 461829 [Multi-domain]  Cd Length: 158  Bit Score: 42.16  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2283 KEALEKEKERLQNMDEEEYDaltEEEKltfnQGIQQALRERKKREQERLAKEMQEKKLQQELERQKEedelkrKVKKGKQ 2362
Cdd:pfam06102   55 DEYRKKEIEELKKQLKKTKD---PEEK----EELKRTLQSMESRLKAKKRKDREREVLKEHKKEEKE------KVKQGKK 121
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
2266-2359 1.77e-03

Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar proteins; mS26, also known as mitochondrial 37S ribosomal protein PET12, is a component of the mitochondrial small ribosomal subunit (mt-SSU) of Saccharomyces cerevisiae mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The family also includes a group of uncharacterized proteins from pezizomycotina, which show high sequence similarity with mS26.


Pssm-ID: 467916 [Multi-domain]  Cd Length: 179  Bit Score: 42.54  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2266 AMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEydalTEEEKLTfNQGIQQALRERKKR-----EQERLAKEMQEKKL 2340
Cdd:cd23703     66 GLRELEERKLKTEELRAKRSERKQAERERALNAPE----REDERLT-LPTIESALLGPLMRvrtdpEREERAAKRRANRE 140
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1622916950 2341 QQELERQKE------------------EDELKRKVKK 2359
Cdd:cd23703    141 AKELAKKEAradalhelymnarnfivtEEQLDAAIEE 177
Cgr1 pfam03879
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ...
2274-2361 1.78e-03

Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA processing.


Pssm-ID: 427562 [Multi-domain]  Cd Length: 107  Bit Score: 41.07  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2274 KKEQEERKHKEALekeKERLQNMDEEeydalTEEEKltfNQGIQqALRERKKR--EQERLAKE---MQEKKLQQelerqk 2348
Cdd:pfam03879   33 EKRQEKRLELKAI---KAKEKELKDE-----KEAER---QRRIQ-AIKERREAkeEKERYEELaakMHAKKVER------ 94
                           90
                   ....*....|...
gi 1622916950 2349 eedeLKRKVKKGK 2361
Cdd:pfam03879   95 ----LKRKEKRNK 103
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2269-2356 1.98e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2269 AQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLtfNQGIQQALRERKKREQERLAKEMQEKKLQQELER-- 2346
Cdd:COG1196    329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA--EAELAEAEEELEELAEELLEALRAAAELAAQLEEle 406
                           90
                   ....*....|
gi 1622916950 2347 QKEEDELKRK 2356
Cdd:COG1196    407 EAEEALLERL 416
Motile_Sperm pfam00635
MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These ...
203-269 2.13e-03

MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These proteins oligomerise to form filaments. This family contains many other proteins.


Pssm-ID: 459882  Cd Length: 109  Bit Score: 40.81  E-value: 2.13e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916950  203 PDKLNFSTCPVKYSTQKILLVrNIGNKIAVFHIKTCRP--FSVEPAVGTLNVGESMQLEVEFEPQSVGD 269
Cdd:pfam00635    7 PDLIFFAAPGNKQGTSTLTLK-NTSDKRVAFKVKTTNPkkYRVRPNYGIIKPGESVTITITRQPFDEEP 74
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
2266-2350 2.48e-03

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: 42.33  E-value: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2266 AMKAQEKAKK---------EQEERKHKEAlEKEKERLQNMDEEEydalteeekltfnqgiqqaLRERKKREQERLAKEMQ 2336
Cdd:pfam09756    8 RAKLELKEAKrqqreaeeeEREEREKLEE-KREEEYKEREEREE-------------------EAEKEKEEEERKQEEEQ 67
                           90
                   ....*....|....
gi 1622916950 2337 EKKLQQELERQKEE 2350
Cdd:pfam09756   68 ERKEQEEYEKLKSQ 81
cdk7 TIGR00570
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions ...
2269-2409 2.49e-03

CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions are known are cyclin dependent protein kinases that are components of TFIIH, a complex that is involved in nucleotide excision repair and transcription initiation. Also known as MAT1 (menage a trois 1). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129661 [Multi-domain]  Cd Length: 309  Bit Score: 43.64  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2269 AQEKAKKEQEERKHKEALEKEKERlQNMDEEEYDALTEEEKltfNQGIQQALRERKKREQERLAKEMQEKKLQQELERQK 2348
Cdd:TIGR00570  116 ENTKKKIETYQKENKDVIQKNKEK-STREQEELEEALEFEK---EEEEQRRLLLQKEEEEQQMNKRKNKQALLDELETST 191
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916950 2349 EE-----DELKRKVKKGKQgPIKEEPPPKKSQASNKQVPPFTKVDVKMETIERKISVREPTVSEKE 2409
Cdd:TIGR00570  192 LPaaeliAQHKKNSVKLEM-QVEKPKPEKPNTFSTGIKMGYQISLVPVQKSEEALYPYQPLNIETE 256
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2258-2417 2.55e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2258 LNMAQDYAAMKAQEKAKKEQEE-RKHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQALRERKKREQERLAKEMQ 2336
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEyAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2337 EKKLQQEL----ERQKEEDELKRKVKKGKQGP--IKEEPPPKKSQASNKQVPPFTKVDVKMETIERKISVREptvSEKEE 2410
Cdd:COG4717    148 LEELEERLeelrELEEELEELEAELAELQEELeeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ---EELEE 224

                   ....*..
gi 1622916950 2411 LNKKKRN 2417
Cdd:COG4717    225 LEEELEQ 231
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
2267-2359 2.60e-03

YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.


Pssm-ID: 435583 [Multi-domain]  Cd Length: 160  Bit Score: 41.74  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2267 MKAQEKAKKEQEE--RKHKEALEKEKERLQNMdEEEYDALTEEEKLTFNQ------------GIQQAlRERKKREQERLA 2332
Cdd:pfam16789    9 LDIKKKRVEEAEKvvKDKKRALEKEKEKLAEL-EAERDKVRKHKKAKMQQlrdemdrgttsdKILQM-KRYIKVVKERLK 86
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622916950 2333 KEmqEKKLQ----------QELERQKEEDELKRK-VKK 2359
Cdd:pfam16789   87 QE--EKKVQdqkeqvrtaaRNLEIAREELKKKRQeVEK 122
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
2266-2358 2.65e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 43.51  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2266 AMKAQEKAKKEQEE-RKHKEALEKEKERLQNmDEEEYDA-LTEEEKLTFNQGIQQaLRERKKREQERLAKEMQEK--KLQ 2341
Cdd:cd22656    130 AKKYQDKAAKVVDKlTDFENQTEKDQTALET-LEKALKDlLTDEGGAIARKEIKD-LQKELEKLNEEYAAKLKAKidELK 207
                           90
                   ....*....|....*..
gi 1622916950 2342 QELerQKEEDELKRKVK 2358
Cdd:cd22656    208 ALI--ADDEAKLAAALR 222
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2265-2366 2.69e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2265 AAMKAQEKAKKEQEE-RKHKEALEKEKERLQNMDEEEYDALTE-EEKLTFNQGIQQALRERKKREQERLAK-EMQEKKLQ 2341
Cdd:COG4942     17 AQADAAAEAEAELEQlQQEIAELEKELAALKKEEKALLKQLAAlERRIAALARRIRALEQELAALEAELAElEKEIAELR 96
                           90       100
                   ....*....|....*....|....*..
gi 1622916950 2342 QELERQKEE--DELKRKVKKGKQGPIK 2366
Cdd:COG4942     97 AELEAQKEElaELLRALYRLGRQPPLA 123
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2258-2460 2.70e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.29  E-value: 2.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2258 LNMAQDYAamKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFN-QGIQQALRERKKREQERLA-KEM 2335
Cdd:TIGR02169  667 LFSRSEPA--ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEiEKEIEQLEQEEEKLKERLEeLEE 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2336 QEKKLQQELERQKEE--------DELKRKVKKGKQ--GPIKEEPPPKKSQASNKQVPPFTKVDVKMETIERKISVREPTV 2405
Cdd:TIGR02169  745 DLSSLEQEIENVKSElkeleariEELEEDLHKLEEalNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916950 2406 SEKEELNKKKRNMGDVSMLGLplvQDQEDSEGDVSKDPDKQLA---QRFKAYELTLKD 2460
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDL---KEQIKSIEKEIENLNGKKEeleEELEELEAALRD 879
FliJ pfam02050
Flagellar FliJ protein;
2265-2356 3.23e-03

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 40.73  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2265 AAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQ-------------ALRERKKREQERL 2331
Cdd:pfam02050    3 AARELAEAQRELQQAEEKLEELQQYRAEYQQQLSGAGQGISAAELRNYQAFISQldeaiaqqqqelaQAEAQVEKAREEW 82
                           90       100
                   ....*....|....*....|....*...
gi 1622916950 2332 AKEMQE-KKLQQELERQKEE--DELKRK 2356
Cdd:pfam02050   83 QEARQErKSLEKLREREKKEerKEQNRR 110
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
2262-2359 3.34e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 43.04  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2262 QDYAAMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEY------DALTEEEKLTFNQGI--------QQALRERKKRE 2327
Cdd:pfam02841  151 KLFLEERDKLEAKYNQVPRKGVKAEEVLQEFLQSKEAVEEailqtdQALTAKEKAIEAERAkaeaaeaeQELLREKQKEE 230
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622916950 2328 QERLAKEM-----QEKKLQQ--ELERQKEEDELKRKVKK 2359
Cdd:pfam02841  231 EQMMEAQErsyqeHVKQLIEkmEAEREQLLAEQERMLEH 269
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2261-2355 3.72e-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: 43.89  E-value: 3.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2261 AQDYAAMKAQ--EKAKKEQEERKHKEALEKEKERLQNmdeeEYDALTEEEKLTFNQgiQQALRERKKREQERLAKEMQEk 2338
Cdd:TIGR02168  350 KEELESLEAEleELEAELEELESRLEELEEQLETLRS----KVAQLELQIASLNNE--IERLEARLERLEDRRERLQQE- 422
                           90
                   ....*....|....*..
gi 1622916950 2339 klQQELERQKEEDELKR 2355
Cdd:TIGR02168  423 --IEELLKKLEEAELKE 437
Ebp2 pfam05890
Eukaryotic rRNA processing protein EBP2; This family consists of several Eukaryotic rRNA ...
2261-2361 3.80e-03

Eukaryotic rRNA processing protein EBP2; This family consists of several Eukaryotic rRNA processing protein EBP2 sequences. Ebp2p is required for the maturation of 25S rRNA and 60S subunit assembly. Ebp2p may be one of the target proteins of Rrs1p for executing the signal to regulate ribosome biogenesis. This family also plays a role in chromosome segregation.


Pssm-ID: 461770  Cd Length: 245  Bit Score: 42.59  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2261 AQDyAAMKAQEKAKKEQ-----------EERKHKEALEKEKERLqnMDEEeydalteeekltfnQGIQQALRERKKREQE 2329
Cdd:pfam05890   52 ALA-AVKEARKRLKKLGipfkrpddyfaEMVKSDEHMEKVRQKL--LDEA--------------AAKKASEEARKQRELK 114
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622916950 2330 RLAKEMQEKKLQqelERQKEEDELKRKVKKGK 2361
Cdd:pfam05890  115 KFGKQVQVEKLQ---ERQKEKKETLEKIKKLK 143
MIC19_MIC25 pfam05300
MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ...
2276-2347 4.15e-03

MICOS complex subunit MIC19/MIC25; MIC19 (also known as ChChd3) and MIC25 (also known as ChChd6) are components of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. MIC19 plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.


Pssm-ID: 461615 [Multi-domain]  Cd Length: 173  Bit Score: 41.60  E-value: 4.15e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916950 2276 EQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQQAL-RERKKREQER-----LAKEMQEKklQQELERQ 2347
Cdd:pfam05300   61 EELRKKIKEELYKRLEQEQAKVQEELARLAEREREAAQESLTRAIlRERASTEDERlkaqqLAKQLEEK--EAELKKQ 136
PLN02316 PLN02316
synthase/transferase
2320-2387 4.18e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 43.71  E-value: 4.18e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622916950 2320 LRERKKREQERLAKEMQEKKLQQELERQKEEDELKRKVKKGKQGPIKEEPPPKKSQASNKQVPPFTKV 2387
Cdd:PLN02316   250 LLEEKRRELEKLAKEEAERERQAEEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLLKKASRSADNV 317
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
2270-2362 4.24e-03

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 40.79  E-value: 4.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2270 QEKAKKEQEERKHKEA---------LEKEKERLQNMDEEEydalteeekltfNQGIQQAlrERKKREQERLAKEMQEKKL 2340
Cdd:pfam00836   48 QKKLEAAEERRKSLEAqklkqlaekREKEEEALQKADEEN------------NNFSKMA--EEKLKQKMEAYKENREAQI 113
                           90       100
                   ....*....|....*....|..
gi 1622916950 2341 QQELERQKEEDELKRKVKKGKQ 2362
Cdd:pfam00836  114 AALKEKLKEKEKHVEEVRKNKE 135
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
2268-2417 4.25e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 4.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLtfnqgiqQALRERKKREQERLAKEMqeKKLQQELERQ 2347
Cdd:TIGR04523  417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL-------DNTRESLETQLKVLSRSI--NKIKQNLEQK 487
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622916950 2348 KEedELKRKVKKGKQgpIKEEpppkKSQASNKQVPPFTKVD---VKMETIERKISVREPTVSEKE-ELNKKKRN 2417
Cdd:TIGR04523  488 QK--ELKSKEKELKK--LNEE----KKELEEKVKDLTKKISslkEKIEKLESEKKEKESKISDLEdELNKDDFE 553
PRK12704 PRK12704
phosphodiesterase; Provisional
2268-2367 4.36e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 4.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEERKhKEALEKEKERLQNMDEEEYDALTEEEKlTFNQGIQ--QALRERKKREQERLAKEMQE-KKLQQEL 2344
Cdd:PRK12704    35 EAEEEAKRILEEAK-KEAEAIKKEALLEAKEEIHKLRNEFEK-ELRERRNelQKLEKRLLQKEENLDRKLELlEKREEEL 112
                           90       100
                   ....*....|....*....|...
gi 1622916950 2345 ERQKEEDELKRKVKKGKQGPIKE 2367
Cdd:PRK12704   113 EKKEKELEQKQQELEKKEEELEE 135
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
2299-2356 5.01e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, 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. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain 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: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 38.40  E-value: 5.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916950 2299 EEYdaltEEEKLtfnqgiQQALRERKKREQERLAKEMQEKKLQQELERQ-KEEDELKRK 2356
Cdd:cd22249      9 EEY----EAQLK------KLEEERRKEREEEEKASEELIRKLQEEEERQrKREREEQLK 57
PRK12704 PRK12704
phosphodiesterase; Provisional
2271-2359 5.30e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 5.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2271 EKAKKEQEERKHKEALE-KEK-ERLQNMDEEEYDALTEEEKLTFNQGIQ--QALRER----KKREQERLAKEMQEKKLQQ 2342
Cdd:PRK12704    45 EEAKKEAEAIKKEALLEaKEEiHKLRNEFEKELRERRNELQKLEKRLLQkeENLDRKlellEKREEELEKKEKELEQKQQ 124
                           90
                   ....*....|....*..
gi 1622916950 2343 ELERQKEedELKRKVKK 2359
Cdd:PRK12704   125 ELEKKEE--ELEELIEE 139
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2270-2416 5.33e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 5.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2270 QEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEEKLTFN-QGIQQALRER--KKREQERLAKEmqEKKLQQELER 2346
Cdd:PRK03918   279 EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEiNGIEERIKELeeKEERLEELKKK--LKELEKRLEE 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2347 QKEEDEL----------KRKVKKGKQGPIKEEPPPKKSQASNKQvppfTKVDVKMETIERKISVREPTVSEK----EELN 2412
Cdd:PRK03918   357 LEERHELyeeakakkeeLERLKKRLTGLTPEKLEKELEELEKAK----EEIEEEISKITARIGELKKEIKELkkaiEELK 432

                   ....
gi 1622916950 2413 KKKR 2416
Cdd:PRK03918   433 KAKG 436
PTZ00121 PTZ00121
MAEBL; Provisional
2266-2621 5.79e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 5.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2266 AMKAQEKAKKEQEERKHKEALEKEKERLQNMDEEEYDALTEEE--KLTFNQGIQQALR--ERKKREQERLAKEMQ----- 2336
Cdd:PTZ00121  1120 AKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDarKAEEARKAEDAKKaeAARKAEEVRKAEELRkaeda 1199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2337 ---EKKLQQELERQKEE----DELKR--KVKKGKQGPIKEEPPPKKSQASNKQVPPFTKVDVKMETIERKISVREPTVSE 2407
Cdd:PTZ00121  1200 rkaEAARKAEEERKAEEarkaEDAKKaeAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK 1279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2408 KEELNK--KKRNMGDvsmlglpLVQDQEDSEGDVSKdpdKQLAQRFKAYELTLKDVQNilmywdRKQGVQLppagmEEAA 2485
Cdd:PTZ00121  1280 ADELKKaeEKKKADE-------AKKAEEKKKADEAK---KKAEEAKKADEAKKKAEEA------KKKADAA-----KKKA 1338
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2486 HEPDDQRQVPSGGRRGRKDRERERLEKERTEKERLEREKAERERLEKlRALEERSDWEGEGEEDHEGKKEKDLgvpflni 2565
Cdd:PTZ00121  1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK-KAEEKKKADEAKKKAEEDKKKADEL------- 1410
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2566 qtpdfeglnwKQALESDKlpKGEQAQE--EQTSSSKGGKQKVKE--KTDQVVETQKDKRR 2621
Cdd:PTZ00121  1411 ----------KKAAAAKK--KADEAKKkaEEKKKADEAKKKAEEakKADEAKKKAEEAKK 1458
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
2262-2689 6.49e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 6.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2262 QDYAAMKAQEKAKKEQEERKHKEAlekekerlqnmdEEEYDALTEEEKLTfnQGIQQALRERKKREQ--ERLAKEMQEKK 2339
Cdd:TIGR00618  424 GQLAHAKKQQELQQRYAELCAAAI------------TCTAQCEKLEKIHL--QESAQSLKEREQQLQtkEQIHLQETRKK 489
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2340 lQQELERQKEEDELKRKVKKGKQgpikeEPPPKKSQASNkqVPPFTKvdvKMETIERkisvrepTVSEKEELNKKKRNMG 2419
Cdd:TIGR00618  490 -AVVLARLLELQEEPCPLCGSCI-----HPNPARQDIDN--PGPLTR---RMQRGEQ-------TYAQLETSEEDVYHQL 551
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2420 DVSmlglpLVQDQEDSEGDVSKDPDKQ-LAQRFKAY----ELTLKDVQNILMYWD-----RKQGVQLPPAGMEEAAHEPD 2489
Cdd:TIGR00618  552 TSE-----RKQRASLKEQMQEIQQSFSiLTQCDNRSkediPNLQNITVRLQDLTEklseaEDMLACEQHALLRKLQPEQD 626
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2490 DQRQVPSGG---RRGRKDRERERLEKERTEKERlEREKAERERLEKLRALEERsdwegegeeDHEGKKEKDLgvpfLNIQ 2566
Cdd:TIGR00618  627 LQDVRLHLQqcsQELALKLTALHALQLTLTQER-VREHALSIRVLPKELLASR---------QLALQKMQSE----KEQL 692
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2567 TPDFEGLNWKQAL---ESDKLPKGEQAQEEQTSSSKGGKQKVKEKTDQVVETQKD---KRRVALNRKVISGEPAG----- 2635
Cdd:TIGR00618  693 TYWKEMLAQCQTLlreLETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElmhQARTVLKARTEAHFNNNeevta 772
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622916950 2636 ---TISQLSD--TDLNNFNGQhSQEKFTRL-----NHFRWIVPANGEVTLQVHFSSDEFGNFDQ 2689
Cdd:TIGR00618  773 alqTGAELSHlaAEIQFFNRL-REEDTHLLktleaEIGQEIPSDEDILNLQCETLVQEEEQFLS 835
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2265-2355 6.71e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 6.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2265 AAMKAQEKAKKEQEERKHKEALEKEKERLQN--MDEEEYDALTEEEKLTFNQGIQQALRERKKREQERLAKEMQE-KKLQ 2341
Cdd:COG1196    314 LEERLEELEEELAELEEELEELEEELEELEEelEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELlEALR 393
                           90
                   ....*....|....
gi 1622916950 2342 QELERQKEEDELKR 2355
Cdd:COG1196    394 AAAELAAQLEELEE 407
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
2262-2381 6.84e-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: 42.18  E-value: 6.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2262 QDYAAMKAQEKAKKEQEERK---HKEALE---KEKERL--------QNMDEEEYDALTEEEKLTFNQGIQQALRERKKRE 2327
Cdd:cd16269    145 QLYLEDREKLVEKYRQVPRKgvkAEEVLQeflQSKEAEaeailqadQALTEKEKEIEAERAKAEAAEQERKLLEEQQREL 224
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622916950 2328 QERLAK---------EMQEKKLQQELERQKEEDE--LKRKVKKGKQgpIKEEPPPKKSQASNKQV 2381
Cdd:cd16269    225 EQKLEDqersyeehlRQLKEKMEEERENLLKEQEraLESKLKEQEA--LLEEGFKEQAELLQEEI 287
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2264-2362 8.00e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 8.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2264 YAAMKAQEKAKKEQEERKhkEALEKEKERLQNMDEEEYDALTEEEKLTFNQGIQ--QALRERKKREQERLAKEMQEKK-L 2340
Cdd:COG4717    148 LEELEERLEELRELEEEL--EELEAELAELQEELEELLEQLSLATEEELQDLAEelEELQQRLAELEEELEEAQEELEeL 225
                           90       100
                   ....*....|....*....|....*
gi 1622916950 2341 QQELER---QKEEDELKRKVKKGKQ 2362
Cdd:COG4717    226 EEELEQlenELEAAALEERLKEARL 250
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
2307-2359 8.55e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 8.55e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622916950 2307 EEKLTFNQGIQ--QALR----------ERKKREQERLAKEMQEKKLQQELERQKEEDELKRKVKK 2359
Cdd:PRK00409   513 EDKEKLNELIAslEELEreleqkaeeaEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
2268-2354 9.61e-03

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 39.50  E-value: 9.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2268 KAQEKAKKEQEERKHK-EALEKEKERLqnmdEEEYDALTEEEkltfnqgiqqalrERKKREQERLAKEMQEKKLQQeLER 2346
Cdd:pfam17675   48 KELEKLEKEEEELLQElEELEKEREEL----DAELEALEEEL-------------EALDEEEEEFWREYNALQLQL-LEF 109

                   ....*...
gi 1622916950 2347 QKEEDELK 2354
Cdd:pfam17675  110 QDERDSLE 117
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
2278-2357 9.63e-03

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 39.34  E-value: 9.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2278 EERKHK-----EALEKEKERLQNMdEEEYDALTEEEKLTFNQGIQQAlRERKKREQERL-------AKEMQEKKLQQ-EL 2344
Cdd:cd06503     29 DEREEKiaeslEEAEKAKEEAEEL-LAEYEEKLAEARAEAQEIIEEA-RKEAEKIKEEIlaeakeeAERILEQAKAEiEQ 106
                           90
                   ....*....|...
gi 1622916950 2345 ERQKEEDELKRKV 2357
Cdd:cd06503    107 EKEKALAELRKEV 119
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
2263-2356 9.94e-03

Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar proteins; mS26, also known as mitochondrial 37S ribosomal protein PET12, is a component of the mitochondrial small ribosomal subunit (mt-SSU) of Saccharomyces cerevisiae mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The family also includes a group of uncharacterized proteins from pezizomycotina, which show high sequence similarity with mS26.


Pssm-ID: 467916 [Multi-domain]  Cd Length: 179  Bit Score: 40.23  E-value: 9.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916950 2263 DYAAMKAQEKAKKEQEE--RKH-KEALEKEKERLQNMDEEeydaltEEEKLTFNQGIQQALRERKKREQERL-----AKE 2334
Cdd:cd23703     41 PKSPLSEYQEWKRKMAElrRQNlREGLRELEERKLKTEEL------RAKRSERKQAERERALNAPEREDERLtlptiESA 114
                           90       100
                   ....*....|....*....|..
gi 1622916950 2335 MQEKKLQQELERQKEEDELKRK 2356
Cdd:cd23703    115 LLGPLMRVRTDPEREERAAKRR 136
 
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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