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Conserved domains on  [gi|116008016|ref|NP_001036715|]
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myosin heavy chain-like, isoform G [Drosophila melanogaster]

Protein Classification

class XVIII myosin( domain architecture ID 20383645)

class XVIII myosin such as human unconventional myosin-XVIIIa that may link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi, and contains a myosin head/motor domain with ATP- and actin-binding sites but does not have ATPase activity

CATH:  3.40.850.10
Gene Ontology:  GO:0005524|GO:0051015|GO:0016459
SCOP:  4004054

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
575-1305 0e+00

class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


:

Pssm-ID: 276837 [Multi-domain]  Cd Length: 689  Bit Score: 1031.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd01386     1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLL 734
Cdd:cd01386    81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  735 PERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDShPFISLSQKLEDRHRAANDFMRTVQAFETLNIDAKA 814
Cdd:cd01386   161 LERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNS-FGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  815 VRGIWSILAAIYHLGIAGVTKlgTGSTARTQFANPTAARKASGLLGVNLEDLSSAAF-----GLTQPNAPNGGLSPSKSP 889
Cdd:cd01386   240 QRAIWSILAAIYHLGAAGATK--AASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFkhhlsGGPQQSTTSSGQESPARS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  890 TSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQNPASCGQQVGATLADLRHNYLQERL 969
Cdd:cd01386   318 SSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQERL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  970 QMLFHHTTLVAPRDRYAQELVEIEMDLASEChPGPLISLIDKAPQNHVVRSsqrDLREHDRRGMLWLLDEEAIYPNSNDD 1049
Cdd:cd01386   398 QLLFHERTFVAPLERYKQENVEVDFDLPELS-PGALVALIDQAPQQALVRS---DLRDEDRRGLLWLLDEEALYPGSSDD 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1050 TFLERLFSHYGDREH---HSLLRKCAGPRQFVLHHLQGTNPVLYAVDGWVRHSREHPGIRNAVSLLQDSSREeinrlyig 1126
Cdd:cd01386   474 TFLERLFSHYGDKEGgkgHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE-------- 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1127 sltrgsgamvfcgsfaglegtqslrrvssirrsftTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCYLLQHNAGKHT 1206
Cdd:cd01386   546 -----------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDE 590
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1207 KYTANGspssaagqvSSEEEMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLAS---------NK 1277
Cdd:cd01386   591 RSTSSP---------AAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKklglnsevaDE 661
                         730       740
                  ....*....|....*....|....*...
gi 116008016 1278 DVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd01386   662 RKAVEELLEELDLEKSSYRIGLSQVFFR 689
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
541-2019 9.40e-98

Myosin heavy chain [General function prediction only];


The actual alignment was detected with superfamily member COG5022:

Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 348.99  E-value: 9.40e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  541 NGEQLTVDEDDVE--KQNSPALDLVEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMF 618
Cdd:COG5022    44 DGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSY 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  619 RGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINA--EKVNALCTILEA 696
Cdd:COG5022   124 SGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSieKQILATNPILEA 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  697 FGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENitSE 776
Cdd:COG5022   204 FGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQN--PK 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  777 DSHPFISLSQKLEDRHRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGStarTQFANPTAARKAS 856
Cdd:COG5022   282 DYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNGA---AIFSDNSVLDKAC 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  857 GLLGVNLEDLSSAafgLTQpnapngglspsksPTSDTGHEW---------AWECLEALVIGLYSEALAAVVALINRQICT 927
Cdd:COG5022   359 YLLGIDPSLFVKW---LVK-------------RQIKTGGEWivvplnleqALAIRDSLAKALYSNLFDWIVDRINKSLDH 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  928 SSHTIASIMLIDTPGFQ----NpascgqqvgaTLADLRHNYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDLAsECHPG 1003
Cdd:COG5022   423 SAAASNFIGVLDIYGFEifekN----------SFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKE--GIEWSFI-DYFDN 489
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1004 -PLISLIDKApqnhvvrssqrdlrehDRRGMLWLLDEEAIYPNSNDDTFLERLFSHYgdREHHSLLRKCAGPRQ--FVLH 1080
Cdd:COG5022   490 qPCIDLIEKK----------------NPLGILSLLDEECVMPHATDESFTSKLAQRL--NKNSNPKFKKSRFRDnkFVVK 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1081 HLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDSSREEINRLyigsltrgsgamvfcgsFAGLEGTQSLRRvssirrsF 1160
Cdd:COG5022   552 HYAGD--VEYDVEGFLDKNKD-PLNDDLLELLKASTNEFVSTL-----------------FDDEENIESKGR-------F 604
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1161 TTAGVKRNSIMLQvkftvdgIIDTLRRTGTHFVHCylLQHNAGKhtkytangspssaagqvssEEEMVNVPLLRSQLRGS 1240
Cdd:COG5022   605 PTLGSRFKESLNS-------LMSTLNSTQPHYIRC--IKPNEEK-------------------SPWTFDNQMVLSQLRCC 656
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1241 QVLEAARLHRLGFPESVPLLEFVRRFGLL------AGDLASNKDV--SVEQILAVNELDVASYRIGPSQILFRSGVLSEL 1312
Cdd:COG5022   657 GVLETIRISRAGFPSRWTFDEFVQRYRILspskswTGEYTWKEDTknAVKSILEELVIDSSKYQIGNTKVFFKAGVLAAL 736
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1313 EAKRDVLLSDRIIQLQAFCRGYLARKKMSQRRVQELAVRCIQRNVKAFLAVRDWPWWRLLVRVTPLLNVHRTEEQLKTAN 1392
Cdd:COG5022   737 EDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYL 816
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1393 EELLMLRAKLeKIECDRSEvkAENQKLEAKlSELTVDLAEERSTAHIATERLE-----AETAERLKLEK----ELGDQTN 1463
Cdd:COG5022   817 ACIIKLQKTI-KREKKLRE--TEEVEFSLK-AEVLIQKFGRSLKAKKRFSLLKketiyLQSAQRVELAErqlqELKIDVK 892
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1464 KVKNLQETTEKLEMELICAKSDLngiSEDEDAENEdgvgggvykLKYERVAReLEFTKRrlhtqhEHDLEQLVALKKHLe 1543
Cdd:COG5022   893 SISSLKLVNLELESEIIELKKSL---SSDLIENLE---------FKTELIAR-LKKLLN------NIDLEEGPSIEYVK- 952
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1544 mklsdaYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFdAECQSLQDAV-RQERQAKERYGRE 1622
Cdd:COG5022   953 ------LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL-AELSKQYGALqESTKQLKELPVEV 1025
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1623 KDVLQAEKFTLEQTLADTRL----DLEFK-EEKLASLQRELEEM------TFGGGTEEEFAQLRRSK----NETERRAKE 1687
Cdd:COG5022  1026 AELQSASKIISSESTELSILkplqKLKGLlLLENNQLQARYKALklrrenSLLDDKQLYQLESTENLlktiNVKDLEVTN 1105
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1688 QEEELDEMAGQIQLLEQAKLRLEmtletmrkearresQQRDEELEEVRGN-GYKKIKALECQLETEHEERTLLLREKHEL 1766
Cdd:COG5022  1106 RNLVKPANVLQFIVAQMIKLNLL--------------QEISKFLSQLVNTlEPVFQKLSVLQLELDGLFWEANLEALPSP 1171
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1767 ERRLSSMEDRDRvdrdaEEALnqklrrdlrkYKALLKDAQTQLERLKADTpgKTLIRQLRNqledaESARSLAMKARQTA 1846
Cdd:COG5022  1172 PPFAALSEKRLY-----QSAL----------YDEKSKLSSSEVNDLKNEL--IALFSKIFS-----GWPRGDKLKKLISE 1229
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1847 EAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEqINVSEAE---FKLNEM 1923
Cdd:COG5022  1230 GWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQY-INVGLFNalrTKASSL 1308
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1924 EAERNNLKEQVAEL------QHRLDNV-ENLgdPSMAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKL-- 1994
Cdd:COG5022  1309 RWKSATEVNYNSEElddwcrEFEISDVdEEL--EELIQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQNLKSRYDPAdk 1386
                        1530      1540
                  ....*....|....*....|....*
gi 116008016 1995 QNEVTQSKMREMQAQDVIKKSQKSL 2019
Cdd:COG5022  1387 ENNLPKEILKKIEALLIKQELQLSL 1411
PDZ_canonical super family cl49608
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
337-426 2.35e-33

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


The actual alignment was detected with superfamily member cd06747:

Pssm-ID: 483948 [Multi-domain]  Cd Length: 90  Bit Score: 124.35  E-value: 2.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  337 QLVIRRQksPRQDFGFSLRKAICLDRTESLTSPIFRPVIFAEPGAGGGATGL--LPGDRLIKVNGTPVGELPREIIIEMI 414
Cdd:cd06747     1 EITLKRQ--PTGDFGFSLRRGTIVERGPDDGQELKRTVHFAEPGAGTKNLATglLPGDRLIEVNGVNVENASRDEIIEMI 78
                          90
                  ....*....|..
gi 116008016  415 RNSGEAVTVEVQ 426
Cdd:cd06747    79 RKSGDTVTLKVQ 90
 
Name Accession Description Interval E-value
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
575-1305 0e+00

class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276837 [Multi-domain]  Cd Length: 689  Bit Score: 1031.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd01386     1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLL 734
Cdd:cd01386    81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  735 PERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDShPFISLSQKLEDRHRAANDFMRTVQAFETLNIDAKA 814
Cdd:cd01386   161 LERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNS-FGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  815 VRGIWSILAAIYHLGIAGVTKlgTGSTARTQFANPTAARKASGLLGVNLEDLSSAAF-----GLTQPNAPNGGLSPSKSP 889
Cdd:cd01386   240 QRAIWSILAAIYHLGAAGATK--AASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFkhhlsGGPQQSTTSSGQESPARS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  890 TSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQNPASCGQQVGATLADLRHNYLQERL 969
Cdd:cd01386   318 SSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQERL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  970 QMLFHHTTLVAPRDRYAQELVEIEMDLASEChPGPLISLIDKAPQNHVVRSsqrDLREHDRRGMLWLLDEEAIYPNSNDD 1049
Cdd:cd01386   398 QLLFHERTFVAPLERYKQENVEVDFDLPELS-PGALVALIDQAPQQALVRS---DLRDEDRRGLLWLLDEEALYPGSSDD 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1050 TFLERLFSHYGDREH---HSLLRKCAGPRQFVLHHLQGTNPVLYAVDGWVRHSREHPGIRNAVSLLQDSSREeinrlyig 1126
Cdd:cd01386   474 TFLERLFSHYGDKEGgkgHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE-------- 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1127 sltrgsgamvfcgsfaglegtqslrrvssirrsftTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCYLLQHNAGKHT 1206
Cdd:cd01386   546 -----------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDE 590
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1207 KYTANGspssaagqvSSEEEMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLAS---------NK 1277
Cdd:cd01386   591 RSTSSP---------AAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKklglnsevaDE 661
                         730       740
                  ....*....|....*....|....*...
gi 116008016 1278 DVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd01386   662 RKAVEELLEELDLEKSSYRIGLSQVFFR 689
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
556-1317 3.45e-109

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 364.94  E-value: 3.45e-109
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016    556 NSPALDLVEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQ 635
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016    636 TAYRSLVETRRDQSLIFMGRSGSGKSTSFKHALNYLAlAAGAYNNFINA--EKVNALCTILEAFGNTKTCLNSNATRMTQ 713
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLA-SVSGSNTEVGSveDQILESNPILEAFGNAKTLRNNNSSRFGK 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016    714 LLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLeniTSEDSHPFISLSQKLE---- 789
Cdd:smart00242  160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGL---KSPEDYRYLNQGGCLTvdgi 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016    790 -DrhraANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKlGTGSTARTQFANPTAARKASGLLGVNLEDLSS 868
Cdd:smart00242  237 dD----AEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEE-GRNDNAASTVKDKEELSNAAELLGVDPEELEK 311
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016    869 AafgLTqpnapngglspskSPTSDTGHEW---------AWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLID 939
Cdd:smart00242  312 A---LT-------------KRKIKTGGEVitkplnveqALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLD 375
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016    940 TPGFQNpascgqqvgatladLRH--------NYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDLASECHPGPLISLIDK 1011
Cdd:smart00242  376 IYGFEI--------------FEVnsfeqlciNYANEKLQQFFNQHVFKLEQEEYERE--GIDWTFIDFFDNQDCIDLIEK 439
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   1012 APQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSlLRKCAGPRQFVLHHLQGTnpVLYA 1091
Cdd:smart00242  440 KPP-----------------GILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFS-KPKKKGRTEFIIKHYAGD--VTYD 499
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   1092 VDGWVRHSREhPGIRNAVSLLQDSSreeiNRLyIGSLtrgsgamvfcgsFAGLEGTQSlrrvSSIRrsFTTAGVK-RNSi 1170
Cdd:smart00242  500 VTGFLEKNKD-TLSDDLIELLQSSK----NPL-IASL------------FPSGVSNAG----SKKR--FQTVGSQfKEQ- 554
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   1171 mLQVkftvdgIIDTLRRTGTHFVHCylLQHNAGKhtkytangspssAAGQVSSeeemvnvPLLRSQLRGSQVLEAARLHR 1250
Cdd:smart00242  555 -LNE------LMDTLNSTNPHFIRC--IKPNEEK------------KPGDFDS-------SLVLHQLRYLGVLENIRIRR 606
                           730       740       750       760       770       780       790
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116008016   1251 LGFPESVPLLEFVRRFGLLAGDLASNKDV----SVEQILAVNELDVASYRIGPSQILFRSGVLSELEAKRD 1317
Cdd:smart00242  607 AGFPYRLPFDEFLQRYRVLLPDTWPPWGGdakkACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
Myosin_head pfam00063
Myosin head (motor domain);
563-1305 2.10e-99

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 336.56  E-value: 2.10e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   563 VEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLV 642
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   643 ETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAG--AYNNFINAEKV----NAlctILEAFGNTKTCLNSNATRMTQLLS 716
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGsgSAGNVGRLEEQilqsNP---ILEAFGNAKTVRNNNSSRFGKYIE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   717 LDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSedshpFISLSQKLEDRHRAAN 796
Cdd:pfam00063  158 IQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKD-----YHYLSQSGCYTIDGID 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   797 D---FMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTArtQFANPTAARKASGLLGVNLEDLSSAafgL 873
Cdd:pfam00063  233 DseeFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQA--VPDDTENLQKAASLLGIDSTELEKA---L 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   874 TqpnapngglspskSPTSDTGHEW---------AWECLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGF 943
Cdd:pfam00063  308 C-------------KRRIKTGRETvskpqnveqANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASfIGVLDIYGF 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   944 Q----NpaSCGQqvgatladLRHNYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDLASECHPGPLISLIDKAPqnhvvr 1019
Cdd:pfam00063  375 EifekN--SFEQ--------LCINYVNEKLQQFFNHHMFKLEQEEYVRE--GIEWTFIDFGDNQPCIDLIEKKP------ 436
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1020 ssqrdlrehdrRGMLWLLDEEAIYPNSNDDTFLERLFSHYGDrehHSLLRKcagPRQ-----FVLHHLQGTnpVLYAVDG 1094
Cdd:pfam00063  437 -----------LGILSLLDEECLFPKATDQTFLDKLYSTFSK---HPHFQK---PRLqgethFIIKHYAGD--VEYNVEG 497
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1095 WVRHSREhPGIRNAVSLLQDSSREEINRLYIGSLTRGSGAMVFCGSFAGLEGTQSlrrvssirrSFTTAGVK-RNSIMLq 1173
Cdd:pfam00063  498 FLEKNKD-PLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTPKRTKKK---------RFITVGSQfKESLGE- 566
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1174 vkftvdgIIDTLRRTGTHFVHCylLQHNAGKhtkytangspssAAGQVSSeeemvnvPLLRSQLRGSQVLEAARLHRLGF 1253
Cdd:pfam00063  567 -------LMKTLNSTNPHYIRC--IKPNEKK------------RAGVFDN-------SLVLHQLRCNGVLEGIRIRRAGF 618
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016  1254 PESVPLLEFVRRFGLLAGDLASNKDVS----VEQILAVNELDVASYRIGPSQILFR 1305
Cdd:pfam00063  619 PNRITFQEFVQRYRILAPKTWPKWKGDakkgCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
541-2019 9.40e-98

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 348.99  E-value: 9.40e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  541 NGEQLTVDEDDVE--KQNSPALDLVEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMF 618
Cdd:COG5022    44 DGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSY 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  619 RGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINA--EKVNALCTILEA 696
Cdd:COG5022   124 SGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSieKQILATNPILEA 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  697 FGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENitSE 776
Cdd:COG5022   204 FGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQN--PK 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  777 DSHPFISLSQKLEDRHRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGStarTQFANPTAARKAS 856
Cdd:COG5022   282 DYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNGA---AIFSDNSVLDKAC 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  857 GLLGVNLEDLSSAafgLTQpnapngglspsksPTSDTGHEW---------AWECLEALVIGLYSEALAAVVALINRQICT 927
Cdd:COG5022   359 YLLGIDPSLFVKW---LVK-------------RQIKTGGEWivvplnleqALAIRDSLAKALYSNLFDWIVDRINKSLDH 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  928 SSHTIASIMLIDTPGFQ----NpascgqqvgaTLADLRHNYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDLAsECHPG 1003
Cdd:COG5022   423 SAAASNFIGVLDIYGFEifekN----------SFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKE--GIEWSFI-DYFDN 489
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1004 -PLISLIDKApqnhvvrssqrdlrehDRRGMLWLLDEEAIYPNSNDDTFLERLFSHYgdREHHSLLRKCAGPRQ--FVLH 1080
Cdd:COG5022   490 qPCIDLIEKK----------------NPLGILSLLDEECVMPHATDESFTSKLAQRL--NKNSNPKFKKSRFRDnkFVVK 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1081 HLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDSSREEINRLyigsltrgsgamvfcgsFAGLEGTQSLRRvssirrsF 1160
Cdd:COG5022   552 HYAGD--VEYDVEGFLDKNKD-PLNDDLLELLKASTNEFVSTL-----------------FDDEENIESKGR-------F 604
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1161 TTAGVKRNSIMLQvkftvdgIIDTLRRTGTHFVHCylLQHNAGKhtkytangspssaagqvssEEEMVNVPLLRSQLRGS 1240
Cdd:COG5022   605 PTLGSRFKESLNS-------LMSTLNSTQPHYIRC--IKPNEEK-------------------SPWTFDNQMVLSQLRCC 656
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1241 QVLEAARLHRLGFPESVPLLEFVRRFGLL------AGDLASNKDV--SVEQILAVNELDVASYRIGPSQILFRSGVLSEL 1312
Cdd:COG5022   657 GVLETIRISRAGFPSRWTFDEFVQRYRILspskswTGEYTWKEDTknAVKSILEELVIDSSKYQIGNTKVFFKAGVLAAL 736
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1313 EAKRDVLLSDRIIQLQAFCRGYLARKKMSQRRVQELAVRCIQRNVKAFLAVRDWPWWRLLVRVTPLLNVHRTEEQLKTAN 1392
Cdd:COG5022   737 EDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYL 816
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1393 EELLMLRAKLeKIECDRSEvkAENQKLEAKlSELTVDLAEERSTAHIATERLE-----AETAERLKLEK----ELGDQTN 1463
Cdd:COG5022   817 ACIIKLQKTI-KREKKLRE--TEEVEFSLK-AEVLIQKFGRSLKAKKRFSLLKketiyLQSAQRVELAErqlqELKIDVK 892
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1464 KVKNLQETTEKLEMELICAKSDLngiSEDEDAENEdgvgggvykLKYERVAReLEFTKRrlhtqhEHDLEQLVALKKHLe 1543
Cdd:COG5022   893 SISSLKLVNLELESEIIELKKSL---SSDLIENLE---------FKTELIAR-LKKLLN------NIDLEEGPSIEYVK- 952
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1544 mklsdaYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFdAECQSLQDAV-RQERQAKERYGRE 1622
Cdd:COG5022   953 ------LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL-AELSKQYGALqESTKQLKELPVEV 1025
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1623 KDVLQAEKFTLEQTLADTRL----DLEFK-EEKLASLQRELEEM------TFGGGTEEEFAQLRRSK----NETERRAKE 1687
Cdd:COG5022  1026 AELQSASKIISSESTELSILkplqKLKGLlLLENNQLQARYKALklrrenSLLDDKQLYQLESTENLlktiNVKDLEVTN 1105
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1688 QEEELDEMAGQIQLLEQAKLRLEmtletmrkearresQQRDEELEEVRGN-GYKKIKALECQLETEHEERTLLLREKHEL 1766
Cdd:COG5022  1106 RNLVKPANVLQFIVAQMIKLNLL--------------QEISKFLSQLVNTlEPVFQKLSVLQLELDGLFWEANLEALPSP 1171
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1767 ERRLSSMEDRDRvdrdaEEALnqklrrdlrkYKALLKDAQTQLERLKADTpgKTLIRQLRNqledaESARSLAMKARQTA 1846
Cdd:COG5022  1172 PPFAALSEKRLY-----QSAL----------YDEKSKLSSSEVNDLKNEL--IALFSKIFS-----GWPRGDKLKKLISE 1229
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1847 EAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEqINVSEAE---FKLNEM 1923
Cdd:COG5022  1230 GWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQY-INVGLFNalrTKASSL 1308
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1924 EAERNNLKEQVAEL------QHRLDNV-ENLgdPSMAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKL-- 1994
Cdd:COG5022  1309 RWKSATEVNYNSEElddwcrEFEISDVdEEL--EELIQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQNLKSRYDPAdk 1386
                        1530      1540
                  ....*....|....*....|....*
gi 116008016 1995 QNEVTQSKMREMQAQDVIKKSQKSL 2019
Cdd:COG5022  1387 ENNLPKEILKKIEALLIKQELQLSL 1411
PTZ00014 PTZ00014
myosin-A; Provisional
541-867 8.98e-40

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 160.97  E-value: 8.98e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  541 NGEQLTVDEDDVEKQNSPA-LDLVEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFR 619
Cdd:PTZ00014   75 TNSTFEVKPEHAFNANSQIdPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYR 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  620 GCK-TEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCTILEAFG 698
Cdd:PTZ00014  155 DAKdSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVLEAFG 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  699 NTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITsedS 778
Cdd:PTZ00014  235 NAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLE---E 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  779 HPFISLS----QKLEDrhraANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG---IAGVTKLGTGSTARTQFANPTA 851
Cdd:PTZ00014  312 YKYINPKcldvPGIDD----VKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGnveIEGKEEGGLTDAAAISDESLEV 387
                         330
                  ....*....|....*.
gi 116008016  852 ARKASGLLGVNLEDLS 867
Cdd:PTZ00014  388 FNEACELLFLDYESLK 403
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
1380-2067 9.84e-35

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: 145.70  E-value: 9.84e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1380 NVHRTEEQLKTANEELlmlRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEerstahiaTERLEAETAERL-KLEKEL 1458
Cdd:pfam01576  374 NLEKAKQALESENAEL---QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--------SERQRAELAEKLsKLQSEL 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1459 GDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDgvgggvyKLKYERVARELEFTKRRLHTQHEHDLEQLVAL 1538
Cdd:pfam01576  443 ESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ-------KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNV 515
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1539 KKH---LEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQ- 1614
Cdd:pfam01576  516 ERQlstLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQl 595
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1615 --AKERYGREKDVLQAEKFTLEQTLADTRLDLEF----KEEKLASLQRELEEMTfggGTEEEFA---------------- 1672
Cdd:pfam01576  596 vsNLEKKQKKFDQMLAEEKAISARYAEERDRAEAeareKETRALSLARALEEAL---EAKEELErtnkqlraemedlvss 672
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1673 ---------QLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIK 1743
Cdd:pfam01576  673 kddvgknvhELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVR 752
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1744 ALECQLETEHEERTLLLREKHELERRLSSMEDR-DRVDRDAEEALNQklrrdLRKYKALLKDAQTQLERLKADTpgktli 1822
Cdd:pfam01576  753 ELEAELEDERKQRAQAVAAKKKLELDLKELEAQiDAANKGREEAVKQ-----LKKLQAQMKDLQRELEEARASR------ 821
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1823 RQLRNQLEDAEsarslamKARQTAEAELTEVQAMFDESHRARNDAEEranaahrDRAELQAQIEENEeelgelmKKYSAT 1902
Cdd:pfam01576  822 DEILAQSKESE-------KKLKNLEAELLQLQEDLAASERARRQAQQ-------ERDELADEIASGA-------SGKSAL 880
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1903 VKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLD--NVENLGDPSMAMMS----KRLELRTKELESRL-ELEQA 1975
Cdd:pfam01576  881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEqlTTELAAERSTSQKSesarQQLERQNKELKAKLqEMEGT 960
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1976 TRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDM-----REEFHAVSSREQ--ESLTRRKDLEKKVE 2048
Cdd:pfam01576  961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVllqveDERRHADQYKDQaeKGNSRMKQLKRQLE 1040
                          730
                   ....*....|....*....
gi 116008016  2049 QMESEgAALKNDLRLALQR 2067
Cdd:pfam01576 1041 EAEEE-ASRANAARRKLQR 1058
PDZ_MYO18-like cd06747
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein ...
337-426 2.35e-33

PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MYO18 protein and related domains. MYO18 (also known as myosin XVIIIA, KIAA0216, MysPDZ), a member of the myosin superfamily, is involved in regulating cell protrusion and migration, and Golgi trafficking and morphology, and is required for myoblast adhesion and muscle integrity. The MYO18A/MRCK/LRAP35a complex regulates actomyosin retrograde flow in cell protrusion and migration; the PtdIns(4)P/GOLPH3/MYO18A/F-actin complex is a hub for signals that regulate Golgi trafficking function. The MYO18A PDZ domain binds p190Rho-guanine nucleotide exchange factor (p190RhoGEF), Golgin45, and leucine repeat adaptor protein 1 (Lurap1, also known as Lrap35a). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MYO18-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467229 [Multi-domain]  Cd Length: 90  Bit Score: 124.35  E-value: 2.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  337 QLVIRRQksPRQDFGFSLRKAICLDRTESLTSPIFRPVIFAEPGAGGGATGL--LPGDRLIKVNGTPVGELPREIIIEMI 414
Cdd:cd06747     1 EITLKRQ--PTGDFGFSLRRGTIVERGPDDGQELKRTVHFAEPGAGTKNLATglLPGDRLIEVNGVNVENASRDEIIEMI 78
                          90
                  ....*....|..
gi 116008016  415 RNSGEAVTVEVQ 426
Cdd:cd06747    79 RKSGDTVTLKVQ 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1387-2073 1.11e-23

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: 109.76  E-value: 1.11e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1387 QLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVK 1466
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1467 NLQETTEKLEMELICAKSDLNgISEDEDAENEDgvgggvyklKYERVARELEftkrrlhtQHEHDLEQLVALKKHLEMKL 1546
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLD-ELAEELAELEE---------KLEELKEELE--------SLEAELEELEAELEELESRL 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1547 SDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKdvL 1626
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE--L 452
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1627 QAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAK 1706
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD 532
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1707 LRLEMTLETM-----------RKEARRESQQRDEELE-------EVRGNGYKKIKALECQLETEHEERTLLLRE----KH 1764
Cdd:TIGR02168  533 EGYEAAIEAAlggrlqavvveNLNAAKKAIAFLKQNElgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvkfDP 612
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1765 ELERRLSSMEDRDRVDRDAEEALNQ--KLRRDLR---------------------------KYKALLKDAQTQLERLKAD 1815
Cdd:TIGR02168  613 KLRKALSYLLGGVLVVDDLDNALELakKLRPGYRivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEK 692
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1816 -TPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGE 1894
Cdd:TIGR02168  693 iAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1895 LMKKYSATVKQLNT--EQINVSEAEFK-----LNEMEAERNNLKEQVAELQHRLDNVENlgdpSMAMMSKRLElrtkELE 1967
Cdd:TIGR02168  773 AEEELAEAEAEIEEleAQIEQLKEELKalreaLDELRAELTLLNEEAANLRERLESLER----RIAATERRLE----DLE 844
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1968 SRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKV 2047
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
                          730       740
                   ....*....|....*....|....*.
gi 116008016  2048 EQMESEGAALKNDLRLALQRIADLQQ 2073
Cdd:TIGR02168  925 AQLELRLEGLEVRIDNLQERLSEEYS 950
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1533-2075 6.27e-17

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 87.43  E-value: 6.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1533 EQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMT---NEMNDLRMLLEEqnarnnlLEKKQRKFDAECQSLqDAV 1609
Cdd:PRK03918  165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEevlREINEISSELPE-------LREELEKLEKEVKEL-EEL 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1610 RQERQAKERygrEKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNET-------E 1682
Cdd:PRK03918  237 KEEIEELEK---ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYldelreiE 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1683 RRAKEQEEELDEMAGQIQLLEQAKLRLEMTletmrKEARRESQQRDEELEEvRGNGYKKIKALECQLETEHEERTLLlrE 1762
Cdd:PRK03918  314 KRLSRLEEEINGIEERIKELEEKEERLEEL-----KKKLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTGL--T 385
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1763 KHELERRLSSMEDRDRVDRDAEEALNQKLRRdLRKYKALLKDAQTQLERLKADTP----------GKTLIRQLRNQLEDA 1832
Cdd:PRK03918  386 PEKLEKELEELEKAKEEIEEEISKITARIGE-LKKEIKELKKAIEELKKAKGKCPvcgrelteehRKELLEEYTAELKRI 464
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1833 ESARSLAMKARQTAEAELTEVQAMFDESHRAR---------NDAEERANAAHRDRAELQAQIEENEEELGELMKKysaTV 1903
Cdd:PRK03918  465 EKELKEIEEKERKLRKELRELEKVLKKESELIklkelaeqlKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKG---EI 541
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1904 KQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLdnvENLGDPSMAMMSKRLE---------LRTKELESRLELEQ 1974
Cdd:PRK03918  542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL---EELGFESVEELEERLKelepfyneyLELKDAEKELEREE 618
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1975 ATRARLEVQVnrhKEALEKLQNEVTQSKMREMQAQDVIKK-SQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESE 2053
Cdd:PRK03918  619 KELKKLEEEL---DKAFEELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
                         570       580
                  ....*....|....*....|....*
gi 116008016 2054 GAALKNDL---RLALQRIADLQQAM 2075
Cdd:PRK03918  696 LEKLKEELeerEKAKKELEKLEKAL 720
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
390-427 2.42e-05

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 44.68  E-value: 2.42e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 116008016    390 PGDRLIKVNGTPVGELPREIIIEMIRNSGEAVTVEVQP 427
Cdd:smart00228   46 VGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLR 83
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
390-426 2.65e-04

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 41.50  E-value: 2.65e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 116008016   390 PGDRLIKVNGTPVGELPREIIIEMIRNSGEAVTVEVQ 426
Cdd:pfam00595   45 VGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
1540-1750 7.31e-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: 43.72  E-value: 7.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1540 KHLEMKLSDAYEEVVEQRQVVGQwkrkaQKMTNEMNDLRMLLEEQNARNNLLekKQRKFDAECQSLQDAVRQERQAKERY 1619
Cdd:cd16269    93 KKLMEQLEEKKEEFCKQNEEASS-----KRCQALLQELSAPLEEKISQGSYS--VPGGYQLYLEDREKLVEKYRQVPRKG 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1620 GREKDVLQ---AEKFTLEQTL--ADTRLDLEFKEEKLASLQRELEEMtfgggteeEFAQLRRSKNETERRAKEQEEELDE 1694
Cdd:cd16269   166 VKAEEVLQeflQSKEAEAEAIlqADQALTEKEKEIEAERAKAEAAEQ--------ERKLLEEQQRELEQKLEDQERSYEE 237
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1695 MagqiqlLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYK-KIKALECQLE 1750
Cdd:cd16269   238 H------LRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKeQAELLQEEIR 288
 
Name Accession Description Interval E-value
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
575-1305 0e+00

class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276837 [Multi-domain]  Cd Length: 689  Bit Score: 1031.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd01386     1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLL 734
Cdd:cd01386    81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  735 PERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDShPFISLSQKLEDRHRAANDFMRTVQAFETLNIDAKA 814
Cdd:cd01386   161 LERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNS-FGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  815 VRGIWSILAAIYHLGIAGVTKlgTGSTARTQFANPTAARKASGLLGVNLEDLSSAAF-----GLTQPNAPNGGLSPSKSP 889
Cdd:cd01386   240 QRAIWSILAAIYHLGAAGATK--AASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFkhhlsGGPQQSTTSSGQESPARS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  890 TSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQNPASCGQQVGATLADLRHNYLQERL 969
Cdd:cd01386   318 SSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQERL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  970 QMLFHHTTLVAPRDRYAQELVEIEMDLASEChPGPLISLIDKAPQNHVVRSsqrDLREHDRRGMLWLLDEEAIYPNSNDD 1049
Cdd:cd01386   398 QLLFHERTFVAPLERYKQENVEVDFDLPELS-PGALVALIDQAPQQALVRS---DLRDEDRRGLLWLLDEEALYPGSSDD 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1050 TFLERLFSHYGDREH---HSLLRKCAGPRQFVLHHLQGTNPVLYAVDGWVRHSREHPGIRNAVSLLQDSSREeinrlyig 1126
Cdd:cd01386   474 TFLERLFSHYGDKEGgkgHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE-------- 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1127 sltrgsgamvfcgsfaglegtqslrrvssirrsftTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCYLLQHNAGKHT 1206
Cdd:cd01386   546 -----------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDE 590
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1207 KYTANGspssaagqvSSEEEMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLAS---------NK 1277
Cdd:cd01386   591 RSTSSP---------AAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKklglnsevaDE 661
                         730       740
                  ....*....|....*....|....*...
gi 116008016 1278 DVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd01386   662 RKAVEELLEELDLEKSSYRIGLSQVFFR 689
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
575-1305 3.84e-112

Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276950 [Multi-domain]  Cd Length: 633  Bit Score: 371.92  E-value: 3.84e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKT-EDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd00124     1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  654 GRSGSGKSTSFKHALNYLA-LAAGAYNNFINA-----EKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIAS 727
Cdd:cd00124    81 GESGAGKTETTKLVLKYLAaLSGSGSSKSSSSassieQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  728 ASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDSHPFISLSQKL--EDRHRAANDFMRTVQAF 805
Cdd:cd00124   161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDYLNSSGCdrIDGVDDAEEFQELLDAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  806 ETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLSP 885
Cdd:cd00124   241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEA---LTTRTIKVGGETI 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  886 SKSPTSDTghewAWECLEALVIGLYSEALAAVVALINRQIC--TSSHTIASIMLIDTPGFQNPASCG-QQvgatladLRH 962
Cdd:cd00124   318 TKPLTVEQ----AEDARDALAKALYSRLFDWLVNRINAALSptDAAESTSFIGILDIFGFENFEVNSfEQ-------LCI 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  963 NYLQERLQMLFHHTTLVAPRDRYAQELVEIEMdlasechpgplISLIDKAPqnhVVrssqrDLREHDRRGMLWLLDEEAI 1042
Cdd:cd00124   387 NYANEKLQQFFNQHVFKLEQEEYEEEGIDWSF-----------IDFPDNQD---CL-----DLIEGKPLGILSLLDEECL 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1043 YPNSNDDTFLERLFSHYGDReHHSLLRKCAGPRQFVLHHLQGtnPVLYAVDGWVrhsrehpgIRNavsllQDSSREEINR 1122
Cdd:cd00124   448 FPKGTDATFLEKLYSAHGSH-PRFFSKKRKAKLEFGIKHYAG--DVTYDADGFL--------EKN-----KDTLPPDLVD 511
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1123 LyigsltrgsgamvfcgsfaglegtqsLRRVSSIRRSfttagvkrnsimlqvkftVDGIIDTLRRTGTHFVHCylLQHNA 1202
Cdd:cd00124   512 L--------------------------LRSGSQFRSQ------------------LDALMDTLNSTQPHFVRC--IKPND 545
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1203 GKhtkytangSPSsaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLAS----NKD 1278
Cdd:cd00124   546 EK--------KPG-----------LFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEkasdSKK 606
                         730       740
                  ....*....|....*....|....*..
gi 116008016 1279 VSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd00124   607 AAVLALLLLLKLDSSGYQLGKTKVFLR 633
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
556-1317 3.45e-109

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 364.94  E-value: 3.45e-109
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016    556 NSPALDLVEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQ 635
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016    636 TAYRSLVETRRDQSLIFMGRSGSGKSTSFKHALNYLAlAAGAYNNFINA--EKVNALCTILEAFGNTKTCLNSNATRMTQ 713
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLA-SVSGSNTEVGSveDQILESNPILEAFGNAKTLRNNNSSRFGK 159
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016    714 LLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLeniTSEDSHPFISLSQKLE---- 789
Cdd:smart00242  160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGL---KSPEDYRYLNQGGCLTvdgi 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016    790 -DrhraANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKlGTGSTARTQFANPTAARKASGLLGVNLEDLSS 868
Cdd:smart00242  237 dD----AEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEE-GRNDNAASTVKDKEELSNAAELLGVDPEELEK 311
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016    869 AafgLTqpnapngglspskSPTSDTGHEW---------AWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLID 939
Cdd:smart00242  312 A---LT-------------KRKIKTGGEVitkplnveqALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLD 375
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016    940 TPGFQNpascgqqvgatladLRH--------NYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDLASECHPGPLISLIDK 1011
Cdd:smart00242  376 IYGFEI--------------FEVnsfeqlciNYANEKLQQFFNQHVFKLEQEEYERE--GIDWTFIDFFDNQDCIDLIEK 439
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   1012 APQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSlLRKCAGPRQFVLHHLQGTnpVLYA 1091
Cdd:smart00242  440 KPP-----------------GILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFS-KPKKKGRTEFIIKHYAGD--VTYD 499
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   1092 VDGWVRHSREhPGIRNAVSLLQDSSreeiNRLyIGSLtrgsgamvfcgsFAGLEGTQSlrrvSSIRrsFTTAGVK-RNSi 1170
Cdd:smart00242  500 VTGFLEKNKD-TLSDDLIELLQSSK----NPL-IASL------------FPSGVSNAG----SKKR--FQTVGSQfKEQ- 554
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   1171 mLQVkftvdgIIDTLRRTGTHFVHCylLQHNAGKhtkytangspssAAGQVSSeeemvnvPLLRSQLRGSQVLEAARLHR 1250
Cdd:smart00242  555 -LNE------LMDTLNSTNPHFIRC--IKPNEEK------------KPGDFDS-------SLVLHQLRYLGVLENIRIRR 606
                           730       740       750       760       770       780       790
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116008016   1251 LGFPESVPLLEFVRRFGLLAGDLASNKDV----SVEQILAVNELDVASYRIGPSQILFRSGVLSELEAKRD 1317
Cdd:smart00242  607 AGFPYRLPFDEFLQRYRVLLPDTWPPWGGdakkACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
Myosin_head pfam00063
Myosin head (motor domain);
563-1305 2.10e-99

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 336.56  E-value: 2.10e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   563 VEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLV 642
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   643 ETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAG--AYNNFINAEKV----NAlctILEAFGNTKTCLNSNATRMTQLLS 716
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGsgSAGNVGRLEEQilqsNP---ILEAFGNAKTVRNNNSSRFGKYIE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   717 LDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSedshpFISLSQKLEDRHRAAN 796
Cdd:pfam00063  158 IQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKD-----YHYLSQSGCYTIDGID 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   797 D---FMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTArtQFANPTAARKASGLLGVNLEDLSSAafgL 873
Cdd:pfam00063  233 DseeFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQA--VPDDTENLQKAASLLGIDSTELEKA---L 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   874 TqpnapngglspskSPTSDTGHEW---------AWECLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGF 943
Cdd:pfam00063  308 C-------------KRRIKTGRETvskpqnveqANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASfIGVLDIYGF 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016   944 Q----NpaSCGQqvgatladLRHNYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDLASECHPGPLISLIDKAPqnhvvr 1019
Cdd:pfam00063  375 EifekN--SFEQ--------LCINYVNEKLQQFFNHHMFKLEQEEYVRE--GIEWTFIDFGDNQPCIDLIEKKP------ 436
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1020 ssqrdlrehdrRGMLWLLDEEAIYPNSNDDTFLERLFSHYGDrehHSLLRKcagPRQ-----FVLHHLQGTnpVLYAVDG 1094
Cdd:pfam00063  437 -----------LGILSLLDEECLFPKATDQTFLDKLYSTFSK---HPHFQK---PRLqgethFIIKHYAGD--VEYNVEG 497
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1095 WVRHSREhPGIRNAVSLLQDSSREEINRLYIGSLTRGSGAMVFCGSFAGLEGTQSlrrvssirrSFTTAGVK-RNSIMLq 1173
Cdd:pfam00063  498 FLEKNKD-PLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTPKRTKKK---------RFITVGSQfKESLGE- 566
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1174 vkftvdgIIDTLRRTGTHFVHCylLQHNAGKhtkytangspssAAGQVSSeeemvnvPLLRSQLRGSQVLEAARLHRLGF 1253
Cdd:pfam00063  567 -------LMKTLNSTNPHYIRC--IKPNEKK------------RAGVFDN-------SLVLHQLRCNGVLEGIRIRRAGF 618
                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016  1254 PESVPLLEFVRRFGLLAGDLASNKDVS----VEQILAVNELDVASYRIGPSQILFR 1305
Cdd:pfam00063  619 PNRITFQEFVQRYRILAPKTWPKWKGDakkgCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
541-2019 9.40e-98

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 348.99  E-value: 9.40e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  541 NGEQLTVDEDDVE--KQNSPALDLVEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMF 618
Cdd:COG5022    44 DGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSY 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  619 RGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINA--EKVNALCTILEA 696
Cdd:COG5022   124 SGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSieKQILATNPILEA 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  697 FGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENitSE 776
Cdd:COG5022   204 FGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQN--PK 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  777 DSHPFISLSQKLEDRHRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGStarTQFANPTAARKAS 856
Cdd:COG5022   282 DYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNGA---AIFSDNSVLDKAC 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  857 GLLGVNLEDLSSAafgLTQpnapngglspsksPTSDTGHEW---------AWECLEALVIGLYSEALAAVVALINRQICT 927
Cdd:COG5022   359 YLLGIDPSLFVKW---LVK-------------RQIKTGGEWivvplnleqALAIRDSLAKALYSNLFDWIVDRINKSLDH 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  928 SSHTIASIMLIDTPGFQ----NpascgqqvgaTLADLRHNYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDLAsECHPG 1003
Cdd:COG5022   423 SAAASNFIGVLDIYGFEifekN----------SFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKE--GIEWSFI-DYFDN 489
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1004 -PLISLIDKApqnhvvrssqrdlrehDRRGMLWLLDEEAIYPNSNDDTFLERLFSHYgdREHHSLLRKCAGPRQ--FVLH 1080
Cdd:COG5022   490 qPCIDLIEKK----------------NPLGILSLLDEECVMPHATDESFTSKLAQRL--NKNSNPKFKKSRFRDnkFVVK 551
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1081 HLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDSSREEINRLyigsltrgsgamvfcgsFAGLEGTQSLRRvssirrsF 1160
Cdd:COG5022   552 HYAGD--VEYDVEGFLDKNKD-PLNDDLLELLKASTNEFVSTL-----------------FDDEENIESKGR-------F 604
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1161 TTAGVKRNSIMLQvkftvdgIIDTLRRTGTHFVHCylLQHNAGKhtkytangspssaagqvssEEEMVNVPLLRSQLRGS 1240
Cdd:COG5022   605 PTLGSRFKESLNS-------LMSTLNSTQPHYIRC--IKPNEEK-------------------SPWTFDNQMVLSQLRCC 656
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1241 QVLEAARLHRLGFPESVPLLEFVRRFGLL------AGDLASNKDV--SVEQILAVNELDVASYRIGPSQILFRSGVLSEL 1312
Cdd:COG5022   657 GVLETIRISRAGFPSRWTFDEFVQRYRILspskswTGEYTWKEDTknAVKSILEELVIDSSKYQIGNTKVFFKAGVLAAL 736
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1313 EAKRDVLLSDRIIQLQAFCRGYLARKKMSQRRVQELAVRCIQRNVKAFLAVRDWPWWRLLVRVTPLLNVHRTEEQLKTAN 1392
Cdd:COG5022   737 EDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYL 816
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1393 EELLMLRAKLeKIECDRSEvkAENQKLEAKlSELTVDLAEERSTAHIATERLE-----AETAERLKLEK----ELGDQTN 1463
Cdd:COG5022   817 ACIIKLQKTI-KREKKLRE--TEEVEFSLK-AEVLIQKFGRSLKAKKRFSLLKketiyLQSAQRVELAErqlqELKIDVK 892
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1464 KVKNLQETTEKLEMELICAKSDLngiSEDEDAENEdgvgggvykLKYERVAReLEFTKRrlhtqhEHDLEQLVALKKHLe 1543
Cdd:COG5022   893 SISSLKLVNLELESEIIELKKSL---SSDLIENLE---------FKTELIAR-LKKLLN------NIDLEEGPSIEYVK- 952
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1544 mklsdaYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFdAECQSLQDAV-RQERQAKERYGRE 1622
Cdd:COG5022   953 ------LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL-AELSKQYGALqESTKQLKELPVEV 1025
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1623 KDVLQAEKFTLEQTLADTRL----DLEFK-EEKLASLQRELEEM------TFGGGTEEEFAQLRRSK----NETERRAKE 1687
Cdd:COG5022  1026 AELQSASKIISSESTELSILkplqKLKGLlLLENNQLQARYKALklrrenSLLDDKQLYQLESTENLlktiNVKDLEVTN 1105
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1688 QEEELDEMAGQIQLLEQAKLRLEmtletmrkearresQQRDEELEEVRGN-GYKKIKALECQLETEHEERTLLLREKHEL 1766
Cdd:COG5022  1106 RNLVKPANVLQFIVAQMIKLNLL--------------QEISKFLSQLVNTlEPVFQKLSVLQLELDGLFWEANLEALPSP 1171
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1767 ERRLSSMEDRDRvdrdaEEALnqklrrdlrkYKALLKDAQTQLERLKADTpgKTLIRQLRNqledaESARSLAMKARQTA 1846
Cdd:COG5022  1172 PPFAALSEKRLY-----QSAL----------YDEKSKLSSSEVNDLKNEL--IALFSKIFS-----GWPRGDKLKKLISE 1229
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1847 EAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEqINVSEAE---FKLNEM 1923
Cdd:COG5022  1230 GWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQY-INVGLFNalrTKASSL 1308
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1924 EAERNNLKEQVAEL------QHRLDNV-ENLgdPSMAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKL-- 1994
Cdd:COG5022  1309 RWKSATEVNYNSEElddwcrEFEISDVdEEL--EELIQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQNLKSRYDPAdk 1386
                        1530      1540
                  ....*....|....*....|....*
gi 116008016 1995 QNEVTQSKMREMQAQDVIKKSQKSL 2019
Cdd:COG5022  1387 ENNLPKEILKKIEALLIKQELQLSL 1411
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
575-1305 4.02e-91

class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276951 [Multi-domain]  Cd Length: 662  Bit Score: 311.71  E-value: 4.02e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd01377     1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNfiNAEKVNALCT----------ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQ 724
Cdd:cd01377    81 ESGAGKTENTKKVIQYLASVAASSKK--KKESGKKKGTledqilqanpILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  725 IASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENitSEDSHPFISLSQK----LEDrhraANDFMR 800
Cdd:cd01377   159 IAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTG--DPSYYFFLSQGELtidgVDD----AEEFKL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  801 TVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARtqFANPTAARKASGLLGVNLEDLSSAafgLTQPNapn 880
Cdd:cd01377   233 TDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAE--LDGTEEADKAAHLLGVNSSDLLKA---LLKPR--- 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  881 gglspSKsptsdTGHEW---------AWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----Npa 947
Cdd:cd01377   305 -----IK-----VGREWvtkgqnkeqVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN-- 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  948 SCGQqvgatladLRHNYLQERLQMLFHHTTLVAPRDRYAQElvEIE-------MDLAsechpgPLISLIDKAPQnhvvrs 1020
Cdd:cd01377   373 SFEQ--------LCINYTNEKLQQFFNHHMFVLEQEEYKKE--GIEwtfidfgLDLQ------PTIDLIEKPNM------ 430
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1021 sqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFS-HYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHS 1099
Cdd:cd01377   431 -----------GILSILDEECVFPKATDKTFVEKLYSnHLGKSKNFKKPKPKKSEAHFILKHYAGD--VEYNIDGWLEKN 497
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1100 REhPGIRNAVSLLQDSSREEINRL---YIGSLTRGSGAMVFCGSFaglegtqslRRVSSI-RRSFttagvkrNSIMlqvk 1175
Cdd:cd01377   498 KD-PLNENVVALLKKSSDPLVASLfkdYEESGGGGGKKKKKGGSF---------RTVSQLhKEQL-------NKLM---- 556
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1176 ftvdgiiDTLRRTGTHFVHCYLLQHN--AGKhtkytangspssaagqvsseeemVNVPLLRSQLRGSQVLEAARLHRLGF 1253
Cdd:cd01377   557 -------TTLRSTHPHFVRCIIPNEEkkPGK-----------------------IDAPLVLHQLRCNGVLEGIRICRKGF 606
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016 1254 PESVPLLEFVRRFGLLAGDLASNKDVS----VEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd01377   607 PNRIIFAEFKQRYSILAPNAIPKGFDDgkaaCEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
575-1305 3.50e-83

class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276952 [Multi-domain]  Cd Length: 673  Bit Score: 289.22  E-value: 3.50e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14920     1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAA----GAYNNFINAEKVNALCT---ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIAS 727
Cdd:cd14920    81 ESGAGKTENTKKVIQYLAHVAsshkGRKDHNIPGELERQLLQanpILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  728 ASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENItseDSHPFISLSQKLEDRHRAANDFMRTVQAFET 807
Cdd:cd14920   161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGF---NNYRFLSNGYIPIPGQQDKDNFQETMEAMHI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  808 LNIDAKAVRGIWSILAAIYHLGiaGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLSPSK 887
Cdd:cd14920   238 MGFSHEEILSMLKVVSSVLQFG--NISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRA---ILTPRIKVGRDYVQK 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  888 SPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGFQ----NpascgqqvgaTLADLRH 962
Cdd:cd14920   313 AQTK----EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFEifelN----------SFEQLCI 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  963 NYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEchpgPLISLIDKaPQNhvvrssqrdlrehdRRGMLWLLDE 1039
Cdd:cd14920   379 NYTNEKLQQLFNHTMFILEQEEYQREGIEwnfIDFGLDLQ----PCIDLIER-PAN--------------PPGVLALLDE 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1040 EAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDSSREE 1119
Cdd:cd14920   440 ECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGK--VDYKADEWLMKNMD-PLNDNVATLLHQSSDRF 516
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1120 INRLYigsltrgsgamvfcgsfAGLEGTQSLRRVSSIRRSFTTAGVKRNSIMLQV-----KFTVDGIIDTLRRTGTHFVH 1194
Cdd:cd14920   517 VAELW-----------------KDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTvgqlyKESLTKLMATLRNTNPNFVR 579
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1195 CYLLQHnagkhtkytangspSSAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGD-- 1272
Cdd:cd14920   580 CIIPNH--------------EKRAGKLDPH-------LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNai 638
                         730       740       750
                  ....*....|....*....|....*....|....*.
gi 116008016 1273 ---LASNKDVSVEQILAVnELDVASYRIGPSQILFR 1305
Cdd:cd14920   639 pkgFMDGKQACERMIRAL-ELDPNLYRIGQSKIFFR 673
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
575-1305 6.28e-81

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276876 [Multi-domain]  Cd Length: 674  Bit Score: 282.64  E-value: 6.28e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14911     1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAA-------------GAYNNFINAEKVNALCT---ILEAFGNTKTCLNSNATRMTQLLSLD 718
Cdd:cd14911    81 ESGAGKTENTKKVIQFLAYVAaskpkgsgavphpAVNPAVLIGELEQQLLQanpILEAFGNAKTVKNDNSSRFGKFIRIN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  719 FDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITsedSHPFISLSQKLEDRHRAANDF 798
Cdd:cd14911   161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVK---SYAFLSNGSLPVPGVDDYAEF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  799 MRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTArtQFANPTAARKASGLLGVNLEDLSSAafgLTQPNA 878
Cdd:cd14911   238 QATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQA--TLPDNTVAQKIAHLLGLSVTDMTRA---FLTPRI 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  879 PNGGLSPSKSPTSDTgHEWAwecLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGFQ----Npascgqqv 953
Cdd:cd14911   313 KVGRDFVTKAQTKEQ-VEFA---VEAIAKACYERMFKWLVNRINRSLDRTKRQGASfIGILDMAGFEifelN-------- 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  954 gaTLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIE-MDLASECHpgPLISLIDKApqnhvvrssqrdlrehdrRG 1032
Cdd:cd14911   381 --SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKfIDFGLDLQ--PTIDLIDKP------------------GG 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1033 MLWLLDEEAIYPNSNDDTFLERLFSHYGdrEHHSLLRK-CAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSL 1111
Cdd:cd14911   439 IMALLDEECWFPKATDKTFVDKLVSAHS--MHPKFMKTdFRGVADFAIVHYAGR--VDYSAAKWLMKNMD-PLNENIVSL 513
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1112 LQDSSREEINRLYIGSLTRGSGAmvfcgsfAGLEGTQSLRRvssirrsfTTAGVKRNSIMLqVKFTVDGIIDTLRRTGTH 1191
Cdd:cd14911   514 LQGSQDPFVVNIWKDAEIVGMAQ-------QALTDTQFGAR--------TRKGMFRTVSHL-YKEQLAKLMDTLRNTNPN 577
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1192 FVHCYLLQHN--AGKhtkytangspssaagqvsseeemVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLL 1269
Cdd:cd14911   578 FVRCIIPNHEkrAGK-----------------------IDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 634
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|
gi 116008016 1270 AGDLAS----NKDVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14911   635 TPNVIPkgfmDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
575-1305 5.23e-78

class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276895 [Multi-domain]  Cd Length: 676  Bit Score: 273.83  E-value: 5.23e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14932     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNfiNAEKVNALCT-------------ILEAFGNTKTCLNSNATRMTQLLSLDFDQ 721
Cdd:cd14932    81 ESGAGKTENTKKVIQYLAYVASSFKT--KKDQSSIALShgelekqllqanpILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  722 TGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITsedSHPFISLSQKLEDRHRAANDFMRT 801
Cdd:cd14932   159 NGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYS---KYRFLSNGNVTIPGQQDKELFAET 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  802 VQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKlgTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNG 881
Cdd:cd14932   236 MEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKK--ERNSDQASMPDDTAAQKVCHLLGMNVTDFTRA---ILSPRIKVG 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  882 GLSPSKSPTsdtgHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGFQ----NpascgqqvgaT 956
Cdd:cd14932   311 RDYVQKAQT----QEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFEifelN----------S 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  957 LADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIE-MDLASECHpgPLISLIDKApqnhvvrssqrdlreHDRRGMLW 1035
Cdd:cd14932   377 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSfIDFGLDLQ--PCIELIEKP---------------NGPPGILA 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1036 LLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDS 1115
Cdd:cd14932   440 LLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDADFCIIHYAGK--VDYKANEWLMKNMD-PLNENVATLLNQS 516
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1116 SREeinrlYIGSLTRGSGAMVFCGSFAGLEgtqslrrvSSIRRSFTTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHC 1195
Cdd:cd14932   517 TDK-----FVSELWKDVDRIVGLDKVAGMG--------ESLHGAFKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRC 583
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1196 YLLQHnagkhtkytangspSSAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGD--- 1272
Cdd:cd14932   584 IIPNH--------------EKKAGKLAHH-------LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNaip 642
                         730       740       750
                  ....*....|....*....|....*....|....*
gi 116008016 1273 --LASNKDVSVEQILAVnELDVASYRIGPSQILFR 1305
Cdd:cd14932   643 kgFMDGKQACVLMVKAL-ELDPNLYRIGQSKVFFR 676
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
575-1305 8.50e-75

class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276885 [Multi-domain]  Cd Length: 673  Bit Score: 264.57  E-value: 8.50e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14921     1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAA----GAYNNFINAEKVNALCT---ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIAS 727
Cdd:cd14921    81 ESGAGKTENTKKVIQYLAVVAsshkGKKDTSITGELEKQLLQanpILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  728 ASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSED--SHPFISLSQKLEDRHraandFMRTVQAF 805
Cdd:cd14921   161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTflSNGFVPIPAAQDDEM-----FQETLEAM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  806 ETLNIDAKAVRGIWSILAAIYHLGIAGVTKlgTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLSP 885
Cdd:cd14921   236 SIMGFSEEEQLSILKVVSSVLQLGNIVFKK--ERNTDQASMPDNTAAQKVCHLMGINVTDFTRS---ILTPRIKVGRDVV 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  886 SKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIM-LIDTPGFQNPAScgqqvgATLADLRHNY 964
Cdd:cd14921   311 QKAQTK----EQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFEIFEV------NSFEQLCINY 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  965 LQERLQMLFHHTTLVAPRDRYAQELVEIE-MDLASECHpgPLISLIDkapqnhvvrssqrdlREHDRRGMLWLLDEEAIY 1043
Cdd:cd14921   381 TNEKLQQLFNHTMFILEQEEYQREGIEWNfIDFGLDLQ--PCIELIE---------------RPNNPPGVLALLDEECWF 443
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1044 PNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDSSREeinrl 1123
Cdd:cd14921   444 PKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSIIHYAGK--VDYNASAWLTKNMD-PLNDNVTSLLNASSDK----- 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1124 YIGSLTRGSGAMVfcgsfaGLEGTQSLRRVSSIRRSFTTAGVKRNSIMLqVKFTVDGIIDTLRRTGTHFVHCYLLQHnag 1203
Cdd:cd14921   516 FVADLWKDVDRIV------GLDQMAKMTESSLPSASKTKKGMFRTVGQL-YKEQLGKLMTTLRNTTPNFVRCIIPNH--- 585
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1204 khtkytangspSSAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGD-----LASNKD 1278
Cdd:cd14921   586 -----------EKRSGKLDAF-------LVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANaipkgFMDGKQ 647
                         730       740
                  ....*....|....*....|....*..
gi 116008016 1279 VSVEQILAVnELDVASYRIGPSQILFR 1305
Cdd:cd14921   648 ACILMIKAL-ELDPNLYRIGQSKIFFR 673
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
576-1305 2.80e-73

class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276834  Cd Length: 647  Bit Score: 259.17  E-value: 2.80e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRgcKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd01383     2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  656 SGSGKSTSFKHALNYLAlAAGAYNNFINAEKVNALCtILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLP 735
Cdd:cd01383    80 SGAGKTETAKIAMQYLA-ALGGGSSGIENEILQTNP-ILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  736 ERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELhleNITSEDSHPFISLSQKLE-DRHRAANDFMRTVQAFETLNIDAKA 814
Cdd:cd01383   158 EKSRVVQLANGERSYHIFYQLCAGASPALREKL---NLKSASEYKYLNQSNCLTiDGVDDAKKFHELKEALDTVGISKED 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  815 VRGIWSILAAIYHLGiaGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLSPSKSPTsdtg 894
Cdd:cd01383   235 QEHIFQMLAAVLWLG--NISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLA---LSTRKIQAGGDKIVKKLT---- 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  895 HEWAWECLEALVIGLYSEALAAVVALINRQICTSSH-TIASIMLIDTPGFQ----NpascgqqvgaTLADLRHNYLQERL 969
Cdd:cd01383   306 LQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRrTGRSISILDIYGFEsfqkN----------SFEQLCINYANERL 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  970 QMLFHHTTLVAPRDRYAQELVE---IEMDLASEChpgplISLIDKAPQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNS 1046
Cdd:cd01383   376 QQHFNRHLFKLEQEEYELDGIDwtkVDFEDNQEC-----LDLIEKKPL-----------------GLISLLDEESNFPKA 433
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1047 NDDTFLERLFSH-------YGDREhhsllrkcagpRQFVLHHLQGTnpVLYAVDGWVRHSRE--HPGIrnaVSLLQDSSr 1117
Cdd:cd01383   434 TDLTFANKLKQHlksnscfKGERG-----------GAFTIRHYAGE--VTYDTSGFLEKNRDllHSDL---IQLLSSCS- 496
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1118 eeinrlyiGSLTRgsgamvfcgSFAGLEGTQSLRRVSSIRRSftTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCyl 1197
Cdd:cd01383   497 --------CQLPQ---------LFASKMLDASRKALPLTKAS--GSDSQKQSVATKFKGQLFKLMQRLENTTPHFIRC-- 555
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1198 lqhnagkhTKYTANGSPSsaagqvSSEEEMVnvpllRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLASNK 1277
Cdd:cd01383   556 --------IKPNNKQLPG------VFDQDLV-----LQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSAS 616
                         730       740       750
                  ....*....|....*....|....*....|....
gi 116008016 1278 D------VSVEQILAVNEldvASYRIGPSQILFR 1305
Cdd:cd01383   617 QdplstsVAILQQFNILP---EMYQVGYTKLFFR 647
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
575-1305 3.53e-73

class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276883 [Multi-domain]  Cd Length: 670  Bit Score: 259.64  E-value: 3.53e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14919     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALC----TILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASL 730
Cdd:cd14919    81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLlqanPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  731 QVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLEnitSEDSHPFISLSQKLEDRHRAANDFMRTVQAFETLNI 810
Cdd:cd14919   161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE---PYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  811 DAKAVRGIWSILAAIYHLGIAGVTKlgTGSTARTQFANPTAARKASGLLGVNLEDLSSaafGLTQPNAPNGGLSPSKSPT 890
Cdd:cd14919   238 PEEEQMGLLRVISGVLQLGNIVFKK--ERNTDQASMPDNTAAQKVSHLLGINVTDFTR---GILTPRIKVGRDYVQKAQT 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  891 SdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGFQnpascgqqvgatLADLRH------N 963
Cdd:cd14919   313 K----EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILDIAGFE------------IFDLNSfeqlciN 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  964 YLQERLQMLFHHTTLVAPRDRYAQELVEIE-MDLASECHpgPLISLIDKAPqnhvvrssqrdlrehDRRGMLWLLDEEAI 1042
Cdd:cd14919   377 YTNEKLQQLFNHTMFILEQEEYQREGIEWNfIDFGLDLQ--PCIDLIEKPA---------------GPPGILALLDEECW 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1043 YPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDSSREeinr 1122
Cdd:cd14919   440 FPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCIIHYAGK--VDYKADEWLMKNMD-PLNDNIATLLHQSSDK---- 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1123 lYIGSLTRGSGAMVFCGSFAGLEGTQSLRRVSSIRRSFTTAGvkrnsimLQVKFTVDGIIDTLRRTGTHFVHCYLLQHna 1202
Cdd:cd14919   513 -FVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVG-------QLYKEQLAKLMATLRNTNPNFVRCIIPNH-- 582
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1203 gkhtkytangspSSAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGD-----LASNK 1277
Cdd:cd14919   583 ------------EKKAGKLDPH-------LVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNsipkgFMDGK 643
                         730       740
                  ....*....|....*....|....*...
gi 116008016 1278 DVSVEQILAVnELDVASYRIGPSQILFR 1305
Cdd:cd14919   644 QACVLMIKAL-ELDSNLYRIGQSKVFFR 670
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
575-1305 1.30e-70

class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276899 [Multi-domain]  Cd Length: 675  Bit Score: 251.91  E-value: 1.30e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd15896     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAY------NNFINA-----EKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTG 723
Cdd:cd15896    81 ESGAGKTENTKKVIQYLAHVASSHktkkdqNSLALShgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  724 QIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENItseDSHPFISLSQKLEDRHRAANDFMRTVQ 803
Cdd:cd15896   161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENY---NNYRFLSNGNVTIPGQQDKDLFTETME 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  804 AFETLNIDAKAVRGIWSILAAIYHLGIAGVTKlgTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGL 883
Cdd:cd15896   238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKK--ERHTDQASMPDNTAAQKVCHLMGMNVTDFTRA---ILSPRIKVGRD 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  884 SPSKSPTsdtgHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGFQNPAScgqqvgATLADLRH 962
Cdd:cd15896   313 YVQKAQT----QEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFEIFEL------NSFEQLCI 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  963 NYLQERLQMLFHHTTLVAPRDRYAQELVEIE-MDLASECHpgPLISLIDKAPQNhvvrssqrdlrehdrRGMLWLLDEEA 1041
Cdd:cd15896   383 NYTNEKLQQLFNHTMFILEQEEYQREGIEWSfIDFGLDLQ--PCIDLIEKPASP---------------PGILALLDEEC 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1042 IYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDSSREEIN 1121
Cdd:cd15896   446 WFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEADFCIIHYAGK--VDYKADEWLMKNMD-PLNDNVATLLNQSTDKFVS 522
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1122 RLY-----IGSLTRGSGAMVFCGSFAGLEGTqslrrvssirrsFTTAGvkrnsimLQVKFTVDGIIDTLRRTGTHFVHCY 1196
Cdd:cd15896   523 ELWkdvdrIVGLDKVSGMSEMPGAFKTRKGM------------FRTVG-------QLYKEQLSKLMATLRNTNPNFVRCI 583
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1197 LLQHnagkhtkytangspSSAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGD---- 1272
Cdd:cd15896   584 IPNH--------------EKKAGKLDPH-------LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNaipk 642
                         730       740       750
                  ....*....|....*....|....*....|....
gi 116008016 1273 -LASNKDVSVEQILAVnELDVASYRIGPSQILFR 1305
Cdd:cd15896   643 gFMDGKQACVLMIKSL-ELDPNLYRIGQSKVFFR 675
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
575-1305 8.67e-66

class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276893 [Multi-domain]  Cd Length: 670  Bit Score: 237.69  E-value: 8.67e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14930     1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAA----GAYNNFINAEKVNALCT---ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIAS 727
Cdd:cd14930    81 ESGAGKTENTKKVIQYLAHVAsspkGRKEPGVPGELERQLLQanpILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  728 ASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSE---DSHPFISLSQKLEdrhraanDFMRTVQA 804
Cdd:cd14930   161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYrflTNGPSSSPGQERE-------LFQETLES 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  805 FETLNIDAKAVRGIWSILAAIYHLGIAGVTKlgTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLS 884
Cdd:cd14930   234 LRVLGFSHEEITSMLRMVSAVLQFGNIVLKR--ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRA---LLTPRIKVGRDY 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  885 PSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIM-LIDTPGFQNpascgQQVGaTLADLRHN 963
Cdd:cd14930   309 VQKAQTK----EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFEI-----FQLN-SFEQLCIN 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  964 YLQERLQMLFHHTTLVAPRDRYAQE-----LVEIEMDLAsechpgPLISLIDkapqnhvvrssqrdlREHDRRGMLWLLD 1038
Cdd:cd14930   379 YTNEKLQQLFNHTMFVLEQEEYQREgipwtFLDFGLDLQ------PCIDLIE---------------RPANPPGLLALLD 437
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1039 EEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDSSRE 1118
Cdd:cd14930   438 EECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVLHYAGK--VDYKANEWLMKNMD-PLNDNVAALLHQSTDR 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1119 EINRLYigsltrgsgamvfcgsfAGLEGTQSLRRVSSIRRSfTTAGVKRNSIMLQV----KFTVDGIIDTLRRTGTHFVH 1194
Cdd:cd14930   515 LTAEIW-----------------KDVEGIVGLEQVSSLGDG-PPGGRPRRGMFRTVgqlyKESLSRLMATLSNTNPSFVR 576
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1195 CYLLQHnagkhtkytangspSSAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLA 1274
Cdd:cd14930   577 CIVPNH--------------EKRAGKLEPR-------LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 635
                         730       740       750
                  ....*....|....*....|....*....|....*
gi 116008016 1275 S----NKDVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14930   636 PkgfmDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
575-1305 2.31e-63

class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276839  Cd Length: 644  Bit Score: 229.66  E-value: 2.31e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14872     1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNFinAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLL 734
Cdd:cd14872    81 ESGAGKTEATKQCLSFFAEVAGSTNGV--EQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  735 PERQRAGRRLGHEHSFHIMTRLLAGAAGllqkeLHLENITSEDSHPFISLSQKLEDRH-RAANDFMRTVQAFETLNIDAK 813
Cdd:cd14872   159 LEKSRVVYQIKGERNFHIFYQLLASPDP-----ASRGGWGSSAAYGYLSLSGCIEVEGvDDVADFEEVVLAMEQLGFDDA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  814 AVRGIWSILAAIYHLGIAGVTKLGTGSTARTQ-FANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLSPSKSPTSD 892
Cdd:cd14872   234 DINNVMSLIAAILKLGNIEFASGGGKSLVSGStVANRDVLKEVATLLGVDAATLEEA---LTSRLMEIKGCDPTRIPLTP 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  893 tghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGFQ--NPASCGQqvgatladLRHNYLQERL 969
Cdd:cd14872   311 ---AQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTfIGVLDIFGFEifEKNSFEQ--------LCINFTNEKL 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  970 QMLFHHTTLVAPRDRYAQELVEIEmdlasecHpgplISLIDKAPqnhVVrssqrDLREHDRRGMLWLLDEEAIYPNSNDD 1049
Cdd:cd14872   380 QQHFNQYTFKLEEALYQSEGVKFE-------H----IDFIDNQP---VL-----DLIEKKQPGLMLALDDQVKIPKGSDA 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1050 TFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRhsrehpgiRNAVSLLQDssreeinrLYIgsLT 1129
Cdd:cd14872   441 TFMIAANQTHAAKSTFVYAEVRTSRTEFIVKHYAGD--VTYDITGFLE--------KNKDTLQKD--------LYV--LL 500
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1130 RGSGAMVFCGSFAGLEGTQSLRRVssirrsfTTAGvkrnsimlQVKFTVDGIIDTLRRTGTHFVHCylLQHNAGKHtkyt 1209
Cdd:cd14872   501 SSSKNKLIAVLFPPSEGDQKTSKV-------TLGG--------QFRKQLSALMTALNATEPHYIRC--VKPNQEKR---- 559
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1210 angsPSSAAGQVSSEeemvnvpllrsQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLL----AGDLASNKDVSVEQIL 1285
Cdd:cd14872   560 ----ARLFDGFMSLE-----------QLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLvktiAKRVGPDDRQRCDLLL 624
                         730       740
                  ....*....|....*....|
gi 116008016 1286 AVNELDVASYRIGPSQILFR 1305
Cdd:cd14872   625 KSLKQDFSKVQVGKTRVLYR 644
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
576-1305 2.35e-63

class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276878 [Multi-domain]  Cd Length: 668  Bit Score: 230.32  E-value: 2.35e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd14913     2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  656 SGSGKSTSFKHALNYLALAAgAYNNFINAEKVNALCT----------ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQI 725
Cdd:cd14913    82 SGAGKTVNTKRVIQYFATIA-ATGDLAKKKDSKMKGTledqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  726 ASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenITSEDSHPFISLSQKLEDRHRAANDFMRTVQAF 805
Cdd:cd14913   161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLI--TTNPYDYPFISQGEILVASIDDAEELLATDSAI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  806 ETLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSAafgLTQPNAPNGG 882
Cdd:cd14913   239 DILGFTPEEKSGLYKLTGAVMHYG-----NMKFKQKQREEQAEPDGtevADKTAYLMGLNSSDLLKA---LCFPRVKVGN 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  883 LSPSKSPTSDTGHewawECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTLA 958
Cdd:cd14913   311 EYVTKGQTVDQVH----HAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEifeyN----------SLE 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  959 DLRHNYLQERLQMLFHHTTLVAPRDRYAQE-----LVEIEMDLASeChpgplISLIDKApqnhvvrssqrdlrehdrRGM 1033
Cdd:cd14913   377 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEgiewtFIDFGMDLAA-C-----IELIEKP------------------MGI 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1034 LWLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVS 1110
Cdd:cd14913   433 FSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRAEahFSLIHYAGT--VDYSVSGWLEKNKD-PLNETVVG 509
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1111 LLQDSSREEINRLYigsltrgsgamvfcGSFAGLEGTQSLRRVSSIR-RSF-TTAGVKRNSImlqvkftvDGIIDTLRRT 1188
Cdd:cd14913   510 LYQKSSNRLLAHLY--------------ATFATADADSGKKKVAKKKgSSFqTVSALFRENL--------NKLMSNLRTT 567
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1189 GTHFVHCYLlqhnagkhtkytANGSPSSAAgqvsseeemVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGL 1268
Cdd:cd14913   568 HPHFVRCII------------PNETKTPGA---------MEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRV 626
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|...
gi 116008016 1269 L------AGDLASNKDvSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14913   627 LnasaipEGQFIDSKK-ACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
575-1305 3.64e-60

class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276892 [Multi-domain]  Cd Length: 662  Bit Score: 220.62  E-value: 3.64e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14929     1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNF----INAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASL 730
Cdd:cd14929    81 ESGAGKTVNTKHIIQYFATIAAMIESKkklgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  731 QVLLPERQRAGRRLGHEHSFHIMTRLLAGaagllQKELHLENITSEDSHPFISLS------QKLEDrhraANDFMRTVQA 804
Cdd:cd14929   161 DIYLLEKSRVIFQQPGERNYHIFYQILSG-----KKELRDLLLVSANPSDFHFCScgavavESLDD----AEELLATEQA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  805 FETLNIDAKAVRGIWSILAAIYHLgiaGVTKLGTGSTARTQFANPTA-ARKASGLLGVNLEDLSSaafGLTQPNAPNGGL 883
Cdd:cd14929   232 MDILGFLPDEKYGCYKLTGAIMHF---GNMKFKQKPREEQLEADGTEnADKAAFLMGINSSELVK---GLIHPRIKVGNE 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  884 SPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTLAD 959
Cdd:cd14929   306 YVTRSQNI----EQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEildyN----------SLEQ 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  960 LRHNYLQERLQMLFHHTTLVAPRDRYAQELVE-IEMDLASECHpgPLISLIDKApqnhvvrssqrdlrehdrRGMLWLLD 1038
Cdd:cd14929   372 LCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDwVSIDFGLDLQ--ACIDLIEKP------------------MGIFSILE 431
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1039 EEAIYPNSNDDTFLERLF-SHYGDREHhslLRKCAGPRQ-----FVLHHLQGTNPvlYAVDGWVRHSRehpGIRN--AVS 1110
Cdd:cd14929   432 EECMFPKATDLTFKTKLFdNHFGKSVH---FQKPKPDKKkfeahFELVHYAGVVP--YNISGWLEKNK---DLLNetVVA 503
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1111 LLQDSSREEINRLYIGSLTRGSgAMVFcGSFAGLEGTqSLRRVSSIRrsfttagvkrnsimlqvKFTVDGIIDTLRRTGT 1190
Cdd:cd14929   504 VFQKSSNRLLASLFENYISTDS-AIQF-GEKKRKKGA-SFQTVASLH-----------------KENLNKLMTNLKSTAP 563
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1191 HFVHCYllqhNAGKhtkytaNGSPSsaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLL- 1269
Cdd:cd14929   564 HFVRCI----NPNV------NKIPG-----------VLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILn 622
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|.
gi 116008016 1270 -----AGDLASNKDVSvEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14929   623 prtfpKSKFVSSRKAA-EELLGSLEIDHTQYRFGITKVFFK 662
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
575-1277 1.21e-59

class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276866 [Multi-domain]  Cd Length: 655  Bit Score: 218.89  E-value: 1.21e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMF------RGCKTEDMPPHVYSLAQTAYRSLVETRR-- 646
Cdd:cd14901     1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  647 --DQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINA-------EKVNALCTILEAFGNTKTCLNSNATRMTQLLSL 717
Cdd:cd14901    81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNAterenvrDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  718 DFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAgllQKELHLENITSEDSHPFISLSQKLeDRHRAAND 797
Cdd:cd14901   161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGAS---SDELHALGLTHVEEYKYLNSSQCY-DRRDGVDD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  798 ---FMRTVQAFETLNIDAKAVRGIWSILAAIYHLG-IAGVTKLGTGSTarTQFANPTAARKASGLLGVNLEDLSSaafGL 873
Cdd:cd14901   237 svqYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGnLCFVKKDGEGGT--FSMSSLANVRAACDLLGLDMDVLEK---TL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  874 TQPNAPNGG------LSPSKSPTSDtghewaweclEALVIGLYSEALAAVVALINRQICTSSHTIAS--IMLIDTPGFQN 945
Cdd:cd14901   312 CTREIRAGGeyitmpLSVEQALLTR----------DVVAKTLYAQLFDWLVDRINESIAYSESTGASrfIGIVDIFGFEI 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  946 PAScgqqvgATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVeiemdlasechPGPLISLidkaPQNHVVRSsqrdL 1025
Cdd:cd14901   382 FAT------NSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAI-----------PWTFVEY----PNNDACVA----M 436
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1026 REHDRRGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREHPGi 1105
Cdd:cd14901   437 FEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGA--VCYATDGFCDKNKDHVH- 513
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1106 RNAVSLLQDSSREeinrlYIGSltrgsgamvfcgsfaglegtqslrrvssirrsfttagvkrnSIMLQVKFTVDGIIDTL 1185
Cdd:cd14901   514 SEALALLRTSSNA-----FLSS-----------------------------------------TVVAKFKVQLSSLLEVL 547
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1186 RRTGTHFVHCYllqhnagkhtkytangSPSSAAgqvsSEEEMvNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRR 1265
Cdd:cd14901   548 NATEPHFIRCI----------------KPNDVL----SPSEF-DAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHT 606
                         730
                  ....*....|..
gi 116008016 1266 FGLLAGDLASNK 1277
Cdd:cd14901   607 YSCLAPDGASDT 618
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
576-1305 2.79e-57

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276877 [Multi-domain]  Cd Length: 673  Bit Score: 212.28  E-value: 2.79e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd14912     2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  656 SGSGKSTSFKHALNYLA------------LAAGAYNNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTG 723
Cdd:cd14912    82 SGAGKTVNTKRVIQYFAtiavtgekkkeeITSGKMQGTLEDQIISA-NPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  724 QIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenITSEDSHPFISLSQKLEDRHRAANDFMRTVQ 803
Cdd:cd14912   161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLI--TTNPYDYPFVSQGEISVASIDDQEELMATDS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  804 AFETLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSAafgLTQPNAPN 880
Cdd:cd14912   239 AIDILGFTNEEKVSIYKLTGAVMHYG-----NLKFKQKQREEQAEPDGtevADKAAYLQSLNSADLLKA---LCYPRVKV 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  881 GGLSPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaT 956
Cdd:cd14912   311 GNEYVTKGQTV----EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEifdfN----------S 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  957 LADLRHNYLQERLQMLFHHTTLVAPRDRYAQE-----LVEIEMDLASechpgpLISLIDKApqnhvvrssqrdlrehdrR 1031
Cdd:cd14912   377 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEgiewtFIDFGMDLAA------CIELIEKP------------------M 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1032 GMLWLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNA 1108
Cdd:cd14912   433 GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKGKAEahFSLIHYAGV--VDYNITGWLDKNKD-PLNETV 509
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1109 VSLLQDSSREEINRLYIGSLT-RGSGAmvfcGSFA---GLEGTQSLRRVSSIRRSfttagvkrnsimlqvkfTVDGIIDT 1184
Cdd:cd14912   510 VGLYQKSAMKTLAYLFSGAQTaEGASA----GGGAkkgGKKKGSSFQTVSALFRE-----------------NLNKLMTN 568
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1185 LRRTGTHFVHCYLlqhnagkhtkytangsPSSAAGQVSSEEEMVnvpllRSQLRGSQVLEAARLHRLGFPESVPLLEFVR 1264
Cdd:cd14912   569 LRSTHPHFVRCII----------------PNETKTPGAMEHELV-----LHQLRCNGVLEGIRICRKGFPSRILYADFKQ 627
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*..
gi 116008016 1265 RFGLL------AGDLASNKDVSvEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14912   628 RYKVLnasaipEGQFIDSKKAS-EKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
575-1305 1.74e-56

class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276953 [Multi-domain]  Cd Length: 676  Bit Score: 210.20  E-value: 1.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14927     1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCT-------------ILEAFGNTKTCLNSNATRMTQLLSLDFDQ 721
Cdd:cd14927    81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTggtledqiieanpAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  722 TGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELhLENITSEDSHpFISLSQKLEDRHRAANDFMRT 801
Cdd:cd14927   161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML-LVSMNPYDYH-FCSQGVTTVDNMDDGEELMAT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  802 VQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQfaNPTAARKASGLLGVNLEDLSSaafGLTQPNAPNG 881
Cdd:cd14927   239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAD--GTESADKAAYLMGVSSADLLK---GLLHPRVKVG 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  882 GLSPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTL 957
Cdd:cd14927   314 NEYVTKGQSV----EQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEifefN----------SF 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  958 ADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEchpgPLISLIDKApqnhvvrssqrdlrehdrRGML 1034
Cdd:cd14927   380 EQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEwvfIDFGLDLQ----ACIDLIEKP------------------LGIL 437
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1035 WLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLH----HLQGTNPvlYAVDGWVRHSREhPGIRNAVS 1110
Cdd:cd14927   438 SILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKYEAHfevvHYAGVVP--YNIVGWLDKNKD-PLNETVVA 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1111 LLQDSSREEINRL---YIGSLTRGSGAmvfcgsfaglEGTQSLRRVSSirrSFTTAGvkrnsimlQV-KFTVDGIIDTLR 1186
Cdd:cd14927   515 IFQKSQNKLLATLyenYVGSDSTEDPK----------SGVKEKRKKAA---SFQTVS--------QLhKENLNKLMTNLR 573
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1187 RTGTHFVHCYLLQHNAgkhtkytangSPSsaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRF 1266
Cdd:cd14927   574 ATQPHFVRCIIPNETK----------TPG-----------VMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRY 632
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....
gi 116008016 1267 GLL-----AGDLASNKDVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14927   633 RILnpsaiPDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
576-1305 3.75e-56

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276875 [Multi-domain]  Cd Length: 671  Bit Score: 208.82  E-value: 3.75e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd14910     2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  656 SGSGKSTSFKHALNYLA------------LAAGAYNNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTG 723
Cdd:cd14910    82 SGAGKTVNTKRVIQYFAtiavtgekkkeeATSGKMQGTLEDQIISA-NPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  724 QIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenITSEDSHPFISLSQKLEDRHRAANDFMRTVQ 803
Cdd:cd14910   161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLI--TTNPYDYAFVSQGEITVPSIDDQEELMATDS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  804 AFETLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSAafgLTQPNAPN 880
Cdd:cd14910   239 AIEILGFTSDERVSIYKLTGAVMHYG-----NMKFKQKQREEQAEPDGtevADKAAYLQNLNSADLLKA---LCYPRVKV 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  881 GGLSPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaT 956
Cdd:cd14910   311 GNEYVTKGQTV----QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEifdfN----------S 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  957 LADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIE-----MDLASechpgpLISLIDKApqnhvvrssqrdlrehdrR 1031
Cdd:cd14910   377 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEfidfgMDLAA------CIELIEKP------------------M 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1032 GMLWLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNA 1108
Cdd:cd14910   433 GIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPAKGKVEahFSLIHYAGT--VDYNIAGWLDKNKD-PLNETV 509
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1109 VSLLQDSSREEINRLYIGSltRGSGAMVFCGSFAGLEGTQSLRRVSSIRRSfttagvkrnsimlqvkfTVDGIIDTLRRT 1188
Cdd:cd14910   510 VGLYQKSSMKTLALLFSGA--AAAEAEEGGGKKGGKKKGSSFQTVSALFRE-----------------NLNKLMTNLRST 570
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1189 GTHFVHCYLlqhnagkhtkytangsPSSAAGQVSSEEEMVnvpllRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGL 1268
Cdd:cd14910   571 HPHFVRCII----------------PNETKTPGAMEHELV-----LHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|...
gi 116008016 1269 L------AGDLASNKDVSvEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14910   630 LnasaipEGQFIDSKKAS-EKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
576-1305 3.98e-56

class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276887 [Multi-domain]  Cd Length: 671  Bit Score: 208.77  E-value: 3.98e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd14923     2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  656 SGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCT----------ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQI 725
Cdd:cd14923    82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQGTledqiiqanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  726 ASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLEniTSEDSHPFISLSQKLEDRHRAANDFMRTVQAF 805
Cdd:cd14923   162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIS--TNPFDFPFVSQGEVTVASIDDSEELLATDNAI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  806 ETLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSaafGLTQPNAPNGg 882
Cdd:cd14923   240 DILGFSSEEKVGIYKLTGAVMHYG-----NMKFKQKQREEQAEPDGtevADKAGYLMGLNSAEMLK---GLCCPRVKVG- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  883 lspSKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTLA 958
Cdd:cd14923   311 ---NEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEifdfN----------SLE 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  959 DLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIE-----MDLASechpgpLISLIDKApqnhvvrssqrdlrehdrRGM 1033
Cdd:cd14923   378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEfidfgMDLAA------CIELIEKP------------------MGI 433
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1034 LWLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVS 1110
Cdd:cd14923   434 FSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGKAEahFSLVHYAGT--VDYNIAGWLDKNKD-PLNETVVG 510
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1111 LLQDSSREEINRLYigsltrgsgamvfcGSFAGLEGTQSlrrvSSIRRSFTTAGVKRNSIMLQVKFTVDGIIDTLRRTGT 1190
Cdd:cd14923   511 LYQKSSLKLLSFLF--------------SNYAGAEAGDS----GGSKKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHP 572
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1191 HFVHCYLlqhnaGKHTKytangSPSsaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLL- 1269
Cdd:cd14923   573 HFVRCLI-----PNETK-----TPG-----------VMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILn 631
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|.
gi 116008016 1270 -----AGDLASNKDVSvEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14923   632 asaipEGQFIDSKNAS-EKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
575-1305 6.33e-56

class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276896 [Multi-domain]  Cd Length: 659  Bit Score: 207.96  E-value: 6.33e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14934     1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNFINA-----EKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASAS 729
Cdd:cd14934    81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGkgsleDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  730 LQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenITSEDSHPFISLSQKLEDRHRAANDFMRTVQAFETLN 809
Cdd:cd14934   161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLL--VPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  810 IDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFAN---PTAARKASGLLGVNLEDLSSaafGLTQPNAPNGGLSPS 886
Cdd:cd14934   239 FSAEEKIGVYKLTGGIMHFG-----NMKFKQKPREEQAEvdtTEVADKVAHLMGLNSGELQK---GITRPRVKVGNEFVQ 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  887 KSPTSDTGHewawECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTLADLRH 962
Cdd:cd14934   311 KGQNMEQCN----NSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEifefN----------SFEQLCI 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  963 NYLQERLQMLFHHTTLVAPRDRYAQE-----LVEIEMDLASeChpgplISLIDKApqnhvvrssqrdlrehdrRGMLWLL 1037
Cdd:cd14934   377 NFTNEKLQQFFNHHMFVLEQEEYKREgiewvFIDFGLDLQA-C-----IDLLEKP------------------MGIFSIL 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1038 DEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCA---GPR-QFVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQ 1113
Cdd:cd14934   433 EEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGkgkGPEaHFELVHYAGT--VGYNITGWLEKNKD-PLNETVVGLFQ 509
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1114 DSSreeinrLYIGSLtrgsgamvFCGSFAGLEGTQSLRRVSSIrrsFTTAGVKRNSImlqvkftvDGIIDTLRRTGTHFV 1193
Cdd:cd14934   510 KSS------LGLLAL--------LFKEEEAPAGSKKQKRGSSF---MTVSNFYREQL--------NKLMTTLHSTAPHFV 564
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1194 HCYLlqhnagkHTKYTANGspssaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDL 1273
Cdd:cd14934   565 RCIV-------PNEFKQSG--------------VVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNV 623
                         730       740       750
                  ....*....|....*....|....*....|....*..
gi 116008016 1274 -----ASNKDVSvEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14934   624 ipqgfVDNKKAS-ELLLGSIDLDVNEYKIGHTKVFFR 659
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
576-1305 6.66e-56

class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276879 [Multi-domain]  Cd Length: 671  Bit Score: 208.43  E-value: 6.66e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd14915     2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  656 SGSGKSTSFKHALNYLALAA------------GAYNNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTG 723
Cdd:cd14915    82 SGAGKTVNTKRVIQYFATIAvtgekkkeeaasGKMQGTLEDQIISA-NPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  724 QIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELhlenITSEDSHPFISLSQ------KLEDRHraanD 797
Cdd:cd14915   161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEML----LITTNPYDFAFVSQgeitvpSIDDQE----E 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  798 FMRTVQAFETLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSAafgLT 874
Cdd:cd14915   233 LMATDSAVDILGFSADEKVAIYKLTGAVMHYG-----NMKFKQKQREEQAEPDGtevADKAAYLTSLNSADLLKA---LC 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  875 QPNAPNGGLSPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----Npascg 950
Cdd:cd14915   305 YPRVKVGNEYVTKGQTV----QQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEifdfN----- 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  951 qqvgaTLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIE-----MDLASechpgpLISLIDKApqnhvvrssqrdl 1025
Cdd:cd14915   376 -----SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEfidfgMDLAA------CIELIEKP------------- 431
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1026 rehdrRGMLWLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREh 1102
Cdd:cd14915   432 -----MGIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPAKGKAEahFSLVHYAGT--VDYNIAGWLDKNKD- 503
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1103 PGIRNAVSLLQDSSREEINRLYIG---SLTRGSGamvfcGSFAGLEGTQSLRRVSSIRRSfttagvkrnsimlqvkfTVD 1179
Cdd:cd14915   504 PLNETVVGLYQKSGMKTLAFLFSGgqtAEAEGGG-----GKKGGKKKGSSFQTVSALFRE-----------------NLN 561
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1180 GIIDTLRRTGTHFVHCYLlqhnagkhtkytangsPSSAAGQVSSEEEMVnvpllRSQLRGSQVLEAARLHRLGFPESVPL 1259
Cdd:cd14915   562 KLMTNLRSTHPHFVRCLI----------------PNETKTPGAMEHELV-----LHQLRCNGVLEGIRICRKGFPSRILY 620
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|..
gi 116008016 1260 LEFVRRFGLL------AGDLASNKDVSvEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14915   621 ADFKQRYKVLnasaipEGQFIDSKKAS-EKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
581-1305 4.28e-55

class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276849 [Multi-domain]  Cd Length: 661  Bit Score: 205.64  E-value: 4.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  581 LRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGK 660
Cdd:cd14883     7 LKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGESGAGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  661 STSFKHALNYLAlAAGAYNNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLPERQRA 740
Cdd:cd14883    87 TETTKLILQYLC-AVTNNHSWVEQQILEA-NTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLEQSRI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  741 GRRLGHEHSFHIMTRLLAGAAGL--LQKELHLENItsEDSHpFISLSQ--KLEDRHRAaNDFMRTVQAFETLNIDAKAVR 816
Cdd:cd14883   165 TFQAPGERNYHVFYQLLAGAKHSkeLKEKLKLGEP--EDYH-YLNQSGciRIDNINDK-KDFDHLRLAMNVLGIPEEMQE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  817 GIWSILAAIYHLGIAGVTKLgTGSTARTQFANPTAARKASGLLGVNLEDLSSAaFGLTQPNAP-NGGLSPSKsptsdtgH 895
Cdd:cd14883   241 GIFSVLSAILHLGNLTFEDI-DGETGALTVEDKEILKIVAKLLGVDPDKLKKA-LTIRQINVRgNVTEIPLK-------V 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  896 EWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQNPAScgqqvgATLADLRHNYLQERLQMLFHH 975
Cdd:cd14883   312 QEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKV------NSFEQLCINYTNEKLHKFFNH 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  976 TTLVAPRDRYAQELVE---IEMDLASEChpgplISLIDKAPqnhvvrssqrdlrehdrRGMLWLLDEEAIYPNSNDDTFL 1052
Cdd:cd14883   386 YVFKLEQEEYEKEGINwshIVFTDNQEC-----LDLIEKPP-----------------LGILKLLDEECRFPKGTDLTYL 443
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1053 ERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSRE-HPgiRNAVSLLQDSSREEINRLYigsltrg 1131
Cdd:cd14883   444 EKLHAAHEKHPYYEKPDRRRWKTEFGVKHYAGE--VTYTVQGFLDKNKDtQQ--DDLFDLMSRSKNKFVKELF------- 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1132 sgamVFCGSFAGLEGTQSLRRVSSIRRSfttaGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCylLQHNAGKhtkytan 1211
Cdd:cd14883   513 ----TYPDLLALTGLSISLGGDTTSRGT----SKGKPTVGDTFKHQLQSLVDVLSATQPWYVRC--IKPNSLK------- 575
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1212 gspssaagqvssEEEMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLA-----GDLASNKDvSVEQILA 1286
Cdd:cd14883   576 ------------EPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDprarsADHKETCG-AVRALMG 642
                         730
                  ....*....|....*....
gi 116008016 1287 VNELDVASYRIGPSQILFR 1305
Cdd:cd14883   643 LGGLPEDEWQVGKTKVFLR 661
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
577-1305 7.32e-55

class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276882 [Multi-domain]  Cd Length: 668  Bit Score: 204.97  E-value: 7.32e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  577 VLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRS 656
Cdd:cd14918     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  657 GSGKSTSFKHALNYLALAA----------GAYNNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIA 726
Cdd:cd14918    83 GAGKTVNTKRVIQYFATIAvtgekkkeesGKMQGTLEDQIISA-NPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  727 SASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenITSEDSHPFISLSQKLEDRHRAANDFMRTVQAFE 806
Cdd:cd14918   162 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLI--TTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  807 TLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSAafgLTQPNAPNGGL 883
Cdd:cd14918   240 ILGFTPEEKVSIYKLTGAVMHYG-----NMKFKQKQREEQAEPDGtevADKAAYLQSLNSADLLKA---LCYPRVKVGNE 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  884 SPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTLAD 959
Cdd:cd14918   312 YVTKGQTV----QQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEifdfN----------SLEQ 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  960 LRHNYLQERLQMLFHHTTLVAPRDRYAQE-----LVEIEMDLASechpgpLISLIDKApqnhvvrssqrdlrehdrRGML 1034
Cdd:cd14918   378 LCINFTNEKLQQFFNHHMFVLEQEEYKKEgiewtFIDFGMDLAA------CIELIEKP------------------LGIF 433
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1035 WLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSL 1111
Cdd:cd14918   434 SILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAEahFSLIHYAGT--VDYNITGWLDKNKD-PLNDTVVGL 510
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1112 LQDSSREEINRLYigsltrgsgamvfcGSFAGLEGTqslrrvSSIRRSFTTAGVKRNSIMLQVKFTVDGIIDTLRRTGTH 1191
Cdd:cd14918   511 YQKSAMKTLASLF--------------STYASAEAD------SGAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPH 570
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1192 FVHCYLlqhnagkhtkytangsPSSAAGQVSSEEEMVnvpllRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLL-- 1269
Cdd:cd14918   571 FVRCII----------------PNETKTPGAMEHELV-----LHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLna 629
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|
gi 116008016 1270 ----AGDLASNKDVSvEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14918   630 saipEGQFIDSKKAS-EKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
575-1305 1.83e-54

class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.


Pssm-ID: 276835  Cd Length: 647  Bit Score: 203.29  E-value: 1.83e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd01384     1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  654 GRSGSGKSTSFKHALNYLALAAGAYNNFINA--EKV---NALctiLEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASA 728
Cdd:cd01384    81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRSveQQVlesNPL---LEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  729 SLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenitsEDSHPFISLSQ----KLEDRHRaANDFMRTVQA 804
Cdd:cd01384   158 AIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKL-----KDPKQFHYLNQskcfELDGVDD-AEEYRATRRA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  805 FETLNIDAKAVRGIWSILAAIYHLG-IAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPN--APNG 881
Cdd:cd01384   232 MDVVGISEEEQDAIFRVVAAILHLGnIEFSKGEEDDSSVPKDEKSEFHLKAAAELLMCDEKALEDA---LCKRVivTPDG 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  882 GLSPSKSPTSdtghewAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpaSCGQqvgatl 957
Cdd:cd01384   309 IITKPLDPDA------ATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFEsfktN--SFEQ------ 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  958 adLRHNYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDlasechpgpLISLIDkapqNHVVrssqRDLREHDRRGMLWLL 1037
Cdd:cd01384   375 --FCINLANEKLQQHFNQHVFKMEQEEYTKE--EIDWS---------YIEFVD----NQDV----LDLIEKKPGGIIALL 433
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1038 DEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKcaGPRQFVLHHLQGtnPVLYAVDGWVRHSR-----EHpgirnaVSLL 1112
Cdd:cd01384   434 DEACMFPRSTHETFAQKLYQTLKDHKRFSKPKL--SRTDFTIDHYAG--DVTYQTDLFLDKNKdyvvaEH------QALL 503
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1113 QDSSREEINRLYIGSLTRGsgamvfcgsfaglegtqslrrvssirrsfTTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHF 1192
Cdd:cd01384   504 NASKCPFVAGLFPPLPREG-----------------------------TSSSSKFSSIGSRFKQQLQELMETLNTTEPHY 554
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1193 VHCylLQHNagkhtkytangspssaagQVSSEEEMVNVPLLRsQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGD 1272
Cdd:cd01384   555 IRC--IKPN------------------NLLKPGIFENANVLQ-QLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPE 613
                         730       740       750
                  ....*....|....*....|....*....|....*.
gi 116008016 1273 LASNKD---VSVEQILAVNELDvaSYRIGPSQILFR 1305
Cdd:cd01384   614 VLKGSDdekAACKKILEKAGLK--GYQIGKTKVFLR 647
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
576-1305 5.97e-54

class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276881 [Multi-domain]  Cd Length: 668  Bit Score: 202.26  E-value: 5.97e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd14917     2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  656 SGSGKSTSFKHALNYLALAAgAYNNFINAEKVNALCTI----------LEAFGNTKTCLNSNATRMTQLLSLDFDQTGQI 725
Cdd:cd14917    82 SGAGKTVNTKRVIQYFAVIA-AIGDRSKKDQTPGKGTLedqiiqanpaLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  726 ASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENitSEDSHPFISLSQKLEDRHRAANDFMRTVQAF 805
Cdd:cd14917   161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITN--NPYDYAFISQGETTVASIDDAEELMATDNAF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  806 ETLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSaafGLTQPNAPNGg 882
Cdd:cd14917   239 DVLGFTSEEKNSMYKLTGAIMHFG-----NMKFKQKQREEQAEPDGteeADKSAYLMGLNSADLLK---GLCHPRVKVG- 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  883 lspSKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTLA 958
Cdd:cd14917   310 ---NEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEifdfN----------SFE 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  959 DLRHNYLQERLQMLFHHTTLVAPRDRYAQE-----LVEIEMDLASechpgpLISLIDKApqnhvvrssqrdlrehdrRGM 1033
Cdd:cd14917   377 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEgiewtFIDFGMDLQA------CIDLIEKP------------------MGI 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1034 LWLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVS 1110
Cdd:cd14917   433 MSILEEECMFPKATDMTFKAKLFdNHLGKSNNFQKPRNIKGKPEahFSLIHYAGT--VDYNIIGWLQKNKD-PLNETVVG 509
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1111 LLQDSSREEINRLYIGslTRGSGAMVFCGSFAGLEGTqSLRRVSSIRRSfttagvkrnsimlqvkfTVDGIIDTLRRTGT 1190
Cdd:cd14917   510 LYQKSSLKLLSNLFAN--YAGADAPIEKGKGKAKKGS-SFQTVSALHRE-----------------NLNKLMTNLRSTHP 569
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1191 HFVHCYLlqhnaGKHTKytangSPSsaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLL- 1269
Cdd:cd14917   570 HFVRCII-----PNETK-----SPG-----------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILn 628
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|.
gi 116008016 1270 -----AGDLASNKDvSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14917   629 paaipEGQFIDSRK-GAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
575-1279 3.79e-53

class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276840 [Multi-domain]  Cd Length: 651  Bit Score: 199.64  E-value: 3.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd14873     1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  654 GRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNAL-------CTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIA 726
Cdd:cd14873    81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVeqailesSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  727 SASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAgllQKELHLENITSEDSHPFISLSQKLEDRH-RAANDFMRTVQAF 805
Cdd:cd14873   161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLE---HEEREEFYLSTPENYHYLNQSGCVEDKTiSDQESFREVITAM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  806 ETLNIDAKAVRGIWSILAAIYHLG-IAGVTKLGtgstarTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGG-- 882
Cdd:cd14873   238 EVMQFSKEEVREVSRLLAGILHLGnIEFITAGG------AQVSFKTALGRSAELLGLDPTQLTDA---LTQRSMFLRGee 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  883 -LSPSKSptsdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHtIASIMLIDTPGFQNpascgQQVGaTLADLR 961
Cdd:cd14873   309 iLTPLNV-------QQAVDSRDSLAMALYARCFEWVIKKINSRIKGKED-FKSIGILDIFGFEN-----FEVN-HFEQFN 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  962 HNYLQERLQMLFHHTTLVAPRDRYAQELVEIE----MDLAsEChpgplISLIDKapqnhvvrssqrdlrehdRRGMLWLL 1037
Cdd:cd14873   375 INYANEKLQEYFNKHIFSLEQLEYSREGLVWEdidwIDNG-EC-----LDLIEK------------------KLGLLALI 430
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1038 DEEAIYPNSNDDTFLERLfsHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhpGIRNAV-SLLQDSS 1116
Cdd:cd14873   431 NEESHFPQATDSTLLEKL--HSQHANNHFYVKPRVAVNNFGVKHYAGE--VQYDVRGILEKNRD--TFRDDLlNLLRESR 504
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1117 REEINRLYIGSLTRGSGAMVFCGSfaglegtqslrrvssirrsfttaGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCy 1196
Cdd:cd14873   505 FDFIYDLFEHVSSRNNQDTLKCGS-----------------------KHRRPTVSSQFKDSLHSLMATLSSSNPFFVRC- 560
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1197 lLQHNAGKHTkytangspssaagqvsseeEMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLASN 1276
Cdd:cd14873   561 -IKPNMQKMP-------------------DQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALP 620

                  ...
gi 116008016 1277 KDV 1279
Cdd:cd14873   621 EDV 623
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
576-1305 4.38e-53

class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276831 [Multi-domain]  Cd Length: 629  Bit Score: 198.92  E-value: 4.38e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYA-SNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd01380     2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNFINAE-KVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVL 733
Cdd:cd01380    82 ESGAGKTVSAKYAMRYFATVGGSSSGETQVEeKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  734 LPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenitsEDSHPFISLSQ-------KLEDrhraANDFMRTVQAFE 806
Cdd:cd01380   162 LLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHL-----GSAEDFFYTNQggspvidGVDD----AAEFEETRKALT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  807 TLNIDAKAVRGIWSILAAIYHLGiaGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLSPS 886
Cdd:cd01380   233 LLGISEEEQMEIFRILAAILHLG--NVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKW---LCKRKIVTRSEVIV 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  887 KSPTsdtgHEWAWECLEALVIGLYSEALAAVVALINRQICTS-SHTIAS-IMLIDTPGFQnpascgqqvgatladlrH-- 962
Cdd:cd01380   308 KPLT----LQQAIVARDALAKHIYAQLFDWIVDRINKALASPvKEKQHSfIGVLDIYGFE-----------------Tfe 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  963 ---------NYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDLASECHPGPLISLIDkapqnhvvrssqrdlrehDRRGM 1033
Cdd:cd01380   367 vnsfeqfciNYANEKLQQQFNQHVFKLEQEEYVKE--EIEWSFIDFYDNQPCIDLIE------------------GKLGI 426
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1034 LWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSR-----EHpgirna 1108
Cdd:cd01380   427 LDLLDEECRLPKGSDENWAQKLYNQHLKKPNKHFKKPRFSNTAFIVKHFADD--VEYQVEGFLEKNRdtvseEH------ 498
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1109 VSLLQDSsreEINRLYIGSLTRgsgamvfcgsfaglegtQSLrrvssirrsfttagvkrNSIMlqvkftvdgiiDTLRRT 1188
Cdd:cd01380   499 LNVLKAS---KNRKKTVGSQFR-----------------DSL-----------------ILLM-----------ETLNST 530
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1189 GTHFVHCyllqhnagkhTKytangsPSSAAGQVSSEEEMVnvpllRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGL 1268
Cdd:cd01380   531 TPHYVRC----------IK------PNDEKLPFTFDPKRV-----VQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRV 589
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|
gi 116008016 1269 LAG---DLASNKDVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd01380   590 LLPskeWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
575-1305 8.76e-53

class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276861 [Multi-domain]  Cd Length: 644  Bit Score: 198.47  E-value: 8.76e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14896     1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYL-ALAAGAYNNfiNAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFdQTGQIASASLQVL 733
Cdd:cd14896    81 HSGSGKTEAAKKIVQFLsSLYQDQTED--RLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVSHY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  734 LPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLEnitSEDSHPFISLSQKLEDRHRA-ANDFMRTVQAFETLNIDA 812
Cdd:cd14896   158 LLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQ---GPETYYYLNQGGACRLQGKEdAQDFEGLLKALQGLGLCA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  813 KAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQ--PNAPNGGLSPSKSPt 890
Cdd:cd14896   235 EELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEIHTAARLLQVPPERLEGA---VTHrvTETPYGRVSRPLPV- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  891 sdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSH--TIASIMLIDTPGFQNPASCGqqvgatLADLRHNYLQER 968
Cdd:cd14896   311 -----EGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEaeSDATIGVVDAYGFEALRVNG------LEQLCINLASER 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  969 LQMLFHHTTLVAPRDRYAQELVeiemdlasECHPGPLislidkapqnhVVRSSQRDLREHDRRGMLWLLDEEAIYPNSND 1048
Cdd:cd14896   380 LQLFSSQTLLAQEEEECQRELL--------PWVPIPQ-----------PPRESCLDLLVDQPHSLLSILDDQTWLSQATD 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1049 DTFLERLFSHYGDrehHSLLRKCAGPRQ-FVLHHLQGtnPVLYAVDGWVRHSREHpgIRNAVSLLQDSSReeinrlyigs 1127
Cdd:cd14896   441 HTFLQKCHYHHGD---HPSYAKPQLPLPvFTVRHYAG--TVTYQVHKFLNRNRDQ--LDPAVVEMLAQSQ---------- 503
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1128 ltrgsgamvfcgsfaglegtqsLRRVSSI-RRSFTTAGVKRNSIMLQVKF--TVDGIIDTLRRTGTHFVHCylLQHNAGK 1204
Cdd:cd14896   504 ----------------------LQLVGSLfQEAEPQYGLGQGKPTLASRFqqSLGDLTARLGRSHVYFIHC--LNPNPGK 559
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1205 HTKytangspssaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDlaSNKDVSVEQI 1284
Cdd:cd14896   560 LPG-------------------LFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSE--RQEALSDRER 618
                         730       740
                  ....*....|....*....|....*.
gi 116008016 1285 LAVNELDVAS-----YRIGPSQILFR 1305
Cdd:cd14896   619 CGAILSQVLGaesplYHLGATKVLLK 644
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
575-1270 1.65e-52

class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276857 [Multi-domain]  Cd Length: 656  Bit Score: 197.67  E-value: 1.65e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMA--PLsLYSEKVVSMFRgcKTEDM----PPHVYSLAQTAYRSL----VET 644
Cdd:cd14892     1 APLLDVLRRRYERDAIYTFTADILISINPYKsiPL-LYDVPGFDSQR--KEEATasspPPHVFSIAERAYRAMkgvgKGQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  645 RRDQSLIFMGRSGSGKSTSFKHALNYLA----LAAGAYNNFINA---EKVNAlC-----TILEAFGNTKTCLNSNATRMT 712
Cdd:cd14892    78 GTPQSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAAnahESIEE-CvllsnLILEAFGNAKTIRNDNSSRFG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  713 QLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLlqKELHLENITSEDSHpFISLSQKLE-DR 791
Cdd:cd14892   157 KYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDAN--ENAALELTPAESFL-FLNQGNCVEvDG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  792 HRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAAF 871
Cdd:cd14892   234 VDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  872 GLTQPNAPNGGLSPSKSPtsdtghEWAWECLEALVIGLYSEALAAVVALINRqiCTSSHTIASIMLIDTPGFQNPASC-- 949
Cdd:cd14892   314 TQTTSTARGSVLEIKLTA------REAKNALDALCKYLYGELFDWLISRINA--CHKQQTSGVTGGAASPTFSPFIGIld 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  950 --GQQVGAT--LADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEChpgplISLIDKAPQnhvvrssq 1022
Cdd:cd14892   386 ifGFEIMPTnsFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDvsaIEFQDNQDC-----LDLIQKKPL-------- 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1023 rdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFsHYGDREHHSLLRKcagPR----QFVLHHLQGTnpVLYAVDGWVrh 1098
Cdd:cd14892   453 ---------GLLPLLEEQMLLKRKTTDKQLLTIY-HQTHLDKHPHYAK---PRfecdEFVLRHYAGD--VTYDVHGFL-- 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1099 srehpgIRNAVSLLQDssreeinrlyigsltrgsgamvfcgsfaglegtqsLRRVSSIRRSFTTagvkrnsimlqvkfTV 1178
Cdd:cd14892   516 ------AKNNDNLHDD-----------------------------------LRDLLRSSSKFRT--------------QL 540
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1179 DGIIDTLRRTGTHFVHCylLQHNAGKhtkytangspssAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVP 1258
Cdd:cd14892   541 AELMEVLWSTTPSYIKC--IKPNNLK------------FPGGFSCE-------LVRDQLIYSGVLEVVRIRREGFPIRRQ 599
                         730
                  ....*....|..
gi 116008016 1259 LLEFVRRFGLLA 1270
Cdd:cd14892   600 FEEFYEKFWPLA 611
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
576-1305 2.38e-52

class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276880 [Multi-domain]  Cd Length: 670  Bit Score: 197.59  E-value: 2.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd14916     2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  656 SGSGKSTSFKHALNYLALAAG----AYNNFINAEKVNALCTI------LEAFGNTKTCLNSNATRMTQLLSLDFDQTGQI 725
Cdd:cd14916    82 SGAGKTVNTKRVIQYFASIAAigdrSKKENPNANKGTLEDQIiqanpaLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  726 ASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENitSEDSHPFISLSQKLEDRHRAANDFMRTVQAF 805
Cdd:cd14916   162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTN--NPYDYAFVSQGEVSVASIDDSEELLATDSAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  806 ETLNIDAKAVRGIWSILAAIYHLGiagvtKLGTGSTARTQFANPTA---ARKASGLLGVNLEDLSSaafGLTQPNAPNGG 882
Cdd:cd14916   240 DVLGFTAEEKAGVYKLTGAIMHYG-----NMKFKQKQREEQAEPDGtedADKSAYLMGLNSADLLK---GLCHPRVKVGN 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  883 LSPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ----NpascgqqvgaTLA 958
Cdd:cd14916   312 EYVTKGQSV----QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEifdfN----------SFE 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  959 DLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIE-----MDLASechpgpLISLIDKApqnhvvrssqrdlrehdrRGM 1033
Cdd:cd14916   378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEfidfgMDLQA------CIDLIEKP------------------MGI 433
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1034 LWLLDEEAIYPNSNDDTFLERLF-SHYGDREHHSLLRKCAGPRQ--FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVS 1110
Cdd:cd14916   434 MSILEEECMFPKASDMTFKAKLYdNHLGKSNNFQKPRNVKGKQEahFSLVHYAGT--VDYNILGWLEKNKD-PLNETVVG 510
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1111 LLQDSSREEINRL---YIGSLTRGSGAmvfcgSFAGLEGTQSLRRVSSIRRSfttagvkrnsimlqvkfTVDGIIDTLRR 1187
Cdd:cd14916   511 LYQKSSLKLMATLfstYASADTGDSGK-----GKGGKKKGSSFQTVSALHRE-----------------NLNKLMTNLKT 568
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1188 TGTHFVHCYLlqhnagkhtkytangsPSSaagqvSSEEEMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFG 1267
Cdd:cd14916   569 THPHFVRCII----------------PNE-----RKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 627
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....
gi 116008016 1268 LL------AGDLASNKDvSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14916   628 ILnpaaipEGQFIDSRK-GAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
572-1096 2.85e-52

class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276845 [Multi-domain]  Cd Length: 647  Bit Score: 196.62  E-value: 2.85e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  572 LNEASVLHCLRQRYASNLIHTKAGPT-LLVVNPMAPLSLYSEKV----VSMFRGC---KTEDMPPHVYSLAQTAYRSLVE 643
Cdd:cd14879     1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPYKYLSSNSDASlgeyGSEYYDTtsgSKEPLPPHAYDLAARAYLRMRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  644 TRRDQSLIFMGRSGSGKSTSFKHALN-YLALAAGAYNNFINAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQT 722
Cdd:cd14879    81 RSEDQAVVFLGETGSGKSESRRLLLRqLLRLSSHSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNER 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  723 GQIASA-SLQVLLpERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSE-----------DSHPFISLSQKLED 790
Cdd:cd14879   161 GRLIGAkVLDYRL-ERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYallasygchplPLGPGSDDAEGFQE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  791 rhraandfMRTvqAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAa 870
Cdd:cd14879   240 --------LKT--ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGEESAVVKNTDVLDIVAAFLGVSPEDLETS- 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  871 fgLTqpnapngglspSKspTSDTGHEWAWECLEA---------LVIGLYSEALAAVVALINRQICTSSHTIAS-IMLIDT 940
Cdd:cd14879   309 --LT-----------YK--TKLVRKELCTVFLDPegaaaqrdeLARTLYSLLFAWVVETINQKLCAPEDDFATfISLLDF 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  941 PGFQNPASCGqqvGATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIE----MDlASEC------HPGPLISLID 1010
Cdd:cd14879   374 PGFQNRSSTG---GNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPatsyFD-NSDCvrllrgKPGGLLGILD 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1011 KAPqnhvvrssqrdlrehdRRgmlwlldeeaiYPNSNDDTFLERLFSHYGDreHHSLLRKCA-----GPRQFVLHHLQGt 1085
Cdd:cd14879   450 DQT----------------RR-----------MPKKTDEQMLEALRKRFGN--HSSFIAVGNfatrsGSASFTVNHYAG- 499
                         570
                  ....*....|.
gi 116008016 1086 nPVLYAVDGWV 1096
Cdd:cd14879   500 -EVTYSVEGFL 509
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
575-1305 4.36e-52

class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276862 [Multi-domain]  Cd Length: 635  Bit Score: 196.06  E-value: 4.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDM-PPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd14897     1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  654 GRSGSGKSTSFKHALNYLALAAGAYNNFINaEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVL 733
Cdd:cd14897    81 GESGAGKTESTKYMIKHLMKLSPSDDSDLL-DKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  734 LPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENI-------TSEDSHPFISLSQKLEDRHRAANDF---MRTVq 803
Cdd:cd14897   160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPdchrilrDDNRNRPVFNDSEELEYYRQMFHDLtniMKLI- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  804 AFETLNIDAkavrgIWSILAAIYHlgIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAAFGLTQpnapnggL 883
Cdd:cd14897   239 GFSEEDISV-----IFTILAAILH--LTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVN-------T 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  884 SPSKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIA-----SIMLIDTPGFQNPASCGqqvgatLA 958
Cdd:cd14897   305 IRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQImtrgpSIGILDMSGFENFKINS------FD 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  959 DLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEmDLASECHpGPLISLIDKAPQnhvvrssqrdlrehdrrGMLWLLD 1038
Cdd:cd14897   379 QLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR-DIEYHDN-DDVLELFFKKPL-----------------GILPLLD 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1039 EEAIYPNSNDDTFLERLFSHYGDREHH--SLLRKCAgprqFVLHHLQGTnpVLYAVDGWVRHSREHPGIrNAVSLLQDSS 1116
Cdd:cd14897   440 EESTFPQSTDSSLVQKLNKYCGESPRYvaSPGNRVA----FGIRHYAEQ--VTYDADGFLEKNRDNLSS-DIVGCLLNSN 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1117 REEINRLYIGSLTRgsgamvfcgSFAGLegtqsLRRVSSIRRSFTTAgVKRNSIMLQVKFTVDgiidtlrrtgthfvhcy 1196
Cdd:cd14897   513 NEFISDLFTSYFKR---------SLSDL-----MTKLNSADPLFVRC-IKPNNFLRPNKFDDE----------------- 560
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1197 llqhnagkhtkytangspssaagqvsseeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDlaSN 1276
Cdd:cd14897   561 -----------------------------------LVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDF--SN 603
                         730       740       750
                  ....*....|....*....|....*....|..
gi 116008016 1277 KDVSVEQILAVNELDVAS---YRIGPSQILFR 1305
Cdd:cd14897   604 KVRSDDLGKCQKILKTAGikgYQFGKTKVFLK 635
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
575-1305 5.71e-52

class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276868 [Multi-domain]  Cd Length: 658  Bit Score: 196.15  E-value: 5.71e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPL-SLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd14903     1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLpELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  654 GRSGSGKSTSFKHALNYLALAAGAYNNFInAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVL 733
Cdd:cd14903    81 GESGAGKTETTKILMNHLATIAGGLNDST-IKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  734 LPERQRAGRRLGHEHSFHIMTRLLagAAGLLQKELHLENiTSEDSHPFISLSQKLEDRHRAANdFMRTVQAFETLNIDAK 813
Cdd:cd14903   160 LLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDS-ANECAYTGANKTIKIEGMSDRKH-FARTKEALSLIGVSEE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  814 AVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAAFGLTQPNAPNGGLSPSKSptsdt 893
Cdd:cd14903   236 KQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK----- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  894 ghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQNpascgqqvgatladLRH--------NYL 965
Cdd:cd14903   311 --DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEH--------------FKHnsfeqfciNYA 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  966 QERLQMLFHHTTLVAPRDRYAQElvEIEMDLASECHPGPLISLIDkapqnhvvrssqrdlrehDRRGMLWLLDEEAIYPN 1045
Cdd:cd14903   375 NEKLQQKFTQDVFKTVQIEYEEE--GIRWAHIDFADNQDVLAVIE------------------DRLGIISLLNDEVMRPK 434
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1046 SNDDTFLERLFSHYGDREHHSLLRKCAgPRQFVLHHLQGtnPVLYAVDGWVRHSREhpgirnavSLLQDSSreeinrlyi 1125
Cdd:cd14903   435 GNEESFVSKLSSIHKDEQDVIEFPRTS-RTQFTIKHYAG--PVTYESLGFLEKHKD--------ALLPDLS--------- 494
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1126 gSLTRGSG----AMVFCGSFAGLEGTQSLRRVSSIRRSFTTAGVKrnSIMLQVKFTVDGIIDTLRRTGTHFVHCyllqhn 1201
Cdd:cd14903   495 -DLMRGSSkpflRMLFKEKVESPAAASTSLARGARRRRGGALTTT--TVGTQFKDSLNELMTTIRSTNVHYVRC------ 565
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1202 agkhTKYTANGSPSSAagqvssEEEMVNvpllrSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAgDLASNKDVSV 1281
Cdd:cd14903   566 ----IKPNSIKSPTEL------DHLMVV-----SQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFL-PEGRNTDVPV 629
                         730       740
                  ....*....|....*....|....*....
gi 116008016 1282 ----EQILAVNELDV-ASYRIGPSQILFR 1305
Cdd:cd14903   630 aercEALMKKLKLESpEQYQMGLTRIYFQ 658
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
576-1270 2.00e-51

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276830 [Multi-domain]  Cd Length: 633  Bit Score: 194.03  E-value: 2.00e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGR 655
Cdd:cd01379     2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  656 SGSGKSTSFKHALNYLALAAGAYNNFINaEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLP 735
Cdd:cd01379    82 SGAGKTESANLLVQQLTVLGKANNRTLE-EKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  736 ERQRAGRRLGHEHSFHIMTRLLAGAA--GLLQKELHLENITSEDSHPFISLSQKLEDRHRAANDFMRTVQAFETLNIDAK 813
Cdd:cd01379   161 EKSRVVHQAIGERNFHIFYYIYAGLAedKKLAKYKLPENKPPRYLQNDGLTVQDIVNNSGNREKFEEIEQCFKVIGFTKE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  814 AVRGIWSILAAIYHLGIAGVTKLGTG--STARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGLSPSKSPTS 891
Cdd:cd01379   241 EVDSVYSILAAILHIGDIEFTEVESNhqTDKSSRISNPEALNNVAKLLGIEADELQEA---LTSHSVVTRGETIIRNNTV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  892 DTghewAWECLEALVIGLYSEALAAVVALINRQICTSSHTIA---SIMLIDTPGFQN-PASCGQQVGATLADlrhnylqE 967
Cdd:cd01379   318 EE----ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSASDeplSIGILDIFGFENfQKNSFEQLCINIAN-------E 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  968 RLQMLFHHTTLVAPRDRYAQELVeiemdlasechPGPLISLIDKAPqnhVVrssqrDLREHDRRGMLWLLDEEAIYPNSN 1047
Cdd:cd01379   387 QIQYYFNQHIFAWEQQEYLNEGI-----------DVDLIEYEDNRP---LL-----DMFLQKPMGLLALLDEESRFPKAT 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1048 DDTFLERLfsHYGDREHHSLLRKCAGPrQFVLHHLQGTnpVLYAVDGWVRHSREH--PGIrnaVSLLQDSSReeinrlyi 1125
Cdd:cd01379   448 DQTLVEKF--HNNIKSKYYWRPKSNAL-SFGIHHYAGK--VLYDASGFLEKNRDTlpPDV---VQLLRSSEN-------- 511
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1126 gsltrgsgamvfcgsfaglegtqslrrvSSIRRsfTTAGVKRNSIM-LQVKFTVdgiidtlrrtGT-HFVHCylLQHNAG 1203
Cdd:cd01379   512 ----------------------------PLVRQ--TVATYFRYSLMdLLSKMVV----------GQpHFVRC--IKPNDS 549
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1204 KhtkytangspssAAGQVSSEEEMVnvpllrsQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLA 1270
Cdd:cd01379   550 R------------QAGKFDREKVLK-------QLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLA 597
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
575-1269 1.90e-50

class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276832  Cd Length: 648  Bit Score: 191.31  E-value: 1.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd01381     1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYnNFINaEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLL 734
Cdd:cd01381    81 ESGAGKTESTKLILQYLAAISGQH-SWIE-QQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  735 PERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenitsEDSHPFISLSQ----KLEDRHRAAnDFMRTVQAFETLNI 810
Cdd:cd01381   159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLEL-----GDASDYYYLTQgnclTCEGRDDAA-EFADIRSAMKVLMF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  811 DAKAVRGIWSILAAIYHLG----IAGVTKlgtgSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGGlsps 886
Cdd:cd01381   233 TDEEIWDIFKLLAAILHLGnikfEATVVD----NLDASEVRDPPNLERAAKLLEVPKQDLVDA---LTTRTIFTRG---- 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  887 KSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIA---SIMLIDTPGFQNPA--SCGQqvgatladLR 961
Cdd:cd01381   302 ETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSsrtSIGVLDIFGFENFEvnSFEQ--------LC 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  962 HNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEChpgplISLIDKAPQNhvvrssqrdlrehdrrgMLWLLD 1038
Cdd:cd01381   374 INFANENLQQFFVRHIFKLEQEEYDKEGINwqhIEFVDNQDV-----LDLIALKPMN-----------------IMSLID 431
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1039 EEAIYPNSNDDTFLERLFSHYGDREHHsLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSRE--HPGIRNavsLLQDSS 1116
Cdd:cd01381   432 EESKFPKGTDQTMLEKLHSTHGNNKNY-LKPKSDLNTSFGINHFAGV--VFYDTRGFLEKNRDtfSADLLQ---LVQSSK 505
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1117 REEINRLYIGSLTRGSgamvfcgsfaglegtqslrrvSSIRRSFTTAGVKRNSImlqvkftvDGIIDTLRRTGTHFVHCy 1196
Cdd:cd01381   506 NKFLKQLFNEDISMGS---------------------ETRKKSPTLSSQFRKSL--------DQLMKTLSACQPFFVRC- 555
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116008016 1197 lLQHNAGKHTKYTangspssaagqvssEEEMVnvplLRsQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLL 1269
Cdd:cd01381   556 -IKPNEYKKPMLF--------------DRELC----VR-QLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL 608
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
581-1094 3.23e-50

class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276829  Cd Length: 652  Bit Score: 190.83  E-value: 3.23e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  581 LRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGK 660
Cdd:cd01378     7 LKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESGAGK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  661 STSFKHALNYLALAAGAYNNFINAEKVNALCT--ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLPERQ 738
Cdd:cd01378    87 TEASKRIMQYIAAVSGGSESEVERVKDMLLASnpLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  739 RAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLEnitSEDSHPFISLSQKLE-DRHRAANDFMRTVQAFETLNIDAKAVRG 817
Cdd:cd01378   167 RVVGQIKGERNFHIFYQLLKGASQEYLQELGLQ---RPEQYYYYSKSGCFDvDGIDDAADFKEVLNAMKVIGFTEEEQDS 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  818 IWSILAAIYHLG-IAGVTKLGTGSTARTQFANPTAARkasgLLGVNLEDLSSAafgLT--QPNAPNGGLSPSKSPTSDTG 894
Cdd:cd01378   244 IFRILAAILHLGnIQFAEDEEGNAAISDTSVLDFVAY----LLGVDPDQLEKA---LThrTIETGGGGRSVYEVPLNVEQ 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  895 hewAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIM-LIDTPGF----QNpaSCGQqvgatladLRHNYLQERL 969
Cdd:cd01378   317 ---AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIgVLDIYGFeifeKN--SFEQ--------FCINYVNEKL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  970 QMLFHHTTLVAPRDRYAQELVEIEmdlasechPgplISLIDkapqNHVVrssqRDLREHDRRGMLWLLDEE-AIYPNSND 1048
Cdd:cd01378   384 QQIFIELTLKAEQEEYVREGIEWT--------P---IKYFN----NKII----CDLIEEKPPGIFAILDDAcLTAGDATD 444
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 116008016 1049 DTFLERLFSHYGDREHHS--LLRKCAGPRQFVLHHLQGtnPVLYAVDG 1094
Cdd:cd01378   445 QTFLQKLNQLFSNHPHFEcpSGHFELRRGEFRIKHYAG--DVTYNVEG 490
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
575-1305 4.52e-50

class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276855 [Multi-domain]  Cd Length: 662  Bit Score: 190.37  E-value: 4.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPL-SLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLV----ETRRDQS 649
Cdd:cd14890     1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIpDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIqsgvLDPSNQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  650 LIFMGRSGSGKSTSFKHALNYLALAAGaYNNFINAEKVNALCT------------------ILEAFGNTKTCLNSNATRM 711
Cdd:cd14890    81 IIISGESGAGKTEATKIIMQYLARITS-GFAQGASGEGEAASEaieqtlgsledrvlssnpLLESFGNAKTLRNDNSSRF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  712 TQLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLEniTSEDShpFISLSQKLEDR 791
Cdd:cd14890   160 GKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQ--TPVEY--FYLRGECSSIP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  792 HRA-ANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG-----IAGVTKLGTGSTARtqfanPTaARKASGLLGVNLED 865
Cdd:cd14890   236 SCDdAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGnvdfeSENDTTVLEDATTL-----QS-LKLAAELLGVNEDA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  866 LSSAAfgLTQPNAPNGglspsKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQn 945
Cdd:cd14890   310 LEKAL--LTRQLFVGG-----KTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFE- 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  946 pasCGQQvgATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEC----------HPGPLISLIDka 1012
Cdd:cd14890   382 ---KFEW--NTFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDwqyITFNDNQACleliegkvngKPGIFITLDD-- 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1013 pqNHVVRSSQRDLR----EHDRRGmlwlldeeaiyPNSNDDTflerlFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpV 1088
Cdd:cd14890   455 --CWRFKGEEANKKfvsqLHASFG-----------RKSGSGG-----TRRGSSQHPHFVHPKFDADKQFGIKHYAGD--V 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1089 LYAVDGWVRHSREHpgirnavslLQDSSREEINrlyigsltrgsgamvfcgsfaglEGTQSLRRVssirrsfttagvkrn 1168
Cdd:cd14890   515 IYDASGFNEKNNET---------LNAEMKELIK-----------------------QSRRSIREV--------------- 547
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1169 SIMLQVKFTVDGIIDTLRRTGTHFVHCylLQHNagkhtkytangsPSSAAGQVSSEEemvnvpLLRsQLRGSQVLEAARL 1248
Cdd:cd14890   548 SVGAQFRTQLQELMAKISLTNPRYVRC--IKPN------------ETKAPGKFDGLD------CLR-QLKYSGMMEAIQI 606
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1249 HRLGFPESVPLLEFVRRFGLLAGDlASNKDVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14890   607 RQQGFALREEHDSFFYDFQVLLPT-AENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
575-1269 1.78e-49

class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276867 [Multi-domain]  Cd Length: 716  Bit Score: 189.72  E-value: 1.78e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPL-SLYSEKVVSMFRGCKT--------EDMPPHVYSLAQTAYRSLV-ET 644
Cdd:cd14902     1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLpDLYSESQLNAYKASMTstspvsqlSELPPHVFAIGGKAFGGLLkPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  645 RRDQSLIFMGRSGSGKSTSFKHALNYLAlAAGAYNNFINAEKVNA-------LCT--ILEAFGNTKTCLNSNATRMTQLL 715
Cdd:cd14902    81 RRNQSILVSGESGSGKTESTKFLMQFLT-SVGRDQSSTEQEGSDAveigkriLQTnpILESFGNAQTIRNDNSSRFGKFI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  716 SLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENitSEDSHPFISLSQKLEDRHRAA 795
Cdd:cd14902   160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQK--GGKYELLNSYGPSFARKRAVA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  796 ND----FMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGtGSTARTQFANPTAAR--KASGLLGVNLEDLSSA 869
Cdd:cd14902   238 DKyaqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEN-GQEDATAVTAASRFHlaKCAELMGVDVDKLETL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  870 afgLTQPNAPNGG------LSPsksptsdtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTI---------AS 934
Cdd:cd14902   317 ---LSSREIKAGVevmvlkLTP----------EQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVsisdedeelAT 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  935 IMLIDTPGFQNPASCGqqvgatLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEChpgplISLIDK 1011
Cdd:cd14902   384 IGILDIFGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDwknISYPSNAAC-----LALFDD 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1012 APQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREhhsllrkcagprQFVLHHLQGTnpVLYA 1091
Cdd:cd14902   453 KSN-----------------GLFSLLDQECLMPKGSNQALSTKFYRYHGGLG------------QFVVHHFAGR--VCYN 501
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1092 VDGWVRHSREH-PGirNAVSLLQDSSREEInrLYIGSLTRgsgamvfCGSFAGLEGTQSLRRVSSIRRSfttagvkrnSI 1170
Cdd:cd14902   502 VEQFVEKNTDAlPA--DASDILSSSSNEVV--VAIGADEN-------RDSPGADNGAAGRRRYSMLRAP---------SV 561
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1171 MLQVKFTVDGIIDTLRRTGTHFVHCylLQHNAGKHTKYTangspssaagqvsSEEEMVnvpllrSQLRGSQVLEAARLHR 1250
Cdd:cd14902   562 SAQFKSQLDRLIVQIGRTEAHYVRC--LKPNEVKKPGIF-------------DRERMV------EQMRSVGVLEAVRIAR 620
                         730
                  ....*....|....*....
gi 116008016 1251 LGFPESVPLLEFVRRFGLL 1269
Cdd:cd14902   621 HGYSVRLAHASFIELFSGF 639
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
575-1305 9.94e-49

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276874  Cd Length: 666  Bit Score: 186.58  E-value: 9.94e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14909     1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNAL-------CTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIAS 727
Cdd:cd14909    81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLedqvvqtNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  728 ASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEdsHPFISLSQKLEDRHRAANDFMRTVQAFET 807
Cdd:cd14909   161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYD--YYIVSQGKVTVPNVDDGEEFSLTDQAFDI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  808 LNIDAKAVRGIWSILAAIYHLGIAGVTKLGtgstaRTQFANPTAAR---KASGLLGVNLEDLSSAafgLTQPNAPNGGLS 884
Cdd:cd14909   239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRG-----REEQAEQDGEEeggRVSKLFGCDTAELYKN---LLKPRIKVGNEF 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  885 PSKSPTSDTghewAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQNPASCGqqvgatLADLRHNY 964
Cdd:cd14909   311 VTQGRNVQQ----VTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG------FEQLCINF 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  965 LQERLQMLFHHTTLVAPRDRYAQE-----LVEIEMDLASeChpgplISLIDKApqnhvvrssqrdlrehdrRGMLWLLDE 1039
Cdd:cd14909   381 TNEKLQQFFNHHMFVLEQEEYKREgidwaFIDFGMDLLA-C-----IDLIEKP------------------MGILSILEE 436
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1040 EAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQ----FVLHHLQGTnpVLYAVDGWVRHSREhPGIRNAVSLLQDS 1115
Cdd:cd14909   437 ESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQqaahFAIAHYAGC--VSYNITGWLEKNKD-PLNDTVVDQFKKS 513
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1116 SreeiNRLYIGSLTRGSGAMvfcgsfAGLEGTQSLRRvssirrsftTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHC 1195
Cdd:cd14909   514 Q----NKLLIEIFADHAGQS------GGGEQAKGGRG---------KKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRC 574
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1196 YLlqHNAGKHTKytangspssaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLA- 1274
Cdd:cd14909   575 II--PNEMKQPG-------------------VVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIq 633
                         730       740       750
                  ....*....|....*....|....*....|...
gi 116008016 1275 --SNKDVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14909   634 geEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
575-1305 4.54e-46

class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276838 [Multi-domain]  Cd Length: 657  Bit Score: 178.41  E-value: 4.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd01387     1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNFInAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQtGQIASASLQVLL 734
Cdd:cd01387    81 ESGSGKTEATKLIMQYLAAVNQRRNNLV-TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  735 PERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenitsEDSHPFISLSQKLEDR---HRAANDFMRTVQAFETLNID 811
Cdd:cd01387   159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGL-----QEAEKYFYLNQGGNCEiagKSDADDFRRLLAAMQVLGFS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  812 AKAVRGIWSILAAIYHLG---------IAGVTKLGTGSTARTQFanptaarkASGLLGVNLEDLSSA-AFGLTQPNAPNg 881
Cdd:cd01387   234 SEEQDSIFRILASVLHLGnvyfhkrqlRHGQEGVSVGSDAEIQW--------VAHLLQISPEGLQKAlTFKVTETRRER- 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  882 glspSKSPTSDtghEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQNPAScgqqvgATLADLR 961
Cdd:cd01387   305 ----IFTPLTI---DQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSE------NSFEQLC 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  962 HNYLQERLQMLFHHTTLVAPRDRYAQELVE-IEMDLASEChpgPLISLIDKAPQnhvvrssqrdlrehdrrGMLWLLDEE 1040
Cdd:cd01387   372 INYANENLQYYFNKHVFKLEQEEYIREQIDwTEIAFADNQ---PVINLISKKPV-----------------GILHILDDE 431
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1041 AIYPNSNDDTFLERLFSHYGDREHHSllRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSRehpgirnavsllqDSSREEI 1120
Cdd:cd01387   432 CNFPQATDHSFLEKCHYHHALNELYS--KPRMPLPEFTIKHYAGQ--VWYQVHGFLDKNR-------------DQLRQDV 494
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1121 NRLYIGSLTRGSGAMvfcgsFAGLEGTQSLRRVSSIRRSFTTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCylLQH 1200
Cdd:cd01387   495 LELLVSSRTRVVAHL-----FSSHRAQTDKAPPRLGKGRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRC--LKP 567
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1201 NAGKHTKytangspssaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRF-GLLAGDLASNKDV 1279
Cdd:cd01387   568 NHKKEPM-------------------LFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYrCLVALKLPRPAPG 628
                         730       740
                  ....*....|....*....|....*....
gi 116008016 1280 SVEQILAVNELDVAS---YRIGPSQILFR 1305
Cdd:cd01387   629 DMCVSLLSRLCTVTPkdmYRLGATKVFLR 657
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
575-1305 3.40e-45

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 176.03  E-value: 3.40e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd01385     1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYL-ALAAGAYNNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVL 733
Cdd:cd01385    81 ESGSGKTESTNFLLHHLtALSQKGYGSGVEQTILGA-GPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  734 LPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLEniTSEDSHpFISLSQ-KLEDRHRAANDFMRTVQAFETLNIDA 812
Cdd:cd01385   160 LLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLK--QPEDYH-YLNQSDcYTLEGEDEKYEFERLKQAMEMVGFLP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  813 KAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAPNGG---LSPSKSP 889
Cdd:cd01385   237 ETQRQIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVLDIISELLRVKEETLLEA---LTTKKTVTVGetlILPYKLP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  890 TSDTGHEWAWECLEALV---IGLYSEAlaavvALINRQIcTSSHTIASIMLIDTPGFQNpascgqqVGA-TLADLRHNYL 965
Cdd:cd01385   314 EAIATRDAMAKCLYSALfdwIVLRINH-----ALLNKKD-LEEAKGLSIGVLDIFGFED-------FGNnSFEQFCINYA 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  966 QERLQMLFHHTTLVAPRDRYAQE---LVEIEMDLASEChpgplISLIDKAPQnhvvrssqrdlrehdrrGMLWLLDEEAI 1042
Cdd:cd01385   381 NEHLQYYFNQHIFKLEQEEYKKEgisWHNIEYTDNTGC-----LQLISKKPT-----------------GLLCLLDEESN 438
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1043 YPNSNDDTFLERLFSHYGDREHHSL--LRKCAgprqFVLHHLQGTnpVLYAVDGWVRHSREH--PGIrnaVSLLQDSS-- 1116
Cdd:cd01385   439 FPGATNQTLLAKFKQQHKDNKYYEKpqVMEPA----FIIAHYAGK--VKYQIKDFREKNLDLmrPDI---VAVLRSSSsa 509
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1117 --REEINRLYIGSLTRGSGAMVFCGSFAGLEGTQSLRRVSSI------RRSFTTAGVKRN-----SIMLQVKFTVDGIID 1183
Cdd:cd01385   510 fvRELIGIDPVAVFRWAVLRAFFRAMAAFREAGRRRAQRTAGhsltlhDRTTKSLLHLHKkkkppSVSAQFQTSLSKLME 589
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1184 TLRRTGTHFVHCylLQHNAGKhtkytangspssaaGQVSSEEEMVnvplLRsQLRGSQVLEAARLHRLGFPESVPLLEFV 1263
Cdd:cd01385   590 TLGQAEPFFIRC--IKSNAEK--------------KPLRFDDELV----LR-QLRYTGMLETVRIRRSGYSVRYTFQEFI 648
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|...
gi 116008016 1264 RRFG-LLAGDLASNKDvSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd01385   649 TQFQvLLPKGLISSKE-DIKDFLEKLNLDRDNYQIGKTKVFLK 690
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
575-1195 1.07e-44

class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276833  Cd Length: 649  Bit Score: 173.97  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd01382     1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  654 GRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVL 733
Cdd:cd01382    81 GESGAGKTESTKYILRYLTESWGSGAGPIEQRILEA-NPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  734 LPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELhLENITSEDshpfislsqkledrhraANDFMRTVQAFETLNIDAK 813
Cdd:cd01382   160 LLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-LKDPLLDD-----------------VGDFIRMDKAMKKIGLSDE 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  814 AVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPT--AARKASGLLGVNLEDLSSAafgLTQP--NAPNGGLS----- 884
Cdd:cd01382   222 EKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSeqSLEYAAELLGLDQDELRVS---LTTRvmQTTRGGAKgtvik 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  885 -PSKSptsdtgHEwAWECLEALVIGLYSEALAAVVALINRQI--CTSSHTIAsimLIDTPGFQNpascgqqvgatladLR 961
Cdd:cd01382   299 vPLKV------EE-ANNARDALAKAIYSKLFDHIVNRINQCIpfETSSYFIG---VLDIAGFEY--------------FE 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  962 H--------NYLQERLQMLFHHTTLvaprdRYAQELVEIEmdlasechpG---PLISLIDKapQNHVvrssqrDLREHDR 1030
Cdd:cd01382   355 VnsfeqfciNYCNEKLQQFFNERIL-----KEEQELYEKE---------GlgvKEVEYVDN--QDCI------DLIEAKL 412
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1031 RGMLWLLDEEAIYPNSNDDTFLERLFSHYGDrehHSLLrkcAGPRQ--------------FVLHHLQGTnpVLYAVDGWV 1096
Cdd:cd01382   413 VGILDLLDEESKLPKPSDQHFTSAVHQKHKN---HFRL---SIPRKsklkihrnlrddegFLIRHFAGA--VCYETAQFI 484
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1097 R------H-SREhpgirnavSLLQDSSREEINRLYIGSLTRGSGamvfcgsfaglegtqslRRVSSIRRSFTTAGVKRNS 1169
Cdd:cd01382   485 EknndalHaSLE--------SLICESKDKFIRSLFESSTNNNKD-----------------SKQKAGKLSFISVGNKFKT 539
                         650       660
                  ....*....|....*....|....*.
gi 116008016 1170 IMLQvkftvdgIIDTLRRTGTHFVHC 1195
Cdd:cd01382   540 QLNL-------LMDKLRSTGTSFIRC 558
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
576-1270 3.70e-44

class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276860 [Multi-domain]  Cd Length: 704  Bit Score: 173.22  E-value: 3.70e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSekvVSMFRgcktEDMP------PHVYSLAQTAYRSL------- 641
Cdd:cd14895     2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYR----EEMPgwtalpPHVFSIAEGAYRSLrrrlhep 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  642 VETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCT--------ILEAFGNTKTCLNSNATRMTQ 713
Cdd:cd14895    75 GASKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGsellsanpILESFGNARTLRNDNSSRFGK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  714 LLSLDF-----DQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDSHpFISLSQ-- 786
Cdd:cd14895   155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQEFQ-YISGGQcy 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  787 KLEDRHRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG--IAGVTKLGTGSTARTQFANPTAARKA--------- 855
Cdd:cd14895   234 QRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGnvLFVASSEDEGEEDNGAASAPCRLASAspssltvqq 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  856 -----SGLLGVNLEDLSSAafgLTQPNAPNGGlspsKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALIN-----RQI 925
Cdd:cd14895   314 hldivSKLFAVDQDELVSA---LTTRKISVGG----ETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNsaspqRQF 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  926 CTSSHTIAS------IMLIDTPGFQNPAScgqqvgATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDL 996
Cdd:cd14895   387 ALNPNKAANkdttpcIAVLDIFGFEEFEV------NQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKwnaVDYED 460
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  997 ASEChpgplISLIDKAPQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQ 1076
Cdd:cd14895   461 NSVC-----LEMLEQRPS-----------------GIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADVA 518
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1077 FVLHHLQGTnpVLYAVDGWVRHSREHPGiRNAVSLLQDSSREEINRLyigsltrgsgamvfCGSFAGLEGTQ-SLRRVSS 1155
Cdd:cd14895   519 FQIHHYAGA--VRYQAEGFCEKNKDQPN-AELFSVLGKTSDAHLREL--------------FEFFKASESAElSLGQPKL 581
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1156 IRRSFTTAGVKRNSimlQVKFTVDGIIDTLRRTGTHFVHCYllqhnagkhtkytangSPSSAagqvsSEEEMVNVPLLRS 1235
Cdd:cd14895   582 RRRSSVLSSVGIGS---QFKQQLASLLDVVQQTQTHYIRCI----------------KPNDE-----SASDQFDMAKVSS 637
                         730       740       750
                  ....*....|....*....|....*....|....*
gi 116008016 1236 QLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLA 1270
Cdd:cd14895   638 QLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
575-1270 2.34e-42

class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276853 [Multi-domain]  Cd Length: 667  Bit Score: 167.18  E-value: 2.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPL-SLYSEKVVSMFRGcKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd14888     1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIpGLYSDEMLLKFIQ-PSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  654 GRSGSGKSTSFKHALNYLAlAAGAYN----NFINAE--KVNALctiLEAFGNTKTCLNSNATRMTQLLSLDFDQT----- 722
Cdd:cd14888    80 GESGAGKTESTKYVMKFLA-CAGSEDikkrSLVEAQvlESNPL---LEAFGNARTLRNDNSSRFGKFIELQFSKLkskrm 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  723 ----GQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLE-----------------NITSEDSHP- 780
Cdd:cd14888   156 sgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEendeklakgadakpisiDMSSFEPHLk 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  781 FISLSQKLEDRHRAAND---FMRTVQAFETLNIDAKAVRGIWSILAAIYHLG-IAGVTKLGTGSTARTQFANPTAARKAS 856
Cdd:cd14888   236 FRYLTKSSCHELPDVDDleeFESTLYAMQTVGISPEEQNQIFSIVAAILYLGnILFENNEACSEGAVVSASCTDDLEKVA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  857 GLLGVNLEDLSSAafgLTQPNAPNGGLSPSKSPTSDTghewAWECLEALVIGLYSEALAAVVALINRQIC-TSSHTIASI 935
Cdd:cd14888   316 SLLGVDAEDLLNA---LCYRTIKTAHEFYTKPLRVDE----AEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFC 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  936 MLIDTPGFQN-PASCGQQvgatladLRHNYLQERLQMLFHHTTLVAPRDRYAQElvEIEMDlasechpgPLislidKAPQ 1014
Cdd:cd14888   389 GVLDIFGFECfQLNSFEQ-------LCINFTNERLQQFFNNFVFKCEEKLYIEE--GISWN--------PL-----DFPD 446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1015 NhvvrSSQRDLREHDRRGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKcaGPRQFVLHHLQGtnPVLYAVDG 1094
Cdd:cd14888   447 N----QDCVDLLQEKPLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVKT--DPNSFVIVHFAG--PVKYCSDG 518
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1095 WVRHSREHPGIrNAVSLLQDSSREEINRLYIGSLTRGSgamvfcgsfaglEGTQSLRRVSSIRRSFttagvkRNSImlqv 1174
Cdd:cd14888   519 FLEKNKDQLSV-DAQEVIKNSKNPFISNLFSAYLRRGT------------DGNTKKKKFVTVSSEF------RNQL---- 575
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1175 kftvDGIIDTLRRTGTHFVHCyllqhnagkhTKYTANGSPssaagqvsSEEEMVNVpllRSQLRGSQVLEAARLHRLGFP 1254
Cdd:cd14888   576 ----DVLMETIDKTEPHFIRC----------IKPNSQNVP--------DLFDRISV---NEQLKYGGVLQAVQVSRAGYP 630
                         730
                  ....*....|....*.
gi 116008016 1255 ESVPLLEFVRRFGLLA 1270
Cdd:cd14888   631 VRLSHAEFYNDYRILL 646
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
575-1305 2.31e-41

class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276869  Cd Length: 653  Bit Score: 163.96  E-value: 2.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPL-SLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd14904     1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIdNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  654 GRSGSGKSTSFKHALNYLALAAGAYNNFINAeKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVL 733
Cdd:cd14904    81 GESGAGKTETTKIVMNHLASVAGGRKDKTIA-KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  734 LPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLEnitSEDSHPFI--SLSQKLEDRHRAANDFMRTVQAFETLNID 811
Cdd:cd14904   160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLD---PNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSLIGLD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  812 AKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDlssaAFGLTQPNAPNGGLSPSKSPTS 891
Cdd:cd14904   237 NDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQVAKMLGLPTTRIEE----ALCNRSVVTRNESVTVPLAPVE 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  892 dtghewAWECLEALVIGLYSEALAAVVALINRQICTSSHTI-ASIMLIDTPGFQNPASCGqqvgatLADLRHNYLQERLQ 970
Cdd:cd14904   313 ------AEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIkGQIGVLDIFGFEDFAHNG------FEQFCINYANEKLQ 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  971 MLFHHTTLVAPRDRYAQElvEIEMDLASECHPGPLISLIDkapqnhvvrssqrdlrehDRRGMLWLLDEEAIYPNSNDDT 1050
Cdd:cd14904   381 QKFTTDVFKTVEEEYIRE--GLQWDHIEYQDNQGIVEVID------------------GKMGIIALMNDHLRQPRGTEEA 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1051 FLERLFSHYGDREHHSLLRKCAGPR-QFVLHHLQGtnPVLYAVDGWVRHSREHPGiRNAVSLLQDSSREEINRLYIGSLT 1129
Cdd:cd14904   441 LVNKIRTNHQTKKDNESIDFPKVKRtQFIINHYAG--PVTYETVGFMEKHRDTLQ-NDLLDLVLLSSLDLLTELFGSSEA 517
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1130 RGSGAMvfcgsfaglegtqslrrvsSIRRSFTTAgvkRNSIMLQVKFTVDGIIDTLRRTGTHFVHCyllqhnagkhTKYT 1209
Cdd:cd14904   518 PSETKE-------------------GKSGKGTKA---PKSLGSQFKTSLSQLMDNIKTTNTHYVRC----------IKPN 565
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1210 ANGSPSSAAGQVSSEeemvnvpllrsQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLASNKDV---SVEQILA 1286
Cdd:cd14904   566 ANKSPTEFDKRMVVE-----------QLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSKDVrrtCSVFMTA 634
                         730
                  ....*....|....*....
gi 116008016 1287 VNELDVASYRIGPSQILFR 1305
Cdd:cd14904   635 IGRKSPLEYQIGKSLIYFK 653
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
575-1094 5.72e-40

class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276872 [Multi-domain]  Cd Length: 669  Bit Score: 159.81  E-value: 5.72e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRGCKTE--------DMPPHVYSLAQTAYRSLVETR 645
Cdd:cd14907     1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  646 RDQSLIFMGRSGSGKSTSFKHALNYLalaAGAYNNFINAEKVNALCT---------------------ILEAFGNTKTCL 704
Cdd:cd14907    81 KKQAIVISGESGAGKTENAKYAMKFL---TQLSQQEQNSEEVLTLTSsiratskstksieqkilscnpILEAFGNAKTVR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  705 NSNATRMTQLLSLDFD-QTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDSHPFIS 783
Cdd:cd14907   158 NDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDRYDYLK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  784 LSQKLEdrHRAAND---FMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLG 860
Cdd:cd14907   238 KSNCYE--VDTINDeklFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSPCCVKNKETLQIIAKLLG 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  861 VNLEDLSSAAfgLTQPNAPNGGL--SPSKSPtsdtghewawEC---LEALVIGLYSEALAAVVALINRQI--------CT 927
Cdd:cd14907   316 IDEEELKEAL--TTKIRKVGNQVitSPLSKK----------ECinnRDSLSKELYDRLFNWLVERLNDTImpkdekdqQL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  928 SSHTIASIMLIDTPGFQNPASCG-QQvgatladLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEMDLASECHPGPLI 1006
Cdd:cd14907   384 FQNKYLSIGLLDIFGFEVFQNNSfEQ-------LCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLNQLSYTDNQDVI 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1007 SLIDKAPQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRqFVLHHLQGtn 1086
Cdd:cd14907   457 DLLDKPPI-----------------GIFNLLDDSCKLATGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAK-- 516

                  ....*...
gi 116008016 1087 PVLYAVDG 1094
Cdd:cd14907   517 EVEYNIEG 524
PTZ00014 PTZ00014
myosin-A; Provisional
541-867 8.98e-40

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 160.97  E-value: 8.98e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  541 NGEQLTVDEDDVEKQNSPA-LDLVEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFR 619
Cdd:PTZ00014   75 TNSTFEVKPEHAFNANSQIdPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYR 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  620 GCK-TEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCTILEAFG 698
Cdd:PTZ00014  155 DAKdSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVLEAFG 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  699 NTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITsedS 778
Cdd:PTZ00014  235 NAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLE---E 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  779 HPFISLS----QKLEDrhraANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG---IAGVTKLGTGSTARTQFANPTA 851
Cdd:PTZ00014  312 YKYINPKcldvPGIDD----VKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGnveIEGKEEGGLTDAAAISDESLEV 387
                         330
                  ....*....|....*.
gi 116008016  852 ARKASGLLGVNLEDLS 867
Cdd:PTZ00014  388 FNEACELLFLDYESLK 403
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
577-1305 5.51e-39

class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276854  Cd Length: 659  Bit Score: 156.61  E-value: 5.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  577 VLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLV----ETRRDQSLIF 652
Cdd:cd14889     3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  653 MGRSGSGKSTSFKHALNYL-ALAAGAYNNFINAEKVNALctiLEAFGNTKTCLNSNATRMTQLLSLDFdQTGQIASASLQ 731
Cdd:cd14889    83 SGESGAGKTESTKLLLRQImELCRGNSQLEQQILQVNPL---LEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  732 VLLPERQRAGRRLGHEHSFHIMTRLLAGAAgLLQKELHleNITSEDSHPFISlsqkledrHRAANDfmRTVQAFETLN-- 809
Cdd:cd14889   159 EYLLEKSRVVHQDGGEENFHIFYYMFAGIS-AEDRENY--GLLDPGKYRYLN--------NGAGCK--REVQYWKKKYde 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  810 -IDAKAVRG--------IWSILAAIYHLGiaGVTKLGTGSTA-RTQFANPTAARKASGLLGVNLEDLSSAafgLTQPNAP 879
Cdd:cd14889   226 vCNAMDMVGfteqeevdMFTILAGILSLG--NITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKT---LTCTVTF 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  880 NGGLSPSKSPTSdtghEWAWECLEALVIGLYSEALAAVVALINRQIC---TSSHTIASIMLIDTPGFQNPA-SCGQQVGA 955
Cdd:cd14889   301 TRGEQIQRHHTK----QQAEDARDSIAKVAYGRVFGWIVSKINQLLApkdDSSVELREIGILDIFGFENFAvNRFEQACI 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  956 TLADlrhnylqERLQMLFHHTTLVAPRDRYAQElvEIEMDLASECHPGPLISLIDKAPQnhvvrssqrdlrehdrrGMLW 1035
Cdd:cd14889   377 NLAN-------EQLQYFFNHHIFLMEQKEYKKE--GIDWKEITYKDNKPILDLFLNKPI-----------------GILS 430
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1036 LLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAgpRQFVLHHLQGTnpVLYAVDGWVRHSREH--PGIRnavSLLQ 1113
Cdd:cd14889   431 LLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSKS--PKFTVNHYAGK--VTYNASGFLEKNRDTipASIR---TLFI 503
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1114 DSSREEINRLYIGSLTRgsgamvfcgsfaglEGTQSLRRVSSIRRSFTTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFV 1193
Cdd:cd14889   504 NSATPLLSVLFTATRSR--------------TGTLMPRAKLPQAGSDNFNSTRKQSVGAQFKHSLGVLMEKMFAASPHFV 569
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1194 HCYLLQHNagkhtkytangspsSAAGQVSSEeemvnvpLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFG--LLAG 1271
Cdd:cd14889   570 RCIKPNHV--------------KVPGQLDSK-------YIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKilLCEP 628
                         730       740       750
                  ....*....|....*....|....*....|....
gi 116008016 1272 DLASNKDvSVEQILavNELDVASYRIGPSQILFR 1305
Cdd:cd14889   629 ALPGTKQ-SCLRIL--KATKLVGWKCGKTRLFFK 659
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
575-1289 4.49e-38

class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276871 [Multi-domain]  Cd Length: 715  Bit Score: 154.75  E-value: 4.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRGCKT-EDMPPHVYSLAQTAYRSLVETRRDQSLIF 652
Cdd:cd14906     1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  653 MGRSGSGKSTSFKHALNYLALAAGAY----------NNFINAEKVNAlCTILEAFGNTKTCLNSNATRMTQLLSLDFDQT 722
Cdd:cd14906    81 SGESGSGKTEASKTILQYLINTSSSNqqqnnnnnnnNNSIEKDILTS-NPILEAFGNSRTTKNHNSSRFGKFLKIEFRSS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  723 -GQIASASLQVLLPERQRAGRRLGHEH-SFHIMTRLLAGAAGLLQKELHLENITSEDSH---------PFISLSQKLEDR 791
Cdd:cd14906   160 dGKIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYldarddvisSFKSQSSNKNSN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  792 HRAAND----FMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAA-RKASGLLGVNLEDL 866
Cdd:cd14906   240 HNNKTEsiesFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASlESVSKLLGYIESVF 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  867 SSAafgLTQPNAPNGGLSPSKSPTSDTGHewAWECLEALVIGLYSEALAAVVALINR-----------QICTSSHTIASI 935
Cdd:cd14906   320 KQA---LLNRNLKAGGRGSVYCRPMEVAQ--SEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFI 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  936 MLIDTPGFQNPAScgqqvgATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVeiemdlasechPGPLISLIDKapqn 1015
Cdd:cd14906   395 GVLDIFGFENLSS------NSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGI-----------PWSNSNFIDN---- 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1016 hvvrSSQRDLREHDRRGMLWLLDEEAIYPNSNDDTFLERLFSHYgdREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGW 1095
Cdd:cd14906   454 ----KECIELIEKKSDGILSLLDDECIMPKGSEQSLLEKYNKQY--HNTNQYYQRTLAKGTLGIKHFAGD--VTYQTDGW 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1096 VRHSRehpgirnavsllqDSSREEINRLyigsLTRGSGAMVfcgsfAGLEGTQSLRRVSSIRRSfttagVKRNSIMLQVK 1175
Cdd:cd14906   526 LEKNR-------------DSLYSDVEDL----LLASSNFLK-----KSLFQQQITSTTNTTKKQ-----TQSNTVSGQFL 578
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1176 FTVDGIIDTLRRTGTHFVHCylLQHNagkhtkytangspssaagqVSSEEEMVNVPLLRSQLRGSQVLEAARLHRLGFPE 1255
Cdd:cd14906   579 EQLNQLIQTINSTSVHYIRC--IKPN-------------------QTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSY 637
                         730       740       750
                  ....*....|....*....|....*....|....
gi 116008016 1256 SVPLLEFVRRFGLLAGDLasNKDVSVEQILAVNE 1289
Cdd:cd14906   638 RRDFNQFFSRYKCIVDMY--NRKNNNNPKLASQL 669
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
575-1305 9.17e-37

class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276852  Cd Length: 725  Bit Score: 150.57  E-value: 9.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYAS--------NLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRR 646
Cdd:cd14887     1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  647 DQSLIFMGRSGSGKSTSFKHALNYLALAA---GAYNNFINAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTG 723
Cdd:cd14887    81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  724 QIASASLQVLLPERQRAGRRLGHEHSFHIMTRLL-AGAAGLLQKELHLEnitsEDSHPFislsqkledrhraanDFMRTV 802
Cdd:cd14887   161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCnAAVAAATQKSSAGE----GDPEST---------------DLRRIT 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  803 QAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTA------ARKASGLLGVnlEDLSSaafGLTQP 876
Cdd:cd14887   222 AAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSvgceetAADRSHSSEV--KCLSS---GLKVT 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  877 NAPNGGL-SPSKSPTSDTGHEWAWECLEALVI------------------------GLYSEALAAVVALINRQICTSSHT 931
Cdd:cd14887   297 EASRKHLkTVARLLGLPPGVEGEEMLRLALVSrsvretrsffdldgaaaardaackNLYSRAFDAVVARINAGLQRSAKP 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  932 IAS--------------IMLIDTPGFQNPASCGQQvgaTLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEMDLA 997
Cdd:cd14887   377 SESdsdedtpsttgtqtIGILDLFGFEDLRNHSKN---RLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCS 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  998 SECHPGPLISLIDKAPQNHV-------VRSSQRDLREHDRRGMLWLL-DEEAIYPNSNDDTFLERLFSHYGDREHHSLLR 1069
Cdd:cd14887   454 AFPFSFPLASTLTSSPSSTSpfsptpsFRSSSAFATSPSLPSSLSSLsSSLSSSPPVWEGRDNSDLFYEKLNKNIINSAK 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1070 KCAGPR-------QFVLHHLQGTnpVLYAVDGWVRHSRehpgirnavsllqDSSREEINRLYIGsltrgsgamvfCGSFA 1142
Cdd:cd14887   534 YKNITPalsrenlEFTVSHFACD--VTYDARDFCRANR-------------EATSDELERLFLA-----------CSTYT 587
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1143 GLEGTQSLRRVSSIRRsfttagvKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCylLQHNAGKHTKytangspssaagqvs 1222
Cdd:cd14887   588 RLVGSKKNSGVRAISS-------RRSTLSAQFASQLQQVLKALQETSCHFIRC--VKPNRVQEAG--------------- 643
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1223 seeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRF-GLLAGDL--ASNKDVSVEQILAVNELDVASYRIGP 1299
Cdd:cd14887   644 ----IFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYeTKLPMALreALTPKMFCKIVLMFLEINSNSYTFGK 719

                  ....*.
gi 116008016 1300 SQILFR 1305
Cdd:cd14887   720 TKIFFR 725
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
575-1305 3.92e-35

class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276856  Cd Length: 645  Bit Score: 144.80  E-value: 3.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIH--TKAGPTLLVVNPMAPLSlysEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETR---RDQS 649
Cdd:cd14891     1 AGILHNLEERSKLDNQRpyTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  650 LIFMGRSGSGKSTSFKHALNYL--------ALAAGAYNNFINAEKVNALCT---------ILEAFGNTKTCLNSNATRMT 712
Cdd:cd14891    78 IVISGESGAGKTETSKIILRFLttravggkKASGQDIEQSSKKRKLSVTSLderlmdtnpILESFGNAKTLRNHNSSRFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  713 QLLSLDF-DQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITsedshPFISLSQ----K 787
Cdd:cd14891   158 KFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPE-----DFIYLNQsgcvS 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  788 LEDRHRAANdFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGT--GSTARTQFANPTAARKASGLLGVNLED 865
Cdd:cd14891   233 DDNIDDAAN-FDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTseGEAEIASESDKEALATAAELLGVDEEA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  866 LSSAafgLTQP-------------NAPNGGLSPsksptsdtghewaweclEALVIGLYSEALAAVVALINRQICTSSHTI 932
Cdd:cd14891   312 LEKV---ITQReivtrgetftikrNAREAVYSR-----------------DAIAKSIYERLFLWIVQQINTSLGHDPDPL 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  933 ASIMLIDTPGFQN--PASCGQQvgatladLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEMDLAS---EChpgplIS 1007
Cdd:cd14891   372 PYIGVLDIFGFESfeTKNDFEQ-------LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPdnrEC-----LD 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1008 LIDKAPQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGD-----REHHSLLRKCagprqFVLHHL 1082
Cdd:cd14891   440 LIASKPN-----------------GILPLLDNEARNPNPSDAKLNETLHKTHKRhpcfpRPHPKDMREM-----FIVKHY 497
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1083 QGTnpVLYAVDGWVRhsrehpgiRNAVSLLQDssreeinrlyIGSLTRGSGAmvFCGSFAGLEGTQSLRRVSSIRrsftt 1162
Cdd:cd14891   498 AGT--VSYTIGSFID--------KNNDIIPED----------FEDLLASSAK--FSDQMQELVDTLEATRCNFIR----- 550
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1163 aGVKRNSIMlqvkftvdgiidtlrRTGtHFVHCYLLQhnagkhtkytangspssaagqvsseeemvnvpllrsQLRGSQV 1242
Cdd:cd14891   551 -CIKPNAAM---------------KVG-VFDNRYVVD------------------------------------QLRCSGI 577
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116008016 1243 LEAARLHRLGFPESVPLLEFVRRFGLLAGD----LASNKDVS-VEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14891   578 LQTCEVLKVGLPTRVTYAELVDVYKPVLPPsvtrLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
1380-2067 9.84e-35

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: 145.70  E-value: 9.84e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1380 NVHRTEEQLKTANEELlmlRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEerstahiaTERLEAETAERL-KLEKEL 1458
Cdd:pfam01576  374 NLEKAKQALESENAEL---QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--------SERQRAELAEKLsKLQSEL 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1459 GDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDgvgggvyKLKYERVARELEFTKRRLHTQHEHDLEQLVAL 1538
Cdd:pfam01576  443 ESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ-------KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNV 515
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1539 KKH---LEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQ- 1614
Cdd:pfam01576  516 ERQlstLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQl 595
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1615 --AKERYGREKDVLQAEKFTLEQTLADTRLDLEF----KEEKLASLQRELEEMTfggGTEEEFA---------------- 1672
Cdd:pfam01576  596 vsNLEKKQKKFDQMLAEEKAISARYAEERDRAEAeareKETRALSLARALEEAL---EAKEELErtnkqlraemedlvss 672
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1673 ---------QLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIK 1743
Cdd:pfam01576  673 kddvgknvhELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVR 752
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1744 ALECQLETEHEERTLLLREKHELERRLSSMEDR-DRVDRDAEEALNQklrrdLRKYKALLKDAQTQLERLKADTpgktli 1822
Cdd:pfam01576  753 ELEAELEDERKQRAQAVAAKKKLELDLKELEAQiDAANKGREEAVKQ-----LKKLQAQMKDLQRELEEARASR------ 821
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1823 RQLRNQLEDAEsarslamKARQTAEAELTEVQAMFDESHRARNDAEEranaahrDRAELQAQIEENEeelgelmKKYSAT 1902
Cdd:pfam01576  822 DEILAQSKESE-------KKLKNLEAELLQLQEDLAASERARRQAQQ-------ERDELADEIASGA-------SGKSAL 880
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1903 VKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLD--NVENLGDPSMAMMS----KRLELRTKELESRL-ELEQA 1975
Cdd:pfam01576  881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEqlTTELAAERSTSQKSesarQQLERQNKELKAKLqEMEGT 960
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1976 TRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDM-----REEFHAVSSREQ--ESLTRRKDLEKKVE 2048
Cdd:pfam01576  961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVllqveDERRHADQYKDQaeKGNSRMKQLKRQLE 1040
                          730
                   ....*....|....*....
gi 116008016  2049 QMESEgAALKNDLRLALQR 2067
Cdd:pfam01576 1041 EAEEE-ASRANAARRKLQR 1058
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
575-1269 4.88e-34

class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276873 [Multi-domain]  Cd Length: 682  Bit Score: 141.58  E-value: 4.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFR--GC-------KTEDMPPHVYSLAQTAYRSLV-ET 644
Cdd:cd14908     1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLlrsqgieSPQALGPHVFAIADRSYRQMMsEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  645 RRDQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINA----------EKVNALCTILEAFGNTKTCLNSNATRMTQL 714
Cdd:cd14908    81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgeelgklsimDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  715 LSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQK--ELHLENITSEDSHPFISLS------- 785
Cdd:cd14908   161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyEFHDGITGGLQLPNEFHYTgqggapd 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  786 -QKLEDRhraaNDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG---IAGVTKLGTGSTArtQFANPTAARKASGLLGV 861
Cdd:cd14908   241 lREFTDE----DGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGqleFESKEEDGAAEIA--EEGNEKCLARVAKLLGV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  862 NLEDLSSAafgLTQPNAPNGGlspsKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQI-CTSSHTI-ASIMLID 939
Cdd:cd14908   315 DVDKLLRA---LTSKIIVVRG----KEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInWENDKDIrSSVGVLD 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  940 TPGFQNPAScgqqvgATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEChpgplislidkapqnh 1016
Cdd:cd14908   388 IFGFECFAH------NSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEwafIEFPDNQDC---------------- 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1017 vvrssqRDLREHDRRGMLWLLDEEAIYP-NSNDDTFLERLFSHY---GDREHHSLLRKCAGPRQ-----FVLHHlqgtnp 1087
Cdd:cd14908   446 ------LDTIQAKKKGILTMLDDECRLGiRGSDANYASRLYETYlpeKNQTHSENTRFEATSIQktkliFAVRH------ 513
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1088 vlYAvdGWVRHSREhpgirnavSLLQDSSREEInrlyigSLTRGSgamvfcgSFAglEGTqslrrvssirrsfttagvkr 1167
Cdd:cd14908   514 --FA--GQVQYTVE--------TTFCEKNKDEI------PLTADS-------LFE--SGQ-------------------- 546
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1168 nsimlQVKFTVDGIIDTLRRTGTHFVHCYllqhnagkhtkytangSPSSAAgqvssEEEMVNVPLLRSQLRGSQVLEAAR 1247
Cdd:cd14908   547 -----QFKAQLHSLIEMIEDTDPHYIRCI----------------KPNDAA-----KPDLVTRKRVTEQLRYGGVLEAVR 600
                         730       740
                  ....*....|....*....|..
gi 116008016 1248 LHRLGFPESVPLLEFVRRFGLL 1269
Cdd:cd14908   601 VARSGYPVRLPHKDFFKRYRML 622
PDZ_MYO18-like cd06747
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein ...
337-426 2.35e-33

PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MYO18 protein and related domains. MYO18 (also known as myosin XVIIIA, KIAA0216, MysPDZ), a member of the myosin superfamily, is involved in regulating cell protrusion and migration, and Golgi trafficking and morphology, and is required for myoblast adhesion and muscle integrity. The MYO18A/MRCK/LRAP35a complex regulates actomyosin retrograde flow in cell protrusion and migration; the PtdIns(4)P/GOLPH3/MYO18A/F-actin complex is a hub for signals that regulate Golgi trafficking function. The MYO18A PDZ domain binds p190Rho-guanine nucleotide exchange factor (p190RhoGEF), Golgin45, and leucine repeat adaptor protein 1 (Lurap1, also known as Lrap35a). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MYO18-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467229 [Multi-domain]  Cd Length: 90  Bit Score: 124.35  E-value: 2.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  337 QLVIRRQksPRQDFGFSLRKAICLDRTESLTSPIFRPVIFAEPGAGGGATGL--LPGDRLIKVNGTPVGELPREIIIEMI 414
Cdd:cd06747     1 EITLKRQ--PTGDFGFSLRRGTIVERGPDDGQELKRTVHFAEPGAGTKNLATglLPGDRLIEVNGVNVENASRDEIIEMI 78
                          90
                  ....*....|..
gi 116008016  415 RNSGEAVTVEVQ 426
Cdd:cd06747    79 RKSGDTVTLKVQ 90
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
575-866 5.48e-32

class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276843  Cd Length: 649  Bit Score: 135.12  E-value: 5.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGC-KTEDMPPHVYSLAQTAYRSLVETRRDQSLIFM 653
Cdd:cd14876     1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDApDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  654 GRSGSGKSTSFKHALNYLALAA-GAYNNFINaEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQV 732
Cdd:cd14876    81 GESGAGKTEATKQIMRYFASAKsGNMDLRIQ-TAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  733 LLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENItseDSHPFISLS----QKLEDRhraaNDFMRTVQAFETL 808
Cdd:cd14876   160 FLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGL---KEYKFLNPKcldvPGIDDV----ADFEEVLESLKSM 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116008016  809 NIDAKAVRGIWSILAAIYHLG---IAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDL 866
Cdd:cd14876   233 GLTEEQIDTVFSIVSGVLLLGnvkITGKTEQGVDDAAAISNESLEVFKEACSLLFLDPEAL 293
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
576-1280 8.28e-32

class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276865  Cd Length: 627  Bit Score: 134.28  E-value: 8.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPL-SLYS----EKVVSMF--RGCKTED-----MPPHVYSLAQTAYRSLVE 643
Cdd:cd14900     2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLpGLYSsdtmAKYLLSFeaRSSSTRNkgsdpMPPHIYQVAGEAYKAMML 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  644 TRR----DQSLIFMGRSGSGKSTSFKHALNYLAlAAGAYNNFIN----------AEKVNALCTILEAFGNTKTCLNSNAT 709
Cdd:cd14900    82 GLNgvmsDQSILVSGESGSGKTESTKFLMEYLA-QAGDNNLAASvsmgkstsgiAAKVLQTNILLESFGNARTLRNDNSS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  710 RMTQLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAgllqkelhlenitsedshpfislsqkle 789
Cdd:cd14900   161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGAS---------------------------- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  790 DRHRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG--IAGVTKLGTGSTARTQFANPT--AARKASG-LLGVNLE 864
Cdd:cd14900   213 EAARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGnlTFEHDENSDRLGQLKSDLAPSsiWSRDAAAtLLSVDAT 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  865 DLSSAafgLTQPNAPNGGLSPSKSPTSDTghewAWECLEALVIGLYSEALAAVVALINR-----QICTSSHTIASIMLID 939
Cdd:cd14900   293 KLEKA---LSVRRIRAGTDFVSMKLSAAQ----ANNARDALAKALYGRLFDWLVGKMNAflkmdDSSKSHGGLHFIGILD 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  940 TPGFQN-PASCGQQvgatladLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEChpgplISLIDKAPQn 1015
Cdd:cd14900   366 IFGFEVfPKNSFEQ-------LCINFANETLQQQFNDYVFKAEQREYESQGVDwkyVEFCDNQDC-----VNLISQRPT- 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1016 hvvrssqrdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGW 1095
Cdd:cd14900   433 ----------------GILSLIDEECVMPKGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGH--VEYSTDGF 494
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1096 VRHSRehpgirnavsllqDSSREEINRLYigsltrgsgamVFCGSFaglegtqslrrvssirrsfttagvkrnsimlqvK 1175
Cdd:cd14900   495 LEKNK-------------DVLHQEAVDLF-----------VYGLQF---------------------------------K 517
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1176 FTVDGIIDTLRRTGTHFVHCylLQHNagkhtkytangspSSAAGQVSSEEEMVNvpllrsQLRGSQVLEAARLHRLGFPE 1255
Cdd:cd14900   518 EQLTTLLETLQQTNPHYVRC--LKPN-------------DLCKAGIYERERVLN------QLRCNGVMEAVRVARAGFPI 576
                         730       740
                  ....*....|....*....|....*
gi 116008016 1256 SVPLLEFVRRFGLLAGDLASNKDVS 1280
Cdd:cd14900   577 RLLHDEFVARYFSLARAKNRLLAKK 601
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
575-869 2.42e-31

class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276844 [Multi-domain]  Cd Length: 656  Bit Score: 133.02  E-value: 2.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFR---GCKTEDMPPHVYSLAQTAYRSLVETRRDQSLI 651
Cdd:cd14878     1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  652 FMGRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCtILEAFGNTKTCLNSNATRMTQLLSLDF-DQTGQIASASL 730
Cdd:cd14878    81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFKHVNC-ILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  731 QVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITsedSHPFisLSQKL-EDRHRAANDFMRT-----VQA 804
Cdd:cd14878   160 YTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLC---AHRY--LNQTMrEDVSTAERSLNREklavlKQA 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016  805 FETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTqfANPTAARKASGLLGVNLEDLSSA 869
Cdd:cd14878   235 LNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFV--SDLQLLEQVAGMLQVSTDELASA 297
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
575-1270 2.71e-31

class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276846 [Multi-domain]  Cd Length: 658  Bit Score: 133.05  E-value: 2.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRGC-KTEDMPPHVYSLAQTAYR---SLVETRrDQS 649
Cdd:cd14880     1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAApQPQKLKPHIFTVGEQTYRnvkSLIEPV-NQS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  650 LIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNAL-------CTILEAFGNTKTCLNSNATRMTQLLSLDFDQT 722
Cdd:cd14880    80 IVVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIeqrilnsNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  723 GQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDSHPfiSLSQKLEDrhraaNDFMRTV 802
Cdd:cd14880   160 QQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLP--NPERNLEE-----DCFEVTR 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  803 QAFETLNIDAKAVRGIWSILAAIYHLGiagvtklgtgstaRTQFANPTAARKASGLLGVNLEDLSSAAFGLTQPNAP--- 879
Cdd:cd14880   233 EAMLHLGIDTPTQNNIFKVLAGLLHLG-------------NIQFADSEDEAQPCQPMDDTKESVRTSALLLKLPEDHlle 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  880 ---------NGGLSPSKSPTSDTGHEWAWECLEALViglYSEALAAVVALINRQICTSSHTIAS-IMLIDTPGFQN-PAS 948
Cdd:cd14880   300 tlqirtiraGKQQQVFKKPCSRAECDTRRDCLAKLI---YARLFDWLVSVINSSICADTDSWTTfIGLLDVYGFESfPEN 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  949 cgqqvgaTLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEmdlasechpgpLISLIDKapQNHVvrssqrDLREH 1028
Cdd:cd14880   377 -------SLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWS-----------FINYQDN--QTCL------DLIEG 430
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1029 DRRGMLWLLDEEAIYPNSND----DTFLERLFSHYGDREHHSLLRKcagpRQFVLHHLQGtnPVLYAVDGWVRHSREhPG 1104
Cdd:cd14880   431 SPISICSLINEECRLNRPSSaaqlQTRIESALAGNPCLGHNKLSRE----PSFIVVHYAG--PVRYHTAGLVEKNKD-PV 503
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1105 IRNAVSLLQDSSREEINRLyigsltrgsgamvfcgsFAGLEGTQSLRRVSSIRRSfttAGVkrnSIMLQVKFTVDGIIDT 1184
Cdd:cd14880   504 PPELTRLLQQSQDPLLQKL-----------------FPANPEEKTQEEPSGQSRA---PVL---TVVSKFKASLEQLLQV 560
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1185 LRRTGTHFVHCylLQHNAGkhtkytangspssAAGQVSSEEEMVnvpllrSQLRGSQVLEAARLHRLGFPESVPLLEFVR 1264
Cdd:cd14880   561 LHSTTPHYIRC--IKPNSQ-------------CQAQTFLQEEVL------SQLEACGLVETIHISAAGFPIRVSHQNFVE 619

                  ....*.
gi 116008016 1265 RFGLLA 1270
Cdd:cd14880   620 RYKLLR 625
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
575-1305 9.41e-30

class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276897  Cd Length: 637  Bit Score: 127.82  E-value: 9.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYsekvVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14937     1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLaLAAGAYNNFINaekvNALCT---ILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQ 731
Cdd:cd14937    77 ESGSGKTEASKLVIKYY-LSGVKEDNEIS----NTLWDsnfILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  732 VLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELhleNITSEDSHPFISLSQKLEDRHRAANDFMRTVQAFETLNI- 810
Cdd:cd14937   152 IFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKY---KIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMh 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  811 DAKavRGIWSILAAIYHLG---IAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDL---------SSAAFGLTQPNA 878
Cdd:cd14937   229 DMK--DDLFLTLSGLLLLGnveYQEIEKGGKTNCSELDKNNLELVNEISNLLGINYENLkdclvftekTIANQKIEIPLS 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  879 PNGGLSPSKSPTSDtghewaweclealvigLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQnpascgQQVGATLA 958
Cdd:cd14937   307 VEESVSICKSISKD----------------LYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFE------IFSKNSLE 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  959 DLRHNYLQERLQMLFHHTTLVAPRDRYAQElveiemdlasechpGPLISLIDKAPQNHVVrssqrDLREhDRRGMLWLLD 1038
Cdd:cd14937   365 QLLINIANEEIHSIYLYIVYEKETELYKAE--------------DILIESVKYTTNESII-----DLLR-GKTSIISILE 424
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1039 EEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGpRQFVLHHLqgTNPVLYAVDGWVRHSREHPGiRNAVSLLQDSSRE 1118
Cdd:cd14937   425 DSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDIN-KNFVIKHT--VSDVTYTITNFISKNKDILP-SNIVRLLKVSNNK 500
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1119 EINRLYigsltrgsgamvfcgsfAGLEGTQSLRRvssirrsfttagvkRNSIMLQVKFTVDGIIDTLRRTGTHFVHCylL 1198
Cdd:cd14937   501 LVRSLY-----------------EDVEVSESLGR--------------KNLITFKYLKNLNNIISYLKSTNIYFIKC--I 547
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1199 QHNAGKhtkytangspssaagqvssEEEMVNVPLLRSQLRGSQVLEAARLhRLGFPESVPLLEFVRRFGLLagDLASNKD 1278
Cdd:cd14937   548 KPNENK-------------------EKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYL--DYSTSKD 605
                         730       740       750
                  ....*....|....*....|....*....|..
gi 116008016 1279 VSVEQ-----ILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14937   606 SSLTDkekvsMILQNTVDPDLYKVGKTMVFLK 637
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
575-1305 7.91e-27

class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276851  Cd Length: 650  Bit Score: 118.84  E-value: 7.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRGCKTE-----DMPPHVYSLAQTAYRSLVETRRDQ 648
Cdd:cd14886     1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  649 SLIFMGRSGSGKSTSFKHALNYLalaagAYNNFINAEKVNALC----TILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQ 724
Cdd:cd14886    81 SCIVSGESGAGKTETAKQLMNFF-----AYGHSTSSTDVQSLIlgsnPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  725 IASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITS---------------EDSHPFISLSQKLE 789
Cdd:cd14886   156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESynflnaskcydapgiDDQKEFAPVRSQLE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  790 D--RHRAANDFMRTVQAFETL-NIDAKAvrgiwsilaaiyhlgiagVTKLGTGSTARtqFANPTAARKASGLLGVNLEDL 866
Cdd:cd14886   236 KlfSKNEIDSFYKCISGILLAgNIEFSE------------------EGDMGVINAAK--ISNDEDFGKMCELLGIESSKA 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  867 SSAAfgLTQPNAPNGglspsKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQ-- 944
Cdd:cd14886   296 AQAI--ITKVVVINN-----ETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEff 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  945 --NpascgqqvgaTLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEMDLASEchPGPLISLIDKAPQnhvvrssq 1022
Cdd:cd14886   369 erN----------TYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFTD--NSNVLAVFDKPNL-------- 428
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1023 rdlrehdrrGMLWLLDEEAIYPNSNDDTFLERLFSHYGDrehHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSReH 1102
Cdd:cd14886   429 ---------SIFSFLEEQCLIQTGSSEKFTSSCKSKIKN---NSFIPGKGSQCNFTIVHTAAT--VTYNTEEFVDKNK-H 493
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1103 PGIRNAVSLLQDSsreeinrlyigsltrgsgamvfcgsfaglegTQSLRRVSSIRRSFTTAGVKRNSIMLQVKFTVDGII 1182
Cdd:cd14886   494 KLSVDILELLMGS-------------------------------TNPIVNKAFSDIPNEDGNMKGKFLGSTFQLSIDQLM 542
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1183 DTLRRTGTHFVHCylLQHNAGKHTKYTANGSpssaagqvsseeemvnvplLRSQLRGSQVLEAAR-LHRlGFPESVPLLE 1261
Cdd:cd14886   543 KTLSATKSHFIRC--IKTNQDKVPNKYETKS-------------------VYNQLISLSIFESIQtIHR-GFAYNDTFEE 600
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|
gi 116008016 1262 FVRRFGLL------AGDLASNKDVSVEQILAVNELDVASYRIGPSQILFR 1305
Cdd:cd14886   601 FFHRNKILishnssSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
578-1195 1.40e-24

class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276858  Cd Length: 741  Bit Score: 111.99  E-value: 1.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  578 LHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLY----------SEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRD 647
Cdd:cd14893     4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYtpdhmqaynkSREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  648 QSLIFMGRSGSGKSTSFKHALNYL------------ALAAGAYNNFINAEKVNALcTILEAFGNTKTCLNSNATRMTQLL 715
Cdd:cd14893    84 QAVILLGGMGAGKSEAAKLIVQYLceigdeteprpdSEGASGVLHPIGQQILHAF-TILEAFGNAATRQNRNSSRFAKMI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  716 SLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAG--LLQKELHLENITSEdshpFISLSQKLEDRHR 793
Cdd:cd14893   163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMNKCVNE----FVMLKQADPLATN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  794 ---AANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG--------IAGVTKLGTGSTARTQFANPTAARKASGLLGVN 862
Cdd:cd14893   239 falDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGnvdfvpdpEGGKSVGGANSTTVSDAQSCALKDPAQILLAAK 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  863 LEDLSSAA----FGLTQPNAPNGGLSPSkSPTSDTGHEwAWECLEALVIGLYS-------EALAAVVALINRQICTSSHT 931
Cdd:cd14893   319 LLEVEPVVldnyFRTRQFFSKDGNKTVS-SLKVVTVHQ-ARKARDTFVRSLYEslfnflvETLNGILGGIFDRYEKSNIV 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  932 IAS--IMLIDTPGFQNPAScgQQVGatLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEMDLASEchpgpliSLI 1009
Cdd:cd14893   397 INSqgVHVLDMVGFENLTP--SQNS--FDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVENRLTVN-------SNV 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1010 D-KAPQNHVVrssqrDLREHDRRGMLWLLDEEAIYPNSNDDTFLERLFShyGDREHHSLLRKCAG----------PRQ-- 1076
Cdd:cd14893   466 DiTSEQEKCL-----QLFEDKPFGIFDLLTENCKVRLPNDEDFVNKLFS--GNEAVGGLSRPNMGadttneylapSKDwr 538
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1077 --FVLHHLQGTnpVLYAVDGWvrHSREHPGIRNAVSLLQDSSREEINRlyigslTRGSGAMVFCGSFAGLEGTQSLRRVS 1154
Cdd:cd14893   539 llFIVQHHCGK--VTYNGKGL--SSKNMLSISSTCAAIMQSSKNAVLH------AVGAAQMAAASSEKAAKQTEERGSTS 608
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*
gi 116008016 1155 S-IRRSFTTAGVKRN---SIMLQVKFTVDGIIDTLRRTGTHFVHC 1195
Cdd:cd14893   609 SkFRKSASSARESKNitdSAATDVYNQADALLHALNHTGKNFLVC 653
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
576-829 3.24e-24

class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276898 [Multi-domain]  Cd Length: 713  Bit Score: 110.70  E-value: 3.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKT-EDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14938     2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCiEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAA----GAYNNFINAEKVNALC------------------TILEAFGNTKTCLNSNATRMT 712
Cdd:cd14938    82 ESGSGKSEIAKNIINFIAYQVkgsrRLPTNLNDQEEDNIHNeentdyqfnmsemlkhvnVVMEAFGNAKTVKNNNSSRFS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  713 QLLSLDFDQTgQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSedshpfISLSQKLEDRH 792
Cdd:cd14938   162 KFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIEN------YSMLNNEKGFE 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 116008016  793 RAANDFMRTVQAFETLNI---DAKAVRGIWSILAAIYHLG 829
Cdd:cd14938   235 KFSDYSGKILELLKSLNYifdDDKEIDFIFSVLSALLLLG 274
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
575-1269 3.25e-24

class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276842 [Multi-domain]  Cd Length: 664  Bit Score: 110.67  E-value: 3.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYAS-NLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDM-PPHVYSLAQTAYRSL-VETRRDQSLI 651
Cdd:cd14875     1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFNAIfVQGLGNQSVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  652 FMGRSGSGKSTSFKHALNYLA-LAAGAYNNFIN---AEKVNALCT----ILEAFGNTKTCLNSNATRMTQLLSLDFDQTG 723
Cdd:cd14875    81 ISGESGSGKTENAKMLIAYLGqLSYMHSSNTSQrsiADKIDENLKwsnpVMESFGNARTVRNDNSSRFGKYIKLYFDPTS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  724 QIASASLQV-LLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKEL-HLEniTSED------SHPFISL---SQKLEDrh 792
Cdd:cd14875   161 GVMVGGQTVtYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLK--TAQDykclngGNTFVRRgvdGKTLDD-- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  793 raANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLgiaGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAAFG 872
Cdd:cd14875   237 --AHEFQNVRHALSMIGVELETQNSIFRVLASILHL---MEVEFESDQNDKAQIADETPFLTACRLLQLDPAKLRECFLV 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  873 LTQPNApnggLSPSKSPTSDTGHEWAWeClEALVIGLYSEALAAVVALINRQI-CTSSHTIAsimLIDTPGFQNPASCGq 951
Cdd:cd14875   312 KSKTSL----VTILANKTEAEGFRNAF-C-KAIYVGLFDRLVEFVNASITPQGdCSGCKYIG---LLDIFGFENFTRNS- 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  952 qvgatLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVE---IEMDLASEChpgplISLIDKApqnhvvrssqrdlreh 1028
Cdd:cd14875   382 -----FEQLCINYANESLQNHYNKYTFINDEEECRREGIQipkIEFPDNSEC-----VNMFDQK---------------- 435
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1029 dRRGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTnpVLYAVDGWVRHSREhpGIRNA 1108
Cdd:cd14875   436 -RTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPKSTIPNQFGVNHYAAF--VNYNTDEWLEKNTD--ALKED 510
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1109 VSLLQDSSREEinrlYIGSLTrgsgamvfcgsfaglegtqSLRRVSSiRRSFTTAgvkrnsIMLQVKFTvdGIIDTLRRT 1188
Cdd:cd14875   511 MYECVSNSTDE----FIRTLL-------------------STEKGLA-RRKQTVA------IRFQRQLT--DLRTELEST 558
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1189 GTHFVHCyllqhnagkhTKYTANGSPSsaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGL 1268
Cdd:cd14875   559 ETQFIRC----------IKPNMEASPS-----------FLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYL 617

                  .
gi 116008016 1269 L 1269
Cdd:cd14875   618 I 618
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1387-2073 1.11e-23

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: 109.76  E-value: 1.11e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1387 QLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVK 1466
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1467 NLQETTEKLEMELICAKSDLNgISEDEDAENEDgvgggvyklKYERVARELEftkrrlhtQHEHDLEQLVALKKHLEMKL 1546
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLD-ELAEELAELEE---------KLEELKEELE--------SLEAELEELEAELEELESRL 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1547 SDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKdvL 1626
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE--L 452
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1627 QAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAK 1706
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD 532
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1707 LRLEMTLETM-----------RKEARRESQQRDEELE-------EVRGNGYKKIKALECQLETEHEERTLLLRE----KH 1764
Cdd:TIGR02168  533 EGYEAAIEAAlggrlqavvveNLNAAKKAIAFLKQNElgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvkfDP 612
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1765 ELERRLSSMEDRDRVDRDAEEALNQ--KLRRDLR---------------------------KYKALLKDAQTQLERLKAD 1815
Cdd:TIGR02168  613 KLRKALSYLLGGVLVVDDLDNALELakKLRPGYRivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEK 692
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1816 -TPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGE 1894
Cdd:TIGR02168  693 iAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1895 LMKKYSATVKQLNT--EQINVSEAEFK-----LNEMEAERNNLKEQVAELQHRLDNVENlgdpSMAMMSKRLElrtkELE 1967
Cdd:TIGR02168  773 AEEELAEAEAEIEEleAQIEQLKEELKalreaLDELRAELTLLNEEAANLRERLESLER----RIAATERRLE----DLE 844
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1968 SRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKV 2047
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
                          730       740
                   ....*....|....*....|....*.
gi 116008016  2048 EQMESEGAALKNDLRLALQRIADLQQ 2073
Cdd:TIGR02168  925 AQLELRLEGLEVRIDNLQERLSEEYS 950
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
576-1281 2.03e-23

class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276863  Cd Length: 578  Bit Score: 107.29  E-value: 2.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEdmpPHVYSLAQTAYRSLVeTRRDQSLIFMGR 655
Cdd:cd14898     2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKNYSHVE---PHVYDVAEASVQDLL-VHGNQTIVISGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  656 SGSGKSTSFKHALNYLaLAAGAYNNFINaEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDqtGQIASASLQVLLP 735
Cdd:cd14898    78 SGSGKTENAKLVIKYL-VERTASTTSIE-KLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  736 ERQRAGRRLGHEHSFHIMTRLLAgaagllQKELHLENitseDSHPFISLSQKLEDRHRAANDFMRTVQAFETLNIdaKAV 815
Cdd:cd14898   154 EKSRVTHHEKGERNFHIFYQFCA------SKRLNIKN----DFIDTSSTAGNKESIVQLSEKYKMTCSAMKSLGI--ANF 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  816 RGIWSILAAIYHLGI-----AGVTKLgTGSTARTQFANptaarkasgLLGVNLEDLSSAAFgltqpnapnGGLSPSKSPT 890
Cdd:cd14898   222 KSIEDCLLGILYLGSiqfvnDGILKL-QRNESFTEFCK---------LHNIQEEDFEESLV---------KFSIQVKGET 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  891 SDTGH--EWAWECLEALVIGLYSEALAAVVALINRqiCTSSHTIASIMLIDTPGFQNPASCGqqvgatLADLRHNYLQER 968
Cdd:cd14898   283 IEVFNtlKQARTIRNSMARLLYSNVFNYITASINN--CLEGSGERSISVLDIFGFEIFESNG------LDQLCINWTNEK 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  969 LQMLFHHTTLVAPRDRYAQELVEiemdlasechpgplISLIDKAPQNHVVRSSQRDLrehdrrGMLWLLDEEAIYPNSND 1048
Cdd:cd14898   355 IQNDFIKKMFRAKQGMYKEEGIE--------------WPDVEFFDNNQCIRDFEKPC------GLMDLISEESFNAWGNV 414
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1049 DTFLERLFSHYGDRehhslLRKCAGPRQFVLHHlqgTNPVLYAVDGWVrhsrehpgirnavsllqDSSREEINRLYIGSL 1128
Cdd:cd14898   415 KNLLVKIKKYLNGF-----INTKARDKIKVSHY---AGDVEYDLRDFL-----------------DKNREKGQLLIFKNL 469
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1129 trgsgamvfcgsfaGLEGTQSlrrvssirrsfttagvkRNSIMLQVKFTVDGIIDTLRRTGTHFVHCylLQHNAGKHTKy 1208
Cdd:cd14898   470 --------------LINDEGS-----------------KEDLVKYFKDSMNKLLNSINETQAKYIKC--IRPNEECRPW- 515
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116008016 1209 tangspssaagqvsseeeMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLASNKDVSV 1281
Cdd:cd14898   516 ------------------CFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLFEVVDYRK 570
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
575-1274 5.66e-23

class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276841 [Multi-domain]  Cd Length: 628  Bit Score: 106.49  E-value: 5.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFrgcktedmppHVYSLAQTAYRSLVE-TRRDQSLIFM 653
Cdd:cd14874     1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSmSSNAESIVFG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  654 GRSGSGKSTSFKHALNYLALAAgayNNFINAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFdQTGQIASASLQVL 733
Cdd:cd14874    71 GESGSGKSYNAFQVFKYLTSQP---KSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKYT 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  734 LP-ERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLenitsEDSHPFISLSQ--KLEDRHRAANDFMRTVQAFETLNI 810
Cdd:cd14874   147 VPlEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGI-----KGLQKFFYINQgnSTENIQSDVNHFKHLEDALHVLGF 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  811 DAKAVRGIWSILAAIYHLG-IAGVTKLGTGSTART-QFANPTAARKASGLLGVNLEDLSSAafgltqpnapnggLSPSKS 888
Cdd:cd14874   222 SDDHCISIYKIISTILHIGnIYFRTKRNPNVEQDVvEIGNMSEVKWVAFLLEVDFDQLVNF-------------LLPKSE 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  889 PTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTiASIMLIDTPGFQNPASCGqqvgatLADLRHNYLQER 968
Cdd:cd14874   289 DGTTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHT-GVISILDHYGFEKYNNNG------VEEFLINSVNER 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  969 LQMLFHHTTLVAPRDRYAQELVEIEMDLASECHPGPLISLIDKAPQnhvvrssqrdlrehdrrGMLWLLDEEAIYPNSND 1048
Cdd:cd14874   362 IENLFVKHSFHDQLVDYAKDGISVDYKVPNSIENGKTVELLFKKPY-----------------GLLPLLTDECKFPKGSH 424
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1049 DTFLERLFSHYGDREHHSLLRkcAGPR-QFVLHHLQGTnpVLYAVDGWVRHSREHPGIrNAVSLLQDSSREEINRLYigs 1127
Cdd:cd14874   425 ESYLEHCNLNHTDRSSYGKAR--NKERlEFGVRHCIGT--TWYNVTDFFSRNKRIISL-SAVQLLRSSKNPIIGLLF--- 496
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1128 ltrgsgamvfcgsfaglegtqslrrvssirRSFTtaGVKRNSIMLQVKFTVDG---IIDTLRRTGTHFVHCyLLQHNAGK 1204
Cdd:cd14874   497 ------------------------------ESYS--SNTSDMIVSQAQFILRGaqeIADKINGSHAHFVRC-IKSNNERQ 543
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116008016 1205 HTKYtangspssaagqvsseeemvNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFG-LLAGDLA 1274
Cdd:cd14874   544 PKKF--------------------DIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRcLLPGDIA 594
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
575-1096 1.47e-22

class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276850 [Multi-domain]  Cd Length: 685  Bit Score: 105.37  E-value: 1.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  575 ASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPL-SLYSEKVVSMFRGCKT-------EDMPPHVYSLAQTAYRSLVETRR 646
Cdd:cd14884     1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLkELYDQDVMNVYLHKKSnsaasaaPFPKAHIYDIANMAYKNMRGKLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  647 DQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQ----- 721
Cdd:cd14884    81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventq 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  722 ----TGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAA----------------GLLQ--KELHLENITSEDSH 779
Cdd:cd14884   161 knmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSdedlarrnlvrncgvyGLLNpdESHQKRSVKGTLRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  780 PFISLSQKLEDRHRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGiagvtklgtgstartqfanPTAARKASGLL 859
Cdd:cd14884   241 GSDSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLG-------------------NRAYKAAAECL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  860 GVNLEDLSSaafgLTQPNAPNGGLSPSKSPTSDtghEWAWECLEALVIGLYSEALAAVVALINR--------------QI 925
Cdd:cd14884   302 QIEEEDLEN----VIKYKNIRVSHEVIRTERRK---ENATSTRDTLIKFIYKKLFNKIIEDINRnvlkckekdesdneDI 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  926 CTSSHTIASIMliDTPGFQNPAscgqqvGATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEMDLASECHpgPL 1005
Cdd:cd14884   375 YSINEAIISIL--DIYGFEELS------GNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYS--DT 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1006 ISLIDKAPQN--HVVRSSQRDLREHDRRGMLWLLDEEAIYpnsnddtFLERLFShYG-----DREHHSLLRKCAgPRQFV 1078
Cdd:cd14884   445 LIFIAKIFRRldDITKLKNQGQKKTDDHFFRYLLNNERQQ-------QLEGKVS-YGfvlnhDADGTAKKQNIK-KNIFF 515
                         570
                  ....*....|....*...
gi 116008016 1079 LHHLQGtnPVLYAVDGWV 1096
Cdd:cd14884   516 IRHYAG--LVTYRINNWI 531
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
1385-2053 2.24e-22

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: 105.64  E-value: 2.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1385 EEQLKTANEellmLRAKLEKIecdRSEVKAENQKLEAKLSELT--VDLAEERSTA----------HIA--TERLEAETAE 1450
Cdd:pfam01576   46 QEQLQAETE----LCAEAEEM---RARLAARKQELEEILHELEsrLEEEEERSQQlqnekkkmqqHIQdlEEQLDEEEAA 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1451 RLKLEKELGDQTNKVKNLQETT-------EKLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLKYERVARELEFTKRR 1523
Cdd:pfam01576  119 RQKLQLEKVTTEAKIKKLEEDIllledqnSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1524 lhtqHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQ 1603
Cdd:pfam01576  199 ----EEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQIS 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1604 SLQDAVRQERQAKERYGREK----DVLQAEKFTLEQTLADTRLDLEFK---EEKLASLQRELEEMTfgGGTEEEFAQLRR 1676
Cdd:pfam01576  275 ELQEDLESERAARNKAEKQRrdlgEELEALKTELEDTLDTTAAQQELRskrEQEVTELKKALEEET--RSHEAQLQEMRQ 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1677 SKNETerrakeqeeeLDEMAGQIQLLEQAKLRLEMTLETMRKEaRRESQQRDEELEEVRGNGYKKIKALECQLETEHEER 1756
Cdd:pfam01576  353 KHTQA----------LEELTEQLEQAKRNKANLEKAKQALESE-NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARL 421
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1757 TLLLREKHELERRLSSMEDR-DRVDRDAEEALNQ--KLRRDLRKYKALLKDAQTQL-ERLKADTPGKTLIRQ-------L 1825
Cdd:pfam01576  422 SESERQRAELAEKLSKLQSElESVSSLLNEAEGKniKLSKDVSSLESQLQDTQELLqEETRQKLNLSTRLRQledernsL 501
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1826 RNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYS----- 1900
Cdd:pfam01576  502 QEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNrlqqe 581
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1901 ---ATVKQLNTEQI--NVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRT---KELE----- 1967
Cdd:pfam01576  582 lddLLVDLDHQRQLvsNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALeakEELErtnkq 661
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1968 -----------------SRLELEQATRArLEVQVNRHKEALEKLQNEVTqskmremQAQDVIKKSQKSLRDMREEF-HAV 2029
Cdd:pfam01576  662 lraemedlvsskddvgkNVHELERSKRA-LEQQVEEMKTQLEELEDELQ-------ATEDAKLRLEVNMQALKAQFeRDL 733
                          730       740
                   ....*....|....*....|....
gi 116008016  2030 SSREQESLTRRKDLEKKVEQMESE 2053
Cdd:pfam01576  734 QARDEQGEEKRRQLVKQVRELEAE 757
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
576-1101 3.01e-22

class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276870  Cd Length: 673  Bit Score: 104.40  E-value: 3.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLS-LYSEKVVSMFRgcKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14905     2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNFINaEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLL 734
Cdd:cd14905    80 ESGSGKSENTKIIIQYLLTTDLSRSKYLR-DYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  735 PERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENItseDSHPFI----SLSQKLEDRHRAandFMRTVQAFETLNI 810
Cdd:cd14905   159 LDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDI---NSYHYLnqggSISVESIDDNRV---FDRLKMSFVFFDF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  811 DAKAVRGIWSILAAIYHLGIAGVTKlgtgSTARTQFANPTAarkasgllgvnLEDLS-SAAFGLTQpnAPNGGLSPSKSP 889
Cdd:cd14905   233 PSEKIDLIFKTLSFIIILGNVTFFQ----KNGKTEVKDRTL-----------IESLShNITFDSTK--LENILISDRSMP 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  890 TSDtghewAWECLEALVIGLYSEALAAVVALINRQICTS--SHTIAsimLIDTPGFQNPASCGQQvgatlaDLRHNYLQE 967
Cdd:cd14905   296 VNE-----AVENRDSLARSLYSALFHWIIDFLNSKLKPTqySHTLG---ILDLFGQESSQLNGYE------QFSINFLEE 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  968 RLQMLFHHTTLVAPRDRYAQELVeiemdlasechpgPLISLIDKAPQNHVVRSSQRdlrehdrrgMLWLLDEEAIYPNSN 1047
Cdd:cd14905   362 RLQQIYLQTVLKQEQREYQTERI-------------PWMTPISFKDNEESVEMMEK---------IINLLDQESKNINSS 419
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 116008016 1048 DDTFLERLfSHYGDReHHSLLRKcagPRQFVLHHLQGTnpVLYAVDGWVRHSRE 1101
Cdd:cd14905   420 DQIFLEKL-QNFLSR-HHLFGKK---PNKFGIEHYFGQ--FYYDVRGFIIKNRD 466
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
576-1280 6.62e-22

class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276848  Cd Length: 642  Bit Score: 102.90  E-value: 6.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRgCKTE-DMPPHVYSLAQTAYRSLVETRRDQSLIFMG 654
Cdd:cd14882     2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYR-CKSRsDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  655 RSGSGKSTSFKHALNYLALAAGAYNNfiNAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLL 734
Cdd:cd14882    81 ESYSGKTTNARLLIKHLCYLGDGNRG--ATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  735 PERQRAGRRLGHEHSFHIMTRLLAG--AAGLLqKELHLEN------ITSEDSHPFISLSQKLEDRHRAANDFMRTVQAFE 806
Cdd:cd14882   159 LEKLRVSTTDGNQSNFHIFYYFYDFieAQNRL-KEYNLKAgrnyryLRIPPEVPPSKLKYRRDDPEGNVERYKEFEEILK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  807 TLNIDAKAVRGIWSILAAIYHLGIAGVTKlGTGStarTQFANPTAARKASGLLGVnleDLSSAAFGLTQPNAPNGGLSPS 886
Cdd:cd14882   238 DLDFNEEQLETVRKVLAAILNLGEIRFRQ-NGGY---AELENTEIASRVAELLRL---DEKKFMWALTNYCLIKGGSAER 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  887 KSPTSDTghewAWECLEALVIGLYSEALAAVVALIN------RQICTSSHtiaSIMLIDTPGFQnpasCGQQVGatLADL 960
Cdd:cd14882   311 RKHTTEE----ARDARDVLASTLYSRLVDWIINRINmkmsfpRAVFGDKY---SISIHDMFGFE----CFHRNR--LEQL 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  961 RHNYLQErlQMLFHhttlvaprdrYAQELVEIEMdLASECHPGPLISLidkapqNHVVRSSQRDLREHDRRGMLWLLDeE 1040
Cdd:cd14882   378 MVNTLNE--QMQYH----------YNQRIFISEM-LEMEEEDIPTINL------RFYDNKTAVDQLMTKPDGLFYIID-D 437
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1041 AIYPNSNDDTFLERLfshygdREHHSLLRKCAGPRQFVLHHLQGTnpVLYavdgwvrHSREhpgirnavslLQDSSREEI 1120
Cdd:cd14882   438 ASRSCQDQNYIMDRI------KEKHSQFVKKHSAHEFSVAHYTGR--IIY-------DARE----------FADKNRDFV 492
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1121 NRLYIGSLTRGSGAMVfcgsfaglegtQSLRRVSSIRRSFTTAGVKRNSIMLQVKFTVDGIidtlRRTGTHFVHCYLlqh 1200
Cdd:cd14882   493 PPEMIETMRSSLDESV-----------KLMFTNSQVRNMRTLAATFRATSLELLKMLSIGA----NSGGTHFVRCIR--- 554
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1201 nagKHTKYTANGSPSsaagqvsseeEMVnvpllRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLASNKDVS 1280
Cdd:cd14882   555 ---SDLEYKPRGFHS----------EVV-----RQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDFDETVEMT 616
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1563-2104 7.52e-21

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 100.40  E-value: 7.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1563 WKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRL 1642
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1643 DLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARR 1722
Cdd:COG1196   310 RRRELEERLEELEEELAE------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1723 ESQQRDEELEEVRgNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALL 1802
Cdd:COG1196   384 LAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1803 KDAQTQLERLKAdtpGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRAR----------------ND 1866
Cdd:COG1196   463 ELLAELLEEAAL---LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavligveaayeAA 539
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1867 AEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNT-EQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVE 1945
Cdd:COG1196   540 LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1946 NLgdpsmammSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREE 2025
Cdd:COG1196   620 DT--------LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 2026 FHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAMEEEGEEELSESDESLSSVGSISDLEDRLR 2104
Cdd:COG1196   692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1387-2045 9.87e-21

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 100.01  E-value: 9.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1387 QLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVK 1466
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1467 NLQETTEKLEMELicaksdlngisededaenedgvgggvyklkyervareleftkrrlhTQHEHDLEQLVALKKHLEMKL 1546
Cdd:COG1196   313 ELEERLEELEEEL----------------------------------------------AELEEELEELEEELEELEEEL 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1547 SDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVL 1626
Cdd:COG1196   347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1627 QAEKFTLEQTLADTRLDLEFKEEKLASLQRELEemtfgggteeefaQLRRSKNETERRAKEQEEELDEMAGQIQlleqak 1706
Cdd:COG1196   427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEE-------------ALLELLAELLEEAALLEAALAELLEELA------ 487
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1707 lrlemtletmRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKhelerrlssmedrdRVDRDAEEA 1786
Cdd:COG1196   488 ----------EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA--------------AYEAALEAA 543
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1787 LNQKLRRDLRkykALLKDAQTQLERLKADTPGK----TLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAM---FDE 1859
Cdd:COG1196   544 LAAALQNIVV---EDDEVAAAAIEYLKAAKAGRatflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARyyvLGD 620
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1860 SHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEfklNEMEAERNNLKEQVAELQH 1939
Cdd:COG1196   621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE---AELEELAERLAEEELELEE 697
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1940 RLDNVENLgdpsmAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSL 2019
Cdd:COG1196   698 ALLAEEEE-----ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 116008016 2020 RDMR-----------EEFHAVSSREQESLTRRKDLEK 2045
Cdd:COG1196   773 EREIealgpvnllaiEEYEELEERYDFLSEQREDLEE 809
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1507-2057 1.02e-20

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 100.01  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1507 KLKYERVARELEFTKRRLHtQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQvvgqwkrKAQKMTNEMNDLRMLLEEQNA 1586
Cdd:COG1196   217 ELKEELKELEAELLLLKLR-ELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELELEEAQA 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1587 RNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfggg 1666
Cdd:COG1196   289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE------ 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1667 TEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRgngyKKIKALE 1746
Cdd:COG1196   363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA----ELEEEEE 438
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1747 CQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKykALLKDAQTQLERLKADTPGKTLIRQLR 1826
Cdd:COG1196   439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLL 516
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1827 NQL------------------EDAESARSLAMKARQTAEAELTEVQAMFDESHRA--------RNDAEERANAAHRDRAE 1880
Cdd:COG1196   517 AGLrglagavavligveaayeAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflplDKIRARAALAAALARGA 596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1881 LQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMS---- 1956
Cdd:COG1196   597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAalle 676
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1957 --KRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQ 2034
Cdd:COG1196   677 aeAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756
                         570       580
                  ....*....|....*....|...
gi 116008016 2035 ESLTRRKDLEKKVEQMESEGAAL 2057
Cdd:COG1196   757 PEPPDLEELERELERLEREIEAL 779
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1400-2062 2.37e-20

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: 98.99  E-value: 2.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1400 AKLEKIECDRSEVKAENQKLEAKLSELTVDLaeERstahIATERLEAETAERLKLEKELGDQTNKVKNLQETTEKLEmel 1479
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLDLIIDEKRQQL--ER----LRREREKAERYQALLKEKREYEGYELLKEKEALERQKE--- 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1480 icaksdlNGISEDEDAENEdgvgggVYKLKYERVARELEftkrrlhtqhehdLEQLVALKKHLEMKLSDAYEEvvEQRQV 1559
Cdd:TIGR02169  241 -------AIERQLASLEEE------LEKLTEEISELEKR-------------LEEIEQLLEELNKKIKDLGEE--EQLRV 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1560 vgqwKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLAD 1639
Cdd:TIGR02169  293 ----KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1640 TRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETER-------RAKEQEEELDEMAGQIQLLEQAKLRLEMT 1712
Cdd:TIGR02169  369 LRAELEEVDKEFAETRDELKDY------REKLEKLKREINELKReldrlqeELQRLSEELADLNAAIAGIEAKINELEEE 442
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1713 LETMRKEARrESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLR 1792
Cdd:TIGR02169  443 KEDKALEIK-KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1793 ------RDLRKYK------------ALLK--------DAQTQLERLKADTPGK------TLIRQLRNQL----------- 1829
Cdd:TIGR02169  522 gvhgtvAQLGSVGeryataievaagNRLNnvvveddaVAKEAIELLKRRKAGRatflplNKMRDERRDLsilsedgvigf 601
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1830 -------------------------EDAESARSLAMKAR----------------------------------------- 1843
Cdd:TIGR02169  602 avdlvefdpkyepafkyvfgdtlvvEDIEAARRLMGKYRmvtlegelfeksgamtggsraprggilfsrsepaelqrlre 681
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1844 ---------QTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVS 1914
Cdd:TIGR02169  682 rleglkrelSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1915 EAEFKLNEMEAERNNLKEQVAEL-----QHRLDNVENLGDpSMAMMSKRLELRTKELESRLELEQATRARLEvqvnrhkE 1989
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELS-KLEEEVSRIEARLREIEQKLNRLTLEKEYLE-------K 833
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116008016  1990 ALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLR 2062
Cdd:TIGR02169  834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
576-1271 1.18e-19

class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276847 [Multi-domain]  Cd Length: 633  Bit Score: 95.95  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  576 SVLHCLRQRYASNLIHTKAGPTLLVVNPM----APLSLYSEKVVSMFrgcktedmpPHVYSLAQTAYRSLVETRRDQSLI 651
Cdd:cd14881     2 AVMKCLQARFYAKEFFTNVGPILLSVNPYrdvgNPLTLTSTRSSPLA---------PQLLKVVQEAVRQQSETGYPQAII 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  652 FMGRSGSGKSTSFKHALNYL-ALAAG-----AYNNfinaekVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQtGQI 725
Cdd:cd14881    73 LSGTSGSGKTYASMLLLRQLfDVAGGgpetdAFKH------LAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GAL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  726 ASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDSHpFISLSQKLEDRHRAANDFmrtvQAF 805
Cdd:cd14881   146 YRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPANLR-YLSHGDTRQNEAEDAARF----QAW 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  806 ETlnidAKAVRGI-----WSILAAIYHLGiagvtklgtgstaRTQFANP----------TAARKASGLLGVnledlSSAA 870
Cdd:cd14881   221 KA----CLGILGIpfldvVRVLAAVLLLG-------------NVQFIDGgglevdvkgeTELKSVAALLGV-----SGAA 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  871 F--GLTQPNAPNGGlSPSKSPTSDtghEWAWECLEALVIGLYSEALAAVVALIN--RQICTSSHTIA---SIMLIDTPGF 943
Cdd:cd14881   279 LfrGLTTRTHNARG-QLVKSVCDA---NMSNMTRDALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGF 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  944 QNPAScgqqvgATLADLRHNYLQERLQMlFHHT-----TLVAPRDRYAQelVEIEMDLASEChpgPLISLIdkapqnhvv 1018
Cdd:cd14881   355 EDPKP------SQLEHLCINLCAETMQH-FYNThifksSIESCRDEGIQ--CEVEVDYVDNV---PCIDLI--------- 413
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1019 rSSQRDlrehdrrGMLWLLDEEAiYPNSNDDTFLERLFSHYgdREHHSLLR-KCAGPRQFVLHHLQGTnpVLYavdgwvr 1097
Cdd:cd14881   414 -SSLRT-------GLLSMLDVEC-SPRGTAESYVAKIKVQH--RQNPRLFEaKPQDDRMFGIRHFAGR--VVY------- 473
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1098 hsrehpgirNAVSLLqDSSREEINRLYIGSLTRGSgamvfCgSFAGLEGTQslrrvssirrSFTTagvkrnsimlqvkfT 1177
Cdd:cd14881   474 ---------DASDFL-DTNRDVVPDDLVAVFYKQN-----C-NFGFATHTQ----------DFHT--------------R 513
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1178 VDGIIDTLRRTGTHFVHCyllqhnagkhTKYTANGSPSSAAGQVSSEeemvnvpllrsQLRGSQVLEAARLHRLGFPESV 1257
Cdd:cd14881   514 LDNLLRTLVHARPHFVRC----------IRSNTTETPNHFDRGTVVR-----------QIRSLQVLETVNLMAGGYPHRM 572
                         730
                  ....*....|....
gi 116008016 1258 PLLEFVRRFGLLAG 1271
Cdd:cd14881   573 RFKAFNARYRLLAP 586
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1385-2103 3.10e-19

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: 95.52  E-value: 3.10e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1385 EEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEA------KLSELTVDLAEERSTAHIAteRLEAETAERLKLEKEL 1458
Cdd:TIGR02169  169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRerekaeRYQALLKEKREYEGYELLK--EKEALERQKEAIERQL 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1459 GDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGG-----GVYKLKYERVARELEFTKRRLHtQHEHDLE 1533
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekiGELEAEIASLERSIAEKERELE-DAEERLA 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1534 QLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQnarnnllekkqrkfDAECQSLQDAVRQER 1613
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV--------------DKEFAETRDELKDYR 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1614 QAKERYGREK-------DVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggTEEEFAQLRRSKNETERRAK 1686
Cdd:TIGR02169  392 EKLEKLKREInelkrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-----ALEIKKQEWKLEQLAADLSK 466
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1687 EQEEELDEMAGQIQL-LEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLeTEHEERTLLLREKhE 1765
Cdd:TIGR02169  467 YEQELYDLKEEYDRVeKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL-GSVGERYATAIEV-A 544
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1766 LERRLSSMEDRDrvDRDAEEALNQKLRRDLRKYKAL----LKDAQTQLERLKADTPGKTLI------RQLRNQ------- 1828
Cdd:TIGR02169  545 AGNRLNNVVVED--DAVAKEAIELLKRRKAGRATFLplnkMRDERRDLSILSEDGVIGFAVdlvefdPKYEPAfkyvfgd 622
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1829 ---LEDAESARSLAMKARQ-TAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVK 1904
Cdd:TIGR02169  623 tlvVEDIEAARRLMGKYRMvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEN 702
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1905 QLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVE-NLGDPSMAMMSKRLELrtKELESRLEleqatraRLEVQ 1983
Cdd:TIGR02169  703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEeDLSSLEQEIENVKSEL--KELEARIE-------ELEED 773
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1984 VNRHKEALEKLQNEVTQSKmremqaqdvIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRL 2063
Cdd:TIGR02169  774 LHKLEEALNDLEARLSHSR---------IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|
gi 116008016  2064 ALQRIADLQQAMEEEGEEELSESDESLSSVGSISDLEDRL 2103
Cdd:TIGR02169  845 LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1511-2075 1.47e-17

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: 89.73  E-value: 1.47e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1511 ERVARELEFTKRRLHTQHE-----HDL-EQLVALKKHLE-MKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEE 1583
Cdd:TIGR02168  192 EDILNELERQLKSLERQAEkaeryKELkAELRELELALLvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1584 QNARNNLLEKKQRKFDAECQSLQ----DAVRQERQAKER---YGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQR 1656
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALAneisRLEQQKQILRERlanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1657 ELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRG 1736
Cdd:TIGR02168  352 ELESL------EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1737 NGYK----KIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVdrdAEEALnQKLRRDLRKYKALLKDAQTQLERL 1812
Cdd:TIGR02168  426 LLKKleeaELKELQAELEELEEELEELQEELERLEEALEELREELEE---AEQAL-DAAERELAQLQARLDSLERLQENL 501
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1813 KADTPGKTLIRQLRNQL--------------EDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERA------- 1871
Cdd:TIGR02168  502 EGFSEGVKALLKNQSGLsgilgvlselisvdEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTflpldsi 581
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1872 -----NAAHRDRAELQAQIEENEEELGELMKKYSATV--------------------KQLNTEQINVS------------ 1914
Cdd:TIGR02168  582 kgteiQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvddldnalelaKKLRPGYRIVTldgdlvrpggvi 661
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1915 -------------------EAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGD-------------PSMAMMSKRLELR 1962
Cdd:TIGR02168  662 tggsaktnssilerrreieELEEKIEELEEKIAELEKALAELRKELEELEEELEqlrkeleelsrqiSALRKDLARLEAE 741
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1963 TKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKD 2042
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
                          650       660       670
                   ....*....|....*....|....*....|...
gi 116008016  2043 LEKKVEQMESEGAALKNDLRLALQRIADLQQAM 2075
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDI 854
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1612-2069 1.87e-17

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 89.23  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1612 ERQAK--ERYgrekDVLQAEKFTLEQTLAdtRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAKEQE 1689
Cdd:COG1196   206 ERQAEkaERY----RELKEELKELEAELL--LLKLRELEAELEELEAELEE------LEAELEELEAELAELEAELEELR 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1690 EELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQR---DEELEEVRgngyKKIKALECQLETEHEERTLLLREKHEL 1766
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRrelEERLEELE----EELAELEEELEELEEELEELEEELEEA 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1767 ERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADtpgKTLIRQLRNQLEDAESARSLAMKARQTA 1846
Cdd:COG1196   350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL---AAQLEELEEAEEALLERLERLEEELEEL 426
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1847 EAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEeneeelgelmkkysATVKQLNTEQINVSEAEFKLNEMEAE 1926
Cdd:COG1196   427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA--------------ELLEEAALLEAALAELLEELAEAAAR 492
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1927 RNNLKEQVAELQHRLDNV-ENLGDPSMAMMSKRL-ELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMR 2004
Cdd:COG1196   493 LLLLLEAEADYEGFLEGVkAALLLAGLRGLAGAVaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 2005 EMQAQ--DVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIA 2069
Cdd:COG1196   573 RATFLplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1576-1949 5.23e-17

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: 88.19  E-value: 5.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1576 DLRMLLEEQ------NARNNLLEKKQRKFDAECQSLQDAVRQ--------ERQAK--ERYgREkdvLQAEKFTLEQTLAD 1639
Cdd:TIGR02168  156 ERRAIFEEAagiskyKERRKETERKLERTRENLDRLEDILNElerqlkslERQAEkaERY-KE---LKAELRELELALLV 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1640 TRLD-----LEFKEEKLASLQRELEEMTFG-GGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLemtl 1713
Cdd:TIGR02168  232 LRLEelreeLEELQEELKEAEEELEELTAElQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL---- 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1714 etmrkearresQQRDEELEevrgngyKKIKALECQLETEHEERTLLLREKHELERRLSSMEdrdrVDRDAEEALNQKLRR 1793
Cdd:TIGR02168  308 -----------RERLANLE-------RQLEELEAQLEELESKLDELAEELAELEEKLEELK----EELESLEAELEELEA 365
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1794 DLRKYKALLKDAQTQLERLKADtpgktlIRQLRNQLEdaesarsLAMKARQTAEAELTEVQAMFDESHRARNDAEERANA 1873
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSK------VAQLELQIA-------SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016  1874 AhrDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGD 1949
Cdd:TIGR02168  433 A--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1533-2075 6.27e-17

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 87.43  E-value: 6.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1533 EQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMT---NEMNDLRMLLEEqnarnnlLEKKQRKFDAECQSLqDAV 1609
Cdd:PRK03918  165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEevlREINEISSELPE-------LREELEKLEKEVKEL-EEL 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1610 RQERQAKERygrEKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNET-------E 1682
Cdd:PRK03918  237 KEEIEELEK---ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYldelreiE 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1683 RRAKEQEEELDEMAGQIQLLEQAKLRLEMTletmrKEARRESQQRDEELEEvRGNGYKKIKALECQLETEHEERTLLlrE 1762
Cdd:PRK03918  314 KRLSRLEEEINGIEERIKELEEKEERLEEL-----KKKLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTGL--T 385
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1763 KHELERRLSSMEDRDRVDRDAEEALNQKLRRdLRKYKALLKDAQTQLERLKADTP----------GKTLIRQLRNQLEDA 1832
Cdd:PRK03918  386 PEKLEKELEELEKAKEEIEEEISKITARIGE-LKKEIKELKKAIEELKKAKGKCPvcgrelteehRKELLEEYTAELKRI 464
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1833 ESARSLAMKARQTAEAELTEVQAMFDESHRAR---------NDAEERANAAHRDRAELQAQIEENEEELGELMKKysaTV 1903
Cdd:PRK03918  465 EKELKEIEEKERKLRKELRELEKVLKKESELIklkelaeqlKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKG---EI 541
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1904 KQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLdnvENLGDPSMAMMSKRLE---------LRTKELESRLELEQ 1974
Cdd:PRK03918  542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL---EELGFESVEELEERLKelepfyneyLELKDAEKELEREE 618
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1975 ATRARLEVQVnrhKEALEKLQNEVTQSKMREMQAQDVIKK-SQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESE 2053
Cdd:PRK03918  619 KELKKLEEEL---DKAFEELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
                         570       580
                  ....*....|....*....|....*
gi 116008016 2054 GAALKNDL---RLALQRIADLQQAM 2075
Cdd:PRK03918  696 LEKLKEELeerEKAKKELEKLEKAL 720
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1385-2053 1.44e-16

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 86.27  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1385 EEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELtvdlaEERStahiatERLEAETAERLKLEKELGDQTNK 1464
Cdd:PRK03918  192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-----EELK------EEIEELEKELESLEGSKRKLEEK 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1465 VKNLQETTEKLEMELICAKSDLNGISEDEDaenedgvgggvYKLKYERVARELEFTKRRLHtQHEHDLEQLVALKKHLEM 1544
Cdd:PRK03918  261 IRELEERIEELKKEIEELEEKVKELKELKE-----------KAEEYIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEE 328
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1545 KLSDAyeevveqrqvvgqwkrkaQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDaecQSLQDAVRQERQAKERYGREKD 1624
Cdd:PRK03918  329 RIKEL------------------EEKEERLEELKKKLKELEKRLEELEERHELYE---EAKAKKEELERLKKRLTGLTPE 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1625 VLqaekftleqtladtrldlefkEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAG------- 1697
Cdd:PRK03918  388 KL---------------------EKELEELEKAKEEI------EEEISKITARIGELKKEIKELKKAIEELKKakgkcpv 440
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1698 -QIQLLEQAKLRL--EMTLETmrKEARRESQQRDEELEEVRgngyKKIKALECQLETEHEERTL--LLREKHELERRLSS 1772
Cdd:PRK03918  441 cGRELTEEHRKELleEYTAEL--KRIEKELKEIEEKERKLR----KELRELEKVLKKESELIKLkeLAEQLKELEEKLKK 514
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1773 MeDRDRVDRDAEEAlnQKLRRDLRKYKALLKDAQTQLERLKadtPGKTLIRQLRNQLEDAESARS-LAMKARQTAEAELT 1851
Cdd:PRK03918  515 Y-NLEELEKKAEEY--EKLKEKLIKLKGEIKSLKKELEKLE---ELKKKLAELEKKLDELEEELAeLLKELEELGFESVE 588
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1852 EVQAMFDESHRARNDAEERANAAHRDRAELqaqieeneeelgelmkkysatvKQLNTEQINVSEAEFKLNEMEAERNNLK 1931
Cdd:PRK03918  589 ELEERLKELEPFYNEYLELKDAEKELEREE----------------------KELKKLEEELDKAFEELAETEKRLEELR 646
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1932 EQVAELQHRLDNVENlgdpsmammsKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDv 2011
Cdd:PRK03918  647 KELEELEKKYSEEEY----------EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK- 715
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|..
gi 116008016 2012 IKKSQKSLRDMREEFhavssREQESLTRRKDLeKKVEQMESE 2053
Cdd:PRK03918  716 LEKALERVEELREKV-----KKYKALLKERAL-SKVGEIASE 751
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1451-1811 2.45e-16

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: 85.88  E-value: 2.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1451 RLKLEKELGDQTNKVKNLQETTEKLEMELICAKSDLngisedEDAENEdgvgggvyklkyERVARELEFTKRRLHTQHEH 1530
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKEL------EELEEE------------LEQLRKELEELSRQISALRK 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1531 DL-------EQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQ 1603
Cdd:TIGR02168  734 DLarleaevEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1604 SLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETER 1683
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL------ESELEALLNERASLEE 887
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1684 RAKEQEEELDEMAGQIQlleqaklrlemTLETMRKEARRESQQRDEELEEVRgNGYKKIKALECQLE---TEHEERTLLL 1760
Cdd:TIGR02168  888 ALALLRSELEELSEELR-----------ELESKRSELRRELEELREKLAQLE-LRLEGLEVRIDNLQerlSEEYSLTLEE 955
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016  1761 REKHELERRLSSMEDRDRVDR-------------DAEEAL-NQKLRRD-LRKYKALLKDAQTQLER 1811
Cdd:TIGR02168  956 AEALENKIEDDEEEARRRLKRlenkikelgpvnlAAIEEYeELKERYDfLTAQKEDLTEAKETLEE 1021
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1761-2073 8.46e-16

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: 83.96  E-value: 8.46e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1761 REKHELERRLSSMEDRDRVDRDAEEALNQkLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAE-SARSLA 1839
Cdd:TIGR02169  153 VERRKIIDEIAGVAEFDRKKEKALEELEE-VEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEgYELLKE 231
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1840 MKA----RQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKK--YSATVKQLNTEQI-- 1911
Cdd:TIGR02169  232 KEAlerqKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkiGELEAEIASLERSia 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1912 ----NVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRtKELESRLELEQATRARLEVQVNRH 1987
Cdd:TIGR02169  312 ekerELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL-EDLRAELEEVDKEFAETRDELKDY 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1988 KEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQR 2067
Cdd:TIGR02169  391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470

                   ....*.
gi 116008016  2068 IADLQQ 2073
Cdd:TIGR02169  471 LYDLKE 476
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1432-2062 1.84e-15

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 82.78  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1432 EERSTAHIATERLEAETAERL-KLEKELGDQtnKVKNLQETTEKLEMELicakSDLngiseDEDAENedgvgggvYKLKY 1510
Cdd:PRK02224  169 ERASDARLGVERVLSDQRGSLdQLKAQIEEK--EEKDLHERLNGLESEL----AEL-----DEEIER--------YEEQR 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1511 ERVARELEFTKRRLhTQHEHDLEQLVALK---KHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNAR 1587
Cdd:PRK02224  230 EQARETRDEADEVL-EEHEERREELETLEaeiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1588 NNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVL--------------QAEKFTLEQTLADTRLDLEFKEEKLAS 1653
Cdd:PRK02224  309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLredaddleeraeelREEAAELESELEEAREAVEDRREEIEE 388
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1654 LQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQlleqaklRLEMTLETMRKearresqqRDEELEE 1733
Cdd:PRK02224  389 LEEEIEEL------RERFGDAPVDLGNAEDFLEELREERDELREREA-------ELEATLRTARE--------RVEEAEA 447
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1734 VRGNGykkiKALECQLETEHEERTLLLREKHE----LERRLSSMEDRdrvdrdaEEALNQKLRRdlrkyKALLKDAQTQL 1809
Cdd:PRK02224  448 LLEAG----KCPECGQPVEGSPHVETIEEDRErveeLEAELEDLEEE-------VEEVEERLER-----AEDLVEAEDRI 511
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1810 ERL--KADTPGKtLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIee 1887
Cdd:PRK02224  512 ERLeeRREDLEE-LIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI-- 588
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1888 neeelgelmkkysatvkqlntEQINvseaefKLNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLElRTKELE 1967
Cdd:PRK02224  589 ---------------------ESLE------RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRE-RKRELE 640
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1968 SRLELEQATRARLEVQvnRHKEALEKLQNEVTQSKMREMQAQDVI---KKSQKSLRDMREEFHAVSSREQesltRRKDLE 2044
Cdd:PRK02224  641 AEFDEARIEEAREDKE--RAEEYLEQVEEKLDELREERDDLQAEIgavENELEELEELRERREALENRVE----ALEALY 714
                         650
                  ....*....|....*...
gi 116008016 2045 KKVEQMESEGAALKNDLR 2062
Cdd:PRK02224  715 DEAEELESMYGDLRAELR 732
PTZ00121 PTZ00121
MAEBL; Provisional
1336-2057 1.91e-15

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 83.27  E-value: 1.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1336 ARKKMSQRRVQEL----AVRCIQ-----RNVKAFLAVRDWPWWRLLVRVTPLLNVHRTEEQLKTANEEllMLRAKLEKIE 1406
Cdd:PTZ00121 1181 ARKAEEVRKAEELrkaeDARKAEaarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEE--RNNEEIRKFE 1258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1407 CDRSEVKAENQ---KLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVKNLQETTEKLEMELIcak 1483
Cdd:PTZ00121 1259 EARMAHFARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK--- 1335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1484 sdlngiSEDEDAENEDGVGggvyKLKYERVARELEFTKRRlhtqhehdlEQLVALKKHLEMKLSDAYEEVVEQRQVVGQW 1563
Cdd:PTZ00121 1336 ------KKAEEAKKAAEAA----KAEAEAAADEAEAAEEK---------AEAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1564 KRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAEcqSLQDAVRQERQAKERYGREKDVLQAEKFtleqtladtrld 1643
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD--EAKKKAEEAKKADEAKKKAEEAKKAEEA------------ 1462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1644 lefkeEKLASLQRELEEMtfgggteEEFAQLRRSKNETERRAKEQEEELDEMAGQiqllEQAKLRLEmtlETMRKEARRE 1723
Cdd:PTZ00121 1463 -----KKKAEEAKKADEA-------KKKAEEAKKADEAKKKAEEAKKKADEAKKA----AEAKKKAD---EAKKAEEAKK 1523
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1724 SQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLK 1803
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1804 DAQTQLERLKADTPGKTLIRQLRNqledAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDraelqa 1883
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKK----AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED------ 1673
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1884 qieeneeelgelmKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDnvenlgdpsmammskrlELRT 1963
Cdd:PTZ00121 1674 -------------KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE-----------------ELKK 1723
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1964 KELESRLELEQATRARLEvqvnrHKEALEKLQNEVTQSKmremQAQDVIKKSQKSLRDMREEFHAVSSRE--QESLTRRK 2041
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEE-----DKKKAEEAKKDEEEKK----KIAHLKKEEEKKAEEIRKEKEAVIEEEldEEDEKRRM 1794
                         730
                  ....*....|....*.
gi 116008016 2042 DLEKKVEQMESEGAAL 2057
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANI 1810
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1678-2026 2.77e-15

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: 82.41  E-value: 2.77e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1678 KNETERRAKEQEEELD-------EMAGQIQLLE-QAKL------------RLEMTLETMR-KEARRESQQRDEELEEVRg 1736
Cdd:TIGR02168  174 RKETERKLERTRENLDrledilnELERQLKSLErQAEKaerykelkaelrELELALLVLRlEELREELEELQEELKEAE- 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1737 ngyKKIKALECQLETEHEERTLLLREKHELERRLssmedrdrvdrdaeealnQKLRRDLRKYKALLKDAQTQLERLKADt 1816
Cdd:TIGR02168  253 ---EELEELTAELQELEEKLEELRLEVSELEEEI------------------EELQKELYALANEISRLEQQKQILRER- 310
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1817 pgktlIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELM 1896
Cdd:TIGR02168  311 -----LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1897 KKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDnvenlgdpsmammskrlELRTKELESRLELEQAT 1976
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE-----------------EAELKELQAELEELEEE 448
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 116008016  1977 RARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQ---KSLRDMREEF 2026
Cdd:TIGR02168  449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarlDSLERLQENL 501
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1584-2073 3.04e-15

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 82.03  E-value: 3.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1584 QNARNNLLEKKqRKFDAECQSLQDAVRQERQAKERYGREKDvlqaEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTf 1663
Cdd:PRK03918  161 ENAYKNLGEVI-KEIKRRIERLEKFIKRTENIEELIKEKEK----ELEEVLREINEISSELPELREELEKLEKEVKELE- 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1664 ggGTEEEFAQLRRSKNETERRAKEQEEELDEmagqiqlleqaklrlemtLETMRKEARRESqqrdEELEEVRGNgYKKIK 1743
Cdd:PRK03918  235 --ELKEEIEELEKELESLEGSKRKLEEKIRE------------------LEERIEELKKEI----EELEEKVKE-LKELK 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1744 ALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRdLRKYKALLKDAQTQLERLKADTPGKTLIR 1823
Cdd:PRK03918  290 EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER-LEELKKKLKELEKRLEELEERHELYEEAK 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1824 QLRNQLEDAESarSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEE---------------N 1888
Cdd:PRK03918  369 AKKEELERLKK--RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelT 446
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1889 EEELGELMKKYSATVKQLNTEQINVSEAEFKLN----EMEAERNN---------LKEQVAELQHRLD--NVENLGDPS-- 1951
Cdd:PRK03918  447 EEHRKELLEEYTAELKRIEKELKEIEEKERKLRkelrELEKVLKKeseliklkeLAEQLKELEEKLKkyNLEELEKKAee 526
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1952 ---MAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHA 2028
Cdd:PRK03918  527 yekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLE 606
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 116008016 2029 VSSREQE---SLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQ 2073
Cdd:PRK03918  607 LKDAEKElerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1379-1937 5.24e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 81.52  E-value: 5.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1379 LNVHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKEL 1458
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1459 gdqtnkvKNLQETTEKLEMELICAKSDLNGISEDEDAENEDgvgggvyklKYERVARELEFTKRRLHTQHEhdLEQLVAL 1538
Cdd:COG1196   354 -------EEAEAELAEAEEALLEAEAELAEAEEELEELAEE---------LLEALRAAAELAAQLEELEEA--EEALLER 415
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1539 KKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAEcqsLQDAVRQERQAKER 1618
Cdd:COG1196   416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA---LAELLEELAEAAAR 492
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1619 YGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEqeeeldemagQ 1698
Cdd:COG1196   493 LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA----------A 562
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1699 IQLLEQAKLRlEMTLETMRKEARRESQQRDEELEEVrgngykkikalecqleteHEERTLLLREKHELERRLSSMEDRDR 1778
Cdd:COG1196   563 IEYLKAAKAG-RATFLPLDKIRARAALAAALARGAI------------------GAAVDLVASDLREADARYYVLGDTLL 623
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1779 VDRDAEEALNQKLRRdLRKYKALLKDAQTQLERLKADtpGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFD 1858
Cdd:COG1196   624 GRTLVAARLEAALRR-AVTLAGRLREVTLEGEGGSAG--GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 1859 ESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAEL 1937
Cdd:COG1196   701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
598-710 5.50e-15

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 74.69  E-value: 5.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  598 LLVVNPMAPLSLYSEKVV-SMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAG 676
Cdd:cd01363     2 LVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAF 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 116008016  677 AYNNfINAEKVNALCT---------------ILEAFGNTKTCLNSNATR 710
Cdd:cd01363    82 NGIN-KGETEGWVYLTeitvtledqilqanpILEAFGNAKTTRNENSSR 129
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
1384-2063 6.72e-15

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 80.92  E-value: 6.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1384 TEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVD----LAEERSTAHIATERLE--AETAERLKLEKE 1457
Cdd:pfam05483   97 IEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdlIKENNATRHLCNLLKEtcARSAEKTKKYEY 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1458 LGDQTNKV-KNLQETTEKLemelICAKSDLNGISEDEDAENEdgvgggvYKLK--YERVARELEFTKRRLH--------- 1525
Cdd:pfam05483  177 EREETRQVyMDLNNNIEKM----ILAFEELRVQAENARLEMH-------FKLKedHEKIQHLEEEYKKEINdkekqvsll 245
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1526 ----TQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKK-QRKFDA 1600
Cdd:pfam05483  246 liqiTEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDlQIATKT 325
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1601 ECQSLQDA---VRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLA----SLQR---ELEEMT-FGGGTEE 1669
Cdd:pfam05483  326 ICQLTEEKeaqMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKkssELEEMTkFKNNKEV 405
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1670 EFAQLRRSKNETERRAKEQEEeLDEMAGQIQLLEQaklRLEMTLETmrkearRESQQRDEELE----EVRGNGY-KKIKA 1744
Cdd:pfam05483  406 ELEELKKILAEDEKLLDEKKQ-FEKIAEELKGKEQ---ELIFLLQA------REKEIHDLEIQltaiKTSEEHYlKEVED 475
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1745 LECQLETEHEERTLLLREKHELerrlsSMEDRDRVDRDAEEALnqklrrDLRKYKALLKDAQTQLERLkadtpgktlIRQ 1824
Cdd:pfam05483  476 LKTELEKEKLKNIELTAHCDKL-----LLENKELTQEASDMTL------ELKKHQEDIINCKKQEERM---------LKQ 535
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1825 LRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQ--------------IEENEE 1890
Cdd:pfam05483  536 IENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnnlkkqienknknIEELHQ 615
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1891 ELGELMKKYSATVKQLNTEQInvseaefKLNEMEAERNNLKEQVAELqhrLDNVENlgdpsmammskrlELRTKELESRL 1970
Cdd:pfam05483  616 ENKALKKKGSAENKQLNAYEI-------KVNKLELELASAKQKFEEI---IDNYQK-------------EIEDKKISEEK 672
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1971 ELEQATRARLEVQvnrhkEALeKLQNEV---TQSKMREMQAQDVIKKSQ--KSLRDMREEFHAVSSREQESLTRRKDLEK 2045
Cdd:pfam05483  673 LLEEVEKAKAIAD-----EAV-KLQKEIdkrCQHKIAEMVALMEKHKHQydKIIEERDSELGLYKNKEQEQSSAKAALEI 746
                          730
                   ....*....|....*...
gi 116008016  2046 KVEQMESEGAALKNDLRL 2063
Cdd:pfam05483  747 ELSNIKAELLSLKKQLEI 764
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1383-1803 1.00e-14

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 80.49  E-value: 1.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1383 RTEEQLKTANEELLMLRAKLEKIECDRSEV---KAENQKLEAKLSELtvdlaEERstaHIATERLEAETAERLKLEKELG 1459
Cdd:PRK03918  311 EIEKRLSRLEEEINGIEERIKELEEKEERLeelKKKLKELEKRLEEL-----EER---HELYEEAKAKKEELERLKKRLT 382
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1460 DQT-----NKVKNLQETTEKLEME---LICAKSDLNGISED-EDAENEDGVGGGVYKLkyerVAREL-EFTKRRLHTQHE 1529
Cdd:PRK03918  383 GLTpekleKELEELEKAKEEIEEEiskITARIGELKKEIKElKKAIEELKKAKGKCPV----CGRELtEEHRKELLEEYT 458
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1530 HDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKR--KAQKMTNEMNDLRMLLEEQNARNnlLEKKQRKFDaECQSLQD 1607
Cdd:PRK03918  459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEE--LEKKAEEYE-KLKEKLI 535
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1608 AVRQERQAKERYGREKDVLQAEKFTLEQTLADtrldlefKEEKLASLQRELEEMTFGGGTE------------EEFAQLR 1675
Cdd:PRK03918  536 KLKGEIKSLKKELEKLEELKKKLAELEKKLDE-------LEEELAELLKELEELGFESVEEleerlkelepfyNEYLELK 608
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1676 RSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEE 1755
Cdd:PRK03918  609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKR 688
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 116008016 1756 RTLLLREKHELERRLSSMEDRDRVDRDAEEALN--QKLRRDLRKYKALLK 1803
Cdd:PRK03918  689 REEIKKTLEKLKEELEEREKAKKELEKLEKALErvEELREKVKKYKALLK 738
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1383-1981 1.42e-14

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 79.72  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1383 RTEEQLKTANEELLMLRAKLEKIEcdrSEVKaENQKLEAKLSELTVDLAEERSTAHIATERLEaETAERLK-LEKELGDQ 1461
Cdd:PRK03918  204 EVLREINEISSELPELREELEKLE---KEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIR-ELEERIEeLKKEIEEL 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1462 TNKVKNLQETTEKLE--MELICAKSDLNgiseDEDAENEDGVGGGVYKLK-YERVARELEFTKRRLhtqhEHDLEQLVAL 1538
Cdd:PRK03918  279 EEKVKELKELKEKAEeyIKLSEFYEEYL----DELREIEKRLSRLEEEINgIEERIKELEEKEERL----EELKKKLKEL 350
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1539 KKHLEmKLSDAYEEVVEQRQVVGQWKR-KAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQdavrqerqaKE 1617
Cdd:PRK03918  351 EKRLE-ELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK---------KE 420
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1618 RYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAG 1697
Cdd:PRK03918  421 IKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRI------EKELKEIEEKERKLRKELRELEKVLKKESE 494
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1698 QIQLLEQAKL--RLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHE---ERTLLLREKHELERRLSS 1772
Cdd:PRK03918  495 LIKLKELAEQlkELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAE 574
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1773 MEDR-DRVDRDAEEALNQKLRRDLRKYKAL--LKDAQTQLERLkadtpgKTLIRQLRNQLEDAESARSLAMKARQTAEAE 1849
Cdd:PRK03918  575 LLKElEELGFESVEELEERLKELEPFYNEYleLKDAEKELERE------EKELKKLEEELDKAFEELAETEKRLEELRKE 648
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1850 LTEVQAMFDES--HRARNDAEERANAAHRDRAELQaqieeneeelgelmkkysatvkqlnteqinvsEAEFKLNEMEAER 1927
Cdd:PRK03918  649 LEELEKKYSEEeyEELREEYLELSRELAGLRAELE--------------------------------ELEKRREEIKKTL 696
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 116008016 1928 NNLKEQVAELQHRLDNVENLGdpsmAMMSKRLELRTKELESRLELEQATRARLE 1981
Cdd:PRK03918  697 EKLKEELEEREKAKKELEKLE----KALERVEELREKVKKYKALLKERALSKVG 746
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1382-2075 4.86e-14

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: 78.17  E-value: 4.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1382 HRTEEQLKTANEELlmlrAKLEKIecdRSEVKAENQKLE--AKLSELTVDLAEERSTAHIA--TERLEAETAERLKLEKE 1457
Cdd:TIGR02168  175 KETERKLERTRENL----DRLEDI---LNELERQLKSLErqAEKAERYKELKAELRELELAllVLRLEELREELEELQEE 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1458 LGDQTNKVKNLQETTEKLEMELicakSDLNG-ISEDEDAENEdgvgggvYKLKYERVARELEftkrRLhtqhEHDLEQLV 1536
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKL----EELRLeVSELEEEIEE-------LQKELYALANEIS----RL----EQQKQILR 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1537 ALKKHLEMKLsdayEEVVEQRQvvgQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAK 1616
Cdd:TIGR02168  309 ERLANLERQL----EELEAQLE---ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1617 ERygrekdvLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERraKEQEEELDEMA 1696
Cdd:TIGR02168  382 ET-------LRSKVAQLELQIASLNNEIERLEARLERLEDRRER------LQQEIEELLKKLEEAEL--KELQAELEELE 446
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1697 GQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVR--GNGYKKIKALECQLETEHEERTLLLREKHELERRLSSME 1774
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAqlQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLS 526
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1775 DRDRVDRDAEEALNQKLRRDLRKYkaLLKDAQTQLERLKADTP---GKTLIRQL------------RNQLEDAESARSLA 1839
Cdd:TIGR02168  527 ELISVDEGYEAAIEAALGGRLQAV--VVENLNAAKKAIAFLKQnelGRVTFLPLdsikgteiqgndREILKNIEGFLGVA 604
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1840 MKARQTAEAELTEVQAMFDESH-----------RARNDAEER------------------ANAAHRDRAELQAQIEENEE 1890
Cdd:TIGR02168  605 KDLVKFDPKLRKALSYLLGGVLvvddldnalelAKKLRPGYRivtldgdlvrpggvitggSAKTNSSILERRREIEELEE 684
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1891 ELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDpSMAMMSKRLELRTKELESRL 1970
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKELTELEAEI 763
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1971 ELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQM 2050
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
                          730       740
                   ....*....|....*....|....*
gi 116008016  2051 ESEGAALKNDLRLALQRIADLQQAM 2075
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELI 868
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
1394-2062 6.12e-14

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: 78.09  E-value: 6.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1394 ELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTvdlAEERSTAHIATERLEAETAERLKLEKELGDQTNKVKNLQETTE 1473
Cdd:TIGR00618  167 ELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLT---LRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHA 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1474 KLEMELicaksdlngisedeDAENEdgvgggvyKLKYERVARELEFTKRRLHTQhehdLEQLVALKKHLEmkLSDAYEEV 1553
Cdd:TIGR00618  244 YLTQKR--------------EAQEE--------QLKKQQLLKQLRARIEELRAQ----EAVLEETQERIN--RARKAAPL 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1554 VEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQE---RQAKERYGREKDVLQAEK 1630
Cdd:TIGR00618  296 AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEihiRDAHEVATSIREISCQQH 375
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1631 fTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAklrlE 1710
Cdd:TIGR00618  376 -TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITC----T 450
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1711 MTLETMRKEARRESQQRDEELEEVRGNgYKKIKALECQLETEHEERTLLLREKH-ELERRLSSMEDRdRVDRDAEEALNQ 1789
Cdd:TIGR00618  451 AQCEKLEKIHLQESAQSLKEREQQLQT-KEQIHLQETRKKAVVLARLLELQEEPcPLCGSCIHPNPA-RQDIDNPGPLTR 528
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1790 KLRRDLRKYKALLK-------DAQTQLERLKADTPGKTLIRQ-------LRNQL-EDAESARSLAMKARQTAEAELTEVQ 1854
Cdd:TIGR00618  529 RMQRGEQTYAQLETseedvyhQLTSERKQRASLKEQMQEIQQsfsiltqCDNRSkEDIPNLQNITVRLQDLTEKLSEAED 608
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1855 AMFDESHRARNDAEERANaaHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKlnEMEAERNNLKEQv 1934
Cdd:TIGR00618  609 MLACEQHALLRKLQPEQD--LQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLP--KELLASRQLALQ- 683
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1935 aELQHRLDNVENLGDPSMAMMSKRLELRTKELESRLELEQ------ATRARLEVQVNRHKEALEKLQNE----------- 1997
Cdd:TIGR00618  684 -KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEienassSLGSDLAAREDALNQSLKELMHQartvlkartea 762
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016  1998 -------VTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKD----LEKKVEQMESEGAALKNDLR 2062
Cdd:TIGR00618  763 hfnnneeVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdediLNLQCETLVQEEEQFLSRLE 838
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
1383-2000 6.17e-14

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: 78.09  E-value: 6.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1383 RTEEQLKTANE--ELLMLRAKLEKI--ECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETaERLKLEKEL 1458
Cdd:TIGR00618  184 MEFAKKKSLHGkaELLTLRSQLLTLctPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE-EQLKKQQLL 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1459 GDQTNKVKNLQETTEKLE-----MELICAKSDLNGISEdEDAENEDGVGGGVYKLKYERVARELEFTKRRLHTQHEHDLE 1533
Cdd:TIGR00618  263 KQLRARIEELRAQEAVLEetqerINRARKAAPLAAHIK-AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIE 341
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1534 QLVALKKHL---EMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRkfDAECQSLQDAVR 1610
Cdd:TIGR00618  342 EQRRLLQTLhsqEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQR--EQATIDTRTSAF 419
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1611 QERQAKERYGREKDVLQAEKFTL-EQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFA-QLRRSKNETERRAKEQ 1688
Cdd:TIGR00618  420 RDLQGQLAHAKKQQELQQRYAELcAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHlQETRKKAVVLARLLEL 499
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1689 EEELDEMAGQ--------------------IQLLEQAKLRLEMTLETMRKEARRESQQR---DEELEEVRGNGYK---KI 1742
Cdd:TIGR00618  500 QEEPCPLCGScihpnparqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRaslKEQMQEIQQSFSIltqCD 579
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1743 KALECQL--------------ETEHEERTLLLREKHELERRLSSMEDRDRV---DRDAEEALNQKLRRDLRKYKALLKDA 1805
Cdd:TIGR00618  580 NRSKEDIpnlqnitvrlqdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVrlhLQQCSQELALKLTALHALQLTLTQER 659
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1806 QTQLERLKADTPgKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQI 1885
Cdd:TIGR00618  660 VREHALSIRVLP-KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARE 738
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1886 EENEEELGELMKKYSATVKQLNTEQINVSEAEF-------KLNEMEAERNNLKEQVAELQHRLdnvenlgdpsmAMMSKR 1958
Cdd:TIGR00618  739 DALNQSLKELMHQARTVLKARTEAHFNNNEEVTaalqtgaELSHLAAEIQFFNRLREEDTHLL-----------KTLEAE 807
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 116008016  1959 LELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQ 2000
Cdd:TIGR00618  808 IGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH 849
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1545-1993 6.48e-14

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 77.50  E-value: 6.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1545 KLSDAYEEVVEQRQVVGQWKRKaqkmTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQsLQDAVRQERQAKERYGREKD 1624
Cdd:COG4717    72 ELKELEEELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1625 VLQAEKFTLEQtLADTRLDLEFKEEKLASLQRELEE--MTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLL 1702
Cdd:COG4717   147 RLEELEERLEE-LRELEEELEELEAELAELQEELEEllEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1703 EQAKLRLEMTLETMRKEARRESQQR-----------DEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLS 1771
Cdd:COG4717   226 EEELEQLENELEAAALEERLKEARLllliaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1772 SMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKAdtpgktlIRQLRNQLEDAESARSLAmKARQTAEAELT 1851
Cdd:COG4717   306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE-------LQELLREAEELEEELQLE-ELEQEIAALLA 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1852 EVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATvkQLNTEqinVSEAEFKLNEMEAERNNLK 1931
Cdd:COG4717   378 EAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEE---LEELEEELEELEEELEELR 452
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116008016 1932 EQVAELQHRLDNVENLGDPSMAmmskRLELRTKELESRLELEQATRARLEVQV-NRHKEALEK 1993
Cdd:COG4717   453 EELAELEAELEQLEEDGELAEL----LQELEELKAELRELAEEWAALKLALELlEEAREEYRE 511
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1380-2052 1.10e-13

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: 77.02  E-value: 1.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1380 NVHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERstahiaterLEAETAERLKLEKELG 1459
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE---------LEELEEELEELQEELE 457
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1460 DQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDA-----ENEDGVGGGVYKLKYERVARELEF--TKRRLHTQHEHDL 1532
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSlerlqENLEGFSEGVKALLKNQSGLSGILgvLSELISVDEGYEA 537
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1533 EQLVALKKHLEMKLSDAYEEVVeqRQVVGQWKRKAQKMT-----------NEMNDLRMLLEEQNARNNLLEkkQRKFDAE 1601
Cdd:TIGR02168  538 AIEAALGGRLQAVVVENLNAAK--KAIAFLKQNELGRVTflpldsikgteIQGNDREILKNIEGFLGVAKD--LVKFDPK 613
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1602 --------------CQSLQDAVRQERQAKERY------------------GREKDVL-----QAEKFTLEQTLADTRLDL 1644
Cdd:TIGR02168  614 lrkalsyllggvlvVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSsilerRREIEELEEKIEELEEKI 693
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1645 EFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLEtmrkearres 1724
Cdd:TIGR02168  694 AELEKALAELRKELEEL------EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT---------- 757
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1725 qqrdeELEEvrgngykKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRdLRKYKALLKD 1804
Cdd:TIGR02168  758 -----ELEA-------EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNEEAANLRE 824
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1805 AQTQLERLKADTpgKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQ 1884
Cdd:TIGR02168  825 RLESLERRIAAT--ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1885 IEeneeelgelmkkysatvkqlnteqinvsEAEFKLNEMEAERNNLKEQVAELQHRLDnvenlgdpsmammskRLELRTK 1964
Cdd:TIGR02168  903 LR----------------------------ELESKRSELRRELEELREKLAQLELRLE---------------GLEVRID 939
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1965 ELESRL-ELEQATRARLEVQVNRHKEALEKLQNEVTQskmremqaqdvIKKSQKSLRDMR----EEFHAVSSREQESLTR 2039
Cdd:TIGR02168  940 NLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKR-----------LENKIKELGPVNlaaiEEYEELKERYDFLTAQ 1008
                          730
                   ....*....|...
gi 116008016  2040 RKDLEKKVEQMES 2052
Cdd:TIGR02168 1009 KEDLTEAKETLEE 1021
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1381-1884 2.24e-13

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 75.85  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1381 VHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGD 1460
Cdd:PRK02224  281 VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1461 QTNKVKNLQETTEKLEMELICAKSDLNGIsEDEDAENEDGVGGGVYKLkyERVARELEftkrrlhtQHEHDLEQLVALKK 1540
Cdd:PRK02224  361 LREEAAELESELEEAREAVEDRREEIEEL-EEEIEELRERFGDAPVDL--GNAEDFLE--------ELREERDELREREA 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1541 HLEMKLSDAYEEVVEQRQVVGQWK-------RKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQER 1613
Cdd:PRK02224  430 ELEATLRTARERVEEAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED 509
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1614 QAKERYGREKDVlqaekftlEQTLADTRLDLEFKEEKLASLQRELEEmtfgggteeefaqLRRSKNETERRAKEQEEELD 1693
Cdd:PRK02224  510 RIERLEERREDL--------EELIAERRETIEEKRERAEELRERAAE-------------LEAEAEEKREAAAEAEEEAE 568
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1694 EMAGQIQLLEQAKLRLEMTLETMRKeaRRESQQRDEELEEVRGNGYKKIKALEcQLETEHEERtllLREKHELERRLSSM 1773
Cdd:PRK02224  569 EAREEVAELNSKLAELKERIESLER--IRTLLAAIADAEDEIERLREKREALA-ELNDERRER---LAEKRERKRELEAE 642
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1774 EDRDRVdrdaEEALNQKLRRDlrKYKALLKDAQTQLERLKADTPGKtlIRQLRNQLEDAESARslamKARQTAEAELTEV 1853
Cdd:PRK02224  643 FDEARI----EEAREDKERAE--EYLEQVEEKLDELREERDDLQAE--IGAVENELEELEELR----ERREALENRVEAL 710
                         490       500       510
                  ....*....|....*....|....*....|.
gi 116008016 1854 QAMFDEshrarndAEERANAAHRDRAELQAQ 1884
Cdd:PRK02224  711 EALYDE-------AEELESMYGDLRAELRQR 734
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1490-2075 3.62e-13

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: 75.39  E-value: 3.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1490 SEDEDAENEDGVGGGVYKLKYERVARELEFTKRRLHTQHEHDLEQLVALKKHLEMKlSDAYEEVVEQRQ--VVGQWKRKA 1567
Cdd:pfam02463  151 KPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA-KKALEYYQLKEKleLEEEYLLYL 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1568 QKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAEcQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLE-- 1645
Cdd:pfam02463  230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKE-EEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLErr 308
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1646 ---------FKEEKLASLQRELEEMTFGGG---TEEEFAQLRRSKNETERRAKEQEEELDE------MAGQIQLLEQAKL 1707
Cdd:pfam02463  309 kvddeeklkESEKEKKKAEKELKKEKEEIEeleKELKELEIKREAEEEEEEELEKLQEKLEqleeelLAKKKLESERLSS 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1708 RLEMTLETMRKEARRESQQRDE-ELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELER----RLSSMEDRDRVDRD 1782
Cdd:pfam02463  389 AAKLKEEELELKSEEEKEAQLLlELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKeeleKQELKLLKDELELK 468
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1783 AEEALNQKLR-RDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQ------A 1855
Cdd:pfam02463  469 KSEDLLKETQlVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYkvaistA 548
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1856 MFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVK----QLNTEQINVSEAEFKLNEMEAERNNLK 1931
Cdd:pfam02463  549 VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLeidpILNLAQLDKATLEADEDDKRAKVVEGI 628
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1932 EQVAELQHRLDNVENLGDPSMAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDV 2011
Cdd:pfam02463  629 LKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE 708
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016  2012 IKKSQKSLRDMREEFHAVSSREQE-SLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAM 2075
Cdd:pfam02463  709 KEELKKLKLEAEELLADRVQEAQDkINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
1574-2070 5.47e-13

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 74.87  E-value: 5.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1574 MNDLR-MLLEEQNARNNLLEKKQRKFDAECQSLQDavRQERQAKERYGREKDVLQAEKFTLEQTLAD-TRLDLEFKEEKL 1651
Cdd:pfam12128  195 FRDVKsMIVAILEDDGVVPPKSRLNRQQVEHWIRD--IQAIAGIMKIRPEFTKLQQEFNTLESAELRlSHLHFGYKSDET 272
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1652 ASLQRELEEMTFGGGTEEEFAQLR----RSKNETERRAKEQEEELDEMAGQIQLLE-QAKLRLEMTLETMRKEARRESQQ 1726
Cdd:pfam12128  273 LIASRQEERQETSAELNQLLRTLDdqwkEKRDELNGELSAADAAVAKDRSELEALEdQHGAFLDADIETAAADQEQLPSW 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1727 RDEeLEEVRgngyKKIKALE-CQLETEHEERTLLLREKHELERRLSSMED--------RDR---VDRDAEEALNQKLRRD 1794
Cdd:pfam12128  353 QSE-LENLE----ERLKALTgKHQDVTAKYNRRRSKIKEQNNRDIAGIKDklakireaRDRqlaVAEDDLQALESELREQ 427
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1795 LRKYKALLKDAQTQLE--------RLKADTPGKTLIRQLRN---QLEDAESARSLAMKARQTAEAELTEVQAMFDESHRA 1863
Cdd:pfam12128  428 LEAGKLEFNEEEYRLKsrlgelklRLNQATATPELLLQLENfdeRIERAREEQEAANAEVERLQSELRQARKRRDQASEA 507
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1864 RNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQ-----LNTEQINVSEAEFKLNEMEAERNNlkeQVAELQ 1938
Cdd:pfam12128  508 LRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQsigkvISPELLHRTDLDPEVWDGSVGGEL---NLYGVK 584
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1939 HRLDNVENlgdPSMAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTqskmremQAQDVIKKSQKS 2018
Cdd:pfam12128  585 LDLKRIDV---PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREET-------FARTALKNARLD 654
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 116008016  2019 LRDMREEFHAVSSREQESLTRRKDL-EKKVEQMESEGAALKNDLRLALQRIAD 2070
Cdd:pfam12128  655 LRRLFDEKQSEKDKKNKALAERKDSaNERLNSLEAQLKQLDKKHQAWLEEQKE 707
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
1385-1995 6.59e-13

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 74.77  E-value: 6.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1385 EEQLKTANEELLMLRAKLEK-IECDRSEVKAENQKLEAKLSELtvdlaeERSTAHIATERLEAETaERLKLEKELGDQTN 1463
Cdd:pfam15921  305 QEQARNQNSMYMRQLSDLEStVSQLRSELREAKRMYEDKIEEL------EKQLVLANSELTEART-ERDQFSQESGNLDD 377
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1464 KVKNLQETTEKLEMELICAKSDlNGISEDEDAENEdgvgggvykLKYERVARELEftKRRLHTQhehdleQLVALKKHLE 1543
Cdd:pfam15921  378 QLQKLLADLHKREKELSLEKEQ-NKRLWDRDTGNS---------ITIDHLRRELD--DRNMEVQ------RLEALLKAMK 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1544 MKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMND----LRMLLEEQNARNNLLEKKQRKFDAECQSLQDavrqerqaKERy 1619
Cdd:pfam15921  440 SECQGQMERQMAAIQGKNESLEKVSSLTAQLEStkemLRKVVEELTAKKMTLESSERTVSDLTASLQE--------KER- 510
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1620 grekdvlQAEKFTLEQTLADTRLDLEFKEekLASLQRELEEMTfGGGTEEEFAQLRRS-KNETERRAKEQEEELDEMAGQ 1698
Cdd:pfam15921  511 -------AIEATNAEITKLRSRVDLKLQE--LQHLKNEGDHLR-NVQTECEALKLQMAeKDKVIEILRQQIENMTQLVGQ 580
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1699 ------IQLLEQAKLRLEMTLETM----------RKEAR-RESQQR--DEELEEVR--GNGYKKIKALEcqleTEHEERT 1757
Cdd:pfam15921  581 hgrtagAMQVEKAQLEKEINDRRLelqefkilkdKKDAKiRELEARvsDLELEKVKlvNAGSERLRAVK----DIKQERD 656
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1758 LLLREKHELERRLSSM-EDRDRVDRDAEEAlNQKLRRDLRKYKALLKDAQTQLErlkadtpgktlirQLRNQLEDAESAR 1836
Cdd:pfam15921  657 QLLNEVKTSRNELNSLsEDYEVLKRNFRNK-SEEMETTTNKLKMQLKSAQSELE-------------QTRNTLKSMEGSD 722
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1837 SLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQieeneeelgelMKKYSATVKQLNTEQinvsea 1916
Cdd:pfam15921  723 GHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEE-----------KNKLSQELSTVATEK------ 785
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016  1917 efklNEMEAERNNLKEQVAELQHRLDNVENLGDpsmammskRLELRTKELESRLELEQATRARLEVQvnrHKEALEKLQ 1995
Cdd:pfam15921  786 ----NKMAGELEVLRSQERRLKEKVANMEVALD--------KASLQFAECQDIIQRQEQESVRLKLQ---HTLDVKELQ 849
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
1385-2061 7.23e-13

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 74.38  E-value: 7.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1385 EEQLKTANEELLMLRAKLEKIECDRsEVKAENQKLEAKLSEltvDLAEE-RSTAHiaterlEAETAERLKlEKELGDQTN 1463
Cdd:pfam15921  102 EKQKFYLRQSVIDLQTKLQEMQMER-DAMADIRRRESQSQE---DLRNQlQNTVH------ELEAAKCLK-EDMLEDSNT 170
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1464 KVKNLQE---TTEKLEMELICAKSDLNGISEDEDAENED-------GVGGGVYKLKYErVARELEFTKRRLHTQHEhdle 1533
Cdd:pfam15921  171 QIEQLRKmmlSHEGVLQEIRSILVDFEEASGKKIYEHDSmstmhfrSLGSAISKILRE-LDTEISYLKGRIFPVED---- 245
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1534 QLVALKKHLEMKL-------SDAYEEVVEQRQV-VGQWKRKAQKMTNEMNDLRMLLE--EQNARN-NLLEKKQRkfdAEC 1602
Cdd:pfam15921  246 QLEALKSESQNKIelllqqhQDRIEQLISEHEVeITGLTEKASSARSQANSIQSQLEiiQEQARNqNSMYMRQL---SDL 322
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1603 QSLQDAVRQE-RQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNET 1681
Cdd:pfam15921  323 ESTVSQLRSElREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKR 402
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1682 --ERRAKEQ------EEELDEMAGQIQlleqaklRLEMTLETMRKEARresQQRDEELEEVRGN--GYKKIKALECQLET 1751
Cdd:pfam15921  403 lwDRDTGNSitidhlRRELDDRNMEVQ-------RLEALLKAMKSECQ---GQMERQMAAIQGKneSLEKVSSLTAQLES 472
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1752 EHEertLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLR-----------------------RDLRKYKALLKDAQTQ 1808
Cdd:pfam15921  473 TKE---MLRKVVEELTAKKMTLESSERTVSDLTASLQEKERaieatnaeitklrsrvdlklqelQHLKNEGDHLRNVQTE 549
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1809 LERLKADTPGK-TLIRQLRNQLEDAESarsLAMKARQTAEAELTEvQAMFDESHRARndaeeranaahrdRAELQaQIEE 1887
Cdd:pfam15921  550 CEALKLQMAEKdKVIEILRQQIENMTQ---LVGQHGRTAGAMQVE-KAQLEKEINDR-------------RLELQ-EFKI 611
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1888 NEEELGELMKKYSATVKQLNTEQINV----SEAEFKLNEMEAERNNLKEQVAELQHRLDNvenlgdpsmamMSKRLELRT 1963
Cdd:pfam15921  612 LKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELNS-----------LSEDYEVLK 680
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1964 KELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQ---ESLTRR 2040
Cdd:pfam15921  681 RNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQfleEAMTNA 760
                          730       740
                   ....*....|....*....|....*...
gi 116008016  2041 -------KDLEKKVEQMESEGAALKNDL 2061
Cdd:pfam15921  761 nkekhflKEEKNKLSQELSTVATEKNKM 788
PRK01156 PRK01156
chromosome segregation protein; Provisional
1378-2026 1.08e-12

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 73.78  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1378 LLNVHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEaklsELTVDLAEERSTAHIATERLEAETAERLKLEKE 1457
Cdd:PRK01156  158 ILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELE----NIKKQIADDEKSHSITLKEIERLSIEYNNAMDD 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1458 ---LGDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEdgvgggvYKLKYERVARELEFTKRRLHTQHEHDLEQ 1534
Cdd:PRK01156  234 ynnLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKE-------LEERHMKIINDPVYKNRNYINDYFKYKND 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1535 LVALKKHLEMKLSD--AYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEqnarnnlLEKKQRKFdaecQSLQDAVRQE 1612
Cdd:PRK01156  307 IENKKQILSNIDAEinKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILE-------LEGYEMDY----NSYLKSIESL 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1613 RQAKERYGREKDVLQAEkftLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKneteRRAKEQEEEL 1692
Cdd:PRK01156  376 KKKIEEYSKNIERMSAF---ISEILKIQEIDPDAIKKELNEINVKLQDI------SSKVSSLNQRI----RALRENLDEL 442
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1693 DEmagqiqlleqaklRLEMtLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSS 1772
Cdd:PRK01156  443 SR-------------NMEM-LNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEY 508
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1773 MEDRDRVDRDAEEALNQKLRRDLRKYK---ALLKDAQTQLERLKADtpgktlIRQLRnqLEDAESARSLAMKA-RQTAEA 1848
Cdd:PRK01156  509 LESEEINKSINEYNKIESARADLEDIKikiNELKDKHDKYEEIKNR------YKSLK--LEDLDSKRTSWLNAlAVISLI 580
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1849 ELTEVQAMFDESHRARNDAEERANaahrdraELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERN 1928
Cdd:PRK01156  581 DIETNRSRSNEIKKQLNDLESRLQ-------EIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKID 653
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1929 NLKEQVAELQHRldnvenlgDPSMAMMSKRL---ELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKmRE 2005
Cdd:PRK01156  654 NYKKQIAEIDSI--------IPDLKEITSRIndiEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDIN-ET 724
                         650       660
                  ....*....|....*....|.
gi 116008016 2006 MQAQDVIKKSQKSLRDMREEF 2026
Cdd:PRK01156  725 LESMKKIKKAIGDLKRLREAF 745
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
1381-1811 2.72e-12

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 72.46  E-value: 2.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1381 VHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGD 1460
Cdd:pfam15921  344 IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD 423
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1461 QTNKVknlqettEKLEMELICAKSDLNGISEDEDAenedGVGGGVYKL-KYERVARELEFTKRRLHTQhehdLEQLVALK 1539
Cdd:pfam15921  424 RNMEV-------QRLEALLKAMKSECQGQMERQMA----AIQGKNESLeKVSSLTAQLESTKEMLRKV----VEELTAKK 488
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1540 KHLEmklsdAYEEVVEQRQVVGQWKRKAQKMTN-EMNDLR-----MLLEEQNARNNllEKKQRKFDAECQSLQ------- 1606
Cdd:pfam15921  489 MTLE-----SSERTVSDLTASLQEKERAIEATNaEITKLRsrvdlKLQELQHLKNE--GDHLRNVQTECEALKlqmaekd 561
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1607 ---DAVRQE----RQAKERYGREKDVLQAEKFTLEQTLADTRLDL-EFK--EEKLASLQRELEEMTfgGGTEEEFAQLRR 1676
Cdd:pfam15921  562 kviEILRQQienmTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELqEFKilKDKKDAKIRELEARV--SDLELEKVKLVN 639
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1677 SKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESqqrdEELEEVRGNGYKKIKALECQLE-TEHEE 1755
Cdd:pfam15921  640 AGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS----EEMETTTNKLKMQLKSAQSELEqTRNTL 715
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116008016  1756 RTLLLREKHELERRLsSMEDRDRVDRDAEEALNQKLR------RDLRKYKALLKDAQTQLER 1811
Cdd:pfam15921  716 KSMEGSDGHAMKVAM-GMQKQITAKRGQIDALQSKIQfleeamTNANKEKHFLKEEKNKLSQ 776
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1387-2047 3.26e-12

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: 71.98  E-value: 3.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1387 QLKTANEELLMLRAKLEKIEcdrSEVKAENQ---KLEAKLSELTVDLAEerstahiaTERLEAETAERL-KLEKELGDQT 1462
Cdd:TIGR04523   90 KLKKNKDKINKLNSDLSKIN---SEIKNDKEqknKLEVELNKLEKQKKE--------NKKNIDKFLTEIkKKEKELEKLN 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1463 NKVKNLQETTEKLEMELICAKSDLNGISEDEDaenedgvgggvyKLKYERVARELEFTkrrlhtqhehDLEQLVALKKHL 1542
Cdd:TIGR04523  159 NKYNDLKKQKEELENELNLLEKEKLNIQKNID------------KIKNKLLKLELLLS----------NLKKKIQKNKSL 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1543 EMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMND----LRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKEr 1618
Cdd:TIGR04523  217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtqtqLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS- 295
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1619 ygrEKDVLQAEKftLEQTLADTRLDLEFKEEKLASLQRELEEMTFG-GGTEEEFAQLRRSKNETERRAKEQEEELDEMAG 1697
Cdd:TIGR04523  296 ---EISDLNNQK--EQDWNKELKSELKNQEKKLEEIQNQISQNNKIiSQLNEQISQLKKELTNSESENSEKQRELEEKQN 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1698 QIQLLE---QAKLRLEMTLETMRKEARRESQQRDEELEEVRgngyKKIKALECQLETEHEERTLLLREKHELERRLSSME 1774
Cdd:TIGR04523  371 EIEKLKkenQSYKQEIKNLESQINDLESKIQNQEKLNQQKD----EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1775 DRDRVdrdaeealnqkLRRDLRKYKALLKDAQTQLERLKAdtpgktLIRQLRNQLEDAESarslamkarqtaeaELTEVQ 1854
Cdd:TIGR04523  447 NQDSV-----------KELIIKNLDNTRESLETQLKVLSR------SINKIKQNLEQKQK--------------ELKSKE 495
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1855 AMFDESHRARNDAEERANAAHRDRAELQAQIeeneeelgelmKKYSATVKQLNTEqinVSEAEFKLNEMEAE--RNNLKE 1932
Cdd:TIGR04523  496 KELKKLNEEKKELEEKVKDLTKKISSLKEKI-----------EKLESEKKEKESK---ISDLEDELNKDDFElkKENLEK 561
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1933 QVAELQHRLDNVENLGDPSMAMMS------KRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEvtqskmrEM 2006
Cdd:TIGR04523  562 EIDEKNKEIEELKQTQKSLKKKQEekqeliDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSI-------IK 634
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 116008016  2007 QAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKV 2047
Cdd:TIGR04523  635 NIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1532-1885 4.71e-12

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: 71.64  E-value: 4.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1532 LEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEmndlrmlLEEQNARNNLLEKKQRKFDAECQSLQDAVRQ 1611
Cdd:TIGR02169  676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1612 ERQAKERYGREKDVLQAEkftleqtladtrldLEFKEEKLASLQRELEEMtfgggteeeFAQLRRSK-NETERRAKEQEE 1690
Cdd:TIGR02169  749 LEQEIENVKSELKELEAR--------------IEELEEDLHKLEEALNDL---------EARLSHSRiPEIQAELSKLEE 805
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1691 ELDEMAGQIQLLEQAKLRLEMTLETMRKEaRRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRL 1770
Cdd:TIGR02169  806 EVSRIEARLREIEQKLNRLTLEKEYLEKE-IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1771 SSME-DRDRVDRDAEEALN--QKLRRDLRKYKALLKDAQTQLERLKADTpgKTLIRQLRNQLEDAESARSLAmKARQTAE 1847
Cdd:TIGR02169  885 GDLKkERDELEAQLRELERkiEELEAQIEKKRKRLSELKAKLEALEEEL--SEIEDPKGEDEEIPEEELSLE-DVQAELQ 961
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 116008016  1848 AELTEVQAM----------FDESHRARNDAEERANAAHRDRAELQAQI 1885
Cdd:TIGR02169  962 RVEEEIRALepvnmlaiqeYEEVLKRLDELKEKRAKLEEERKAILERI 1009
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1379-1842 6.10e-12

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 71.48  E-value: 6.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1379 LNVHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEerstahIATERLEAETAERLKLEKEL 1458
Cdd:COG4913   281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG------NGGDRLEQLEREIERLEREL 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1459 GDQTNKVKNLQETTEKLEMELI-----------CAKSDLNGISEDEDA--ENEDGVGGGVYKLK--YERVARELEFTKRR 1523
Cdd:COG4913   355 EERERRRARLEALLAALGLPLPasaeefaalraEAAALLEALEEELEAleEALAEAEAALRDLRreLRELEAEIASLERR 434
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1524 LHTQHEHDLEQLVALKKHLEMKLSD------------------------------------AYE----EVVEQR------ 1557
Cdd:COG4913   435 KSNIPARLLALRDALAEALGLDEAElpfvgelievrpeeerwrgaiervlggfaltllvppEHYaaalRWVNRLhlrgrl 514
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1558 --QVVGQWKRKAQKMTNEMNDL--RMLLEEQNARNNLLEKKQRKFDAEC----QSLQD---AVRQERQAKERYGR-EKDV 1625
Cdd:COG4913   515 vyERVRTGLPDPERPRLDPDSLagKLDFKPHPFRAWLEAELGRRFDYVCvdspEELRRhprAITRAGQVKGNGTRhEKDD 594
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1626 lqaekftleQTLADTRLDLEFK-EEKLASLQRELeemtfgggteeefAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQ 1704
Cdd:COG4913   595 ---------RRRIRSRYVLGFDnRAKLAALEAEL-------------AELEEELAEAEERLEALEAELDALQERREALQR 652
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1705 AKLRLEMTLETmrKEARRESQQRDEELEEVRgNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDR-DRVDRDA 1783
Cdd:COG4913   653 LAEYSWDEIDV--ASAEREIAELEAELERLD-ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKElEQAEEEL 729
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 1784 EEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKA 1842
Cdd:COG4913   730 DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
1371-2053 1.24e-11

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 70.46  E-value: 1.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1371 LLVRVTPL-LNVHRTEEQLKTANEELLMLRAKLE----------KIECDRS-EVKAENQKLEAKL-SELTVDLAEERSTA 1437
Cdd:TIGR00606  345 LLVEQGRLqLQADRHQEHIRARDSLIQSLATRLEldgfergpfsERQIKNFhTLVIERQEDEAKTaAQLCADLQSKERLK 424
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1438 HIATERLEAETA--------ERLKLEKELGDQTNKVKNLQETTE------KLEMELICAKSDLNGISEDEDAENEDGvgg 1503
Cdd:TIGR00606  425 QEQADEIRDEKKglgrtielKKEILEKKQEELKFVIKELQQLEGssdrilELDQELRKAERELSKAEKNSLTETLKK--- 501
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1504 GVYKLKYERVarELEFTKRRLhtqhEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMND------L 1577
Cdd:TIGR00606  502 EVKSLQNEKA--DLDRKLRKL----DQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpnkkqL 575
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1578 RMLLEEQNARNNLLEKKQRKFDAECQSLQdavrqerQAKERYGREKDVLQAEKFTLEQTLADTrLDLEFKEEKLASLQRE 1657
Cdd:TIGR00606  576 EDWLHSKSKEINQTRDRLAKLNKELASLE-------QNKNHINNELESKEEQLSSYEDKLFDV-CGSQDEESDLERLKEE 647
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1658 LEEMT-----FGGGTEEEFAQLRRSKNETE------RRAKEQEEELDEMAGQIQlleqAKLRLEMT-LETMRKEARRESQ 1725
Cdd:TIGR00606  648 IEKSSkqramLAGATAVYSQFITQLTDENQsccpvcQRVFQTEAELQEFISDLQ----SKLRLAPDkLKSTESELKKKEK 723
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1726 QRDEELEEVRGngykkikalecqletEHEERTLLLREKHELERRLSSmedrdrVDRDAeealnQKLRRDLRKYKALLKDA 1805
Cdd:TIGR00606  724 RRDEMLGLAPG---------------RQSIIDLKEKEIPELRNKLQK------VNRDI-----QRLKNDIEEQETLLGTI 777
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1806 QTQLERLKADTPGKTLIRQLRNQLEDAESArslamKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQI 1885
Cdd:TIGR00606  778 MPEEESAKVCLTDVTIMERFQMELKDVERK-----IAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLI 852
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1886 EENEEElgelMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDPsMAMMSKRLELRTKE 1965
Cdd:TIGR00606  853 QDQQEQ----IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSP-LETFLEKDQQEKEE 927
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1966 LESRLELEqatRARLEVQVNRHKEALEK-------LQNEVTQSKMRE-MQAQDVI--------------KKSQKSLRDMR 2023
Cdd:TIGR00606  928 LISSKETS---NKKAQDKVNDIKEKVKNihgymkdIENKIQDGKDDYlKQKETELntvnaqleecekhqEKINEDMRLMR 1004
                          730       740       750
                   ....*....|....*....|....*....|...
gi 116008016  2024 EEFHAVSSRE---QESLTRRKdLEKKVEQMESE 2053
Cdd:TIGR00606 1005 QDIDTQKIQErwlQDNLTLRK-RENELKEVEEE 1036
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1763-2116 1.40e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1763 KHELERRLSSMEDR-DRVDRDAEEALNQ--KLRRD---LRKYKALlkdaQTQLERLKAdtpgkTL----IRQLRNQLEDA 1832
Cdd:COG1196   174 KEEAERKLEATEENlERLEDILGELERQlePLERQaekAERYREL----KEELKELEA-----ELlllkLRELEAELEEL 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1833 ESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIeeneeelgelmkkySATVKQLNTEQIN 1912
Cdd:COG1196   245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL--------------ARLEQDIARLEER 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1913 VSEAEFKLNEMEAERNNLKEQVAELQhrldnvenlgdpsmammsKRLELRTKEL---ESRLELEQATRARLEVQVNRHKE 1989
Cdd:COG1196   311 RRELEERLEELEEELAELEEELEELE------------------EELEELEEELeeaEEELEEAEAELAEAEEALLEAEA 372
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1990 ALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIA 2069
Cdd:COG1196   373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 116008016 2070 DLQQAMEEEGEEELSESDESLSSVGSISDLEDRLRPVHVKRSSQQSL 2116
Cdd:COG1196   453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1796-2073 1.53e-11

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: 70.09  E-value: 1.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1796 RKYKALLK--DAQTQLERLKAdtpgktLIRQLRNQLEDAESARSLAMKARQTaEAELTEVQAMFdeshrarndAEERANA 1873
Cdd:TIGR02168  173 RRKETERKleRTRENLDRLED------ILNELERQLKSLERQAEKAERYKEL-KAELRELELAL---------LVLRLEE 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1874 AHRDRAELQAQIeeneeelgelmkkySATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLgdpsma 1953
Cdd:TIGR02168  237 LREELEELQEEL--------------KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE------ 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1954 mmSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSRE 2033
Cdd:TIGR02168  297 --ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 116008016  2034 QESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQ 2073
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
1385-1934 1.56e-11

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 70.37  E-value: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1385 EEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTvDLAEERSTAHIATERLEAETAERLKLEKELGDQtnk 1464
Cdd:COG3096   556 EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELA-ARAPAWLAAQDALERLREQSGEALADSQEVTAA--- 631
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1465 vknLQETTEKlEMELIcaksdlngISEDEDAENEdgvgggvyklkyervaRELEFTKRRLHTQHEHDLEQLVALKKHLE- 1543
Cdd:COG3096   632 ---MQQLLER-EREAT--------VERDELAARK----------------QALESQIERLSQPGGAEDPRLLALAERLGg 683
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1544 MKLSDAYEEVV------------EQRQ--VV---GQWKRKAQKMTNEMNDLRmlleeqnarnnLLEKKQRKFDA---ECQ 1603
Cdd:COG3096   684 VLLSEIYDDVTledapyfsalygPARHaiVVpdlSAVKEQLAGLEDCPEDLY-----------LIEGDPDSFDDsvfDAE 752
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1604 SLQDAV------RQERQAK-------ERYGREK--DVLQAEKFTLEQTLADTRLDLEfkeeKLASLQRELEE-------M 1661
Cdd:COG3096   753 ELEDAVvvklsdRQWRYSRfpevplfGRAAREKrlEELRAERDELAEQYAKASFDVQ----KLQRLHQAFSQfvgghlaV 828
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1662 TFGGGTEEEFAQLRRSKNETER-----RAKEQE--EELDEMAGQIQLLE----QAKLRLEMTLETMRKEARRESQQRDEE 1730
Cdd:COG3096   829 AFAPDPEAELAALRQRRSELERelaqhRAQEQQlrQQLDQLKEQLQLLNkllpQANLLADETLADRLEELREELDAAQEA 908
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1731 LEEVRGNGyKKIKALECQLETeheertllLR---EKHE-LERRLSSMEDRDRVDRDAEEALNQKLRRdlRKYKALlKDAQ 1806
Cdd:COG3096   909 QAFIQQHG-KALAQLEPLVAV--------LQsdpEQFEqLQADYLQAKEQQRRLKQQIFALSEVVQR--RPHFSY-EDAV 976
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1807 TQLERlkadtpGKTLIRQLRNQLEDAESARS---LAMKARQTAEAELTEVQAMFDESHRARND----------------- 1866
Cdd:COG3096   977 GLLGE------NSDLNEKLRARLEQAEEARRearEQLRQAQAQYSQYNQVLASLKSSRDAKQQtlqeleqeleelgvqad 1050
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1867 --AEERanaAHRDRAELQAQIEENEEelgelmkKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQV 1934
Cdd:COG3096  1051 aeAEER---ARIRRDELHEELSQNRS-------RRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1300-1721 1.90e-11

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: 69.70  E-value: 1.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1300 SQILFRSGVLSELEAKRDVLLSDRIIQLQAFCR----GYLARKKMSQRRVQELAVRCIQRNVKAFLAVRDWPWWRLLVRV 1375
Cdd:TIGR02168  670 SSILERRREIEELEEKIEELEEKIAELEKALAElrkeLEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1376 TpllnvhRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAetaerlkLE 1455
Cdd:TIGR02168  750 A------QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-------LN 816
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1456 KELGDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEdaenedgvgggvykLKYERVARELEFTKRRLHTQHEHDLEQL 1535
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI--------------ESLAAEIEELEELIEELESELEALLNER 882
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1536 VALKKHLeMKLSDAYEEVVEQRqvvgqwkrkaQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRqerqa 1615
Cdd:TIGR02168  883 ASLEEAL-ALLRSELEELSEEL----------RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS----- 946
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1616 kERYGREKDVLQAEKFTLEqtladtrLDLEFKEEKLASLQRELEEmtFGG---GTEEEFaqlrrskneterraKEQEEEL 1692
Cdd:TIGR02168  947 -EEYSLTLEEAEALENKIE-------DDEEEARRRLKRLENKIKE--LGPvnlAAIEEY--------------EELKERY 1002
                          410       420
                   ....*....|....*....|....*....
gi 116008016  1693 DEMAGQIQLLEQAKLRLEMTLETMRKEAR 1721
Cdd:TIGR02168 1003 DFLTAQKEDLTEAKETLEEAIEEIDREAR 1031
PTZ00121 PTZ00121
MAEBL; Provisional
1410-2055 3.08e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 69.40  E-value: 3.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1410 SEVKAENQKLEAKLSELTVDLAEERSTAHIATERleAETAERLKlEKELGDQTNKVKNLQETTEKLEMELICAKSDLNGI 1489
Cdd:PTZ00121 1090 DEATEEAFGKAEEAKKTETGKAEEARKAEEAKKK--AEDARKAE-EARKAEDARKAEEARKAEDAKRVEIARKAEDARKA 1166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1490 SEDEDAENEdgvgggvyklKYERVARELEFTKRRLHTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQV-----VGQWK 1564
Cdd:PTZ00121 1167 EEARKAEDA----------KKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAeavkkAEEAK 1236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1565 RKAQ--KMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVR---QERQAKERYGRE--KDVLQAEKFTLEQTL 1637
Cdd:PTZ00121 1237 KDAEeaKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKkaeEKKKADEAKKAEekKKADEAKKKAEEAKK 1316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1638 ADtrlDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGqiqllEQAKLR---LEMTLE 1714
Cdd:PTZ00121 1317 AD---EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK-----EEAKKKadaAKKKAE 1388
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1715 TMRK--EARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEAlnQKLR 1792
Cdd:PTZ00121 1389 EKKKadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEA--KKKA 1466
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1793 RDLRKYKALLKDAQtqlERLKADTPGKTlirqlrnqledAESARSLAMKARQTAEAELTEVQAMFDESHRARND---AEE 1869
Cdd:PTZ00121 1467 EEAKKADEAKKKAE---EAKKADEAKKK-----------AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakkAEE 1532
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1870 RANAAHRDRAElqaqieeneeelgelMKKYSATVKQlnTEQINVSEAEFKLNEM--EAERNNLKEQVAELQHRLDnvenl 1947
Cdd:PTZ00121 1533 AKKADEAKKAE---------------EKKKADELKK--AEELKKAEEKKKAEEAkkAEEDKNMALRKAEEAKKAE----- 1590
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1948 gdpsmammSKRLELRTK--ELESRLELEQATRA----------RLEVQVNRHKEALEKLQNEVTQ--SKMREMQAQDVIK 2013
Cdd:PTZ00121 1591 --------EARIEEVMKlyEEEKKMKAEEAKKAeeakikaeelKKAEEEKKKVEQLKKKEAEEKKkaEELKKAEEENKIK 1662
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 116008016 2014 KSQKSLRDMREEFHAVSSRE--------QESLTRRKDLEKKVEQMESEGA 2055
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKaeedekkaAEALKKEAEEAKKAEELKKKEA 1712
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1320-1998 3.76e-11

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: 68.94  E-value: 3.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1320 LSDRIIQLQAFCRGYLARKKMSQRRVQELAVRCIQrnVKAFLAVRDWPWWRLLVRVTPLLNVHR-TEEQLKTANEELLML 1398
Cdd:TIGR02169  320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK--LTEEYAELKEELEDLRAELEEVDKEFAeTRDELKDYREKLEKL 397
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1399 RAKLEKIECDRSEVKAENQKLEAKLSELTVDLA--EERSTAHIAT-----ERLEAETAERLKLEKELGDQTNKVKNLQET 1471
Cdd:TIGR02169  398 KREINELKRELDRLQEELQRLSEELADLNAAIAgiEAKINELEEEkedkaLEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1472 TEKLEMELICAKSDLNgISEDEDAENEDGVGGGVyklkyeRVARELEFTKRRLHTQhehdLEQLVALK----KHLEMKLS 1547
Cdd:TIGR02169  478 YDRVEKELSKLQRELA-EAEAQARASEERVRGGR------AVEEVLKASIQGVHGT----VAQLGSVGeryaTAIEVAAG 546
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1548 DAYEEVVEQRQVVGQW------KRKAQKMT----NEMNDLRMLLE---EQNARN---NLLEKKQRKFDAECQSLQDAVRQ 1611
Cdd:TIGR02169  547 NRLNNVVVEDDAVAKEaiellkRRKAGRATflplNKMRDERRDLSilsEDGVIGfavDLVEFDPKYEPAFKYVFGDTLVV 626
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1612 ER--QAKERYGREKDVlqaekfTLEQTLAD--------------TRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLR 1675
Cdd:TIGR02169  627 EDieAARRLMGKYRMV------TLEGELFEksgamtggsraprgGILFSRSEPAELQRLRERLEGL------KRELSSLQ 694
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1676 RSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMR---KEARRESQQRDEELEEVRgngyKKIKALECQLEtE 1752
Cdd:TIGR02169  695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerlEELEEDLSSLEQEIENVK----SELKELEARIE-E 769
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1753 HEErtlllrEKHELERRLSSMEDRDRVDRDAE-EALNQKLRRDLRKYKALLKDAQTQLERLkadTPGKTLIRQLRN---- 1827
Cdd:TIGR02169  770 LEE------DLHKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREIEQKLNRL---TLEKEYLEKEIQelqe 840
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1828 QLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLN 1907
Cdd:TIGR02169  841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1908 TEQINVSEAEFKLNEMEAERNNLKEQVAE------LQHRLDNVE----NLGDPSMAMMS--KRLELRTKELESRLELEQA 1975
Cdd:TIGR02169  921 ELKAKLEALEEELSEIEDPKGEDEEIPEEelsledVQAELQRVEeeirALEPVNMLAIQeyEEVLKRLDELKEKRAKLEE 1000
                          730       740
                   ....*....|....*....|...
gi 116008016  1976 TRARLEVQVNRhkeaLEKLQNEV 1998
Cdd:TIGR02169 1001 ERKAILERIEE----YEKKKREV 1019
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1649-2075 5.24e-11

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 67.87  E-value: 5.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1649 EKLASLQRELEEMTfggGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLEtmRKEARRESQQRD 1728
Cdd:COG4717    71 KELKELEEELKEAE---EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE--LEALEAELAELP 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1729 EELEEVRgNGYKKIKALECQLETEHEERTLLlREKHELERRLSSMEDRDRVDRDAEEAlnQKLRRDLRKYKALLKDAQTQ 1808
Cdd:COG4717   146 ERLEELE-ERLEELRELEEELEELEAELAEL-QEELEELLEQLSLATEEELQDLAEEL--EELQQRLAELEEELEEAQEE 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1809 LERLKADtpgktlIRQLRNQLEDAESARSLAmKARQTAEAeLTEVQAMFDESHRARNDAEERANAAhRDRAELQAQIEEN 1888
Cdd:COG4717   222 LEELEEE------LEQLENELEAAALEERLK-EARLLLLI-AAALLALLGLGGSLLSLILTIAGVL-FLVLGLLALLFLL 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1889 EEELGELMKKYSATVKQLnTEQINVSEAEFKlNEMEAERNNLKEQVAELQHRLDNVENLgdpsmammsKRLELRTKELES 1968
Cdd:COG4717   293 LAREKASLGKEAEELQAL-PALEELEEEELE-ELLAALGLPPDLSPEELLELLDRIEEL---------QELLREAEELEE 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1969 RLELEQATRARLEVQVNRHKEALEKLQNEVTQSKmREMQAQDVIKKSQKSLRDMREEFHAVSSREQEsltrrKDLEKKVE 2048
Cdd:COG4717   362 ELQLEELEQEIAALLAEAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELE 435
                         410       420
                  ....*....|....*....|....*..
gi 116008016 2049 QMESEGAALKNDLRLALQRIADLQQAM 2075
Cdd:COG4717   436 ELEEELEELEEELEELREELAELEAEL 462
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1532-2067 5.44e-11

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 68.40  E-value: 5.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1532 LEQLVALKKHLEmKLSDAYEEVVEQRQvvgqwkrkaQkmtnemndlRMLLEEQNARNNLLEKKQRKFDaECQSLQDAVR- 1610
Cdd:COG4913   224 FEAADALVEHFD-DLERAHEALEDARE---------Q---------IELLEPIRELAERYAAARERLA-ELEYLRAALRl 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1611 -QERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtFGGGTEEefaQLRRSKNETERRAKEQE 1689
Cdd:COG4913   284 wFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG--NGGDRLE---QLEREIERLERELEERE 358
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1690 EELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALEcQLETEHEErtlLLREKHELERR 1769
Cdd:COG4913   359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR-DLRRELRE---LEAEIASLERR 434
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1770 LSSMEDR--------------DRVD---------------------------------------RDAEEALNQ-KLRRDL 1795
Cdd:COG4913   435 KSNIPARllalrdalaealglDEAElpfvgelievrpeeerwrgaiervlggfaltllvppehyAAALRWVNRlHLRGRL 514
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1796 RKYKALLKDAQTQLERLKADT-PGKTLIRQ------LRNQLED------AESARSLAMKARQ-TAEAELTEVQAMF---D 1858
Cdd:COG4913   515 VYERVRTGLPDPERPRLDPDSlAGKLDFKPhpfrawLEAELGRrfdyvcVDSPEELRRHPRAiTRAGQVKGNGTRHekdD 594
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1859 ESHRARN-----DAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQiNVSEAEFKLNEMEAernnLKEQ 1933
Cdd:COG4913   595 RRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVAS----AERE 669
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1934 VAELQHRLDNVENlGDPSMAMMSKRLElrtkELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIK 2013
Cdd:COG4913   670 IAELEAELERLDA-SSDDLAALEEQLE----ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 116008016 2014 KSQKSLRDmrEEFHAVSSREQESLTRRkDLEKKVEQMESEGAALKNDLRLALQR 2067
Cdd:COG4913   745 LELRALLE--ERFAAALGDAVERELRE-NLEERIDALRARLNRAEEELERAMRA 795
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1619-2028 5.98e-11

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: 68.17  E-value: 5.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1619 YGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggteEEFAQLRRSKNETE-----RRAKEQEEELD 1693
Cdd:TIGR02169  168 FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA-------ERYQALLKEKREYEgyellKEKEALERQKE 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1694 EMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSM 1773
Cdd:TIGR02169  241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1774 EDRdrvdrdaeealNQKLRRDLRKYKALLKDAQTQLERLKADtpgktlIRQLRNQLEDAEsarslamKARQTAEAELTEV 1853
Cdd:TIGR02169  321 EER-----------LAKLEAEIDKLLAEIEELEREIEEERKR------RDKLTEEYAELK-------EELEDLRAELEEV 376
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1854 QAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGelmkkysatvkqlnteqinvsEAEFKLNEMEAERNNLKEQ 1933
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ---------------------RLSEELADLNAAIAGIEAK 435
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1934 VAELQHRLDnvenlgdpsmammSKRLELrtKELESRLELEQATRARLEVQVNRHKEALEKLQNEVT--QSKMREMQAQ-D 2010
Cdd:TIGR02169  436 INELEEEKE-------------DKALEI--KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSklQRELAEAEAQaR 500
                          410
                   ....*....|....*...
gi 116008016  2011 VIKKSQKSLRDMREEFHA 2028
Cdd:TIGR02169  501 ASEERVRGGRAVEEVLKA 518
PTZ00121 PTZ00121
MAEBL; Provisional
1383-1872 7.39e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.24  E-value: 7.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1383 RTEEQLKTANEellMLRAKLEKIECDRSEVKAENQKleaKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQT 1462
Cdd:PTZ00121 1399 KAEEDKKKADE---LKKAAAAKKKADEAKKKAEEKK---KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1463 NKVKNLQETTEKLEmelicaksDLNGISEDEDAENEDGVGGGVYKLKYERvARELEFTKRRLHTQHEHDLEQLVALKKHL 1542
Cdd:PTZ00121 1473 DEAKKKAEEAKKAD--------EAKKKAEEAKKKADEAKKAAEAKKKADE-AKKAEEAKKADEAKKAEEAKKADEAKKAE 1543
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1543 EMKLSDAYEEVVEQRQvvGQWKRKAQKMTNEMNDLRMLLEeqnaRNNLLEKKQRKFDAECQSLQDAVRQERqAKERYGRE 1622
Cdd:PTZ00121 1544 EKKKADELKKAEELKK--AEEKKKAEEAKKAEEDKNMALR----KAEEAKKAEEARIEEVMKLYEEEKKMK-AEEAKKAE 1616
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1623 KDVLQAEKFTLEQTLADTRLDLEFKEE----KLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKE----QEEELDE 1694
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEdekkAAEALKK 1696
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1695 MAGQIQLLEQAKLRLEmtlETMRK--EARRESQQRDEELEEVRGNGYKKIKALEcQLETEHEERTLLLREKHELERRlsS 1772
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEA---EEKKKaeELKKAEEENKIKAEEAKKEAEEDKKKAE-EAKKDEEEKKKIAHLKKEEEKK--A 1770
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1773 MEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTE 1852
Cdd:PTZ00121 1771 EEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFE 1850
                         490       500
                  ....*....|....*....|
gi 116008016 1853 vQAMFDESHRARNDAEERAN 1872
Cdd:PTZ00121 1851 -KHKFNKNNENGEDGNKEAD 1869
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1378-1727 1.05e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 67.10  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1378 LLNVHRTEEQLKTANEELLMLRAKLEKIE---CDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLK- 1453
Cdd:COG4717   124 LLQLLPLYQELEALEAELAELPERLEELEerlEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEe 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1454 -------LEKELGDQTNKVKNLQETTEKLEMELIcAKSDLNGISE------------------DEDAENEDGVGG----- 1503
Cdd:COG4717   204 lqqrlaeLEEELEEAQEELEELEEELEQLENELE-AAALEERLKEarlllliaaallallglgGSLLSLILTIAGvlflv 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1504 -------GVYKLKYERVARELEFTKRRLHTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMND 1576
Cdd:COG4717   283 lgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1577 LRmLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADtrLDLEFKEEKLASLQR 1656
Cdd:COG4717   363 LQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA--LDEEELEEELEELEE 439
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1657 ELEEmtfgggTEEEFAQLRRSKNETERRAK--EQEEELDEMAGQIQLLEQ---------AKLRL-EMTLETMRKEARRES 1724
Cdd:COG4717   440 ELEE------LEEELEELREELAELEAELEqlEEDGELAELLQELEELKAelrelaeewAALKLaLELLEEAREEYREER 513

                  ...
gi 116008016 1725 QQR 1727
Cdd:COG4717   514 LPP 516
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1385-1688 1.05e-10

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: 67.40  E-value: 1.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1385 EEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERST-----AHIATERLEAETAERLKLEKELG 1459
Cdd:TIGR02169  729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndleARLSHSRIPEIQAELSKLEEEVS 808
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1460 DQTNKVKNLQETTEKLEMELICAKSDLNGISED----EDAENEDGVGGGVYKLKYERVARELEftkrrlhtQHEHDLEQL 1535
Cdd:TIGR02169  809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridlKEQIKSIEKEIENLNGKKEELEEELE--------ELEAALRDL 880
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1536 VALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLE--KKQRKFDAECQSLQDAVRQER 1613
Cdd:TIGR02169  881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEdpKGEDEEIPEEELSLEDVQAEL 960
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016  1614 QAKErygREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQ 1688
Cdd:TIGR02169  961 QRVE---EEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI------LERIEEYEKKKREVFMEAFEA 1026
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
1393-2048 1.47e-10

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: 66.77  E-value: 1.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1393 EELLMLRAKLEKIEcdrSEVKAENQKLEAKLSELTVDLAEERSTAHiaTERLEAETAERlklEKELGDQTNKVKNLQETT 1472
Cdd:pfam10174  130 KELFLLRKTLEEME---LRIETQKQTLGARDESIKKLLEMLQSKGL--PKKSGEEDWER---TRRIAEAEMQLGHLEVLL 201
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1473 EKLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLK------YERVARELEFTKRRLHT-------QHEHDLEQLVALK 1539
Cdd:pfam10174  202 DQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKdtkissLERNIRDLEDEVQMLKTngllhteDREEEIKQMEVYK 281
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1540 KHLE-MKlsdayeevveqrQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNN------------LLEKKQRKfdAECQSLQ 1606
Cdd:pfam10174  282 SHSKfMK------------NKIDQLKQELSKKESELLALQTKLETLTNQNSdckqhievlkesLTAKEQRA--AILQTEV 347
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1607 DAVRQERQAKERYGREKDV----LQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETE 1682
Cdd:pfam10174  348 DALRLRLEEKESFLNKKTKqlqdLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENL------QEQLRDKDKQLAGLK 421
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1683 RRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRgngyKKIKALECQLETEH----EERTL 1758
Cdd:pfam10174  422 ERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLK----KENKDLKEKVSALQpeltEKESS 497
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1759 LLREKHELERRLSSMEDRDRVDRDAEEALNQKlRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNqledaesarsl 1838
Cdd:pfam10174  498 LIDLKEHASSLASSGLKKDSKLKSLEIAVEQK-KEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQ----------- 565
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1839 amkarqtaeaeltEVQAMFDESHRARNDAEERANAahrdraelqaqieeneeelgelmkkysatvkqlnteqinvseaef 1918
Cdd:pfam10174  566 -------------EVARYKEESGKAQAEVERLLGI--------------------------------------------- 587
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1919 kLNEMEAERNNLKEQVAELQHRLD--------NVENLGDPSMAMMSKRLELRTkelESRLELEQATRARLEVQVNRHKEA 1990
Cdd:pfam10174  588 -LREVENEKNDKDKKIAELESLTLrqmkeqnkKVANIKHGQQEMKKKGAQLLE---EARRREDNLADNSQQLQLEELMGA 663
                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 116008016  1991 LEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEfhavssreqesltRRKDLEKKVE 2048
Cdd:pfam10174  664 LEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAE-------------RRKQLEEILE 708
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1454-2059 1.83e-10

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: 66.20  E-value: 1.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1454 LEKELGDQTNKVKNLQETTEKLEMELicakSDLNgiseDEDAENEDgvgggvyklKYERVARELEFTKRRLHTqhehDLE 1533
Cdd:TIGR04523   59 LDKNLNKDEEKINNSNNKIKILEQQI----KDLN----DKLKKNKD---------KINKLNSDLSKINSEIKN----DKE 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1534 QLVALKKHLEmKLSDAYEEVVE-QRQVVGQWKRKAQ---KMTNEMNDLRMLLEEqnarnnlLEKKQRKFDAECQSLQ--- 1606
Cdd:TIGR04523  118 QKNKLEVELN-KLEKQKKENKKnIDKFLTEIKKKEKeleKLNNKYNDLKKQKEE-------LENELNLLEKEKLNIQkni 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1607 DAVRQERQAKE-------RYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKN 1679
Cdd:TIGR04523  190 DKIKNKLLKLElllsnlkKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN------TQTQLNQLKDEQN 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1680 ETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEArreSQQRDEELEEVRGNGYKKIKALECQLETEHEERTLL 1759
Cdd:TIGR04523  264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK---EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1760 LREKHELERRLSSME-DRDRVDRDAEEALNQ--KLRRDLRKYKALLKDAQTQLERLKADTPG-KTLIRQLRNQLEDAESA 1835
Cdd:TIGR04523  341 NEQISQLKKELTNSEsENSEKQRELEEKQNEieKLKKENQSYKQEIKNLESQINDLESKIQNqEKLNQQKDEQIKKLQQE 420
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1836 RSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQL--NTEQINV 1913
Cdd:TIGR04523  421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELksKEKELKK 500
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1914 SEAEFKlnEMEAERNNLKEQVAELQHRLDNVENLgdpsmammSKRLELRTKELESRLEL--EQATRARLEVQVNRHKEAL 1991
Cdd:TIGR04523  501 LNEEKK--ELEEKVKDLTKKISSLKEKIEKLESE--------KKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEI 570
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116008016  1992 EKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEfhaVSSREQ--ESLTRR-KDLEKKVEQMESEGAALKN 2059
Cdd:TIGR04523  571 EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE---IEEKEKkiSSLEKElEKAKKENEKLSSIIKNIKS 638
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1384-1883 4.20e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 65.06  E-value: 4.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1384 TEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELtvdlaEERSTAHIATERLEAETAERLKLEKElgDQTN 1463
Cdd:PRK02224  249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL-----EEERDDLLAEAGLDDADAEAVEARRE--ELED 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1464 KVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGggvYKLKYERVARELEFTKRRLHTQHehdlEQLVALKKHLE 1543
Cdd:PRK02224  322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE---LREEAAELESELEEAREAVEDRR----EEIEELEEEIE 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1544 mKLSDAYEEVVEQRqvvGQWKRKAQKMTNEMNDLRMLLEE-----QNARNNlLEKKQRKFDA----EC-QSLQDAVRQER 1613
Cdd:PRK02224  395 -ELRERFGDAPVDL---GNAEDFLEELREERDELREREAEleatlRTARER-VEEAEALLEAgkcpECgQPVEGSPHVET 469
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1614 QAKERYGREKdvlqaekftLEQTLADTRLDLEFKEEKLASLQrELEEmtfgggTEEEFAQLRRSKNETERRAKEQEEELD 1693
Cdd:PRK02224  470 IEEDRERVEE---------LEAELEDLEEEVEEVEERLERAE-DLVE------AEDRIERLEERREDLEELIAERRETIE 533
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1694 EMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVrgngykkiKALECQLETEHEERTLLLRekheLERRLSSM 1773
Cdd:PRK02224  534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV--------AELNSKLAELKERIESLER----IRTLLAAI 601
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1774 ED-RDRVDRDAEEALNQKLRRDLRKykallkdaqtqlERLKADtpgKTLIRQLRNQLEDA--ESARSlamkARQTAEAEL 1850
Cdd:PRK02224  602 ADaEDEIERLREKREALAELNDERR------------ERLAEK---RERKRELEAEFDEAriEEARE----DKERAEEYL 662
                         490       500       510
                  ....*....|....*....|....*....|...
gi 116008016 1851 TEVQAMFDESHRARNDAEERANAAHRDRAELQA 1883
Cdd:PRK02224  663 EQVEEKLDELREERDDLQAEIGAVENELEELEE 695
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
1577-2053 8.01e-10

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 63.76  E-value: 8.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1577 LRMLLEE-QNARNNLLekkqRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQ 1655
Cdd:pfam07888   32 LQNRLEEcLQERAELL----QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1656 RELEEMTfgggteEEFAQLRRSKNETERRAKEQEEEldemagqIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVr 1735
Cdd:pfam07888  108 ASSEELS------EEKDALLAQRAAHEARIRELEED-------IKTLTQRVLERETELERMKERAKKAGAQRKEEEAER- 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1736 gngykkiKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKykallkdaQTQLERLKAD 1815
Cdd:pfam07888  174 -------KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRK--------EAENEALLEE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1816 tpgktlIRQLRNQLEDAEsarslamkarQTAEAELTEVQAMfdESHRARNDAEeranaAHRDRAELqAQIEENEEELGEL 1895
Cdd:pfam07888  239 ------LRSLQERLNASE----------RKVEGLGEELSSM--AAQRDRTQAE-----LHQARLQA-AQLTLQLADASLA 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1896 MKKYSATVKQlnteqinvsEAEFKLNEMEAERNNLKEQVAELQhrldnvenlgdpsmammskrlelrtkELESRLELEQA 1975
Cdd:pfam07888  295 LREGRARWAQ---------ERETLQQSAEADKDRIEKLSAELQ--------------------------RLEERLQEERM 339
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116008016  1976 TRARLEVQVNRHKEAlEKLQNEVTQSKMREMQAqdvikksqkSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESE 2053
Cdd:pfam07888  340 EREKLEVELGREKDC-NRVQLSESRRELQELKA---------SLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
1382-1850 9.79e-10

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: 64.22  E-value: 9.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1382 HRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEA---KLSELTVDLAEERSTAHIATERLEAETAERLKL---E 1455
Cdd:TIGR00618  351 HSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTltqKLQSLCKELDILQREQATIDTRTSAFRDLQGQLahaK 430
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1456 KELGDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLKYERVARELEFTKRRLHTQHEHDLEQL 1535
Cdd:TIGR00618  431 KQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSC 510
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1536 ValkkHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQ--------- 1606
Cdd:TIGR00618  511 I----HPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQcdnrskedi 586
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1607 DAVRQERQAKERYGREKD--------VLQAEKFTLEQTLADTRLDLE---FKEE---KLASLQRELEEMTFgggtEEEFA 1672
Cdd:TIGR00618  587 PNLQNITVRLQDLTEKLSeaedmlacEQHALLRKLQPEQDLQDVRLHlqqCSQElalKLTALHALQLTLTQ----ERVRE 662
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1673 QLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARREsQQRDEELEEVRGNGYKKIKALECQLETE 1752
Cdd:TIGR00618  663 HALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHI-EEYDREFNEIENASSSLGSDLAAREDAL 741
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1753 HEertLLLREKHELERRLSSMEDRDRVDRDAEEALNQKlrrdLRKYKALLKDAQTQLERLKADTPG-KTLIRQLRNQLED 1831
Cdd:TIGR00618  742 NQ---SLKELMHQARTVLKARTEAHFNNNEEVTAALQT----GAELSHLAAEIQFFNRLREEDTHLlKTLEAEIGQEIPS 814
                          490
                   ....*....|....*....
gi 116008016  1832 AESARSLAMKARQTAEAEL 1850
Cdd:TIGR00618  815 DEDILNLQCETLVQEEEQF 833
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1668-2117 1.08e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 63.91  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1668 EEEFAQLRRSKNETERRAKEQEEELDEMAGQiqlLEQAKLRLEMTLETMrkEARRESQQRDEELEEvrgngykKIKALEC 1747
Cdd:PRK02224  198 EKEEKDLHERLNGLESELAELDEEIERYEEQ---REQARETRDEADEVL--EEHEERREELETLEA-------EIEDLRE 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1748 QLETEHEERTLLLREKHELERRLSSMEDRdrvdrdaeealnqklRRDLRkykallkdAQTQLERLKADTpgktlIRQLRN 1827
Cdd:PRK02224  266 TIAETEREREELAEEVRDLRERLEELEEE---------------RDDLL--------AEAGLDDADAEA-----VEARRE 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1828 QLEDAESArslamkARQTAEAELTEVQAMFDESHRARNDA---EERANAAHRDRAELQAQIEENEEELGELMKKYSATVK 1904
Cdd:PRK02224  318 ELEDRDEE------LRDRLEECRVAAQAHNEEAESLREDAddlEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1905 QLNTEQ-------INVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVEN--------------------LGDPSMAMMSK 1957
Cdd:PRK02224  392 EIEELRerfgdapVDLGNAEDFLEELREERDELREREAELEATLRTARErveeaealleagkcpecgqpVEGSPHVETIE 471
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1958 RLELRTKELESRLELEQATRARLEVQVNRhKEALEKLQNEVTQSKMREmqaqdviKKSQKSLRDMREEFHAVSSREQESL 2037
Cdd:PRK02224  472 EDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERR-------EDLEELIAERRETIEEKRERAEELR 543
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 2038 TRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAMEEEGEEELSESDESLSSVgSISDLEDRLRPVHVKRSSQQSLN 2117
Cdd:PRK02224  544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERLREKREALAELN 622
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
1383-2005 1.58e-09

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: 63.30  E-value: 1.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1383 RTEEQLKTANEELLMLRAKLEKIECdrsevKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKEL---- 1458
Cdd:pfam10174  145 RIETQKQTLGARDESIKKLLEMLQS-----KGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELhrrn 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1459 --GDQTNKVKNLQETtekLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLKYERVARELE-------FTKRRLHtQHE 1529
Cdd:pfam10174  220 qlQPDPAKTKALQTV---IEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEvykshskFMKNKID-QLK 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1530 HDLE----QLVALKKHLEM---KLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNArnnLLEKKQRKfdaec 1602
Cdd:pfam10174  296 QELSkkesELLALQTKLETltnQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKES---FLNKKTKQ----- 367
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1603 qsLQDavrqerqakerygrekdvLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETE 1682
Cdd:pfam10174  368 --LQD------------------LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENL------QEQLRDKDKQLAGLK 421
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1683 RRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRgngyKKIKALECQLETEH----EERTL 1758
Cdd:pfam10174  422 ERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLK----KENKDLKEKVSALQpeltEKESS 497
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1759 LLREKHELERRLSSMEDRDRVDRDAEEALNQKlRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLrnqleDAESARSL 1838
Cdd:pfam10174  498 LIDLKEHASSLASSGLKKDSKLKSLEIAVEQK-KEECSKLENQLKKAHNAEEAVRTNPEINDRIRLL-----EQEVARYK 571
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1839 AMKARQTAEAE-----LTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIeeneEELGELMKKYSATVKQL---NTEQ 1910
Cdd:pfam10174  572 EESGKAQAEVErllgiLREVENEKNDKDKKIAELESLTLRQMKEQNKKVANI----KHGQQEMKKKGAQLLEEarrREDN 647
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1911 INVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRTKELESRLELEQ-----------ATRAR 1979
Cdd:pfam10174  648 LADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQeallaaisekdANIAL 727
                          650       660
                   ....*....|....*....|....*.
gi 116008016  1980 LEVQVNRHKealeKLQNEVTQSKmRE 2005
Cdd:pfam10174  728 LELSSSKKK----KTQEEVMALK-RE 748
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1382-2063 1.78e-09

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: 63.45  E-value: 1.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1382 HRTEEQLKTANEELLMLRAKLEKIE-------CDRSEVKAENQKLEAKLSELTVDLAEERS-------TAHIATERLEAE 1447
Cdd:pfam02463  240 DLLQELLRDEQEEIESSKQEIEKEEeklaqvlKENKEEEKEKKLQEEELKLLAKEEEELKSellklerRKVDDEEKLKES 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1448 TAERLKLEKELgdqtnkvKNLQETTEKLEMElicaKSDLNGISEDEDAENEDgvgggvyklkYERVARELEFTKRRLHTQ 1527
Cdd:pfam02463  320 EKEKKKAEKEL-------KKEKEEIEELEKE----LKELEIKREAEEEEEEE----------LEKLQEKLEQLEEELLAK 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1528 HEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKqrkfDAECQSLQD 1607
Cdd:pfam02463  379 KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGK----LTEEKEELE 454
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1608 AVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEM-------------------TFGGGTE 1668
Cdd:pfam02463  455 KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGlkvllalikdgvggriisaHGRLGDL 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1669 EEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELE-EVRGNGYKKIKALEC 1747
Cdd:pfam02463  535 GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEiDPILNLAQLDKATLE 614
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1748 QLETEHEERTLLLREKHELE----RRLSSMEDRDRVDRDAEEALNQKLRR----DLRKYKALLKDAQTQLERLKADTPgK 1819
Cdd:pfam02463  615 ADEDDKRAKVVEGILKDTELtklkESAKAKESGLRKGVSLEEGLAEKSEVkaslSELTKELLEIQELQEKAESELAKE-E 693
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1820 TLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDES--HRARNDAEERANAAHRDRAELQAQIEENEEELGELMK 1897
Cdd:pfam02463  694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKIneELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1898 KYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQV---AELQHRLDNVENLgdpsmamMSKRLELRTKELESRLELEQ 1974
Cdd:pfam02463  774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELkeeAELLEEEQLLIEQ-------EEKIKEEELEELALELKEEQ 846
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1975 ATRARLEVQVNRHKE-ALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESE 2053
Cdd:pfam02463  847 KLEKLAEEELERLEEeITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
                          730
                   ....*....|
gi 116008016  2054 GAALKNDLRL 2063
Cdd:pfam02463  927 AEILLKYEEE 936
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1622-1857 2.69e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 62.63  E-value: 2.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1622 EKDVLQAEKFTLEQ--TLADTRLDLEFKEEKLASLQRELEemtfgggTEEEFAQLRRSKNETER-----RAKEQEEELDE 1694
Cdd:COG4913   220 EPDTFEAADALVEHfdDLERAHEALEDAREQIELLEPIRE-------LAERYAAARERLAELEYlraalRLWFAQRRLEL 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1695 MAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSME 1774
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALG 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1775 DRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKAD-TPGKTLIRQLRNQLEDAESARS------LAMKARQTAE 1847
Cdd:COG4913   373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAlRDLRRELRELEAEIASLERRKSniparlLALRDALAEA 452
                         250
                  ....*....|
gi 116008016 1848 AELTEVQAMF 1857
Cdd:COG4913   453 LGLDEAELPF 462
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
1624-2035 2.87e-09

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 62.01  E-value: 2.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1624 DVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTfggGTEEEFAQLRRSKN---ETERRAKEQE----------E 1690
Cdd:pfam05622   69 EQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEELT---SLAEEAQALKDEMDilrESSDKVKKLEatvetykkklE 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1691 ELDEMAGQIQLLE-------QAKLRLE----------MTLETMRKEARRESQQRDEELeevrgngyKKIKALECQLETEH 1753
Cdd:pfam05622  146 DLGDLRRQVKLLEernaeymQRTLQLEeelkkanalrGQLETYKRQVQELHGKLSEES--------KKADKLEFEYKKLE 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1754 EERTLLLREKhelerrlssmeDRDRVDRDAEEALNQKLR------RDLRKYKALLKDAQTQLERLKADT-PGKTLIRQLR 1826
Cdd:pfam05622  218 EKLEALQKEK-----------ERLIIERDTLRETNEELRcaqlqqAELSQADALLSPSSDPGDNLAAEImPAEIREKLIR 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1827 NQLEDaesaRSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKY--SATVK 1904
Cdd:pfam05622  287 LQHEN----KMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAedSSLLK 362
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1905 QLNTEQINvseaefKLNEMEAERNNLKEQVAELQHRLDNvenlgdpSMAMMSKRLE--LRTKELESRleleqATRARLEV 1982
Cdd:pfam05622  363 QKLEEHLE------KLHEAQSELQKKKEQIEELEPKQDS-------NLAQKIDELQeaLRKKDEDMK-----AMEERYKK 424
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116008016  1983 QVNRHKEALEKLQNEVTQSKMREMQAQDV-IKKSQKSLRDMREEFHAVSS-REQE 2035
Cdd:pfam05622  425 YVEKAKSVIKTLDPKQNPASPPEIQALKNqLLEKDKKIEHLERDFEKSKLqREQE 479
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1383-1731 3.13e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.39  E-value: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1383 RTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERS------------TAHIATERLEAETAE 1450
Cdd:PRK03918  381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEEHRKELLEEYTAE 460
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1451 RLKLEKELGDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLKYERVARELEFTKRRLHTQH-- 1528
Cdd:PRK03918  461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKge 540
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1529 ----EHDLEQLVALKKH---LEMKLSDAYEEVVEqrqVVGQWKRKAQKMtnemndlrmlLEEQNARNNLLEKKQRKFdae 1601
Cdd:PRK03918  541 ikslKKELEKLEELKKKlaeLEKKLDELEEELAE---LLKELEELGFES----------VEELEERLKELEPFYNEY--- 604
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1602 cQSLQDAVRQERQAKERYGREKDVLQAEkftlEQTLADTRLDLEFKEEKLASLQRELEEMTFGG-------------GTE 1668
Cdd:PRK03918  605 -LELKDAEKELEREEKELKKLEEELDKA----FEELAETEKRLEELRKELEELEKKYSEEEYEElreeylelsrelaGLR 679
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 1669 EEFAQLRRSKNETERRAKEQEEELDEM---AGQIQLLEQAKLRLEMTLETMRK---EARRESQQRDEEL 1731
Cdd:PRK03918  680 AELEELEKRREEIKKTLEKLKEELEERekaKKELEKLEKALERVEELREKVKKykaLLKERALSKVGEI 748
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1383-1812 3.23e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 62.09  E-value: 3.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1383 RTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIAT-----ERLEAETAERLKLEKE 1457
Cdd:COG4717    85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElperlEELEERLEELRELEEE 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1458 LGDQTNKVKNLQEtteklEMELICAKSDLNGISEDEDAENEdgvgggvyklkYERVARELEFTKRRLHTQHEHDLEQLVA 1537
Cdd:COG4717   165 LEELEAELAELQE-----ELEELLEQLSLATEEELQDLAEE-----------LEELQQRLAELEEELEEAQEELEELEEE 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1538 LKKHLEMKLSDAYEEVVEQRQ-----------VVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQ 1606
Cdd:COG4717   229 LEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1607 DAVRQER-------QAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEE-----KLASLQRELEEM--TFGGGTEEEFa 1672
Cdd:COG4717   309 ALPALEEleeeeleELLAALGLPPDLSPEELLELLDRIEELQELLREAEEleeelQLEELEQEIAALlaEAGVEDEEEL- 387
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1673 qlrRSKNETERRAKEQEEELDEMAGQI-QLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLET 1751
Cdd:COG4717   388 ---RAALEQAEEYQELKEELEELEEQLeELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 1752 EHEERTL--LLREKHELERRLSSMEDRDRVDRDAEEALnQKLRRDLRKYK--ALLKDAQTQLERL 1812
Cdd:COG4717   465 LEEDGELaeLLQELEELKAELRELAEEWAALKLALELL-EEAREEYREERlpPVLERASEYFSRL 528
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1397-1852 3.74e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 62.09  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1397 MLRAKLEKIEcdRSEVKAENQKLEAKLSELTvDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVKNLQETTEKLE 1476
Cdd:COG4717    46 MLLERLEKEA--DELFKPQGRKPELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1477 MelicAKSDLNGISEDEDAENEdgvgggvyklkYERVARELEFTKRRLHtQHEHDLEQLVALKKHLEMKlsdayeevveQ 1556
Cdd:COG4717   123 K----LLQLLPLYQELEALEAE-----------LAELPERLEELEERLE-ELRELEEELEELEAELAEL----------Q 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1557 RQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLeqt 1636
Cdd:COG4717   177 EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL--- 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1637 LADTRLDLEFKEEKLASLQRELEEMTF--GGGTEEEFAQLRRSKNETERRAKE----------QEEELDEMAGQIQLLEQ 1704
Cdd:COG4717   254 IAAALLALLGLGGSLLSLILTIAGVLFlvLGLLALLFLLLAREKASLGKEAEElqalpaleelEEEELEELLAALGLPPD 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1705 AKLRLEMTLETMRKEARRESQQRDEELEEVRGNGY-KKIKAL--ECQLETEHE--ERTLLLREKHELERRLSSMEDR-DR 1778
Cdd:COG4717   334 LSPEELLELLDRIEELQELLREAEELEEELQLEELeQEIAALlaEAGVEDEEElrAALEQAEEYQELKEELEELEEQlEE 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1779 VDRDAEEALNQ----KLRRDLRKYKALLKDAQTQLERLKADtpgktlIRQLRNQLEDAESARSL--AMKARQTAEAELTE 1852
Cdd:COG4717   414 LLGELEELLEAldeeELEEELEELEEELEELEEELEELREE------LAELEAELEQLEEDGELaeLLQELEELKAELRE 487
mukB PRK04863
chromosome partition protein MukB;
1647-2025 4.07e-09

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 62.28  E-value: 4.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1647 KEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETErRAKEQEEELdeMAGQIQLLEQAKLRLEMtletmrKEARRESQQ 1726
Cdd:PRK04863  784 REKRIEQLRAEREEL------AERYATLSFDVQKLQ-RLHQAFSRF--IGSHLAVAFEADPEAEL------RQLNRRRVE 848
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1727 RDEELEEVRGN------GYKKIKALeCQLETEHEERTLLLREKHELERrlsSMEDRDRVDRdAEEAlnqklRRDLRKYKA 1800
Cdd:PRK04863  849 LERALADHESQeqqqrsQLEQAKEG-LSALNRLLPRLNLLADETLADR---VEEIREQLDE-AEEA-----KRFVQQHGN 918
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1801 LLKDAQTQLERLKADtPGKtlIRQLRNQLEDAESARSLAmKARQTAEAELTEVQAmfdesHRARNDAEERANAAhrdrAE 1880
Cdd:PRK04863  919 ALAQLEPIVSVLQSD-PEQ--FEQLKQDYQQAQQTQRDA-KQQAFALTEVVQRRA-----HFSYEDAAEMLAKN----SD 985
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1881 LQAQIEENEEELGELMKKYSatvKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDnveNLGDPSMAMMSKRLE 1960
Cdd:PRK04863  986 LNEKLRQRLEQAEQERTRAR---EQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQ---DLGVPADSGAEERAR 1059
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 1961 LRTKELESRLeleQATRARlevqvnrhKEALEKlQNEVTQSKMREMQAQdvIKKSQKSLRDMREE 2025
Cdd:PRK04863 1060 ARRDELHARL---SANRSR--------RNQLEK-QLTFCEAEMDNLTKK--LRKLERDYHEMREQ 1110
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1564-1885 4.52e-09

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: 61.68  E-value: 4.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1564 KRKAQKMT-NE-MNDLRMLLEEQNARNNllEKKQRKFDaecQSLQDAVRQERQAKER-YGREKDVLQAEKftLEQTLADT 1640
Cdd:pfam17380  259 RYNGQTMTeNEfLNQLLHIVQHQKAVSE--RQQQEKFE---KMEQERLRQEKEEKAReVERRRKLEEAEK--ARQAEMDR 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1641 RLDLEFKEEKLAsLQRELEemtfgggteeefaqLRRSKNETERRAKEQ--EEELDEMAGQIQLLEQAKLRLEMTLETMRK 1718
Cdd:pfam17380  332 QAAIYAEQERMA-MERERE--------------LERIRQEERKRELERirQEEIAMEISRMRELERLQMERQQKNERVRQ 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1719 EARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLssmedrDRVdRDAEEALNQKLRRdLRKY 1798
Cdd:pfam17380  397 ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM------ERV-RLEEQERQQQVER-LRQQ 468
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1799 KALLKDAQTQLERLKADtpgKTLIRQLRNQ-LEDAESARSLAM----KARQTAEAELTEVQ-AMFDESHRARNDAEERAN 1872
Cdd:pfam17380  469 EEERKRKKLELEKEKRD---RKRAEEQRRKiLEKELEERKQAMieeeRKRKLLEKEMEERQkAIYEEERRREAEEERRKQ 545
                          330
                   ....*....|...
gi 116008016  1873 AAHRDRAELQAQI 1885
Cdd:pfam17380  546 QEMEERRRIQEQM 558
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
1584-2070 5.43e-09

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 61.89  E-value: 5.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1584 QNARNNLLEkkqRKFDAEcQSLQDAVRQ---ERQAKERYGREKDVLQAEKFTLEQTL--ADTRLDLEF----KEEKLASL 1654
Cdd:COG3096   277 ANERRELSE---RALELR-RELFGARRQlaeEQYRLVEMARELEELSARESDLEQDYqaASDHLNLVQtalrQQEKIERY 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1655 QRELEEMTFGggTEEE---FAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAklrLEMtLETmRKEARRESQQRDEEL 1731
Cdd:COG3096   353 QEDLEELTER--LEEQeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQA---LDV-QQT-RAIQYQQAVQALEKA 425
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1732 EEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSsmedrdrvdrDAEEALNQklrrdLRKYKALLKDAQTQLER 1811
Cdd:COG3096   426 RALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLS----------VADAARRQ-----FEKAYELVCKIAGEVER 490
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1812 LKADTPGKTLIRQLRNQledaesaRSLAMKArQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQaqieeneee 1891
Cdd:COG3096   491 SQAWQTARELLRRYRSQ-------QALAQRL-QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE--------- 553
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1892 lgelmkkysatvkQLNTEQinvSEAEFKLNEMEAERNNLKEQVAELQHRLDNVEnlgdpsmammSKRLELRTKELesrle 1971
Cdd:COG3096   554 -------------ELEELL---AELEAQLEELEEQAAEAVEQRSELRQQLEQLR----------ARIKELAARAP----- 602
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1972 leqatrARLEVQvnrhkEALEKLQNEVTQSKmreMQAQDVIKKSQKSLRDMREefhaVSSREQESLTRRKDLEKKVEQME 2051
Cdd:COG3096   603 ------AWLAAQ-----DALERLREQSGEAL---ADSQEVTAAMQQLLERERE----ATVERDELAARKQALESQIERLS 664
                         490
                  ....*....|....*....
gi 116008016 2052 SEGAAlkNDLRlaLQRIAD 2070
Cdd:COG3096   665 QPGGA--EDPR--LLALAE 679
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1647-1885 5.93e-09

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: 60.55  E-value: 5.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1647 KEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQaklrlemtletmrkearrESQQ 1726
Cdd:COG4942    25 AEAELEQLQQEIAE------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ------------------ELAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1727 RDEELEEVRgngyKKIKALECQLEteheertlllREKHELERRLSSMEDRDRVDRDAE----EALNQKLRRdLRKYKALL 1802
Cdd:COG4942    81 LEAELAELE----KEIAELRAELE----------AQKEELAELLRALYRLGRQPPLALllspEDFLDAVRR-LQYLKYLA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1803 KDAQTQLERLKADTPG-KTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAEL 1881
Cdd:COG4942   146 PARREQAEELRADLAElAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225

                  ....
gi 116008016 1882 QAQI 1885
Cdd:COG4942   226 EALI 229
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
1383-1947 8.69e-09

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 61.01  E-value: 8.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1383 RTEEQLKTANEELLMLRAKL-EKIECDRSEVKAENQKLEAKLSELtvDLAEER---------STAHIATERLEAETAERL 1452
Cdd:pfam12128  280 ERQETSAELNQLLRTLDDQWkEKRDELNGELSAADAAVAKDRSEL--EALEDQhgafldadiETAAADQEQLPSWQSELE 357
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1453 KLEKELGDQTNKVKNLQETTEKLEMELICA-KSDLNGISEDEDAENEdgvgggvyklkyervarelefTKRRLHTQHEHD 1531
Cdd:pfam12128  358 NLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIRE---------------------ARDRQLAVAEDD 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1532 LEQL-VALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEmNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVR 1610
Cdd:pfam12128  417 LQALeSELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAANAEVERLQSELR 495
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1611 QER----QAKERYGREKDVLQAEKFTLEQT-----------LADTRLDLEFKEEKLASL-QREL---------------- 1658
Cdd:pfam12128  496 QARkrrdQASEALRQASRRLEERQSALDELelqlfpqagtlLHFLRKEAPDWEQSIGKViSPELlhrtdldpevwdgsvg 575
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1659 EEMTFGGGT------------------EEEFAQLRRSKNETERRAKEQEEELDEMAGQI-----------QLLEQAKLRL 1709
Cdd:pfam12128  576 GELNLYGVKldlkridvpewaaseeelRERLDKAEEALQSAREKQAAAEEQLVQANGELekasreetfarTALKNARLDL 655
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1710 EMTLETMRKEARRESQQRDEEL----EEVRG-NGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDrvdrDAE 1784
Cdd:pfam12128  656 RRLFDEKQSEKDKKNKALAERKdsanERLNSlEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALD----AQL 731
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1785 EALNQKLRRDLRKYKALLKDAQTQLER-LKADTPGKTLIRQLRNQLEDAEsaRSLAMKARQtaEAELTEVQAMFDESHRA 1863
Cdd:pfam12128  732 ALLKAAIAARRSGAKAELKALETWYKRdLASLGVDPDVIAKLKREIRTLE--RKIERIAVR--RQEVLRYFDWYQETWLQ 807
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1864 RNDA-EERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQ--VAELQ-- 1938
Cdd:pfam12128  808 RRPRlATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDanSEQAQgs 887
                          650
                   ....*....|.
gi 116008016  1939 --HRLDNVENL 1947
Cdd:pfam12128  888 igERLAQLEDL 898
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1574-1752 9.60e-09

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: 58.01  E-value: 9.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1574 MNDLRMLLEEQN--ARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKL 1651
Cdd:COG1579     3 PEDLRALLDLQEldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1652 ASL--QRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDE 1729
Cdd:COG1579    83 GNVrnNKEYEAL------QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
                         170       180
                  ....*....|....*....|...
gi 116008016 1730 ELEEVRgngyKKIKALECQLETE 1752
Cdd:COG1579   157 ELEELE----AEREELAAKIPPE 175
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1593-1835 2.02e-08

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: 58.62  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1593 KKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELeemtfgggteeefA 1672
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------------A 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1673 QLRRSKNETERRAKEQEEELDEMAGQIQLL-EQAKLRLEMTLETMRKEARRE------SQQRDEELEEVRGNgYKKIKAL 1745
Cdd:COG4942    87 ELEKEIAELRAELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRRLqylkylAPARREQAEELRAD-LAELAAL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1746 ECQLETEHEERTLLLREKHELERRLSSmedrdrvDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKAdtpgktLIRQL 1825
Cdd:COG4942   166 RAELEAERAELEALLAELEEERAALEA-------LKAERQKLLARLEKELAELAAELAELQQEAEELEA------LIARL 232
                         250
                  ....*....|
gi 116008016 1826 RNQLEDAESA 1835
Cdd:COG4942   233 EAEAAAAAER 242
PTZ00121 PTZ00121
MAEBL; Provisional
1380-1767 2.08e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.15  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1380 NVHRTEEQLKTANEelLMLRAKlEKIECDRSEVKAENQKleaKLSELTVDLAEERSTAHIATERLEAETAERLKL--EKE 1457
Cdd:PTZ00121 1461 EAKKKAEEAKKADE--AKKKAE-EAKKADEAKKKAEEAK---KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKaeEAK 1534
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1458 LGDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGggvykLKYERVARELEFTKRRLHTQHEHDLEQLVA 1537
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA-----LRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1538 --LKKHLEMKL-SDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQ 1614
Cdd:PTZ00121 1610 eeAKKAEEAKIkAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1615 AKERYGREKDvlqaEKFTLEQTladtRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAkeqeEELDE 1694
Cdd:PTZ00121 1690 AAEALKKEAE----EAKKAEEL----KKKEAEEKKKAEELKKAEEE------NKIKAEEAKKEAEEDKKKA----EEAKK 1751
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1695 MAGQIQLLEQAKLRLEMTLETMRKEARRESQQR-DEELEEVRGNGYKKIKALECQLETEHE---ERTLLLREKHELE 1767
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEElDEEDEKRRMEVDKKIKDIFDNFANIIEggkEGNLVINDSKEME 1828
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1405-1877 2.32e-08

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: 59.60  E-value: 2.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1405 IECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKV------KNLQETTEKLEME 1478
Cdd:pfam02463  560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKrakvveGILKDTELTKLKE 639
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1479 LICAKSD--LNGISEDEDAENEDGVGGGVYKLKYERVARELEFTKRRLHTQHEHDLEQLVALKKhLEMKLSDAYEEVVEQ 1556
Cdd:pfam02463  640 SAKAKESglRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK-KEQREKEELKKLKLE 718
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1557 RQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQT 1636
Cdd:pfam02463  719 AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKA 798
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1637 LADTRLDLEFKEEKLASLQRELEEMTFG--GGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLE 1714
Cdd:pfam02463  799 QEEELRALEEELKEEAELLEEEQLLIEQeeKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEE 878
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1715 TMRKEARRESQQRDEELEEVRgNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRD 1794
Cdd:pfam02463  879 LEEQKLKDELESKEEKEKEEK-KELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEE 957
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1795 LRKYKALLKDAQTQLERLKadtpgktlIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAA 1874
Cdd:pfam02463  958 EEERNKRLLLAKEELGKVN--------LMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSI 1029

                   ...
gi 116008016  1875 HRD 1877
Cdd:pfam02463 1030 NKG 1032
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
1648-2104 2.80e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 59.28  E-value: 2.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1648 EEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEmagqIQLLEQAKLRLEMTL---ETMRKEARRES 1724
Cdd:PRK02224  212 ESELAELDEEIERY------EEQREQARETRDEADEVLEEHEERREE----LETLEAEIEDLRETIaetEREREELAEEV 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1725 QQRDEELEEVRgngyKKIKAL--ECQLETEHEERTLLLREkhELERRLSSMEDRDRVDR-DAEEALNQ--KLRRDLRKYK 1799
Cdd:PRK02224  282 RDLRERLEELE----EERDDLlaEAGLDDADAEAVEARRE--ELEDRDEELRDRLEECRvAAQAHNEEaeSLREDADDLE 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1800 ALLKDAQTQLERLKADtpgktlIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRA 1879
Cdd:PRK02224  356 ERAEELREEAAELESE------LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1880 ELQAQIEENEEELGELMKKYSA----TVKQLNTEQINV---SEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLgdPSM 1952
Cdd:PRK02224  430 ELEATLRTARERVEEAEALLEAgkcpECGQPVEGSPHVetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDL--VEA 507
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1953 AMMSKRLELRTKELESRLEL------------------------------EQATRARLEVQVNRH------------KEA 1990
Cdd:PRK02224  508 EDRIERLEERREDLEELIAErretieekreraeelreraaeleaeaeekrEAAAEAEEEAEEAREevaelnsklaelKER 587
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1991 LEKLQNEVTQSKMREMQAQDVikksqKSLRDMREEFHAVSSREQESL----TRRKDLEKKVEQMESEGAalkndlRLALQ 2066
Cdd:PRK02224  588 IESLERIRTLLAAIADAEDEI-----ERLREKREALAELNDERRERLaekrERKRELEAEFDEARIEEA------REDKE 656
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 116008016 2067 RIADLQQAMEEEGEEELSESDESLSSVGSISDLEDRLR 2104
Cdd:PRK02224  657 RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1510-2075 3.72e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 59.16  E-value: 3.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1510 YERVARELEFTKRRLHTqhehdLEQLVALKKHLEmKLSDAYEEVVEQRQVVGQWK--RKAQKMTNEMNDLRMLLEEQNAR 1587
Cdd:COG4913   237 LERAHEALEDAREQIEL-----LEPIRELAERYA-AARERLAELEYLRAALRLWFaqRRLELLEAELEELRAELARLEAE 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1588 NNLLEKKQRKFDAECQSLQDAVRQ-ERQAKERYGREKDVLQAEKFT-------LEQTLADTRLDLEFKEEKLASLQRELE 1659
Cdd:COG4913   311 LERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEErerrrarLEALLAALGLPLPASAEEFAALRAEAA 390
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1660 EmtFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDE------ELEE 1733
Cdd:COG4913   391 A--LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAelpfvgELIE 468
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1734 VRG----------------------------------NGYK--------KIKALECQLETEHEERTLLLRE--------- 1762
Cdd:COG4913   469 VRPeeerwrgaiervlggfaltllvppehyaaalrwvNRLHlrgrlvyeRVRTGLPDPERPRLDPDSLAGKldfkphpfr 548
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1763 ---KHELERRLS------------------------------SMEDRDRVDR------DAEEALN------QKLRRDLRK 1797
Cdd:COG4913   549 awlEAELGRRFDyvcvdspeelrrhpraitragqvkgngtrhEKDDRRRIRSryvlgfDNRAKLAaleaelAELEEELAE 628
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1798 YKALLKDAQTQLERLKADtpgKTLIRQLRNQLEDAESARSLAMKARQTAE---------AELTEVQAMFDESHRARNDAE 1868
Cdd:COG4913   629 AEERLEALEAELDALQER---REALQRLAEYSWDEIDVASAEREIAELEAelerldassDDLAALEEQLEELEAELEELE 705
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1869 ERANAAHRDRAELQAQIeeneeelgelmkkysatvkqlnteqinvseaefklnemeaerNNLKEQVAELQHRLDNVENLG 1948
Cdd:COG4913   706 EELDELKGEIGRLEKEL------------------------------------------EQAEEELDELQDRLEAAEDLA 743
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1949 DPSMAmmsKRLELRTKELESRlELEQATRARLEVQVNRHKEALEKLQNEVTQsKMREMQAQ--DVIKKSQKSLRDmREEF 2026
Cdd:COG4913   744 RLELR---ALLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELER-AMRAFNREwpAETADLDADLES-LPEY 817
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016 2027 HAVSSR-EQESLTRRKD--LEKKVEQMESE----GAALKNDLRLALQRIADLQQAM 2075
Cdd:COG4913   818 LALLDRlEEDGLPEYEErfKELLNENSIEFvadlLSKLRRAIREIKERIDPLNDSL 873
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1802-2032 4.52e-08

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: 57.47  E-value: 4.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1802 LKDAQTQLERLKADtpgktlIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAEL 1881
Cdd:COG4942    22 AAEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1882 QAQIEENEEELGELMKKYSATVKQ------LNTEqiNVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLgdpsmamm 1955
Cdd:COG4942    96 RAELEAQKEELAELLRALYRLGRQpplallLSPE--DFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-------- 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1956 SKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSR 2032
Cdd:COG4942   166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
1383-1727 9.83e-08

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 56.61  E-value: 9.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1383 RTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERS-----TAHIAT--ERLEAETAERLKLE 1455
Cdd:pfam19220   59 QERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIelrdkTAQAEAleRQLAAETEQNRALE 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1456 KELGDQTNKVKNLQETTEKLEMELICAKSDLnGISEDEdaenedgvGGGVYKLKYERVARELEFTKRrlHTQHEHDLEQL 1535
Cdd:pfam19220  139 EENKALREEAQAAEKALQRAEGELATARERL-ALLEQE--------NRRLQALSEEQAAELAELTRR--LAELETQLDAT 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1536 VALKKHLEMKLSdayEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQ-ERQ 1614
Cdd:pfam19220  208 RARLRALEGQLA---AEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAaERR 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1615 AKErygrekdvLQAEKFTLEQTLADTRLDLEFKEEKLASLQR---ELEEMTfgggteEEFAQLRRSKNETERRAKEQEEE 1691
Cdd:pfam19220  285 LKE--------ASIERDTLERRLAGLEADLERRTQQFQEMQRaraELEERA------EMLTKALAAKDAALERAEERIAS 350
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 116008016  1692 L-DEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQR 1727
Cdd:pfam19220  351 LsDRIAELTKRFEVERAALEQANRRLKEELQRERAER 387
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1600-1823 1.81e-07

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: 55.93  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1600 AECQSLQDAVRQERQAKERygrEKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKN 1679
Cdd:COG4942    23 AEAEAELEQLQQEIAELEK---ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA------LEAELAELEKEIA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1680 ETERRAKEQEEELDEMAGQIQLLEQAK-----------LRLEMTLETM------RKEARRESQQRDEELEEVRGNGYKKI 1742
Cdd:COG4942    94 ELRAELEAQKEELAELLRALYRLGRQPplalllspedfLDAVRRLQYLkylapaRREQAEELRADLAELAALRAELEAER 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1743 KALECQLETEHEERTLLLREKHELERRLSSMEDRdrvdRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLI 1822
Cdd:COG4942   174 AELEALLAELEEERAALEALKAERQKLLARLEKE----LAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249

                  .
gi 116008016 1823 R 1823
Cdd:COG4942   250 A 250
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1838-2059 1.97e-07

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: 55.54  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1838 LAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAE 1917
Cdd:COG4942    10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1918 FKLNEMEAERNNLKEQVAEL---------QHRLDNVENLGDPS----MAMMSKRLELRTKELESRLELEQATRARLEVQV 1984
Cdd:COG4942    90 KEIAELRAELEAQKEELAELlralyrlgrQPPLALLLSPEDFLdavrRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 1985 NRHKEALEKLQNEVTQSKmREMQAQdvIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKN 2059
Cdd:COG4942   170 EAERAELEALLAELEEER-AALEAL--KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PTZ00121 PTZ00121
MAEBL; Provisional
1379-2077 2.40e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.30  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1379 LNVHRTEEQLKTANEELLMLRAKLEKIECD-----RSEVKAE-NQKLEAKLSELTVDL-AEERSTAHIATERLEAETAER 1451
Cdd:PTZ00121 1024 FNIEKIEELTEYGNNDDVLKEKDIIDEDIDgnhegKAEAKAHvGQDEGLKPSYKDFDFdAKEDNRADEATEEAFGKAEEA 1103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1452 LKLEKELGDQTNKVKNLQETTEKL-EMELICAKSDLNGISEDEDAENEdgvgggvyklKYERVARELEFTKRRLHTQHEH 1530
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDArKAEEARKAEDARKAEEARKAEDA----------KRVEIARKAEDARKAEEARKAE 1173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1531 DLEQLVALKKHLEMKLSdayEEVveqrqvvgqwkRKAQkmtnemnDLRMLLEEQNARNNLLEKKQRKFDAECQSlqDAVR 1610
Cdd:PTZ00121 1174 DAKKAEAARKAEEVRKA---EEL-----------RKAE-------DARKAEAARKAEEERKAEEARKAEDAKKA--EAVK 1230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1611 QERQAKerygreKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRsKNETERRAKEQE- 1689
Cdd:PTZ00121 1231 KAEEAK------KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK-KADEAKKAEEKKk 1303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1690 -EELDEMAGQIQLLEQAKLRLEMTletmrKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELER 1768
Cdd:PTZ00121 1304 aDEAKKKAEEAKKADEAKKKAEEA-----KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1769 RLSSMEDRDRVDRDAEEAlNQKLRRDLRKYKALLKDAQtqlERLKADtpgktlirQLRNQLEDAESARSLAMKARQTAEA 1848
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEA-KKKAEEDKKKADELKKAAA---AKKKAD--------EAKKKAEEKKKADEAKKKAEEAKKA 1446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1849 EltEVQAMFDESHRARNDAEERANAAHRDRAELQAQieenEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAern 1928
Cdd:PTZ00121 1447 D--EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE----EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK--- 1517
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1929 nlkeqvAELQHRLDNVENLGDPSMAMMSKRLElrtkELESRLELEQATrarlEVQVNRHKEALEKLQNEVTQSKMREMQA 2008
Cdd:PTZ00121 1518 ------AEEAKKADEAKKAEEAKKADEAKKAE----EKKKADELKKAE----ELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 2009 QDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAMEE 2077
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
PDZ_FRMPD1_3_4-like cd06769
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ...
390-425 2.72e-07

PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of FRMPD1, FRMPD3, FRMPD4, and related domains. FRMPD1 (also known as FERM domain-containing protein 2, FRMD2), inhibits the malignant phenotype of lung cancer by activating the Hippo pathway via interaction with WWC3; the FRMPD1 PDZ domain binds WWC3. FRMPD3 is a target gene of the neuron-specific transcription factor NPAS4 that is involved in synaptic plasticity. FRMPD4 (also known as PDZ domain-containing protein 10, PDZD10, PDZK10, PSD-95-interacting regulator of spine morphogenesis, and Preso) regulates dendritic spine morphogenesis, and mGluR1/5 signaling; the FRMPD4 PDZ domain binds PAK-interacting exchange factor-beta (betaPix). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This FRMPD1,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467250 [Multi-domain]  Cd Length: 75  Bit Score: 49.94  E-value: 2.72e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 116008016  390 PGDRLIKVNGTPVGELPREIIIEMIRNSGEAVTVEV 425
Cdd:cd06769    39 PGDQILKINNEPVEDLPRERVIDLIRECKDSIVLTV 74
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1592-1906 3.61e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 3.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1592 EKKQRKfDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLE--QTLADTRLDLEFKEEKLASLQRELEEMTFGGGtee 1669
Cdd:COG4913   610 AKLAAL-EAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASSD--- 685
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1670 EFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKE----ARRESQQRDEELEEVRGN--GYKKIK 1743
Cdd:COG4913   686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaEDLARLELRALLEERFAAalGDAVER 765
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1744 ALECQLETEHE-ERTLLLREKHELERRLSS-----MEDRDRVDRDAEealnqklrrDLRKYKALLKDAQTQ-LERLKADt 1816
Cdd:COG4913   766 ELRENLEERIDaLRARLNRAEEELERAMRAfnrewPAETADLDADLE---------SLPEYLALLDRLEEDgLPEYEER- 835
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1817 pgktlIRQLRNQLEDAESAR--SLAMKARQTAEAELTEVQAM-----FDESHRARNDAEERANAAHRD-RAELQAQIEEN 1888
Cdd:COG4913   836 -----FKELLNENSIEFVADllSKLRRAIREIKERIDPLNDSlkripFGPGRYLRLEARPRPDPEVREfRQELRAVTSGA 910
                         330
                  ....*....|....*...
gi 116008016 1889 EEELGELMKKYSATVKQL 1906
Cdd:COG4913   911 SLFDEELSEARFAALKRL 928
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
1600-1873 5.09e-07

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 54.30  E-value: 5.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1600 AECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKN 1679
Cdd:pfam19220   20 EDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAA------EGELEELVARLA 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1680 ETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGyKKIKALECQLETEHEERTLL 1759
Cdd:pfam19220   94 KLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAE-KALQRAEGELATARERLALL 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1760 LREKH--------------ELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKT----- 1820
Cdd:pfam19220  173 EQENRrlqalseeqaaelaELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRmklea 252
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016  1821 ----------LIRQLRNQLED-------AESARSLAMKARQTAEAELTEVQA-------MFDESHRARNDAEERANA 1873
Cdd:pfam19220  253 ltaraaateqLLAEARNQLRDrdeairaAERRLKEASIERDTLERRLAGLEAdlerrtqQFQEMQRARAELEERAEM 329
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1720-1947 5.78e-07

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: 54.00  E-value: 5.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1720 ARRESQQRDEELEEVRgngyKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRdrvDRDAEEALNQkLRRDLRKYK 1799
Cdd:COG4942    18 QADAAAEAEAELEQLQ----QEIAELEKELAALKKEEKALLKQLAALERRIAALARR---IRALEQELAA-LEAELAELE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1800 ALLKDAQTQLERLKADtpgktLIRQLRnQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARndaEERANAAHRDRA 1879
Cdd:COG4942    90 KEIAELRAELEAQKEE-----LAELLR-ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR---REQAEELRADLA 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116008016 1880 ELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENL 1947
Cdd:COG4942   161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
1762-2074 7.60e-07

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 53.92  E-value: 7.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1762 EKHELER-RLSSMEDRDRVDRDAEEALNQKLR------RDLRKYKALLKDAQTQLERLKADTpgktliRQLRNQLEDAES 1834
Cdd:pfam19220    3 QRNELLRvRLGEMADRLEDLRSLKADFSQLIEpieailRELPQAKSRLLELEALLAQERAAY------GKLRRELAGLTR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1835 ARSLAMKARQTAEAELTEVQAMFDESHRA--------------RNDAEERANAAHRDRAELQAQIEENEEELGELMKKYS 1900
Cdd:pfam19220   77 RLSAAEGELEELVARLAKLEAALREAEAAkeelrielrdktaqAEALERQLAAETEQNRALEEENKALREEAQAAEKALQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1901 ATVKQLNTEQINVSEAEfklNEMEAERNNLKEQVAE---LQHRLDNVENLGDPSMAmmskrlelRTKELESRLELEQATR 1977
Cdd:pfam19220  157 RAEGELATARERLALLE---QENRRLQALSEEQAAElaeLTRRLAELETQLDATRA--------RLRALEGQLAAEQAER 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1978 ARLEVQvnrHKEALEKLQNEVTQSKM-------REMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEqm 2050
Cdd:pfam19220  226 ERAEAQ---LEEAVEAHRAERASLRMklealtaRAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLA-- 300
                          330       340
                   ....*....|....*....|....
gi 116008016  2051 esegaALKNDLRLALQRIADLQQA 2074
Cdd:pfam19220  301 -----GLEADLERRTQQFQEMQRA 319
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1647-2036 7.88e-07

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: 54.59  E-value: 7.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1647 KEEKLA--SLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLL---EQAKLRLEMTLETMRKEAR 1721
Cdd:pfam02463  143 KIEIIAmmKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELklkEQAKKALEYYQLKEKLELE 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1722 RESQQRDEELEEVRgngyKKIKALECQLETEHEERTLLLRekhELERRLSSMEDRDRVDRDAEEAlnQKLRRDLRKYKAL 1801
Cdd:pfam02463  223 EEYLLYLDYLKLNE----ERIDLLQELLRDEQEEIESSKQ---EIEKEEEKLAQVLKENKEEEKE--KKLQEEELKLLAK 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1802 LKDAQtQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVqamfdESHRARNDAEERANAAHRDRAEL 1881
Cdd:pfam02463  294 EEEEL-KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL-----KELEIKREAEEEEEEELEKLQEK 367
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1882 QAQIeeneeelgelmKKYSATVKQLNTEQINVSEAEfkLNEMEAERNNLKEQVAELQHRLDNVEnlgdpsMAMMSKRLEL 1961
Cdd:pfam02463  368 LEQL-----------EEELLAKKKLESERLSSAAKL--KEEELELKSEEEKEAQLLLELARQLE------DLLKEEKKEE 428
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016  1962 RTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQES 2036
Cdd:pfam02463  429 LEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKES 503
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1867-2113 8.79e-07

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: 53.61  E-value: 8.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1867 AEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVEn 1946
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1947 lgdpsmammsKRLELRTKELESRLeleqatrARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEF 2026
Cdd:COG4942    97 ----------AELEAQKEELAELL-------RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 2027 HAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAMEEEGEEELSESDESLSSVGSISDLEDRLRPV 2106
Cdd:COG4942   160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239

                  ....*..
gi 116008016 2107 HVKRSSQ 2113
Cdd:COG4942   240 AERTPAA 246
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1622-1864 1.37e-06

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: 52.84  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1622 EKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQL 1701
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA------LERRIAALARRIRALEQELAALEAELAELEKEIAE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1702 LEQAKLRLEMTLETMRKEARRESQQRDEEL--------EEVRGNGYKK--IKALECQLETEHEERTLLLREKHELERRls 1771
Cdd:COG4942    95 LRAELEAQKEELAELLRALYRLGRQPPLALllspedflDAVRRLQYLKylAPARREQAEELRADLAELAALRAELEAE-- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1772 smedrdrvdRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTpgKTLIRQLRNQLEDAESARSLAMKARQTAEAELT 1851
Cdd:COG4942   173 ---------RAELEALLAELEEERAALEALKAERQKLLARLEKEL--AELAAELAELQQEAEELEALIARLEAEAAAAAE 241
                         250
                  ....*....|...
gi 116008016 1852 EVQAMFDESHRAR 1864
Cdd:COG4942   242 RTPAAGFAALKGK 254
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1532-1870 1.94e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1532 LEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQ 1611
Cdd:COG4372    33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1612 ERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAKEQEEE 1691
Cdd:COG4372   113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES------LQEELAALEQELQALSEAEAEQALD 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1692 ldemagqiQLLEQAKLRLEMTLETmrKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLS 1771
Cdd:COG4372   187 --------ELLKEANRNAEKEEEL--AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1772 SMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELT 1851
Cdd:COG4372   257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
                         330
                  ....*....|....*....
gi 116008016 1852 EVQAMFDESHRARNDAEER 1870
Cdd:COG4372   337 AELADLLQLLLVGLLDNDV 355
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
1384-1735 1.99e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 53.20  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1384 TEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEaetaerlklekELGDQTN 1463
Cdd:pfam15921  473 TKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ-----------HLKNEGD 541
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1464 KVKNLQETTEKLEMELicAKSDLNGISEDEDAEN------EDGVGGGVykLKYERVARELEFTKRRLHTQHEHDLEQLVA 1537
Cdd:pfam15921  542 HLRNVQTECEALKLQM--AEKDKVIEILRQQIENmtqlvgQHGRTAGA--MQVEKAQLEKEINDRRLELQEFKILKDKKD 617
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1538 LK-KHLEMKLSDAYEEVV-------EQRQVVGQWKRKAQKMTNEM----NDLRMLLEE-----QNARNNL--LEKKQRKF 1598
Cdd:pfam15921  618 AKiRELEARVSDLELEKVklvnagsERLRAVKDIKQERDQLLNEVktsrNELNSLSEDyevlkRNFRNKSeeMETTTNKL 697
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1599 DAECQSLQDAVRQERQA-KERYGREKDVLQAEKFTLEQTLAdtrldlefKEEKLASLQRE---LEEMTFGGGTEEEFaqL 1674
Cdd:pfam15921  698 KMQLKSAQSELEQTRNTlKSMEGSDGHAMKVAMGMQKQITA--------KRGQIDALQSKiqfLEEAMTNANKEKHF--L 767
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016  1675 RRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQ--------RDEELEEVR 1735
Cdd:pfam15921  768 KEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQfaecqdiiQRQEQESVR 836
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1384-1833 2.06e-06

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: 53.10  E-value: 2.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1384 TEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEerstahiaterLEAETaERLKLEKElgdqTN 1463
Cdd:TIGR04523  244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ-----------LKSEI-SDLNNQKE----QD 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1464 KVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDgvgggVYKLKYERvaRELEFTKRRLHTQHEHDLEQLVALKKHLE 1543
Cdd:TIGR04523  308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ-----ISQLKKEL--TNSESENSEKQRELEEKQNEIEKLKKENQ 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1544 MKlsdayeevveqrqvvgqwKRKAQKMTNEMNDLRMLLEEQnarnnllEKKQRKFDAECQSLQdavrQERQAKErygREK 1623
Cdd:TIGR04523  381 SY------------------KQEIKNLESQINDLESKIQNQ-------EKLNQQKDEQIKKLQ----QEKELLE---KEI 428
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1624 DVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLE 1703
Cdd:TIGR04523  429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL------ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN 502
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1704 QAKLRLEMTLETMRKEaRRESQQRDEELEEVRGNGYKKIKALECQLETEHEE--RTLLLREKHELERRLSSMEDrdrvDR 1781
Cdd:TIGR04523  503 EEKKELEEKVKDLTKK-ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQ----TQ 577
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 116008016  1782 DAEEALNQKLRRDLRKYKALLKDAQTQLERLkadtpgKTLIRQLRNQLEDAE 1833
Cdd:TIGR04523  578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEK------EKKISSLEKELEKAK 623
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1511-1821 2.49e-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: 52.82  E-value: 2.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1511 ERVARELEfTKRRL---HTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQvvGQWKRKAQKMTNEmnDLRMLLEEQNAR 1587
Cdd:pfam17380  306 EEKAREVE-RRRKLeeaEKARQAEMDRQAAIYAEQERMAMERERELERIRQ--EERKRELERIRQE--EIAMEISRMREL 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1588 NNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKD-VLQAEKFTLEQTLADTRLDLEFKEEKLASLQR-ELEEMTfgg 1665
Cdd:pfam17380  381 ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQqKVEMEQIRAEQEEARQREVRRLEEERAREMERvRLEEQE--- 457
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1666 gTEEEFAQLRRSKNETERRAKEQEEELDEmagQIQLLEQAKLRLEMTLETMRKEARRESQQR---DEELEEVRGNGYkki 1742
Cdd:pfam17380  458 -RQQQVERLRQQEEERKRKKLELEKEKRD---RKRAEEQRRKILEKELEERKQAMIEEERKRkllEKEMEERQKAIY--- 530
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1743 kalecqletEHEERtlllREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDL----RKYKALLKDAQTQLERLKADTPG 1818
Cdd:pfam17380  531 ---------EEERR----REAEEERRKQQEMEERRRIQEQMRKATEERSRLEAmereREMMRQIVESEKARAEYEATTPI 597

                   ...
gi 116008016  1819 KTL 1821
Cdd:pfam17380  598 TTI 600
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
1564-1790 2.56e-06

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 51.74  E-value: 2.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1564 KRKAQKMTNEMNDLRMLLEE----------QNARNNLLEKKQRKFDAEcqsLQDAVRQ-----------ERQAKErYGRE 1622
Cdd:pfam15905   62 KKKSQKNLKESKDQKELEKEiralvqergeQDKRLQALEEELEKVEAK---LNAAVREktslsasvaslEKQLLE-LTRV 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1623 KDVLQAeKF----------TLEQTLADTRLDLEFK-----------EEKLASLQRELEEmtfgggTEEEFAQLRRSKNET 1681
Cdd:pfam15905  138 NELLKA-KFsedgtqkkmsSLSMELMKLRNKLEAKmkevmakqegmEGKLQVTQKNLEH------SKGKVAQLEEKLVST 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1682 ERRAKEQEEELDEMAGQIQLLEQAKLRLEMT------LETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEE 1755
Cdd:pfam15905  211 EKEKIEEKSETEKLLEYITELSCVSEQVEKYkldiaqLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESE 290
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 116008016  1756 RTLLLREKHELERRLSS----MEDRDRVDRDAEEALNQK 1790
Cdd:pfam15905  291 KEELLREYEEKEQTLNAeleeLKEKLTLEEQEHQKLQQK 329
Filament pfam00038
Intermediate filament protein;
1414-1718 5.69e-06

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 50.69  E-value: 5.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1414 AENQKLEAKLSELTVDLAEERSTAHIATER--------LEAETAERLKLEKELGdqtnkvkNLQETTE----KLEMElic 1481
Cdd:pfam00038   25 QQNKLLETKISELRQKKGAEPSRLYSLYEKeiedlrrqLDTLTVERARLQLELD-------NLRLAAEdfrqKYEDE--- 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1482 aksdlngISEDEDAENEdgvgggVYKLKyeRVARELEFTKRRLHTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVG 1561
Cdd:pfam00038   95 -------LNLRTSAEND------LVGLR--KDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1562 QWKRKAQKMTNEMNDLRMLLEEQNARNnlLEKKQRKFDAECQSLQDAVRQE----RQAKE----------RYGREKDVLQ 1627
Cdd:pfam00038  160 MDAARKLDLTSALAEIRAQYEEIAAKN--REEAEEWYQSKLEELQQAAARNgdalRSAKEeitelrrtiqSLEIELQSLK 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1628 AEKFTLEQTLADT--RLDLEFK--EEKLASLQRELEEMtfgggteeefaqlrrsKNETERRAKEQEEELDemagqiqlle 1703
Cdd:pfam00038  238 KQKASLERQLAETeeRYELQLAdyQELISELEAELQET----------------RQEMARQLREYQELLN---------- 291
                          330
                   ....*....|....*
gi 116008016  1704 qAKLRLEMTLETMRK 1718
Cdd:pfam00038  292 -VKLALDIEIATYRK 305
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
1706-2051 5.81e-06

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 51.67  E-value: 5.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1706 KLRLEMTLETMRKEARRESQQRDEELEEVRgngyKKIKALECQLETEHEErtlllreKHELERRLSSMEDRdrvdrdaEE 1785
Cdd:pfam05557    4 LIESKARLSQLQNEKKQMELEHKRARIELE----KKASALKRQLDRESDR-------NQELQKRIRLLEKR-------EA 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1786 ALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESA-RSLAMKARQTAEAELTEVQAM---FDESH 1861
Cdd:pfam05557   66 EAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSElRRQIQRAELELQSTNSELEELqerLDLLK 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1862 RARNDAEERA---NAAHRDRAELQAQIEENEEELGELmKKYSATVKQLNTEQINVSEAEF----------KLNEMEAERN 1928
Cdd:pfam05557  146 AKASEAEQLRqnlEKQQSSLAEAEQRIKELEFEIQSQ-EQDSEIVKNSKSELARIPELEKelerlrehnkHLNENIENKL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1929 NLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRTkELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQA 2008
Cdd:pfam05557  225 LLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQ-ELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLT 303
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 116008016  2009 QDViKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQME 2051
Cdd:pfam05557  304 SSA-RQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ 345
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1385-1927 6.28e-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: 51.51  E-value: 6.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1385 EEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETaERLKLEKELGDQTNK 1464
Cdd:pfam02463  443 QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKAR-SGLKVLLALIKDGVG 521
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1465 VKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLKYERVA--------RELEFTKRRLHTQHEHDLEQLV 1536
Cdd:pfam02463  522 GRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTelplgarkLRLLIPKLKLPLKSIAVLEIDP 601
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1537 ALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNL------------LEKKQRKFDAECQS 1604
Cdd:pfam02463  602 ILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaeksevkasLSELTKELLEIQEL 681
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1605 LQDAVRQERQAKERYGREKDVLQAEKFTLEQT---LADTRLDLEFKEEKLA----SLQRELEEMTFGGGTEEEFAQLRRS 1677
Cdd:pfam02463  682 QEKAESELAKEEILRRQLEIKKKEQREKEELKklkLEAEELLADRVQEAQDkineELKLLKQKIDEEEEEEEKSRLKKEE 761
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1678 KNETERRAKEQEEELDEMAGQIQL------LEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALEcQLET 1751
Cdd:pfam02463  762 KEEEKSELSLKEKELAEEREKTEKlkveeeKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELE-ELAL 840
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1752 EHEERTLLLREKHELERRLSSM----EDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTpGKTLIRQLRN 1827
Cdd:pfam02463  841 ELKEEQKLEKLAEEELERLEEEitkeELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKL-NLLEEKENEI 919
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1828 QLEDAESARSLAMKARQTAEaELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLN 1907
Cdd:pfam02463  920 EERIKEEAEILLKYEEEPEE-LLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
                          570       580
                   ....*....|....*....|
gi 116008016  1908 TEQINVSEAEFKLNEMEAER 1927
Cdd:pfam02463  999 RLEEEKKKLIRAIIEETCQR 1018
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1642-1815 6.48e-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: 49.54  E-value: 6.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1642 LDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEmagqiqlLEQAKLRLEMTLETMRKEAR 1721
Cdd:COG1579    10 LDLQELDSELDRLEHRLKEL------PAELAELEDELAALEARLEAAKTELED-------LEKEIKRLELEIEEVEARIK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1722 RESQQrdeeLEEVRGNgyKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKAL 1801
Cdd:COG1579    77 KYEEQ----LGNVRNN--KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
                         170
                  ....*....|....
gi 116008016 1802 LKDAQTQLERLKAD 1815
Cdd:COG1579   151 LAELEAELEELEAE 164
mukB PRK04863
chromosome partition protein MukB;
1584-1940 9.05e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 51.11  E-value: 9.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1584 QNARNNLLEK--KQRKFDAECQSLQDAvrqERQAKERYGREKDVLQAEKFTLEQTL--ADTRLDL----EFKEEKLASLQ 1655
Cdd:PRK04863  278 ANERRVHLEEalELRRELYTSRRQLAA---EQYRLVEMARELAELNEAESDLEQDYqaASDHLNLvqtaLRQQEKIERYQ 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1656 RELEEMTFGGGTEEEFAQLRRS-KNETERRAKEQEEELDEMAGQIQLLEQAklrLEMtLETmRKEARRESQQRDEELEEV 1734
Cdd:PRK04863  355 ADLEELEERLEEQNEVVEEADEqQEENEARAEAAEEEVDELKSQLADYQQA---LDV-QQT-RAIQYQQAVQALERAKQL 429
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1735 RGN---GYKKIKALECQLETEHEERTLLLREkheLERRLSSMED-RDRVDR------------DAEEALN--QKLRRDLR 1796
Cdd:PRK04863  430 CGLpdlTADNAEDWLEEFQAKEQEATEELLS---LEQKLSVAQAaHSQFEQayqlvrkiagevSRSEAWDvaRELLRRLR 506
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1797 KYKALlkDAQTQLERLKAdtpgKTLIRQLRNQLEDAESARSLAMKARQTAEAElTEVQAMFDESHRARNDAEERANAAHR 1876
Cdd:PRK04863  507 EQRHL--AEQLQQLRMRL----SELEQRLRQQQRAERLLAEFCKRLGKNLDDE-DELEQLQEELEARLESLSESVSEARE 579
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1877 DRAELQAQIEENEEELGELMKK------YSATVKQLNTE------------------QINVSEAEFKLNEMEAERNNLKE 1932
Cdd:PRK04863  580 RRMALRQQLEQLQARIQRLAARapawlaAQDALARLREQsgeefedsqdvteymqqlLERERELTVERDELAARKQALDE 659

                  ....*...
gi 116008016 1933 QVAELQHR 1940
Cdd:PRK04863  660 EIERLSQP 667
PDZ4_GRIP1-2-like cd06686
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
345-430 9.17e-06

PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467174 [Multi-domain]  Cd Length: 99  Bit Score: 46.18  E-value: 9.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  345 SPRQDFGFSLRKAICLdrTESLTSPifrPVI-FAEPGAGGGAT-GLLPGDRLIKVNGTPVGELPREIIIEMIRNSGEAVT 422
Cdd:cd06686    15 DPLKGFGIQLQGGVFA--TETLSSP---PLIsFIEPDSPAERCgVLQVGDRVLSINGIPTEDRTLEEANQLLRDSASKVT 89

                  ....*....
gi 116008016  423 VEVQ-PVAE 430
Cdd:cd06686    90 LEIEfDVAE 98
PRK12705 PRK12705
hypothetical protein; Provisional
1663-1843 1.31e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 50.09  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1663 FGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEE----LEEVRGNG 1738
Cdd:PRK12705   17 LLGVLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEErlvqKEEQLDAR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1739 YKKIKALECQLETehEERTLLLREKhELERRLSSMEDR-DRVDRDAEEALNQ----KLRRDLRKYKALLKDAQTQLERLK 1813
Cdd:PRK12705   97 AEKLDNLENQLEE--REKALSAREL-ELEELEKQLDNElYRVAGLTPEQARKlllkLLDAELEEEKAQRVKKIEEEADLE 173
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 116008016 1814 ADTPGKTLIRQLRNQL-EDAESARSL--------AMKAR 1843
Cdd:PRK12705  174 AERKAQNILAQAMQRIaSETASDLSVsvvpipsdAMKGR 212
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1781-2074 1.34e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.90  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1781 RDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADtpgktlIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDES 1860
Cdd:COG4372    19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREE------LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1861 HRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHR 1940
Cdd:COG4372    93 QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1941 LDNVENlgdpsmAMMSKRLELRTKELESRLELEQATRarlEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLR 2020
Cdd:COG4372   173 LQALSE------AEAEQALDELLKEANRNAEKEEELA---EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 116008016 2021 DMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQA 2074
Cdd:COG4372   244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1540-1884 1.47e-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: 49.53  E-value: 1.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1540 KHLEMKLSDAY------EEVVEQRQVVGQWKRKAQKMTNEMNDLRM-LLEEQNARNNLLEKKQRKFDAE-CQSLQDAVRQ 1611
Cdd:pfam13868    9 RELNSKLLAAKcnkerdAQIAEKKRIKAEEKEEERRLDEMMEEERErALEEEEEKEEERKEERKRYRQElEEQIEEREQK 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1612 ERQAKERYGREKDVLQAEkftLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggteeefaqlRRSKNETERRAKEQEEE 1691
Cdd:pfam13868   89 RQEEYEEKLQEREQMDEI---VERIQEEDQAEAEEKLEKQRQLREEIDEF-------------NEEQAEWKELEKEEERE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1692 LDEmagqiQLLEQAKLRLEMTLETMRKEARREsQQRDEELEEVRGNGYKKIKALEcqletEHEE-RTLLLREKHELERRL 1770
Cdd:pfam13868  153 EDE-----RILEYLKEKAEREEEREAEREEIE-EEKEREIARLRAQQEKAQDEKA-----ERDElRAKLYQEEQERKERQ 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1771 SSMEDRDRvdRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADtpgktliRQLRNQLEDAESARSLAMKARQTAEAEL 1850
Cdd:pfam13868  222 KEREEAEK--KARQRQELQQAREEQIELKERRLAEEAEREEEEFE-------RMLRKQAEDEEIEQEEAEKRRMKRLEHR 292
                          330       340       350
                   ....*....|....*....|....*....|....
gi 116008016  1851 TEVQAMFDESHRARNDAEERANAAHRDRAELQAQ 1884
Cdd:pfam13868  293 RELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1630-1838 1.82e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1630 KFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKN--ETERRAKEQEEELDEMAGQIQLLEQAKL 1707
Cdd:COG3206   163 EQNLELRREEARKALEFLEEQLPELRKELEE------AEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELA 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1708 RLEMTLETMRKEARRESQQRDEELEEVRGNGYK-KIKALECQLET-------EHEERTLLLREKHELERRLSSMEDRDRV 1779
Cdd:COG3206   237 EAEARLAALRAQLGSGPDALPELLQSPVIQQLRaQLAELEAELAElsarytpNHPDVIALRAQIAALRAQLQQEAQRILA 316
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1780 DRDAE----EALNQKLRRDLRKYKALLK---DAQTQLERLKAD-TPGKTLIRQLRNQLEDAESARSL 1838
Cdd:COG3206   317 SLEAElealQAREASLQAQLAQLEARLAelpELEAELRRLEREvEVARELYESLLQRLEEARLAEAL 383
mukB PRK04863
chromosome partition protein MukB;
1634-2067 1.91e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 50.34  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1634 EQTLADTRLDLEFKEEKLASLQRELEEM-----------------TFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMA 1696
Cdd:PRK04863  785 EKRIEQLRAEREELAERYATLSFDVQKLqrlhqafsrfigshlavAFEADPEAELRQLNRRRVELERALADHESQEQQQR 864
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1697 GQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEvrgngyKKIKALECQLETEHEERTLllrekHELERRLSSM--- 1773
Cdd:PRK04863  865 SQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIRE------QLDEAEEAKRFVQQHGNAL-----AQLEPIVSVLqsd 933
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1774 -EDRDRVDRDAEEAlnQKLRRDLRKYKALLKDAQTQLERLK-ADTPGKT-----LIRQLRNQLEDAESARSLAMKARQTA 1846
Cdd:PRK04863  934 pEQFEQLKQDYQQA--QQTQRDAKQQAFALTEVVQRRAHFSyEDAAEMLaknsdLNEKLRQRLEQAEQERTRAREQLRQA 1011
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1847 EAELTE---VQAMFDESHRARND-------------------AEERAnAAHRDraELQAQIEENEEELGELMKKYSATVK 1904
Cdd:PRK04863 1012 QAQLAQynqVLASLKSSYDAKRQmlqelkqelqdlgvpadsgAEERA-RARRD--ELHARLSANRSRRNQLEKQLTFCEA 1088
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1905 QLNTEQINVSEAEFKLNEMEAERNNLK-------EQVAE--LQHRLDNVE--NLGDPSMAMMS-KRLELRTKELESRLEL 1972
Cdd:PRK04863 1089 EMDNLTKKLRKLERDYHEMREQVVNAKagwcavlRLVKDngVERRLHRRElaYLSADELRSMSdKALGALRLAVADNEHL 1168
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1973 EQATR-----ARLEVQVNRHKEALEKLqnevtqskmREMQAQDVIKKSQKslRDMREEFHAVSSREQESLTRRkdlEKKV 2047
Cdd:PRK04863 1169 RDVLRlsedpKRPERKVQFYIAVYQHL---------RERIRQDIIRTDDP--VEAIEQMEIELSRLTEELTSR---EQKL 1234
                         490       500
                  ....*....|....*....|
gi 116008016 2048 eQMESEGAAlkNDLRLALQR 2067
Cdd:PRK04863 1235 -AISSESVA--NIIRKTIQR 1251
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
1384-2051 2.20e-05

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 50.05  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1384 TEEQLKTANEELLMLRAKLEKIECDRSEV-------------KAENQKLEAKLSELTVDL-------------------- 1430
Cdd:TIGR00606  236 SREIVKSYENELDPLKNRLKEIEHNLSKImkldneikalksrKKQMEKDNSELELKMEKVfqgtdeqlndlyhnhqrtvr 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1431 --AEERSTAHIATERLEAE----TAERLKLEKELGDQTNKVKNLQETTEK--LEMELICAKSDLNGISEDEDAENEDGvg 1502
Cdd:TIGR00606  316 ekERELVDCQRELEKLNKErrllNQEKTELLVEQGRLQLQADRHQEHIRArdSLIQSLATRLELDGFERGPFSERQIK-- 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1503 gGVYKLKYERVAREleftkRRLHTQHEHDLEQLVALKKHLEMKLSDayeevvEQRQVVGQWKRKAQKMTNEMNDLRMLLE 1582
Cdd:TIGR00606  394 -NFHTLVIERQEDE-----AKTAAQLCADLQSKERLKQEQADEIRD------EKKGLGRTIELKKEILEKKQEELKFVIK 461
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1583 E-QNAR---NNLLEKKQrkfdaecqSLQDAVRQERQAkerygrEKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQREL 1658
Cdd:TIGR00606  462 ElQQLEgssDRILELDQ--------ELRKAERELSKA------EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQL 527
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1659 EEMTFGGGTEEEFAQLRRSKNETERRAKEQEEelDEMAGQIQLLEQAKLrLEMTLETMRKEARresqQRDEELEEVRgng 1738
Cdd:TIGR00606  528 NHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHS--DELTSLLGYFPNKKQ-LEDWLHSKSKEIN----QTRDRLAKLN--- 597
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1739 yKKIKALEcqlETEHEERtlllREKHELERRLSSMEDR--DRVDRDAEEALNQKLRRDL---RKYKALL----------- 1802
Cdd:TIGR00606  598 -KELASLE---QNKNHIN----NELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIeksSKQRAMLagatavysqfi 669
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1803 ---------------KDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDA 1867
Cdd:TIGR00606  670 tqltdenqsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPEL 749
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1868 EERANAAHRDRAELQAQIEENEEELGELM-KKYSATVKQLNTEQINVSEAEFKLNEMEAER--------------NNLKE 1932
Cdd:TIGR00606  750 RNKLQKVNRDIQRLKNDIEEQETLLGTIMpEEESAKVCLTDVTIMERFQMELKDVERKIAQqaaklqgsdldrtvQQVNQ 829
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1933 QVAELQHRLDNVENLGDPSMAMMSKRLElRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVT--QSKMREM-QAQ 2009
Cdd:TIGR00606  830 EKQEKQHELDTVVSKIELNRKLIQDQQE-QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTevQSLIREIkDAK 908
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|..
gi 116008016  2010 DVIKKSQKSLRDMREefhavssrEQESLTRRKDLEKKVEQME 2051
Cdd:TIGR00606  909 EQDSPLETFLEKDQQ--------EKEELISSKETSNKKAQDK 942
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1715-1885 2.40e-05

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: 48.00  E-value: 2.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1715 TMRKEARR--ESQQRD---EELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMED-----RDRVDRDaE 1784
Cdd:COG1579     1 AMPEDLRAllDLQELDselDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELeieevEARIKKY-E 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1785 EALNQKlrRDLRKYKALLKDAQTqLERLKADTpgKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDEshrAR 1864
Cdd:COG1579    80 EQLGNV--RNNKEYEALQKEIES-LKRRISDL--EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---EL 151
                         170       180
                  ....*....|....*....|.
gi 116008016 1865 NDAEERANAAHRDRAELQAQI 1885
Cdd:COG1579   152 AELEAELEELEAEREELAAKI 172
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
390-427 2.42e-05

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 44.68  E-value: 2.42e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 116008016    390 PGDRLIKVNGTPVGELPREIIIEMIRNSGEAVTVEVQP 427
Cdd:smart00228   46 VGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVTLTVLR 83
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1648-1912 2.71e-05

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 48.37  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1648 EEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQI-QLLEQAKLRLEMtLETMRKEARRESQQ 1726
Cdd:COG1340     7 SSSLEELEEKIEEL------REEIEELKEKRDELNEELKELAEKRDELNAQVkELREEAQELREK-RDELNEKVKELKEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1727 RDEELEEVRGNgYKKIKalecQLETEHEERTLLLREKHELERRLSSMEDR---DRVDRDAEEALNQKLRRdlrkYKALLK 1803
Cdd:COG1340    80 RDELNEKLNEL-REELD----ELRKELAELNKAGGSIDKLRKEIERLEWRqqtEVLSPEEEKELVEKIKE----LEKELE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1804 DAQTQLERLKADTPGKTLIRQLRNQLEDA-ESARSLAMKARQTAEA------ELTEVQAMFDESHRARNDAEERANAAHR 1876
Cdd:COG1340   151 KAKKALEKNEKLKELRAELKELRKEAEEIhKKIKELAEEAQELHEEmielykEADELRKEADELHKEIVEAQEKADELHE 230
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 116008016 1877 DRAELQAQIEENEEELGELMKKYSATVKQLNTEQIN 1912
Cdd:COG1340   231 EIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
1372-2060 2.88e-05

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 49.66  E-value: 2.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1372 LVRVTPllnvHRTEEQLKTANEELLMLRAKLEKIECDrsEVKAENQKLEAKLSELTVDLAEERStahiateRLEaetaer 1451
Cdd:TIGR01612  639 LAKISP----YQVPEHLKNKDKIYSTIKSELSKIYED--DIDALYNELSSIVKENAIDNTEDKA-------KLD------ 699
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1452 lKLEKELGDQTNKVKNLQETTEKLEMELIcaksdlngisedEDAENEdgvgggvyklkyerVARELEFTKRRLHTQHEHD 1531
Cdd:TIGR01612  700 -DLKSKIDKEYDKIQNMETATVELHLSNI------------ENKKNE--------------LLDIIVEIKKHIHGEINKD 752
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1532 LEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDlrmlleeQNARNNLLEkkqrkfdaecqslQDAVRQ 1611
Cdd:TIGR01612  753 LNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYND-------QINIDNIKD-------------EDAKQN 812
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1612 ERQAKErYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGgtEEEFAQL-RRSKNETerrakeQEE 1690
Cdd:TIGR01612  813 YDKSKE-YIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSE--HEQFAELtNKIKAEI------SDD 883
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1691 ELDEMAGQIQlleQAKLRLEMTLETMRKEarresQQRDEELEEVrgNGYKKI-KALECQLETEHEERTLLlreKHELERR 1769
Cdd:TIGR01612  884 KLNDYEKKFN---DSKSLINEINKSIEEE-----YQNINTLKKV--DEYIKIcENTKESIEKFHNKQNIL---KEILNKN 950
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1770 LSSMEDRDRVDRDAEEalnqklrrdlrKYKALLKDAQTQLERLKADTpgktlirqlrnQLEDAESARSLAMKARQTAEAE 1849
Cdd:TIGR01612  951 IDTIKESNLIEKSYKD-----------KFDNTLIDKINELDKAFKDA-----------SLNDYEAKNNELIKYFNDLKAN 1008
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1850 LTEVQA-----MFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKK-YSATVKQLNT---EQINVSEAEFkl 1920
Cdd:TIGR01612 1009 LGKNKEnmlyhQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKeIGKNIELLNKeilEEAEINITNF-- 1086
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1921 nemeaerNNLKEQVaelqhRLDNVENLGDPSMAMMSKRLELRTKELESrleleqatrarLEVQVNRHKEALEKLQNEvTQ 2000
Cdd:TIGR01612 1087 -------NEIKEKL-----KHYNFDDFGKEENIKYADEINKIKDDIKN-----------LDQKIDHHIKALEEIKKK-SE 1142
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116008016  2001 SKMREMQAQ--DVIKKSQKSLRDmrEEFHAVSSREQESLT---RRKDLEKKVEQMESEGAALKND 2060
Cdd:TIGR01612 1143 NYIDEIKAQinDLEDVADKAISN--DDPEEIEKKIENIVTkidKKKNIYDEIKKLLNEIAEIEKD 1205
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
1568-1704 3.32e-05

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 46.82  E-value: 3.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1568 QKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDavrqERQAKERYGREKDVLQAEKftLEQTLADTRLDLEFK 1647
Cdd:pfam15619   63 ARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRD----QLKRLEKLSEDKNLAEREE--LQKKLEQLEAKLEDK 136
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016  1648 EEKLASLQRELEEMTfgggteeefAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQ 1704
Cdd:pfam15619  137 DEKIQDLERKLELEN---------KSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQ 184
mukB PRK04863
chromosome partition protein MukB;
1613-2070 3.39e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.19  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1613 RQAKERYGREKDVLqaekfTLEQTLADTRLDLEFKEEKLASLQRELEEMTFG-GGTEEEFAQLRRSKN--ETERRAKEQE 1689
Cdd:PRK04863  276 RHANERRVHLEEAL-----ELRRELYTSRRQLAAEQYRLVEMARELAELNEAeSDLEQDYQAASDHLNlvQTALRQQEKI 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1690 E----ELDEMagQIQLLEQAKLRLEMTLETMRKEARRES---------------QQRDEE--------------LEEVRG 1736
Cdd:PRK04863  351 EryqaDLEEL--EERLEEQNEVVEEADEQQEENEARAEAaeeevdelksqladyQQALDVqqtraiqyqqavqaLERAKQ 428
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1737 -NGY-----KKIKALECQLETEHEERTLLLRekhELERRLSSmedrdrvdrdAEEALNQklrrdLRKYKALLKDAQTQLE 1810
Cdd:PRK04863  429 lCGLpdltaDNAEDWLEEFQAKEQEATEELL---SLEQKLSV----------AQAAHSQ-----FEQAYQLVRKIAGEVS 490
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1811 RLKADTPGKTLIRQLRNQLEDAESARSLamkarqtaEAELTEVQamfdESHRARNDAEERANAAHrdraelqaqieenee 1890
Cdd:PRK04863  491 RSEAWDVARELLRRLREQRHLAEQLQQL--------RMRLSELE----QRLRQQQRAERLLAEFC--------------- 543
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1891 elgelmkkysatvKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRldnvenlgdpsmammskRLELRT--KELES 1968
Cdd:PRK04863  544 -------------KRLGKNLDDEDELEQLQEELEARLESLSESVSEARER-----------------RMALRQqlEQLQA 593
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1969 RL-ELEQATRARLEVQvnrhkEALEKLQnevTQSKMREMQAQDVIKKSQKSLRDMREefhaVSSREQESLTRRKDLEKKV 2047
Cdd:PRK04863  594 RIqRLAARAPAWLAAQ-----DALARLR---EQSGEEFEDSQDVTEYMQQLLERERE----LTVERDELAARKQALDEEI 661
                         490       500
                  ....*....|....*....|...
gi 116008016 2048 EQMESEGAAlkNDLRlaLQRIAD 2070
Cdd:PRK04863  662 ERLSQPGGS--EDPR--LNALAE 680
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
1381-1823 3.83e-05

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 48.80  E-value: 3.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1381 VHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGD 1460
Cdd:COG5185   161 IKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQD 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1461 QTNKVKNLQETTEKLEmELICAKSDLNGISEDEDAENEDGVGGGVYKLK------YERVARELEFTKRRLHTQHEHDLEQ 1534
Cdd:COG5185   241 PESELEDLAQTSDKLE-KLVEQNTDLRLEKLGENAESSKRLNENANNLIkqfentKEKIAEYTKSIDIKKATESLEEQLA 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1535 LVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNaRNNLLEKKQRKFDAECQSLQDAVRQERQ 1614
Cdd:COG5185   320 AAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV-ELSKSSEELDSFKDTIESTKESLDEIPQ 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1615 AKERYGREkdvlqaekftLEQTLADTrldLEFKEEKLASLQRELEemtfggGTEEEFAQLRRSKNETERRAKEQEEELDE 1694
Cdd:COG5185   399 NQRGYAQE----------ILATLEDT---LKAADRQIEELQRQIE------QATSSNEEVSKLLNELISELNKVMREADE 459
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1695 MAGqiQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSME 1774
Cdd:COG5185   460 ESQ--SRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAH 537
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 116008016 1775 DRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIR 1823
Cdd:COG5185   538 ILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQQAR 586
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
1380-1862 3.86e-05

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: 49.02  E-value: 3.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1380 NVHRTEEQLKTANEELLMLRAKLEKIECDRSEvkAENQKLeaklsELTVDLaeerstahiatERLEAETAERLKLEKELG 1459
Cdd:pfam01576  679 NVHELERSKRALEQQVEEMKTQLEELEDELQA--TEDAKL-----RLEVNM-----------QALKAQFERDLQARDEQG 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1460 DQtnKVKNLQETTEKLEMELicaksdlngisEDEDAENEDGVGGgvyKLKYERVARELEFTKRRLHTQHEHDLEQLvalk 1539
Cdd:pfam01576  741 EE--KRRQLVKQVRELEAEL-----------EDERKQRAQAVAA---KKKLELDLKELEAQIDAANKGREEAVKQL---- 800
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1540 KHLEMKLSDAYEEVVEQRQ----VVGQWKRKAQKMTNEMNDLRMLLEEQNARnnllEKKQRKFDAECQSLQDAVRQERQA 1615
Cdd:pfam01576  801 KKLQAQMKDLQRELEEARAsrdeILAQSKESEKKLKNLEAELLQLQEDLAAS----ERARRQAQQERDELADEIASGASG 876
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1616 KERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRS-KNETERRAKEQEEELDE 1694
Cdd:pfam01576  877 KSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESaRQQLERQNKELKAKLQE 956
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1695 MAGQIqlleqaKLRLEMTLETMrkEArresqqrdeeleevrgngykKIKALECQLETEHEERT----LLLREKHELERRL 1770
Cdd:pfam01576  957 MEGTV------KSKFKSSIAAL--EA--------------------KIAQLEEQLEQESRERQaankLVRRTEKKLKEVL 1008
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1771 SSMEDRdrvdrdaeealnqklRRDLRKYKallkdaqTQLERLKADtpgktlIRQLRNQLEDAESARSLAMKARQTAEAEL 1850
Cdd:pfam01576 1009 LQVEDE---------------RRHADQYK-------DQAEKGNSR------MKQLKRQLEEAEEEASRANAARRKLQREL 1060
                          490
                   ....*....|..
gi 116008016  1851 TEVQAMFDESHR 1862
Cdd:pfam01576 1061 DDATESNESMNR 1072
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
339-426 5.15e-05

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467153 [Multi-domain]  Cd Length: 81  Bit Score: 43.69  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  339 VIRRQKSPRQDFGFSLRkaicldRTESLTSPIFrpVIFAEPGAGGGATGL-LPGDRLIKVNGTPVGELPREIIIEMIRNS 417
Cdd:cd00136     1 TVTLEKDPGGGLGFSIR------GGKDGGGGIF--VSRVEPGGPAARDGRlRVGDRILEVNGVSLEGLTHEEAVELLKSA 72

                  ....*....
gi 116008016  418 GEAVTVEVQ 426
Cdd:cd00136    73 GGEVTLTVR 81
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1818-2005 5.23e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 5.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1818 GKTLIRQLRnQLEDAESARslamKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEElgelmK 1897
Cdd:COG4717    63 GRKPELNLK-ELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY-----Q 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1898 KYSATVKQLNTEQINVSEAEFK---LNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRTKELESRLELEQ 1974
Cdd:COG4717   133 ELEALEAELAELPERLEELEERleeLRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELE 212
                         170       180       190
                  ....*....|....*....|....*....|.
gi 116008016 1975 ATRARLEVQVNRHKEALEKLQNEVTQSKMRE 2005
Cdd:COG4717   213 EELEEAQEELEELEEELEQLENELEAAALEE 243
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
693-829 5.27e-05

class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276859 [Multi-domain]  Cd Length: 871  Bit Score: 48.59  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  693 ILEAFGNTKTCLNSNATRMTQLLSLDF-----DQTGQIASASLQVLLPERQRA----GRRLG--HEHSFHIMTRLLAGAA 761
Cdd:cd14894   255 VLEAFGHATTSMNLNSSRFGKMTTLQVafglhPWEFQICGCHISPFLLEKSRVtserGRESGdqNELNFHILYAMVAGVN 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  762 G-----LLQKELHLENIT-------SEDSHPFISLSQKLEDRHRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLG 829
Cdd:cd14894   335 AfpfmrLLAKELHLDGIDcsaltylGRSDHKLAGFVSKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLWLG 414
PRK12704 PRK12704
phosphodiesterase; Provisional
1682-1872 5.80e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.24  E-value: 5.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1682 ERRAKEQEEELDEMAGQIqlLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLEtEHEERtlllr 1761
Cdd:PRK12704   26 KKIAEAKIKEAEEEAKRI--LEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLL-QKEEN----- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1762 ekheLERRLSSMEDRDRVDRDAEEALNQKLrRDLRK----YKALLKDAQTQLERLKADTpgktlirqlrnqledAESARS 1837
Cdd:PRK12704   98 ----LDRKLELLEKREEELEKKEKELEQKQ-QELEKkeeeLEELIEEQLQELERISGLT---------------AEEAKE 157
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 116008016 1838 LAMKarqTAEAEL-TEVQAMFDESH-RARNDAEERAN 1872
Cdd:PRK12704  158 ILLE---KVEEEArHEAAVLIKEIEeEAKEEADKKAK 191
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
1527-2065 6.74e-05

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 47.98  E-value: 6.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1527 QHEHDLEQLVALkkhLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTN-EMNDLRMLLEEQNARNNLLEKKQRKFDAECQSL 1605
Cdd:pfam15964   64 QHSHAVNQLKAL---LQQQTKKENELSPRRRKLSPSRTSEDESSSLpTVHDLVPIINDQSQYIHHLEAEVKFCKEELSEM 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1606 QDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQlRRSKNETERRA 1685
Cdd:pfam15964  141 KQRVQVVVLENEKLQQELKSQTQEETLREQTLLDSSGNMQNSWCTPEDSRVHQTSKRPASHNLAERLK-SATTGEDEKWR 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1686 KEQEeeldemagQIQLLEQAKLR-LEMTLETMRKEARrESQQRDEELEE--------VRGNGYKKIKALeCQLETEHEEr 1756
Cdd:pfam15964  220 LELE--------KLKLLYEAKTEvLESQVKSLRKDLA-ESQKTCEDLKErlkhkeslVAASTSSRVGGL-CLKCAQHEA- 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1757 tlLLREKHE------LERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYK----ALLKDAQTQLERLKAdtpgktLIR--Q 1824
Cdd:pfam15964  289 --VLAQTHTnvhmqtIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEqvkqAVQMTEEANFEKTKA------LIQceQ 360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1825 LRNQLEDAESARSLAMKARQTAEAEltEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVK 1904
Cdd:pfam15964  361 LKSELERQKERLEKELASQQEKRAQ--EKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQK 438
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1905 QLNTEQINVS----EAEFKLNEmeaerNNLKEQVAELQHRldnvenlgdpsmammskrlELRTKeLESRLELEQATRARL 1980
Cdd:pfam15964  439 QLASQEMDVTkvcgEMRYQLNQ-----TKMKKDEAEKEHR-------------------EYRTK-TGRQLEIKDQEIEKL 493
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1981 EVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAV--------SSREQESLTRRKDLEKKVEQMES 2052
Cdd:pfam15964  494 GLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRLEKESIqqsfsneaKAQALQAQQREQELTQKMQQMEA 573
                          570
                   ....*....|...
gi 116008016  2053 EGAALKNDLRLAL 2065
Cdd:pfam15964  574 QHDKTVNEQYSLL 586
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
1745-2074 9.05e-05

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 47.38  E-value: 9.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1745 LECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQklrrdLRKYKALLKDAQTQLE------RLKADTPG 1818
Cdd:pfam05622   19 LDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLL-----LQKQLEQLQEENFRLEtarddyRIKCEELE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1819 KTLIR-QLRNQledaesarslamkarqtaeaELT----EVQAMFDESHRARNDAEERAnaahrdRAELQAQIEENEEELG 1893
Cdd:pfam05622   94 KEVLElQHRNE--------------------ELTslaeEAQALKDEMDILRESSDKVK------KLEATVETYKKKLEDL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1894 ELMKKysaTVKQL---NTEQI-NVSEAEFKLNEMEAERNNL---KEQVAELQHRLDnvenlgdpSMAMMSKRLELRTKEL 1966
Cdd:pfam05622  148 GDLRR---QVKLLeerNAEYMqRTLQLEEELKKANALRGQLetyKRQVQELHGKLS--------EESKKADKLEFEYKKL 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1967 ESRLELEQATRARLEVQVNRHKEALEKLQneVTQSKMREM-QAQDVIKKSQKSLRDMREEFHAVSSRE------------ 2033
Cdd:pfam05622  217 EEKLEALQKEKERLIIERDTLRETNEELR--CAQLQQAELsQADALLSPSSDPGDNLAAEIMPAEIREklirlqhenkml 294
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 116008016  2034 ---QESLTRRK--DLEKKVEQMESEGAALKNDLRLALQRIADLQQA 2074
Cdd:pfam05622  295 rlgQEGSYRERltELQQLLEDANRRKNELETQNRLANQRILELQQQ 340
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
1524-2004 9.52e-05

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 47.43  E-value: 9.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1524 LHTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQK-------MTNEMNDLRMLLEEQNARNNLLEKKQR 1596
Cdd:pfam05557   77 LNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRaelelqsTNSELEELQERLDLLKAKASEAEQLRQ 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1597 KFDAECQSLQDAvrqERQAKErygrekdvlqaekftLEQTLA---DTRLDLEFKEEKLAS---LQRELEEMtfgggtEEE 1670
Cdd:pfam05557  157 NLEKQQSSLAEA---EQRIKE---------------LEFEIQsqeQDSEIVKNSKSELARipeLEKELERL------REH 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1671 FAQLRrSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEArresqQRDEELEEVRGNGYKKIKALECQLE 1750
Cdd:pfam05557  213 NKHLN-ENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQEL-----QSWVKLAQDTGLNLRSPEDLSRRIE 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1751 TEHEERTLLLREKHELERRLSSMEdrdrvdrdaeeALNQKLRRDLRKYKALLKDAQTQLERLKAdtpgktLIRQLRNQLE 1830
Cdd:pfam05557  287 QLQQREIVLKEENSSLTSSARQLE-----------KARRELEQELAQYLKKIEDLNKKLKRHKA------LVRRLQRRVL 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1831 DAESARSLAMKARQTAEAELTEVQAMFDESHRARnDAEERANAAHRDRAELQAQIEENEEelgelmkkySATVKQLNTEQ 1910
Cdd:pfam05557  350 LLTKERDGYRAILESYDKELTMSNYSPQLLERIE-EAEDMTQKMQAHNEEMEAQLSVAEE---------ELGGYKQQAQT 419
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1911 INVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVEnlgdpsmaMMSKRLELRTKELESRLE-------LEQATRARLEVQ 1983
Cdd:pfam05557  420 LERELQALRQQESLADPSYSKEEVDSLRRKLETLE--------LERQRLREQKNELEMELErrclqgdYDPKKTKVLHLS 491
                          490       500
                   ....*....|....*....|....*...
gi 116008016  1984 VN-------RHKEALEKLQNEVTQSKMR 2004
Cdd:pfam05557  492 MNpaaeayqQRKNQLEKLQAEIERLKRL 519
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
1612-1775 1.03e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.55  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1612 ERQAKERYGREK---DVLQAEkfTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggteEEFAQLRRSKNETERRAKEQ 1688
Cdd:COG2433   356 EKKVPPDVDRDEvkaRVIRGL--SIEEALEELIEKELPEEEPEAEREKEHEE--------RELTEEEEEIRRLEEQVERL 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1689 EEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESqQRDEELEEVRgngyKKIKALECQLETEHEERtlllrekHELER 1768
Cdd:COG2433   426 EAEVEELEAELEEKDERIERLERELSEARSEERREI-RKDREISRLD----REIERLERELEEERERI-------EELKR 493

                  ....*..
gi 116008016 1769 RLSSMED 1775
Cdd:COG2433   494 KLERLKE 500
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1414-1661 1.13e-04

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: 46.68  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1414 AENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVKNLQETTEKLEMELicaksdlngisede 1493
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------------- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1494 daenedgvgggvyklkyERVARELEFTKRRLHTQHEHDLEQLVALKKHLEMklsdAYEEVVEQRQVVGQWKRKAQKMTNE 1573
Cdd:COG4942    86 -----------------AELEKEIAELRAELEAQKEELAELLRALYRLGRQ----PPLALLLSPEDFLDAVRRLQYLKYL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1574 MNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLAS 1653
Cdd:COG4942   145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224

                  ....*...
gi 116008016 1654 LQRELEEM 1661
Cdd:COG4942   225 LEALIARL 232
PDZ4_MAGI-1_3-like cd06734
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
390-427 1.46e-04

PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467216 [Multi-domain]  Cd Length: 84  Bit Score: 42.22  E-value: 1.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 116008016  390 PGDRLIKVNGTPVGELPREIIIEMIRNSGEAVTVEVQP 427
Cdd:cd06734    47 VGDRILAVNGISILNLSHGDIVNLIKDSGLSVTLTIVP 84
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
1515-1832 1.48e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 47.25  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1515 RELEFTKRRLHTQHEH------DLEQLVALKKHLEMklsdAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRML---LEEQN 1585
Cdd:COG3096   292 RELFGARRQLAEEQYRlvemarELEELSARESDLEQ----DYQAASDHLNLVQTALRQQEKIERYQEDLEELterLEEQE 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1586 -----ARNNLLEKKQRKFDAECQ----------------SLQDAVRQERQAKERYGREKDVLQAEKFTLEQtLADTRLDL 1644
Cdd:COG3096   368 evveeAAEQLAEAEARLEAAEEEvdslksqladyqqaldVQQTRAIQYQQAVQALEKARALCGLPDLTPEN-AEDYLAAF 446
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1645 EFKEEKLASLQRELEE-MTFGGGTEEEFAQ----LRRSKNETER-----RAKEQEEELDE---MAGQIQLLEQAKLRLEM 1711
Cdd:COG3096   447 RAKEQQATEEVLELEQkLSVADAARRQFEKayelVCKIAGEVERsqawqTARELLRRYRSqqaLAQRLQQLRAQLAELEQ 526
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1712 TLETMRKE-------ARRESQQRD--EELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRD 1782
Cdd:COG3096   527 RLRQQQNAerlleefCQRIGQQLDaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLA 606
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 116008016 1783 AEEALNQkLRRD----LRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDA 1832
Cdd:COG3096   607 AQDALER-LREQsgeaLADSQEVTAAMQQLLEREREATVERDELAARKQALESQ 659
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1599-1942 1.52e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.45  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1599 DAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLRRSK 1678
Cdd:pfam13868    2 RENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKE------EERKEERKRYR 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1679 NE-----TERRAKEQEEELDEMAGQIQLLE-QAKLRLEMTLETMRKEARRESQQRD-EELEEVRgngyKKIKALECQLET 1751
Cdd:pfam13868   76 QEleeqiEEREQKRQEEYEEKLQEREQMDEiVERIQEEDQAEAEEKLEKQRQLREEiDEFNEEQ----AEWKELEKEEER 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1752 EHEERTLL-LREKHELERRLssmEDRDRVDRDAEEALNQKLRRDLRKykalLKDAQTQLERLKADTPGKTLIRQLR-NQL 1829
Cdd:pfam13868  152 EEDERILEyLKEKAEREEER---EAEREEIEEEKEREIARLRAQQEK----AQDEKAERDELRAKLYQEEQERKERqKER 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1830 EDAESARSLAMKARQTAEAELTEVQAMFDEshrARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTE 1909
Cdd:pfam13868  225 EEAEKKARQRQELQQAREEQIELKERRLAE---EAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
                          330       340       350
                   ....*....|....*....|....*....|...
gi 116008016  1910 QINVSEAEFKlnEMEAERNNLKEQVAELQHRLD 1942
Cdd:pfam13868  302 REEQRAAERE--EELEEGERLREEEAERRERIE 332
Rabaptin pfam03528
Rabaptin;
1725-2060 1.70e-04

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 46.64  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1725 QQRDEELEEVRGNGYKkikaLECQLETEHEERTLLLREKHelerrLSSMEDRDRvdrdaEEALNQKLRRDLRKYKALLKD 1804
Cdd:pfam03528    7 QQRVAELEKENAEFYR----LKQQLEAEFNQKRAKFKELY-----LAKEEDLKR-----QNAVLQEAQVELDALQNQLAL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1805 AQTQLERLKA-----DTPGKTLIRQLRNQLEDAESARSLAMKA-----------------------RQTAEAELTEVQAM 1856
Cdd:pfam03528   73 ARAEMENIKAvatvsENTKQEAIDEVKSQWQEEVASLQAIMKEtvreyevqfhrrleqeraqwnqyRESAEREIADLRRR 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1857 FDESHRARNdAEERANAAHRDRAELQAQIeeneeelgELMKKYSATVKQlnteqiNVSEAEFKLNEMEAERnnlkeqVAE 1936
Cdd:pfam03528  153 LSEGQEEEN-LEDEMKKAQEDAEKLRSVV--------MPMEKEIAALKA------KLTEAEDKIKELEASK------MKE 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1937 LQHRLDnVENLGDPSMAMMSKRLELRTKELEsrlelEQATRARLEVQVNRHKEALEKLQNevTQSKMREMQAQDVIKKSQ 2016
Cdd:pfam03528  212 LNHYLE-AEKSCRTDLEMYVAVLNTQKSVLQ-----EDAEKLRKELHEVCHLLEQERQQH--NQLKHTWQKANDQFLESQ 283
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 116008016  2017 KSL-RDMREEFHAVSS---REQESLTRRKDLEKKVEQMESEGAALKND 2060
Cdd:pfam03528  284 RLLmRDMQRMESVLTSeqlRQVEEIKKKDQEEHKRARTHKEKETLKSD 331
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1381-1735 1.71e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.07  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1381 VHRTEEQLKTANEELLmlRAKLEKIEcdrsevkaENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGD 1460
Cdd:pfam13868    1 LRENSDELRELNSKLL--AAKCNKER--------DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1461 QTNKVKNLQETTEKLEMELICAKSDlngisEDEDAENEDGVgggVYKLKYERVARELEFTKRRLHTQHEHDLeqlvALKK 1540
Cdd:pfam13868   71 RKRYRQELEEQIEEREQKRQEEYEE-----KLQEREQMDEI---VERIQEEDQAEAEEKLEKQRQLREEIDE----FNEE 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1541 HLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAEcQSLQDAVRQERQ--AKER 1618
Cdd:pfam13868  139 QAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDE-KAERDELRAKLYqeEQER 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1619 YGREKDVLQAEK--FTLEQTLADTRLDLEFKEEKLAsLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMA 1696
Cdd:pfam13868  218 KERQKEREEAEKkaRQRQELQQAREEQIELKERRLA-EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELE 296
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 116008016  1697 GQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVR 1735
Cdd:pfam13868  297 KQIEEREEQRAAEREEELEEGERLREEEAERRERIEEER 335
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
1578-2075 1.84e-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: 46.74  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1578 RMLLEEQNARNNLLEKKQRKFDAECQSLQDAVrQERQAKERYGRE-KDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQR 1656
Cdd:pfam10174   45 RALRKEEAARISVLKEQYRVTQEENQHLQLTI-QALQDELRAQRDlNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQS 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1657 ELEEmtfgggTEEEFAQLRRSKNETERR---------------------------AKEQEEELDEMAGQIQLLEQAKLRL 1709
Cdd:pfam10174  124 EHER------QAKELFLLRKTLEEMELRietqkqtlgardesikkllemlqskglPKKSGEEDWERTRRIAEAEMQLGHL 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1710 EMTLETMRKE--ARRESQQRDEELEevrgNGYKKIKALECQLETEHEERTLLLREKHELERRLSS--------MEDRdrv 1779
Cdd:pfam10174  198 EVLLDQKEKEniHLREELHRRNQLQ----PDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMlktngllhTEDR--- 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1780 drdaEEALNQ----------------KLRRDLRKYKALLKDAQTQLERL--------------KADTPGK--------TL 1821
Cdd:pfam10174  271 ----EEEIKQmevykshskfmknkidQLKQELSKKESELLALQTKLETLtnqnsdckqhievlKESLTAKeqraailqTE 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1822 IRQLRNQLEDAESArsLAMKARQ---------TAEAELTEVQAMFDESHRarndaeeRANAAHRDRAELQAQIEENEEEL 1892
Cdd:pfam10174  347 VDALRLRLEEKESF--LNKKTKQlqdlteeksTLAGEIRDLKDMLDVKER-------KINVLQKKIENLQEQLRDKDKQL 417
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1893 GELMKKysatVKQLNTEQINVSEAEFKLNEMEAERN----NLKEQVA-ELQHRLDNVENLG----------DPSMAMMSK 1957
Cdd:pfam10174  418 AGLKER----VKSLQTDSSNTDTALTTLEEALSEKEriieRLKEQRErEDRERLEELESLKkenkdlkekvSALQPELTE 493
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1958 R------LELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQ------DVIKKSQKSLRDMREE 2025
Cdd:pfam10174  494 KesslidLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpeinDRIRLLEQEVARYKEE 573
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116008016  2026 fhavSSREQESLTR-----------RKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAM 2075
Cdd:pfam10174  574 ----SGKAQAEVERllgilreveneKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEM 630
mukB PRK04863
chromosome partition protein MukB;
1529-1842 1.89e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.87  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1529 EHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQkMTNEMNDLRMLLEEqnarnNLLEKKQRKFDAECQSLQDA 1608
Cdd:PRK04863  836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLS-ALNRLLPRLNLLAD-----ETLADRVEEIREQLDEAEEA 909
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1609 VRQERQakerYGRekdvlQAEKftLEQTLADTRLDlefkEEKLASLQRELEEMTfgggteeefAQLRRSKNET------- 1681
Cdd:PRK04863  910 KRFVQQ----HGN-----ALAQ--LEPIVSVLQSD----PEQFEQLKQDYQQAQ---------QTQRDAKQQAfaltevv 965
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1682 ERRAK-EQEEELDEMAGQIQLLEQAKLRLEMtLETMRKEARRESQQRDEELEEvrgngYKKIKA-LECQLETEHEERTLL 1759
Cdd:PRK04863  966 QRRAHfSYEDAAEMLAKNSDLNEKLRQRLEQ-AEQERTRAREQLRQAQAQLAQ-----YNQVLAsLKSSYDAKRQMLQEL 1039
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1760 LREKHELERRL-SSMEDRDRVDRDaeeALNQKLRRDLRKYKALLKdaQTQLERLKADTPGKTL------IRQLRNQLEDA 1832
Cdd:PRK04863 1040 KQELQDLGVPAdSGAEERARARRD---ELHARLSANRSRRNQLEK--QLTFCEAEMDNLTKKLrklerdYHEMREQVVNA 1114
                         330
                  ....*....|
gi 116008016 1833 ESARSLAMKA 1842
Cdd:PRK04863 1115 KAGWCAVLRL 1124
Caldesmon pfam02029
Caldesmon;
1439-1784 2.13e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 46.40  E-value: 2.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1439 IATERLEAETAERLKLeKELGDQTNKVKNLQETTEK-LEMELICAKSdlngiSEDEDAENEDGVgggvyklkYERVAREL 1517
Cdd:pfam02029    7 AARERRRRAREERRRQ-KEEEEPSGQVTESVEPNEHnSYEEDSELKP-----SGQGGLDEEEAF--------LDRTAKRE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1518 EFTKRRLHTQHEHdleqlvalKKHLEMKLSDAYEEVVEQRQVVGQ-----WKRKAQKMTNEMNDLrmllEEQNARNNLLE 1592
Cdd:pfam02029   73 ERRQKRLQEALER--------QKEFDPTIADEKESVAERKENNEEeenssWEKEEKRDSRLGRYK----EEETEIREKEY 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1593 KKQRKFDAECQSLQDAVRQERQAKErygrEKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFA 1672
Cdd:pfam02029  141 QENKWSTEVRQAEEEGEEEEDKSEE----AEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEV 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1673 QLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMT---LETMRKEARRESQQRDE-ELEEVRGNGYKKIKALEcq 1748
Cdd:pfam02029  217 TKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRrqeKESEEFEKLRQKQQEAElELEELKKKREERRKLLE-- 294
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 116008016  1749 letEHEERtlllREKHELERRLSSMEDRDRVDRDAE 1784
Cdd:pfam02029  295 ---EEEQR----RKQEEAERKLREEEEKRRMKEEIE 323
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
390-426 2.65e-04

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 41.50  E-value: 2.65e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 116008016   390 PGDRLIKVNGTPVGELPREIIIEMIRNSGEAVTVEVQ 426
Cdd:pfam00595   45 VGDRILSINGQDVENMTHEEAVLALKGSGGKVTLTIL 81
CCDC144C pfam14915
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ...
1439-1657 2.73e-04

CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.


Pssm-ID: 464371 [Multi-domain]  Cd Length: 304  Bit Score: 45.36  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1439 IATERLEAETAERLKLEKE---LGDqtnkVKNLQETTEKLEMEL-----------ICAKSDLNgISEDEDA------ENE 1498
Cdd:pfam14915    8 IAMLRLEIDTIKNQNQEKEkkyLED----IEILKEKNDDLQKTLklneetltktvFQYNGQLN-VLKAENTmlnsklENE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1499 dgvgggvyKLKYERVARELEFTKRRLHTQhEHDLEQLVALKKHLEMKLSDAYEEvveqrqvvgqWKRKAQKMTNEMNDLR 1578
Cdd:pfam14915   83 --------KQNKERLETEVESYRSRLAAA-IQDHEQSQTSKRDLELAFQRERDE----------WLRLQDKMNFDVSNLR 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1579 mllEEQNARNNLLEKKQRKFDA---ECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDL-------EFKE 1648
Cdd:pfam14915  144 ---DENEILSQQLSKAESKANSlenELHRTRDALREKTLLLESVQRDLSQAQCQKKELEHMYQNEQDKVnkyigkqESLE 220

                   ....*....
gi 116008016  1649 EKLASLQRE 1657
Cdd:pfam14915  221 ERLAQLQSE 229
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1588-1902 2.81e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1588 NNLLEKKQRKFDAECQSLQDAVRQERQAK---ERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFG 1664
Cdd:COG4372    16 FGLRPKTGILIAALSEQLRKALFELDKLQeelEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1665 -GGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIK 1743
Cdd:COG4372    96 lAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1744 ALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIR 1823
Cdd:COG4372   176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 1824 QLRNQLEDAESARslamKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSAT 1902
Cdd:COG4372   256 ILKEIEELELAIL----VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
1610-2062 3.09e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 45.72  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1610 RQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNEterRAKEQE 1689
Cdd:COG5185    89 LKEKKLDTKILQEYVNSLIKLPNYEWSADILISLLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETG---IIKDIF 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1690 EELDEMAGQIQLLEQAKLRLEMTLETMRKEARRES-----QQRDEELEEVRGNGYKKIKALECQLETEHEERtllLREKH 1764
Cdd:COG5185   166 GKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPsgtvnSIKESETGNLGSESTLLEKAKEIINIEEALKG---FQDPE 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1765 ELERRLSSMEDRdrvdrdAEEALNQklRRDLRKYKalLKDAQTQLERLKADTpgKTLIRQLRNQLED-AESARSLAMKAR 1843
Cdd:COG5185   243 SELEDLAQTSDK------LEKLVEQ--NTDLRLEK--LGENAESSKRLNENA--NNLIKQFENTKEKiAEYTKSIDIKKA 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1844 QTAEAELTEvqamfdeSHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQiNVSEAEFKLNEM 1923
Cdd:COG5185   311 TESLEEQLA-------AAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV-ELSKSSEELDSF 382
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1924 EAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRTKELESrlELEQATRARLEVQvnrhkEALEKLQNEVTQSkM 2003
Cdd:COG5185   383 KDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQR--QIEQATSSNEEVS-----KLLNELISELNKV-M 454
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 2004 REMQAqdvikksqKSLRDMREEFHAVSSREQESLtrrKDLEKKVEQMESEGAALKNDLR 2062
Cdd:COG5185   455 READE--------ESQSRLEEAYDEINRSVRSKK---EDLNEELTQIESRVSTLKATLE 502
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
1922-2057 3.23e-04

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 44.43  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1922 EMEAERNNLKEQVAELQHRLDNVENLGDPSMAmmsKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQ- 2000
Cdd:COG1842    55 RLERQLEELEAEAEKWEEKARLALEKGREDLA---REALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEEl 131
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 2001 -SKMREMQAQDvikKSQKSLRDMREEFHAVSSRE-QESLTRrkdLEKKVEQMESEGAAL 2057
Cdd:COG1842   132 kAKKDTLKARA---KAAKAQEKVNEALSGIDSDDaTSALER---MEEKIEEMEARAEAA 184
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
1392-1847 3.27e-04

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 45.95  E-value: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1392 NEELLMLRAKLEKIECDRSEVKAENQKLEA------KLSELTVDLAEERSTAHIATERLEAETAERL-KLEKELGDQTNK 1464
Cdd:PRK10246  362 NNELAGWRAQFSQQTSDREQLRQWQQQLTHaeqklnALPAITLTLTADEVAAALAQHAEQRPLRQRLvALHGQIVPQQKR 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1465 VKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGggvYKLKYERVAR--ELEFTKRRLH----------TQHEHdL 1532
Cdd:PRK10246  442 LAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAD---VKTICEQEARikDLEAQRAQLQagqpcplcgsTSHPA-V 517
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1533 EQLVALKKHLEMKLSDAYEEVVEQRQ-----VVGQWKRKAQKMTNEMNDLRMLLEEQNArnnLLEKKQrkfdAECQSL-- 1605
Cdd:PRK10246  518 EAYQALEPGVNQSRLDALEKEVKKLGeegaaLRGQLDALTKQLQRDESEAQSLRQEEQA---LTQQWQ----AVCASLni 590
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1606 ----QDAVRQERQAKERYGREKDVLqAEKFTLEQTLAD-TRLDLEFK---EEKLASLQRELEEMTFGGGTEEEFAQLRRS 1677
Cdd:PRK10246  591 tlqpQDDIQPWLDAQEEHERQLRLL-SQRHELQGQIAAhNQQIIQYQqqiEQRQQQLLTALAGYALTLPQEDEEASWLAT 669
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1678 KNETERRAKEQEEELDEMAGQIQlleqaklRLEMTLETMRKEARRESQQRDEELEEVRgNGYKKIKALECQLETEHEERT 1757
Cdd:PRK10246  670 RQQEAQSWQQRQNELTALQNRIQ-------QLTPLLETLPQSDDLPHSEETVALDNWR-QVHEQCLSLHSQLQTLQQQDV 741
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1758 LLLREKHELERRL------SSMEDR--------DRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKtlir 1823
Cdd:PRK10246  742 LEAQRLQKAQAQFdtalqaSVFDDQqaflaallDEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDG---- 817
                         490       500
                  ....*....|....*....|....
gi 116008016 1824 qlrnqLEDAESARSLAMKARQTAE 1847
Cdd:PRK10246  818 -----LDLTVTVEQIQQELAQLAQ 836
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1372-1699 3.51e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1372 LVRVTPLLNVHRTEEQLKTANEELLMLRAKLEKIecDRSEVKAENQKLEaKLSELTVDLAEERSTAHIATERLEAETAER 1451
Cdd:PRK03918  482 LRELEKVLKKESELIKLKELAEQLKELEEKLKKY--NLEELEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1452 LKLEKELGDQTNKVKNLQETTEKLEMElicaksdlngiSEDEDaenedgvgggvyklkyERVARELE-FTKRRLHTQH-E 1529
Cdd:PRK03918  559 AELEKKLDELEEELAELLKELEELGFE-----------SVEEL----------------EERLKELEpFYNEYLELKDaE 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1530 HDLEQLVALKKHLEMKLSDAYEEVVEQrqvvgqwKRKAQKMTNEMNDLRMLLEEQNARNnlLEKKQRKFDAECQSLQDAV 1609
Cdd:PRK03918  612 KELEREEKELKKLEEELDKAFEELAET-------EKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAEL 682
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1610 RQERQAKERYGREKDVLQAEKFTLEQtladtrldlefKEEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKeqe 1689
Cdd:PRK03918  683 EELEKRREEIKKTLEKLKEELEEREK-----------AKKELEKLEKALERV------EELREKVKKYKALLKERAL--- 742
                         330
                  ....*....|
gi 116008016 1690 EELDEMAGQI 1699
Cdd:PRK03918  743 SKVGEIASEI 752
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
1622-1855 5.35e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1622 EKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQL 1701
Cdd:COG3883    24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA------LQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1702 LEQAKLRLEMTLE-----------TMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRL 1770
Cdd:COG3883    98 SGGSVSYLDVLLGsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1771 SSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAEL 1850
Cdd:COG3883   178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257

                  ....*
gi 116008016 1851 TEVQA 1855
Cdd:COG3883   258 AAGSA 262
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1822-1993 5.79e-04

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: 43.76  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1822 IRQLRNQLEDAEsarslamKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELM--KKY 1899
Cdd:COG1579    19 LDRLEHRLKELP-------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEY 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1900 SATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVEnlgdpsmammsKRLELRTKELESRLELEQATRAR 1979
Cdd:COG1579    92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE-----------AELEEKKAELDEELAELEAELEE 160
                         170
                  ....*....|....
gi 116008016 1980 LEVQVNRHKEALEK 1993
Cdd:COG1579   161 LEAEREELAAKIPP 174
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
1669-1885 5.83e-04

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: 44.94  E-value: 5.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1669 EEFAQLRRSknETERRAKEQEEEldemagqiQLLEQAKLRLEmtlETMRKEARRESQQRDEELEevrgngYKKIKALECQ 1748
Cdd:pfam15709  340 AERAEMRRL--EVERKRREQEEQ--------RRLQQEQLERA---EKMREELELEQQRRFEEIR------LRKQRLEEER 400
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1749 LETEHEERTLLLREKHELERRlssmedrdrvdRDAEEALNQKLRRDLRKYKallkdaQTQLERLKADtpgKTLIRQLRNQ 1828
Cdd:pfam15709  401 QRQEEEERKQRLQLQAAQERA-----------RQQQEEFRRKLQELQRKKQ------QEEAERAEAE---KQRQKELEMQ 460
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 116008016  1829 LedAESARSLAmkarQTAEAELTEVQAMFDESH-RARNDAEERanaahRDRAELQAQI 1885
Cdd:pfam15709  461 L--AEEQKRLM----EMAEEERLEYQRQKQEAEeKARLEAEER-----RQKEEEAARL 507
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
1668-1910 6.25e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 6.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1668 EEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEArresqqrdEELEEvrgngykKIKALEC 1747
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI--------DKLQA-------EIAEAEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1748 QLETEHEertlllrekhELERRLSSM----EDRDRVD-----RDAEEALNQ--KLRRDLRKYKALLKDAQTQLERLKADT 1816
Cdd:COG3883    80 EIEERRE----------ELGERARALyrsgGSVSYLDvllgsESFSDFLDRlsALSKIADADADLLEELKADKAELEAKK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1817 pgktliRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELM 1896
Cdd:COG3883   150 ------AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
                         250
                  ....*....|....
gi 116008016 1897 KKYSATVKQLNTEQ 1910
Cdd:COG3883   224 AAAAAAAAAAAAAA 237
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
1592-1709 7.27e-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: 43.76  E-value: 7.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1592 EKKQRKFDAECQslqdavrQERQAKERYGREKDvlqaEKFTLEQTLAD-TRLDlefkeEKLASLQRELEEMtfgggteee 1670
Cdd:pfam15991   23 ERKKQEQEAKME-------EERLRREREEREKE----DRMTLEETKEQiLKLE-----KKLADLKEEKHQL--------- 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 116008016  1671 FAQLRRSKNETERR---AKEQeEELDEMAGQIQLLEQAKLRL 1709
Cdd:pfam15991   78 FLQLKKVLHEDETRkrqLKEQ-SELFALQQAAAQVFLPQLSM 118
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
1540-1750 7.31e-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: 43.72  E-value: 7.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1540 KHLEMKLSDAYEEVVEQRQVVGQwkrkaQKMTNEMNDLRMLLEEQNARNNLLekKQRKFDAECQSLQDAVRQERQAKERY 1619
Cdd:cd16269    93 KKLMEQLEEKKEEFCKQNEEASS-----KRCQALLQELSAPLEEKISQGSYS--VPGGYQLYLEDREKLVEKYRQVPRKG 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1620 GREKDVLQ---AEKFTLEQTL--ADTRLDLEFKEEKLASLQRELEEMtfgggteeEFAQLRRSKNETERRAKEQEEELDE 1694
Cdd:cd16269   166 VKAEEVLQeflQSKEAEAEAIlqADQALTEKEKEIEAERAKAEAAEQ--------ERKLLEEQQRELEQKLEDQERSYEE 237
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116008016 1695 MagqiqlLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYK-KIKALECQLE 1750
Cdd:cd16269   238 H------LRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKeQAELLQEEIR 288
PRK12705 PRK12705
hypothetical protein; Provisional
1634-1793 7.47e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 44.31  E-value: 7.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1634 EQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKeQEEELDEMAGQIQLLEQAKLRLEMTL 1713
Cdd:PRK12705   36 ERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQ-KEEQLDARAEKLDNLENQLEEREKAL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1714 ETMRKEARRESQQRDEELEEVRGngykkikalecqlETEHEERTLLLRE-----KHELERRLSSMEDR--DRVDRDAEEA 1786
Cdd:PRK12705  115 SARELELEELEKQLDNELYRVAG-------------LTPEQARKLLLKLldaelEEEKAQRVKKIEEEadLEAERKAQNI 181

                  ....*..
gi 116008016 1787 LNQKLRR 1793
Cdd:PRK12705  182 LAQAMQR 188
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
390-425 8.38e-04

PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the Na+/H+ exchange regulatory cofactor (NHERF) family of multi-PDZ-domain-containing scaffolding proteins (NHERF1-4), and related domains. The NHERF family includes NHERF1 (also known as EBP50), NHERF2 (also known as E3KARP; TKA-1; SIP-1), NHERF3 (also known as CAP70; CLAMP; Napi-Cap-1; PDZD1) and NHERF4 (also known as IKEPP; PDZK2; Napi-Cap-2). NHERF1 and NHERF2 have tandem PDZ domains (PDZ1-2); NHERF3 and NHERF4 have four PDZ domains (PDZ1-4). NHERFs are involved in the regulation of multiple receptors or transporters, such as type II sodium-phosphate cotransporter (Npt2a), purinergic P2Y1 receptor P2Y1R, the beta2-adrenergic receptor (beta2-AR), parathyroid hormone receptor type 1 (PTHR), the lysophosphatidic acid receptors (LPARs), sodium-hydrogen exchanger 3 (NHE3), and cystic fibrosis transmembrane conductance regulator (CFTR). NHERF-PDZ1 domain interaction partners include Npt2a, purinergic P2Y1 receptor, beta2-AR, CFTR, PTHR, NH3, G-protein-coupled receptor kinase 6 (GRK6A), platelet-derived growth factor receptor (PDGFR), B1 subunit of the H+ATPase, cholesterol, receptor for activated C-kinase RACK1, aquaporin 9, among others. The NHERF PDZ2 domain interacts with fewer proteins: NHERF1 PDZ2 binds Npt2a, PTHR, beta-catenin, aquaporin 9, and RACK1; NHERF2 PDZ2 binds LPA2, P2Y1R, and NHE3, cGMP-dependent protein kinase type II (cGKII). NHERF4 PDZ1 and PDZ4 bind the epithelial Ca(2+) channels TRPV5 and TRPV6. NHERF2/NHERF3 heterodimerization is mediated by PDZ domains of NHERF2 and the C-terminal PDZ domain recognition motif of NHERF3. NHERF4 regulates several transporters mediating influx of xenobiotics and nutrients in the small intestine. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This NHERF-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467249 [Multi-domain]  Cd Length: 80  Bit Score: 40.11  E-value: 8.38e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 116008016  390 PGDRLIKVNGTPVGELPREIIIEMIRNSGEAVTVEV 425
Cdd:cd06768    43 DGDRLVEVNGENVEGESHEQVVEKIKASGNQVTLLV 78
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
1385-1618 8.57e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 44.03  E-value: 8.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1385 EEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTV--DLAEERSTAHIATERLEAETAERLKLEKELgdqT 1462
Cdd:pfam15905   93 DKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRvnELLKAKFSEDGTQKKMSSLSMELMKLRNKL---E 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1463 NKVKNLQETTEKLEMELICAKSDLNGISEDedaenedgvgggVYKLKYERVARELEFTKRRLHTQH-EHDLEQLVALKKH 1541
Cdd:pfam15905  170 AKMKEVMAKQEGMEGKLQVTQKNLEHSKGK------------VAQLEEKLVSTEKEKIEEKSETEKlLEYITELSCVSEQ 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1542 LEMK----------LSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARN-NLLEKKQRKFDAECQSLQDAVR 1610
Cdd:pfam15905  238 VEKYkldiaqleelLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELlREYEEKEQTLNAELEELKEKLT 317

                   ....*...
gi 116008016  1611 QERQAKER 1618
Cdd:pfam15905  318 LEEQEHQK 325
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
1655-1946 9.35e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 43.65  E-value: 9.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1655 QRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARresqqrdeelEEV 1734
Cdd:pfam15905   66 QKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLL----------ELT 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1735 RGNGYKKIKALECQleTEHEERTLLLrekhELERRLSSMEDRDRVDRDAEEALNQKLrrdlrkykallKDAQTQLERLKA 1814
Cdd:pfam15905  136 RVNELLKAKFSEDG--TQKKMSSLSM----ELMKLRNKLEAKMKEVMAKQEGMEGKL-----------QVTQKNLEHSKG 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1815 DtpgktlIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARND---AEERANAAHRDRAELQAQIEENEEE 1891
Cdd:pfam15905  199 K------VAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDiaqLEELLKEKNDEIESLKQSLEEKEQE 272
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116008016  1892 LGELMKKYSATVKQLNteqinvSEAEFKLNEMEAERNNLKEQVAELQHRLDNVEN 1946
Cdd:pfam15905  273 LSKQIKDLNEKCKLLE------SEKEELLREYEEKEQTLNAELEELKEKLTLEEQ 321
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
1684-2075 1.04e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 44.41  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1684 RAKEQEEELDEMAG-----QI--QLLEQaklrlemtletmRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEER 1756
Cdd:PRK10246  165 KPKERAELLEELTGteiygQIsaMVFEQ------------HKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEE 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1757 TLLLREKHELERRLSSMEDRDRVDRDAeealnQKLRRDLRKYKALLKDAQTQLERLKADTPGktliRQLRNQLEDAESAR 1836
Cdd:PRK10246  233 KQLLTAQQQQQQSLNWLTRLDELQQEA-----SRRQQALQQALAAEEKAQPQLAALSLAQPA----RQLRPHWERIQEQS 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1837 SLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEEL--GELMKKYSATVKQLNTEQinvs 1914
Cdd:PRK10246  304 AALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRqwNNELAGWRAQFSQQTSDR---- 379
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1915 eaefklnemeAERNNLKEQVAELQHRLDNVENLG-----DPSMAMMSKRLELRTkeLESRLELEQATRARLEVQVNRHKE 1989
Cdd:PRK10246  380 ----------EQLRQWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQRP--LRQRLVALHGQIVPQQKRLAQLQV 447
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1990 ALEKLQNEVTQ-SKMREMQAQDVIKKSQ---------------KSLRDMRE--------------EFHAVSSREQESLT- 2038
Cdd:PRK10246  448 AIQNVTQEQTQrNAALNEMRQRYKEKTQqladvkticeqeariKDLEAQRAqlqagqpcplcgstSHPAVEAYQALEPGv 527
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 116008016 2039 ---RRKDLEKKVEQMESEGAALK---NDLRLALQRIADLQQAM 2075
Cdd:PRK10246  528 nqsRLDALEKEVKKLGEEGAALRgqlDALTKQLQRDESEAQSL 570
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
1820-2023 1.11e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1820 TLIRQLRNQLEDAESARslamkarQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKY 1899
Cdd:COG3883    16 PQIQAKQKELSELQAEL-------EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1900 SATVKQLNTEQINVSEAEF--------------------------KLNEMEAERNNLKEQVAELQHRLDNVENLgdpsma 1953
Cdd:COG3883    89 GERARALYRSGGSVSYLDVllgsesfsdfldrlsalskiadadadLLEELKADKAELEAKKAELEAKLAELEAL------ 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1954 mmSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMR 2023
Cdd:COG3883   163 --KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1685-2025 1.15e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.37  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1685 AKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKA-LECQLETEHEERTLLLREK 1763
Cdd:pfam13868   21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEqIEEREQKRQEEYEEKLQER 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1764 HELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQtQLERLKADtpgKTLIRQLRNQLEDAESARSLAMKAR 1843
Cdd:pfam13868  101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWK-ELEKEEER---EEDERILEYLKEKAEREEEREAERE 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1844 QTAEAELTEVQAMFDESHRARNDAEER------ANAAHRDRAELQAQIEeneeelgelmkkysatvkqlnteqinvsEAE 1917
Cdd:pfam13868  177 EIEEEKEREIARLRAQQEKAQDEKAERdelrakLYQEEQERKERQKERE----------------------------EAE 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1918 FKLNEMEAERNNLKEQVAELQHRLDNVENLgdpsMAMMSKRLELRTKELEsrlELEQATRARLEVQVNRHKEALEKLQNE 1997
Cdd:pfam13868  229 KKARQRQELQQAREEQIELKERRLAEEAER----EEEEFERMLRKQAEDE---EIEQEEAEKRRMKRLEHRRELEKQIEE 301
                          330       340
                   ....*....|....*....|....*...
gi 116008016  1998 VTQSKMREMQAQDVIKKSQKSLRDMREE 2025
Cdd:pfam13868  302 REEQRAAEREEELEEGERLREEEAERRE 329
Filament pfam00038
Intermediate filament protein;
1673-1885 1.18e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 43.37  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1673 QLRRSKNETERRAKEQ--EEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRG-----NGYKKIKA- 1744
Cdd:pfam00038   35 SELRQKKGAEPSRLYSlyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSaendlVGLRKDLDe 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1745 -------LECQLET----------EHEERTLLLREKHELERRLSSMEDRDRVD--------RDAEEALNQKLRRDLRK-Y 1798
Cdd:pfam00038  115 atlarvdLEAKIESlkeelaflkkNHEEEVRELQAQVSDTQVNVEMDAARKLDltsalaeiRAQYEEIAAKNREEAEEwY 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1799 KALLKDAQTQLERLKADTPG-KTLIRQLRNQLedaesarslamkarQTAEAELTEVQAMFDESHRARNDAEERANAAHRD 1877
Cdd:pfam00038  195 QSKLEELQQAAARNGDALRSaKEEITELRRTI--------------QSLEIELQSLKKQKASLERQLAETEERYELQLAD 260
                          250
                   ....*....|..
gi 116008016  1878 ----RAELQAQI 1885
Cdd:pfam00038  261 yqelISELEAEL 272
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1378-1476 1.19e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1378 LLNVHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKE 1457
Cdd:COG4372    37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
                          90
                  ....*....|....*....
gi 116008016 1458 LGDQTNKVKNLQETTEKLE 1476
Cdd:COG4372   117 LEELQKERQDLEQQRKQLE 135
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
1591-1799 1.31e-03

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 42.71  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1591 LEKKQRKFDAECQSLQDAVRQERQAKERygrekdvLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEM--------- 1661
Cdd:pfam00261    6 IKEELDEAEERLKEAMKKLEEAEKRAEK-------AEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAekaadeser 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1662 ------TFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAklrLEmtletmRKEAR-RESQQRDEELEEV 1734
Cdd:pfam00261   79 grkvleNRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGD---LE------RAEERaELAESKIVELEEE 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116008016  1735 RGNGYKKIKALECQlETEHEERTLLLREK-HELERRLSSMEDRdrvDRDAE------EALNQKLRRDLRKYK 1799
Cdd:pfam00261  150 LKVVGNNLKSLEAS-EEKASEREDKYEEQiRFLTEKLKEAETR---AEFAErsvqklEKEVDRLEDELEAEK 217
PLN02939 PLN02939
transferase, transferring glycosyl groups
1721-2053 1.33e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 44.12  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1721 RRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERR-LSSMEDRDRVDRDAEEALNQKLRRDLRKYK 1799
Cdd:PLN02939   41 GFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKsTSSDDDHNRASMQRDEAIAAIDNEQQTNSK 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1800 ALLKDAQTQLERL----KADTPGKTLIRQLRNQ-LEDAE---SARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERA 1871
Cdd:PLN02939  121 DGEQLSDFQLEDLvgmiQNAEKNILLLNQARLQaLEDLEkilTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILE 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1872 NAAHRDRAELQAQIEENEEELGELMKKYS----------ATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRL 1941
Cdd:PLN02939  201 EQLEKLRNELLIRGATEGLCVHSLSKELDvlkeenmllkDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKF 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1942 -------------------DNVENLG----------DPSMAMMSKRLELRTK--ELESRLEleqatrarlevQVNRHKEA 1990
Cdd:PLN02939  281 ivaqedvsklsplqydcwwEKVENLQdlldratnqvEKAALVLDQNQDLRDKvdKLEASLK-----------EANVSKFS 349
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116008016 1991 LEKLqnEVTQSKMR----EMQAQDVIKKSQKSL-RDMREEFHAVSSREQESlTRRKDLEKKVEQMESE 2053
Cdd:PLN02939  350 SYKV--ELLQQKLKlleeRLQASDHEIHSYIQLyQESIKEFQDTLSKLKEE-SKKRSLEHPADDMPSE 414
PRK11281 PRK11281
mechanosensitive channel MscK;
1741-1978 1.36e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.13  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1741 KIKALECQLETEHEERTLllreKHELERRLSSMEDRDRVDRDAEEalnqkLRRDLRKYKALLKDAQTQLERLKADTP--- 1817
Cdd:PRK11281   44 QLDALNKQKLLEAEDKLV----QQDLEQTLALLDKIDRQKEETEQ-----LKQQLAQAPAKLRQAQAELEALKDDNDeet 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1818 ----GKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAmfdeshrarndAEERANAAHRDRAELQAQIEENEEELG 1893
Cdd:PRK11281  115 retlSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQT-----------QPERAQAALYANSQRLQQIRNLLKGGK 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1894 ELMKKYSATVK-QLNTEQINVsEAEFKLNEMEAERNN------------LKEQVAELQHRLDNVENLGDpsmammSKRLE 1960
Cdd:PRK11281  184 VGGKALRPSQRvLLQAEQALL-NAQNDLQRKSLEGNTqlqdllqkqrdyLTARIQRLEHQLQLLQEAIN------SKRLT 256
                         250
                  ....*....|....*...
gi 116008016 1961 LRTKELESRLELEQATRA 1978
Cdd:PRK11281  257 LSEKTVQEAQSQDEAARI 274
Filament pfam00038
Intermediate filament protein;
1765-2071 1.51e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 42.99  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1765 ELERRLSSMEDRDRvdrdAEEALNQKLRRdlrkyKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQ 1844
Cdd:pfam00038    8 ELNDRLASYIDKVR----FLEQQNKLLET-----KISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1845 TAEAELTEVQAMFDESHRARNDAEERANAAHRD-------RAELQAQIEENEEELGELMKKYSATVKQLNT----EQINV 1913
Cdd:pfam00038   79 NLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDldeatlaRVDLEAKIESLKEELAFLKKNHEEEVRELQAqvsdTQVNV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1914 seaefklnEMEAERN-NLKEQVAELQHRLDnvenlgdpSMAMMSKrlelrtKELEsrlELEQATRARLEVQVNRHKEALE 1992
Cdd:pfam00038  159 --------EMDAARKlDLTSALAEIRAQYE--------EIAAKNR------EEAE---EWYQSKLEELQQAAARNGDALR 213
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016  1993 KLQNEVTQSKMReMQAQDVIKKSQKSLRDMREefHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADL 2071
Cdd:pfam00038  214 SAKEEITELRRT-IQSLEIELQSLKKQKASLE--RQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQEL 289
Filament pfam00038
Intermediate filament protein;
1534-1826 1.55e-03

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 42.99  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1534 QLVALKKHLEMKLSDAYEevVEQRQVvgqwKRKAQKMTNEMNDLRMLLEEQNARNNLLEkkqrkfdAECQSLQDAVRQER 1613
Cdd:pfam00038   22 FLEQQNKLLETKISELRQ--KKGAEP----SRLYSLYEKEIEDLRRQLDTLTVERARLQ-------LELDNLRLAAEDFR 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1614 QAKERYGREKDVLQAEKFTLEQTLAD---TRLDLEFKEEklaSLQRELEEMTfgGGTEEEFAQLRRSKNETER------- 1683
Cdd:pfam00038   89 QKYEDELNLRTSAENDLVGLRKDLDEatlARVDLEAKIE---SLKEELAFLK--KNHEEEVRELQAQVSDTQVnvemdaa 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1684 RAKEQEEELDEMAGQI-QLLEQAKLRLEMT----LETMRKEARRES---QQRDEELEEVRgngyKKIKALECQLETehee 1755
Cdd:pfam00038  164 RKLDLTSALAEIRAQYeEIAAKNREEAEEWyqskLEELQQAAARNGdalRSAKEEITELR----RTIQSLEIELQS---- 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116008016  1756 rtlLLREKHELERRLSSMEDRdrvdrdaeealnqkLRRDLRKYKALLKDAQTQLERLKADtpgktLIRQLR 1826
Cdd:pfam00038  236 ---LKKQKASLERQLAETEER--------------YELQLADYQELISELEAELQETRQE-----MARQLR 284
46 PHA02562
endonuclease subunit; Provisional
1815-2018 1.91e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.08  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1815 DTPGKTLIRQLRNQLEDAESARSLAM-----------KARQTAEAELTEVQAMFDEshrarndAEERANAAHRDRAELQA 1883
Cdd:PHA02562  169 DKLNKDKIRELNQQIQTLDMKIDHIQqqiktynknieEQRKKNGENIARKQNKYDE-------LVEEAKTIKAEIEELTD 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1884 QIEENEEElgelMKKYSATVKQLNTEQINVS--------EAEF------------KLNEMEAERNNLKEQVAELQHRLDN 1943
Cdd:PHA02562  242 ELLNLVMD----IEDPSAALNKLNTAAAKIKskieqfqkVIKMyekggvcptctqQISEGPDRITKIKDKLKELQHSLEK 317
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116008016 1944 VENLGDPSMAMMSKRLELRTK--ELESRLELEQATRARLEVQVNRHKEALEKLQNEVT--QSKMREMQAQDVIKKSQKS 2018
Cdd:PHA02562  318 LDTAIDELEEIMDEFNEQSKKllELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVdnAEELAKLQDELDKIVKTKS 396
Caldesmon pfam02029
Caldesmon;
1718-2053 2.21e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.93  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1718 KEARRESQQRDEElEEVRGNGYKKIKALECQLETEHEERTlllrekHELERRLSSMEDRDRvdrDAEEALNQKL-RRDLR 1796
Cdd:pfam02029    5 EEAARERRRRARE-ERRRQKEEEEPSGQVTESVEPNEHNS------YEEDSELKPSGQGGL---DEEEAFLDRTaKREER 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1797 KYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHR 1876
Cdd:pfam02029   75 RQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEE 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1877 DRAELQAQIEENEEELGELMKKYSATVKQLNTEqINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVEnlgDPSMAMMS 1956
Cdd:pfam02029  155 EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKE-KKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVT---TKRRQGGL 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1957 KRLELRTKELESRLELEQatraRLEVQVNRHKEALEKlqnEVTQSKMREMQAQ---DVIKKSQKSLRDMREEfhAVSSRE 2033
Cdd:pfam02029  231 SQSQEREEEAEVFLEAEQ----KLEELRRRRQEKESE---EFEKLRQKQQEAElelEELKKKREERRKLLEE--EEQRRK 301
                          330       340
                   ....*....|....*....|
gi 116008016  2034 QESLTRRKDLEKKVEQMESE 2053
Cdd:pfam02029  302 QEEAERKLREEEEKRRMKEE 321
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1958-2070 2.33e-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: 41.83  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1958 RLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMR--EEFHAVSsREQE 2035
Cdd:COG1579    21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQ-KEIE 99
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 116008016 2036 SLTRRKD---------------LEKKVEQMESEGAALKNDLRLALQRIAD 2070
Cdd:COG1579   100 SLKRRISdledeilelmerieeLEEELAELEAELAELEAELEEKKAELDE 149
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
1382-1850 2.34e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 43.09  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1382 HRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTA-----HIATERLEAETAErLKLEK 1456
Cdd:pfam05701   66 AQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQGIADEASVAakaqlEVAKARHAAAVAE-LKSVK 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1457 ELGDQTNK------------VKNLQETT----------EKLEMELICAKSDLNGISEDEDAENEDGVGGGVYK----LKY 1510
Cdd:pfam05701  145 EELESLRKeyaslvserdiaIKRAEEAVsaskeiektvEELTIELIATKESLESAHAAHLEAEEHRIGAALAReqdkLNW 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1511 ErvaRELEftkrrlhtQHEHDLEQL---VALKKHLEMKLSDAYEEVVEQRQ-----VVGQWKRKAQKMTNE---MNDLRM 1579
Cdd:pfam05701  225 E---KELK--------QAEEELQRLnqqLLSAKDLKSKLETASALLLDLKAelaayMESKLKEEADGEGNEkktSTSIQA 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1580 LLEeqNARNNLLEKKQ--RKFDAECQSLQDAVrqerqakerygrekdvlqaekftleqtlADTRLDLEFKEEKLASLQRe 1657
Cdd:pfam05701  294 ALA--SAKKELEEVKAniEKAKDEVNCLRVAA----------------------------ASLRSELEKEKAELASLRQ- 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1658 LEEMTFGGGTEEEfAQLRRSKNETE---RRAKEQEEELDEMAGQIQL----LEQAKLRLEMTLETMRKeARRESQQRDEE 1730
Cdd:pfam05701  343 REGMASIAVSSLE-AELNRTKSEIAlvqAKEKEAREKMVELPKQLQQaaqeAEEAKSLAQAAREELRK-AKEEAEQAKAA 420
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1731 LE--EVRGNGYKK---------------IKALEcqlETEHEER-----------TLLLREKHELERRLssmedrdrvdRD 1782
Cdd:pfam05701  421 AStvESRLEAVLKeieaakaseklalaaIKALQ---ESESSAEstnqedsprgvTLSLEEYYELSKRA----------HE 487
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116008016  1783 AEEALNQKLRRDLRKYKaLLKDAQTQ-LERLKAdtpgktLIRQLRNQLEDAESARSLAMKARQ---TAEAEL 1850
Cdd:pfam05701  488 AEELANKRVAEAVSQIE-EAKESELRsLEKLEE------VNREMEERKEALKIALEKAEKAKEgklAAEQEL 552
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1440-1763 2.36e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1440 ATERLEAETAERLKLEKELGDQTNKVKNLQETTEKLEmELICAKSDLNGISEDEdaenedgvgggvykLKYERVARELEf 1519
Cdd:COG4913   608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDE--------------IDVASAEREIA- 671
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1520 tkrrlhtQHEHDLEQLVALK---KHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQR 1596
Cdd:COG4913   672 -------ELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1597 KFDAEC------QSLQDAVrqERQAKERYGREKDVLQAEKFTLEQTLADTRL---------------------------- 1642
Cdd:COG4913   745 LELRALleerfaAALGDAV--ERELRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldadleslpeylalld 822
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1643 -----DLEFKEEKLASLQRELeemtfgggTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMT----- 1712
Cdd:COG4913   823 rleedGLPEYEERFKELLNEN--------SIEFVADLLSKLRRAIREIKERIDPLNDSLKRIPFGPGRYLRLEARprpdp 894
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 116008016 1713 ----LETMRKEARRESQQRDEELEEVRgngYKKIKALECQLETEHEERTLLLREK 1763
Cdd:COG4913   895 evreFRQELRAVTSGASLFDEELSEAR---FAALKRLIERLRSEEEESDRRWRAR 946
CCDC73 pfam15818
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...
1430-1830 3.54e-03

Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.


Pssm-ID: 464893 [Multi-domain]  Cd Length: 1048  Bit Score: 42.63  E-value: 3.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1430 LAEERSTAHIATERLEAETAERLKLEKELgdQTNKV---KNLQETTEKLEMELIcAKSD----LNGISEDEDA-ENEDGV 1501
Cdd:pfam15818   76 LEEEKGKYQLATEIKEKEIEGLKETLKAL--QVSKYslqKKVSEMEQKLQLHLL-AKEDhhkqLNEIEKYYATiTGQFGL 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1502 GGGVYKlKYERVARELEFTKRRLHTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQ----WKRKAQKMTNEMNDL 1577
Cdd:pfam15818  153 VKENHG-KLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKVTCQYKMGEeninLTIKEQKFQELQERL 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1578 RMLLE------EQNARnnLLEKKQRKFdAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKL 1651
Cdd:pfam15818  232 NMELElnkkinEEITH--IQEEKQDII-ISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKF 308
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1652 ASLQRELEEmtfgggteeefaQLRRSKNETErrakEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEEL 1731
Cdd:pfam15818  309 LNLQNEHEK------------ALGTWKKHVE----ELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNV 372
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1732 EEVRGNGYkkikalecQLETEHEERTLLLREKHELERRLSSMEDRdrvDRDAEEALNQKlRRDLRKYKALLKDAQTQLER 1811
Cdd:pfam15818  373 PEVNNENS--------EMSTEKSENLIIQKYNSEQEIREENTKSF---CSDTEYRETEK-KKGPPVEEIIIEDLQVLEKS 440
                          410
                   ....*....|....*....
gi 116008016  1812 LKADTpgKTLIRQLRNQLE 1830
Cdd:pfam15818  441 FKNEI--DTSVPQDKNQSE 457
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
1761-1884 4.00e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 39.54  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1761 REKHELERRLSSMEDRDRvdrDAEEALnQKLRRDLRKYKALLKDAQTQLER---LKADTpGKTLiRQLRNQLEDAESARS 1837
Cdd:pfam07926    1 AELSSLQSEIKRLKEEAA---DAEAQL-QKLQEDLEKQAEIAREAQQNYERelvLHAED-IKAL-QALREELNELKAEIA 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 116008016  1838 LAMKARQTAEAELTEVQAMFDEshrARNDAEERANAAHRDRAELQAQ 1884
Cdd:pfam07926   75 ELKAEAESAKAELEESEESWEE---QKKELEKELSELEKRIEDLNEQ 118
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
1552-1721 4.08e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 42.25  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1552 EVVEQRQVVGQWKRKAQKMTNEMN-DLRMLLEEQNARNNLLEKKQRKFDAE--CQSLQDAVRQER--QAKERYGREKDVL 1626
Cdd:pfam15709  356 EQEEQRRLQQEQLERAEKMREELElEQQRRFEEIRLRKQRLEEERQRQEEEerKQRLQLQAAQERarQQQEEFRRKLQEL 435
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1627 QAEKFT--LEQTLADTRLDLEFkEEKLASLQRELEEMTfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGqiqllEQ 1704
Cdd:pfam15709  436 QRKKQQeeAERAEAEKQRQKEL-EMQLAEEQKRLMEMA-----EEERLEYQRQKQEAEEKARLEAEERRQKEE-----EA 504
                          170
                   ....*....|....*..
gi 116008016  1705 AKLRLEMTLETMRKEAR 1721
Cdd:pfam15709  505 ARLALEEAMKQAQEQAR 521
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
1556-1814 4.73e-03

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: 41.56  E-value: 4.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1556 QRQVVGQW---KRKAQK--MTNEMNDLRMLLEEQNARNNLLEKKQRKFDaecqslqdavRQERQAKERygREKDVLQAEK 1630
Cdd:pfam15558   27 QQQAALAWeelRRRDQKrqETLERERRLLLQQSQEQWQAEKEQRKARLG----------REERRRADR--REKQVIEKES 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1631 FTLEQTladtrldlefkEEKLASLQRELEEmtfgggteeEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAklRLE 1710
Cdd:pfam15558   95 RWREQA-----------EDQENQRQEKLER---------ARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQE--RLE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1711 MTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHEL--ERRLSSMEDRDRVDRdaEEALN 1788
Cdd:pfam15558  153 EACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQRsqENYEQLVEERHRELR--EKAQK 230
                          250       260
                   ....*....|....*....|....*.
gi 116008016  1789 QKLRRDLRKYKALLKDAQTQlERLKA 1814
Cdd:pfam15558  231 EEEQFQRAKWRAEEKEEERQ-EHKEA 255
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1727-2074 4.98e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 4.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1727 RDEELEEVRgNGYKKIKALECQLE--TEHEERTLLLREKHELERRLSSMEDRDRvdrdaEEALNQKLRRDLRKYKALLKD 1804
Cdd:pfam13868    1 LRENSDELR-ELNSKLLAAKCNKErdAQIAEKKRIKAEEKEEERRLDEMMEEER-----ERALEEEEEKEEERKEERKRY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1805 AQtqlerlkadtpgktlirQLRNQLEDAESARSLA-MKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQA 1883
Cdd:pfam13868   75 RQ-----------------ELEEQIEEREQKRQEEyEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNE 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1884 QIEENEEELGELMKK-----YSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLgdpsmamMSKR 1958
Cdd:pfam13868  138 EQAEWKELEKEEEREederiLEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDEL-------RAKL 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1959 LELRTKELESRLELEQAT---RARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAvssREQE 2035
Cdd:pfam13868  211 YQEEQERKERQKEREEAEkkaRQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEK---RRMK 287
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 116008016  2036 SLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQA 2074
Cdd:pfam13868  288 RLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1577-1924 5.39e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 5.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1577 LRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKErygrEKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQR 1656
Cdd:COG4372    33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARS----ELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1657 ELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARReSQQRDEELEEVRG 1736
Cdd:COG4372   109 EAEEL------QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA-LEQELQALSEAEA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1737 NGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADT 1816
Cdd:COG4372   182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1817 PGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELM 1896
Cdd:COG4372   262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
                         330       340
                  ....*....|....*....|....*...
gi 116008016 1897 KKYSATVKQLNTEQINVSEAEFKLNEME 1924
Cdd:COG4372   342 LLQLLLVGLLDNDVLELLSKGAEAGVAD 369
PDZ7_MUPP1-PD6_PATJ-like cd06671
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ...
334-426 5.46e-03

PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of MUPP1 and PDZ domain 6 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467159 [Multi-domain]  Cd Length: 96  Bit Score: 38.07  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  334 PPRQLVIRRQksPRQDFGFSL---RKAICLDRTESLTSPIFRPVIfAEPGAGGGATGLLPGDRLIKVNGTPVGELPREII 410
Cdd:cd06671     1 PPRRVELWRE--PGKSLGISIvggRVMGSRLSNGEEIRGIFIKHV-LEDSPAGRNGTLKTGDRILEVNGVDLRNATHEEA 77
                          90
                  ....*....|....*.
gi 116008016  411 IEMIRNSGEAVTVEVQ 426
Cdd:cd06671    78 VEAIRNAGNPVVFLVQ 93
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1643-2071 5.75e-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: 41.93  E-value: 5.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1643 DLEFK--EEKLASLQRELEEmtfgggTEEEFAQLRRSKNETERRAKEQEEeldemagQIQLLEQAKLRL---EMTLETMR 1717
Cdd:TIGR04523   32 DTEEKqlEKKLKTIKNELKN------KEKELKNLDKNLNKDEEKINNSNN-------KIKILEQQIKDLndkLKKNKDKI 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1718 KEARRESQQRDEELEEVRGNGYKK---IKALECQLETEHEERTLLLREKHELERRLSSmedrdrvdrdaeeaLNQKLRrD 1794
Cdd:TIGR04523   99 NKLNSDLSKINSEIKNDKEQKNKLeveLNKLEKQKKENKKNIDKFLTEIKKKEKELEK--------------LNNKYN-D 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1795 LRKYKALLKDAQTQLERLKADTpgKTLIRQLRNQLedaeSARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAA 1874
Cdd:TIGR04523  164 LKKQKEELENELNLLEKEKLNI--QKNIDKIKNKL----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKK 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1875 HRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNN-------------------LKEQVA 1935
Cdd:TIGR04523  238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQlkseisdlnnqkeqdwnkeLKSELK 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1936 ELQHRLDNVENLGDPSMAMMSKrLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEvTQSKMREmqaqdvIKKS 2015
Cdd:TIGR04523  318 NQEKKLEEIQNQISQNNKIISQ-LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE-NQSYKQE------IKNL 389
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116008016  2016 QKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADL 2071
Cdd:TIGR04523  390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
1582-1762 6.16e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.86  E-value: 6.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1582 EEQNARNNLLE--KKQRKFDAECQSLQDAVRQERQ--AKERYGREKDVLQAEKFTLE------QTLADtrlDLEFK---- 1647
Cdd:PRK11448   58 PPCENQHDLLRrlGKEGFLPDEILDVFHKLRKIGNkaVHEFHGDHREALMGLKLAFRlavwfhRTYGK---DWDFKpgpf 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1648 ------EEKLASLQRELEEMtfgggtEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEAR 1721
Cdd:PRK11448  135 vppedpENLLHALQQEVLTL------KQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAA 208
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 116008016 1722 RESQQRDEELEEVRGNGYKKIKAlecqleTEHEERTLL---LRE 1762
Cdd:PRK11448  209 ETSQERKQKRKEITDQAAKRLEL------SEEETRILIdqqLRK 246
PRK12704 PRK12704
phosphodiesterase; Provisional
1622-1793 7.24e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 7.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1622 EKDVLQAEKfTLEQTLADTRLDLE-FKEEKLASLQRELEEMTfgGGTEEEFAQLRRSKNETERRAKEQEEELDEmagQIQ 1700
Cdd:PRK12704   30 EAKIKEAEE-EAKRILEEAKKEAEaIKKEALLEAKEEIHKLR--NEFEKELRERRNELQKLEKRLLQKEENLDR---KLE 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1701 LLEQAKLRLEM----------TLETMRKEARRESQQRDEELEEVRGngykkikalecqlETEHEERTLLLRE-KHELERR 1769
Cdd:PRK12704  104 LLEKREEELEKkekeleqkqqELEKKEEELEELIEEQLQELERISG-------------LTAEEAKEILLEKvEEEARHE 170
                         170       180       190
                  ....*....|....*....|....*....|
gi 116008016 1770 LSSM------EDRDRVDRDAEEALNQKLRR 1793
Cdd:PRK12704  171 AAVLikeieeEAKEEADKKAKEILAQAIQR 200
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1673-1885 7.55e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 7.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1673 QLRRSKNETERRAKEQEEELDEMAGQIQLLEQAklrlemtLETMRKearresQQRDEELEEVRGNGYKKIKALECQLETe 1752
Cdd:COG3206   165 NLELRREEARKALEFLEEQLPELRKELEEAEAA-------LEEFRQ------KNGLVDLSEEAKLLLQQLSELESQLAE- 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1753 heertlLLREKHELERRLSSMEDRDRVDRDAEEALNQKlrRDLRKYKALLKDAQTQLERLKAD-TPGKTLIRQLRNQLED 1831
Cdd:COG3206   231 ------ARAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARyTPNHPDVIALRAQIAA 302
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 116008016 1832 AESA-RSLAMKARQTAEAELTEVQAMFDESHRARNDAEERA---NAAHRDRAELQAQI 1885
Cdd:COG3206   303 LRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLaelPELEAELRRLEREV 360
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
1678-1817 7.71e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 41.17  E-value: 7.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1678 KNETERRAKeQEEELDEMAGQIQLLEQ--AKLRLEM-TLETMRKEARRESQQRDEELEEvRGNGYKK------------- 1741
Cdd:pfam05667  324 ETEEELQQQ-REEELEELQEQLEDLESsiQELEKEIkKLESSIKQVEEELEELKEQNEE-LEKQYKVkkktldllpdaee 401
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1742 -IKALEC----------QLETEHEE-RTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRR---DLRKYKALLKDAQ 1806
Cdd:pfam05667  402 nIAKLQAlvdasaqrlvELAGQWEKhRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEvaeEAKQKEELYKQLV 481
                          170
                   ....*....|.
gi 116008016  1807 TQLERLKADTP 1817
Cdd:pfam05667  482 AEYERLPKDVS 492
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1859-2116 7.74e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.26  E-value: 7.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1859 ESHRARNDAEERANAAHRDR----AELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEaefKLNEMEAERnnlKEQV 1934
Cdd:pfam17380  297 EQERLRQEKEEKAREVERRRkleeAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEE---RKRELERIR---QEEI 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  1935 AELQHRLDNVENLgdpSMAMMSKRLELRtKELES--RLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVI 2012
Cdd:pfam17380  371 AMEISRMRELERL---QMERQQKNERVR-QELEAarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR 446
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016  2013 KKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLAlQRIADLQQAMEEEGEEELSESDESLSS 2092
Cdd:pfam17380  447 EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE-KELEERKQAMIEEERKRKLLEKEMEER 525
                          250       260
                   ....*....|....*....|....
gi 116008016  2093 VGSISDLEDRlRPVHVKRSSQQSL 2116
Cdd:pfam17380  526 QKAIYEEERR-REAEEERRKQQEM 548
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
1641-1762 8.35e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.22  E-value: 8.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1641 RLDLEFKEEKLASLQRELEEMtfgggtEEEFAQLrrsKNETERRAKEQEEELDEmagqiqllEQAKLRLEMTLETMRKEA 1720
Cdd:COG0542   403 RMEIDSKPEELDELERRLEQL------EIEKEAL---KKEQDEASFERLAELRD--------ELAELEEELEALKARWEA 465
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 116008016 1721 RRESQQRDEELEEVRGNGYKKIKALECQL---ETEHEERTLLLRE 1762
Cdd:COG0542   466 EKELIEEIQELKEELEQRYGKIPELEKELaelEEELAELAPLLRE 510
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1958-2073 9.34e-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: 39.91  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116008016 1958 RLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEV--TQSKMREM-----QAQDVIKKSQKSLRDMR--EEFHA 2028
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELedLEKEIKRLeleieEVEARIKKYEEQLGNVRnnKEYEA 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 116008016 2029 VsSREQESLTRRK-DLEKKVEQMESEGAALKNDLRLALQRIADLQQ 2073
Cdd:COG1579    94 L-QKEIESLKRRIsDLEDEILELMERIEELEEELAELEAELAELEA 138
 
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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