NCBI Conserved Domain Search

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

848-1463

4.29e-20

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 97.43 E-value: 4.29e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    848 EIKNEEalkENLKLSMLLDREKSEKVKVQkELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIFNVLERKYNEQHKKVMK 927
Cdd:TIGR02168  217 ELKAEL---RELELALLVLRLEELREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    928 MNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLET 1007
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1008 ALEDEKARF--------------ARQNNTIGDMQKLISELNEKIARF--------DNIALNERNSTR----KIEREKEKL 1061
Cdd:TIGR02168  373 RLEELEEQLetlrskvaqlelqiASLNNEIERLEARLERLEDRRERLqqeieellKKLEEAELKELQaeleELEEELEEL 452

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1062 NEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMM------ADCVKELKDsHKERL------------- 1122
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQenlegfSEGVKALLK-NQSGLsgilgvlselisv 531

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1123 -KEMEQKVEDV--KRKNSKLENENSTQKSQIEtFQRESSVdsdyGRSS-------SGRLSTLGRQYSLTSIGSFSSIrTV 1192
Cdd:TIGR02168  532 dEGYEAAIEAAlgGRLQAVVVENLNAAKKAIA-FLKQNEL----GRVTflpldsiKGTEIQGNDREILKNIEGFLGV-AK 605

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1193 GLGSRKDSISDMTSSMYSL------------RRRDSTYDMTSST-----------IGLQRSPSTSQVMEKERRILELEKE 1249
Cdd:TIGR02168  606 DLVKFDPKLRKALSYLLGGvlvvddldnaleLAKKLRPGYRIVTldgdlvrpggvITGGSAKTNSSILERRREIEELEEK 685

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1250 KAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKNADNLALR---LKKALADCDEWKKK 1326
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqLSKELTELEAEIEE 765

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1327 HEESIVESKTEIL-MERKRAMDRAEACEKETELKQSRmATIESARMELG-----------------GELARTQSELDRCR 1388
Cdd:TIGR02168  766 LEERLEEAEEELAeAEAEIEELEAQIEQLKEELKALR-EALDELRAELTllneeaanlrerlesleRRIAATERRLEDLE 844

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1389 QIIIQLEENLKSQESLGNSFGRHQTNLNFEIE---NLRDENCALKAKIRRQY------------KQIELLTQQDETNDEL 1453
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEallNERASLEEALALLRSELeelseelrelesKRSELRRELEELREKL 924

                          730
                   ....*....|
gi 32566156   1454 NHFENKVERL 1463
Cdd:TIGR02168  925 AQLELRLEGL 934

PRK03918

DNA double-strand break repair ATPase Rad50;

824-1370

1.07e-17

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 89.35 E-value: 1.07e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   824 NRDKERIEELENEKLKLEEEIQEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQgREKLLEKEREFRKTMEE 903
Cdd:PRK03918  175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL-KEEIEELEKELESLEGS 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   904 MEQNEEIFNVLERKYNEQHKKvmkmndvLREYERKIEQLNmEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDE 983
Cdd:PRK03918  254 KRKLEEKIRELEERIEELKKE-------IEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   984 LQNQIQKLSDENNEQRlTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNE-RNSTRKIEREKEKLN 1062
Cdd:PRK03918  326 IEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEIE 404

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1063 EELTTAKEIIQKQAKKIDELK---EECRKRKNEASRLERKL--EDKEAMMADCVKELKDSHKErLKEMEQKVEDVKRKNS 1137
Cdd:PRK03918  405 EEISKITARIGELKKEIKELKkaiEELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEKE-LKEIEEKERKLRKELR 483

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1138 KLENENSTQK---SQIETFQRESSVDSDYGRSSSGRLSTLGRQYSLT---SIGSFSSIRtvGLGSRKDSISDMTSSMYSL 1211
Cdd:PRK03918  484 ELEKVLKKESeliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLkekLIKLKGEIK--SLKKELEKLEELKKKLAEL 561

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1212 RRR-DSTYDMTSSTIGLQRSPSTSQVMEKERRILELEK------EKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTA 1284
Cdd:PRK03918  562 EKKlDELEEELAELLKELEELGFESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1285 NRKQSNQLQETTRQLNSAQ-KNADNLALRLKKALADCDEWKKKHEESI--VESKTEILMERKRAMDRAeacEKETELKQS 1361
Cdd:PRK03918  642 LEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRReeIKKTLEKLKEELEEREKA---KKELEKLEK 718


                  ....*....
gi 32566156  1362 RMATIESAR 1370
Cdd:PRK03918  719 ALERVEELR 727

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

844-1399

8.66e-15

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: 80.22 E-value: 8.66e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    844 IQEMEIKNEEALKENLKLsmlldreKSEKVKVQKELEEVEKQ------GREKL-LEK---EREFRKTMEEMEQNEEIFNV 913
Cdd:pfam01576   77 LHELESRLEEEEERSQQL-------QNEKKKMQQHIQDLEEQldeeeaARQKLqLEKvttEAKIKKLEEDILLLEDQNSK 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    914 LERKYNEQHKKVMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSD 993
Cdd:pfam01576  150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQA 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    994 ENNEQRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQ 1073
Cdd:pfam01576  230 QIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE 309

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1074 KQAKKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETF 1153
Cdd:pfam01576  310 DTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAEL 389

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1154 QRE-SSVDSDYGRSSSGRLSTLGRQYSLTSIGSFSSIRTVGLGSRkdsISDMTSSMYSLrrrdstydmtsstiglqrsps 1232
Cdd:pfam01576  390 QAElRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEK---LSKLQSELESV--------------------- 445

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1233 TSQVMEKERRILELEKEKAAINTDLQLVKRELD-------VYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQkn 1305
Cdd:pfam01576  446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQeetrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQ-- 523

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1306 adnlalrlkkalADCDEWKKKHEE--SIVESKTEilmERKRAMDRAEACEKETELKQSRMATIESARMELGGELARTQSE 1383
Cdd:pfam01576  524 ------------AQLSDMKKKLEEdaGTLEALEE---GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVD 588

                          570
                   ....*....|....*.
gi 32566156   1384 LDRCRQIIIQLEENLK 1399
Cdd:pfam01576  589 LDHQRQLVSNLEKKQK 604

Smc

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

889-1156

6.18e-13

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 6.18e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  889 KLLEKEREFRKTMEEMEQNeeifnvLERkyneqhkkvmkMNDVLREYERKIEQLNMEKTDLEnENQKLRETQNRQDSHYS 968
Cdd:COG1196  169 KYKERKEEAERKLEATEEN------LER-----------LEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELL 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  969 NLEKEVMEKSslIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNER 1048
Cdd:COG1196  231 LLKLRELEAE--LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1049 NSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMAdcvkELKDSHKERLKEMEQK 1128
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL----EAEAELAEAEEELEEL 384

                        250       260
                 ....*....|....*....|....*...
gi 32566156 1129 VEDVKRKNSKLENENSTQKSQIETFQRE 1156
Cdd:COG1196  385 AEELLEALRAAAELAAQLEELEEAEEAL 412

PspC_subgroup_1

NF033838

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...

951-1350

8.32e-06

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.

Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 50.40 E-value: 8.32e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   951 NENQKlrETQNRQDSHYSNLEKEVMEKSSLIDELQNQ--IQKLSDENNEQRLTIAKLETALEDEKarfarqnntigdMQK 1028
Cdd:NF033838   53 NESQK--EHAKEVESHLEKILSEIQKSLDKRKHTQNValNKKLSDIKTEYLYELNVLKEKSEAEL------------TSK 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1029 LISELNEKIARFdnialnernstrkiEREKEKLNEELTTAKEIIQKQAKKIDELKEECRK-------RKNEASRLERKLE 1101
Cdd:NF033838  119 TKKELDAAFEQF--------------KKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRnyptntyKTLELEIAESDVE 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1102 DKEAMMADCVKELKDSH-KERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSVDSDYGRSSSGRLSTLGRQYSL 1180
Cdd:NF033838  185 VKKAELELVKEEAKEPRdEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRR 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1181 TSIGSfssirtVGLGSRKD-SISDMTSSmyslrrrdstydmtSSTIGLQRSPSTSQ-----VMEKERRILELEKeKA--- 1251
Cdd:NF033838  265 AKRGV------LGEPATPDkKENDAKSS--------------DSSVGEETLPSPSLkpekkVAEAEKKVEEAKK-KAkdq 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1252 --------AINT----DLQLVKRELDVYKSQLSAVESEKEslQTANRKQSNQLQETTRqlnsaQKNADnlALRLKKALAD 1319
Cdd:NF033838  324 keedrrnyPTNTyktlELEIAESDVKVKEAELELVKEEAK--EPRNEEKIKQAKAKVE-----SKKAE--ATRLEKIKTD 394

                         410       420       430
                  ....*....|....*....|....*....|.
gi 32566156  1320 cdewKKKHEEsivESKTEILMERKRAMDRAE 1350
Cdd:NF033838  395 ----RKKAEE---EAKRKAAEEDKVKEKPAE 418

Spc7

smart00787

Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...

887-1018

4.58e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.

Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 4.58e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156     887 REKLLEKERE-FRKTMEEMEQNEEIFNVLERKYNEQHKKVMKMNDVLreyERKIEQLNMEKTDLENENQKLretQNRQDS 965
Cdd:smart00787  138 RMKLLEGLKEgLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDAL---EEELRQLKQLEDELEDCDPTE---LDRAKE 211

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 32566156     966 HYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFAR 1018
Cdd:smart00787  212 KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264

Name

Accession

Description

Interval

E-value

MYSc_class_II

cd01377

class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...

97-747

0e+00

Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 956.14 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQ--NDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd01377    1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKrrEEMPPHIFAIADNAYRNMLQDRENQSILITG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFILSSSVSN----------NTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLI 244
Cdd:cd01377   81 ESGAGKTENTKKVIQYLASVAASSkkkkesgkkkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  245 GAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSfLKLSKKVNEYKYLRN---DDSMIDDAETAKMTDEAFTR 321
Cdd:cd01377  161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEK-LLLTGDPSYYFFLSQgelTIDGVDDAEEFKLTDEAFDI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  322 IGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLA 401
Cdd:cd01377  240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  402 KTLSSASAMAKILYERLFGWIVKRCNDAFSvddteSTCRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFM 481
Cdd:cd01377  320 QVVFSVGALAKALYERLFLWLVKRINKTLD-----TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHM 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  482 FAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKP-MGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKskQTQKCS 560
Cdd:cd01377  395 FVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFK--KPKPKK 472

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  561 TIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPV---PVNNLKTRRGTITNSTVSFLYKNQL 637
Cdd:cd01377  473 SEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYeesGGGGGKKKKKGGSFRTVSQLHKEQL 552

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  638 QCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKGA 717
Cdd:cd01377  553 NKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD 632

                        650       660       670
                 ....*....|....*....|....*....|
gi 32566156  718 SEKEKCTLICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd01377  633 DGKAACEKILKALQLDPELYRIGNTKVFFK 662

MYSc

smart00242

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...

78-759

0e+00

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: 876.87 E-value: 0e+00

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156      78 VPSLNNYSEDLCTLTQPNAATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQ--LQNDLPPHVYSVAQ 155
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRgkSRGELPPHVFAIAD 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156     156 NAFHGILKGGRNQSILITGESGAGKTENTKKIIDFILSSSVSN---NTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKF 232
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNtevGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKF 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156     233 IRIEFDENSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYfDNPHKSFLKLsKKVNEYKYLRN----DDSMIDD 308
Cdd:smart00242  161 IEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGA-SEELKKELGL-KSPEDYRYLNQggclTVDGIDD 238

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156     309 AETAKMTDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDV-SFVESMQEVDNIAELLEMKSSKLVDALTQPTI 387
Cdd:smart00242  239 AEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAaSTVKDKEELSNAAELLGVDPEELEKALTKRKI 318

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156     388 KVHDKLIRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTEStcrlsRFIAVLDIAGFEIIEKNSFEQFCIN 467
Cdd:smart00242  319 KTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGST-----YFIGVLDIYGFEIFEVNSFEQLCIN 393

                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156     468 YTNEKLQQFFNHFMFAKEQSDYLEEGIKWTQVNFANHlQPTIDLIE-KPMGILSFLEEECVVPNGSEKSLLEKLCSNLSN 546
Cdd:smart00242  394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDN-QDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKK 472

                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156     547 DSSFKKSKQtqkcSTIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNLKTRRGTitn 626
Cdd:smart00242  473 HPHFSKPKK----KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSKKRFQ--- 545

                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156     627 sTVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSL 706
Cdd:smart00242  546 -TVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRV 624

                           650       660       670       680       690
                    ....*....|....*....|....*....|....*....|....*....|...
gi 32566156     707 LMKNKEQSKGASEKEKCTLICQDAQVRKERYAVGKTKLFCKVGVISELETKRN 759
Cdd:smart00242  625 LLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677

Myosin_head

pfam00063

Myosin head (motor domain);

86-747

0e+00

Myosin head (motor domain);

Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 723.69 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156     86 EDLCTLTQPNAATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILK 163
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYrgKRRGELPPHIFAIADEAYRSMLQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    164 GGRNQSILITGESGAGKTENTKKIIDFILSSSVSNN-----TIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFD 238
Cdd:pfam00063   82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSagnvgRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQFD 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    239 ENSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNyFDNPHKSFLKLSKkVNEYKYLRNDDSM----IDDAETAKM 314
Cdd:pfam00063  162 AKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAG-ASAQLKKELRLTN-PKDYHYLSQSGCYtidgIDDSEEFKI 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    315 TDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLI 394
Cdd:pfam00063  240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETV 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    395 RKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTEStcrlSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQ 474
Cdd:pfam00063  320 SKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEK----ASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQ 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    475 QFFNHFMFAKEQSDYLEEGIKWTQVNFANhLQPTIDLIE-KPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKS 553
Cdd:pfam00063  396 QFFNHHMFKLEQEEYVREGIEWTFIDFGD-NQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKP 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    554 KQTQKcstiRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPV--------NNLKTRRGTIT 625
Cdd:pfam00063  475 RLQGE----THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETaesaaaneSGKSTPKRTKK 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    626 NS--TVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIER 703
Cdd:pfam00063  551 KRfiTVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQR 630

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 32566156    704 YSLLMKNKEQSKGASEKEKCTLICQDAQVRKERYAVGKTKLFCK 747
Cdd:pfam00063  631 YRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674

MYSc

cd00124

Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...

97-747

0e+00

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: 722.84 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY---QLQNDLPPHVYSVAQNAFHGILKGGRNQSILIT 173
Cdd:cd00124    1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYrgkGRSADLPPHVFAVADAAYRAMLRDGQNQSILIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  174 GESGAGKTENTKKIIDFILS--------SSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIG 245
Cdd:cd00124   81 GESGAGKTETTKLVLKYLAAlsgsgsskSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  246 AKIECYLLEKSRVVFQSDGDRNFHIFYQMLSN--------YFDNPHKSFLKLSKKVNEYKYLRNDDsmIDDAETAKMTDE 317
Cdd:cd00124  161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGlsdgareeLKLELLLSYYYLNDYLNSSGCDRIDG--VDDAEEFQELLD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  318 AFTRIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVE--SMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIR 395
Cdd:cd00124  239 ALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEvaDDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETIT 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  396 KNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTESTCRlsrFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQ 475
Cdd:cd00124  319 KPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAESTS---FIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  476 FFNHFMFAKEQSDYLEEGIKWTQVNFANHlQPTIDLIE-KPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSK 554
Cdd:cd00124  396 FFNQHVFKLEQEEYEEEGIDWSFIDFPDN-QDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKK 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  555 QTQKCstirHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHpllkllfppvpvnnlktrrgtitnstvsflYK 634
Cdd:cd00124  475 RKAKL----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------FR 520

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  635 NQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQS 714
Cdd:cd00124  521 SQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEK 600

                        650       660       670
                 ....*....|....*....|....*....|...
gi 32566156  715 KGASEKEKCTLICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd00124  601 ASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633

COG5022

Myosin heavy chain [General function prediction only];

86-1344

0e+00

Myosin heavy chain [General function prediction only];

Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 674.87 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   86 EDLCTLTQPNAATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQN--DLPPHVYSVAQNAFHGILK 163
Cdd:COG5022   69 DDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNrlELEPHVFAIAEEAYRNLLS 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  164 GGRNQSILITGESGAGKTENTKKIIDFILSSSVSNNT----IGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDE 239
Cdd:COG5022  149 EKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVeissIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDE 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  240 NSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNyfDNPHKSFLKLSKKVNEYKYLR--NDDSM--IDDAETAKMT 315
Cdd:COG5022  229 NGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAG--DPEELKKLLLLQNPKDYIYLSqgGCDKIdgIDDAKEFKIT 306

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  316 DEAFTRIGLSEEEKIWIFQILSAVLWIGDIKFGE-RSGldVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLI 394
Cdd:COG5022  307 LDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEdRNG--AAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWI 384

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  395 RKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDafSVDDTESTcrlSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQ 474
Cdd:COG5022  385 VVPLNLEQALAIRDSLAKALYSNLFDWIVDRINK--SLDHSAAA---SNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQ 459

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  475 QFFNHFMFAKEQSDYLEEGIKWTQVNFaNHLQPTIDLIEK--PMGILSFLEEECVVPNGSEKSLLEKLCS--NLSNDSSF 550
Cdd:COG5022  460 QFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKF 538

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  551 KKSKQTQKcstirHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFpPVPVNNLKTRRgtitNSTVS 630
Cdd:COG5022  539 KKSRFRDN-----KFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLF-DDEENIESKGR----FPTLG 608

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  631 FLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKN 710
Cdd:COG5022  609 SRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPS 688

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  711 K----EQSKGASEKEKCTLICQDAQVRKERYAVGKTKLFCKVGVISELETKRNNYISSFIILIQANIRYLNIQKDLIERR 786
Cdd:COG5022  689 KswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQAL 768

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  787 KKLEAVVTIQDNVRQFAELSQWPWYRIYHLTRGLIPRNRDKERIEELENEKLKLEEEIQEMEIKNEEALKENLKLSMLLD 866
Cdd:COG5022  769 KRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLI 848

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  867 REKSEKVKVQKELEEVEK-----QGREKLLEKEREFRKTMEEM-------EQNEEIFNVLERKYNEQHKKVMKMNDVLRE 934
Cdd:COG5022  849 QKFGRSLKAKKRFSLLKKetiylQSAQRVELAERQLQELKIDVksisslkLVNLELESEIIELKKSLSSDLIENLEFKTE 928

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  935 YERKIEQLNME---KTDLENENQKLRETQNRQDSHySNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLeTALED 1011
Cdd:COG5022  929 LIARLKKLLNNidlEEGPSIEYVKLPELNKLHEVE-SKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL-AELSK 1006

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1012 EKARFARQNNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKN 1091
Cdd:COG5022 1007 QYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQL 1086

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1092 EASR-LERKLEDKEAMMADcVKELKDSHKE--------RLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSVDSD 1162
Cdd:COG5022 1087 ESTEnLLKTINVKDLEVTN-RNLVKPANVLqfivaqmiKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANL 1165

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1163 YGRSSSGRLSTLGRQ-------YSLTSIGSFSSIRTVglgsrKDSISDMTSSMYSLrrrDSTYDMTSSTIGLQRSPSTSQ 1235
Cdd:COG5022 1166 EALPSPPPFAALSEKrlyqsalYDEKSKLSSSEVNDL-----KNELIALFSKIFSG---WPRGDKLKKLISEGWVPTEYS 1237

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1236 VMEKERRILELEKEKAAINTDLQLVKRELDVYKSqLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKNADNL--ALRL 1313
Cdd:COG5022 1238 TSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNL-LSSYKLEEEVLPATINSLLQYINVGLFNALRTKASSLRWksATEV 1316

                       1290      1300      1310
                 ....*....|....*....|....*....|.
gi 32566156 1314 KKALADCDEWKKKHEESIVESKTEILMERKR 1344
Cdd:COG5022 1317 NYNSEELDDWCREFEISDVDEELEELIQAVK 1347

MYSc_Myo5

cd01380

class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...

99-745

0e+00

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: 578.34 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   99 VLNALKIRYT-SNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQN--DLPPHVYSVAQNAFHGILKGGRNQSILITGE 175
Cdd:cd01380    3 VLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNmgELDPHIFAIAEEAYRQMARDEKNQSIIVSGE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  176 SGAGKTENTKKIIDFILS---SSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYL 252
Cdd:cd01380   83 SGAGKTVSAKYAMRYFATvggSSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  253 LEKSRVVFQSDGDRNFHIFYQMLSNYfDNPHKSFLKLSKKvNEYKYLRNDDSM----IDDAETAKMTDEAFTRIGLSEEE 328
Cdd:cd01380  163 LEKSRVVFQAEEERNYHIFYQLCAAA-SLPELKELHLGSA-EDFFYTNQGGSPvidgVDDAAEFEETRKALTLLGISEEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  329 KIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLSSAS 408
Cdd:cd01380  241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  409 AMAKILYERLFGWIVKRCNDAFsvdDTESTCRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSD 488
Cdd:cd01380  321 ALAKHIYAQLFDWIVDRINKAL---ASPVKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEE 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  489 YLEEGIKWTQVNFANHlQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSS--FKKSKQTQKcstirHFY 566
Cdd:cd01380  398 YVKEEIEWSFIDFYDN-QPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNT-----AFI 471

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  567 VQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSThpllkllfppvpvNNLKtrrgtitnsTVSFLYKNQLQCLLDTLNS 646
Cdd:cd01380  472 VKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASK-------------NRKK---------TVGSQFRDSLILLMETLNS 529

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  647 SSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKGASEKEKCTLI 726
Cdd:cd01380  530 TTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKTCENIL 609

                        650       660
                 ....*....|....*....|..
gi 32566156  727 C---QDaqvrKERYAVGKTKLF 745
Cdd:cd01380  610 EnliLD----PDKYQFGKTKIF 627

MYSc_Myo8

cd01383

class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...

99-745

0e+00

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: 578.12 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   99 VLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQNDLPPHVYSVAQNAFHGILKGGRNQSILITGESGA 178
Cdd:cd01383    3 VLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDSPHVYAVADTAYREMMRDEINQSIIISGESGA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  179 GKTENTKKIIDFILSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYLLEKSRV 258
Cdd:cd01383   83 GKTETAKIAMQYLAALGGGSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLEKSRV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  259 VFQSDGDRNFHIFYQMLSNYfDNPHKSFLKLsKKVNEYKYLRNDDSM----IDDAETAKMTDEAFTRIGLSEEEKIWIFQ 334
Cdd:cd01383  163 VQLANGERSYHIFYQLCAGA-SPALREKLNL-KSASEYKYLNQSNCLtidgVDDAKKFHELKEALDTVGISKEDQEHIFQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  335 ILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLSSASAMAKIL 414
Cdd:cd01383  241 MLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDALAKAI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  415 YERLFGWIVKRCNDAFSVDDTEStcrlSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSDYLEEGI 494
Cdd:cd01383  321 YASLFDWLVEQINKSLEVGKRRT----GRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDGI 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  495 KWTQVNFANHlQPTIDLIE-KPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQkcstirhFYVQHYAGE 573
Cdd:cd01383  397 DWTKVDFEDN-QECLDLIEkKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGERGGA-------FTIRHYAGE 468

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  574 VHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLL------FPPVPVNNLKTRRGTITNSTVSFLYKNQLQCLLDTLNSS 647
Cdd:cd01383  469 VTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFaskmldASRKALPLTKASGSDSQKQSVATKFKGQLFKLMQRLENT 548

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  648 SAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMknKEQSKGASEK-EKCTLI 726
Cdd:cd01383  549 TPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLL--PEDVSASQDPlSTSVAI 626

                        650
                 ....*....|....*....
gi 32566156  727 CQDAQVRKERYAVGKTKLF 745
Cdd:cd01383  627 LQQFNILPEMYQVGYTKLF 645

MYSc_Myh1_insects_crustaceans

cd14909

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...

97-745

0e+00

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: 569.09 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd14909    1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYrgKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFILS---------SSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIG 245
Cdd:cd14909   81 ESGAGKTENTKKVIAYFATvgaskktdeAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  246 AKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPhKSFLKLSKKVNEYKYLRNDDSMI---DDAETAKMTDEAFTRI 322
Cdd:cd14909  161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGV-KEMCLLSDNIYDYYIVSQGKVTVpnvDDGEEFSLTDQAFDIL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  323 GLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAK 402
Cdd:cd14909  240 GFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQ 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  403 TLSSASAMAKILYERLFGWIVKRCNDAFsvdDTEStcRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMF 482
Cdd:cd14909  320 VTNSIGALCKGVFDRLFKWLVKKCNETL---DTQQ--KRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  483 AKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCSN-LSNDSSFKKSKQTQKCST 561
Cdd:cd14909  395 VLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNThLGKSAPFQKPKPPKPGQQ 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  562 IRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNN-----LKTRRGTITN--STVSFLYK 634
Cdd:cd14909  475 AAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSgggeqAKGGRGKKGGgfATVSSAYK 554

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  635 NQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLmkNKEQS 714
Cdd:cd14909  555 EQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKIL--NPAGI 632

                        650       660       670
                 ....*....|....*....|....*....|..
gi 32566156  715 KGASEKEKCTLICQDA-QVRKERYAVGKTKLF 745
Cdd:cd14909  633 QGEEDPKKAAEIILESiALDPDQYRLGHTKVF 664

MYSc_Myh16

cd14934

class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...

97-745

6.35e-180

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: 550.79 E-value: 6.35e-180

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQ--LQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd14934    1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKgkKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFILS-------SSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAK 247
Cdd:cd14934   81 ESGAGKTENTKKVIQYFANiggtgkqSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  248 IECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLkLSKKVNEYKYLRNDDSMI---DDAETAKMTDEAFTRIGL 324
Cdd:cd14934  161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLL-LVPNPKEYHWVSQGVTVVdnmDDGEELQITDVAFDVLGF 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  325 SEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTL 404
Cdd:cd14934  240 SAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCN 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  405 SSASAMAKILYERLFGWIVKRCNDAFsvdDTESTCRLsrFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAK 484
Cdd:cd14934  320 NSIGALGKAVYDKMFKWLVVRINKTL---DTKMQRQF--FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVL 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  485 EQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCSN-LSNDSSFKKSKQTQKCSTIR 563
Cdd:cd14934  395 EQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNhLGKSSNFLKPKGGKGKGPEA 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  564 HFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFP--PVPVNNLKTRRGTiTNSTVSFLYKNQLQCLL 641
Cdd:cd14934  475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKeeEAPAGSKKQKRGS-SFMTVSNFYREQLNKLM 553

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  642 DTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKGASEKE 721
Cdd:cd14934  554 TTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFVDNKK 633

                        650       660
                 ....*....|....*....|....
gi 32566156  722 KCTLICQDAQVRKERYAVGKTKLF 745
Cdd:cd14934  634 ASELLLGSIDLDVNEYKIGHTKVF 657

MYSc_Myo22

cd14883

class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...

98-747

8.38e-180

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: 550.77 E-value: 8.38e-180

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   98 TVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQ--NDLPPHVYSVAQNAFHGILKGGRNQSILITGE 175
Cdd:cd14883    2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKrmGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  176 SGAGKTENTKKIIDFIlsSSVSNNT--IGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYLL 253
Cdd:cd14883   82 SGAGKTETTKLILQYL--CAVTNNHswVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  254 EKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLKLSKKVNEYKYLRNDDSM-IDDAETAKMTDE---AFTRIGLSEEEK 329
Cdd:cd14883  160 EQSRITFQAPGERNYHVFYQLLAGAKHSKELKEKLKLGEPEDYHYLNQSGCIrIDNINDKKDFDHlrlAMNVLGIPEEMQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  330 IWIFQILSAVLWIGDIKF----GERSGLDvsfVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLS 405
Cdd:cd14883  240 EGIFSVLSAILHLGNLTFedidGETGALT---VEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARD 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  406 SASAMAKILYERLFGWIVKRCNDAFSVDDTEstcrlSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKE 485
Cdd:cd14883  317 NRDAMAKALYSRTFAWLVNHINSCTNPGQKN-----SRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLE 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  486 QSDYLEEGIKWTQVNFANHlQPTIDLIEK-PMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKCSTirh 564
Cdd:cd14883  392 QEEYEKEGINWSHIVFTDN-QECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTE--- 467

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  565 FYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFppVPVNNLKTRRGTITNS-------------TVSF 631
Cdd:cd14883  468 FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELF--TYPDLLALTGLSISLGgdttsrgtskgkpTVGD 545

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  632 LYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNK 711
Cdd:cd14883  546 TFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRA 625

                        650       660       670
                 ....*....|....*....|....*....|....*.
gi 32566156  712 EQSKGASEKEKCTLICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14883  626 RSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661

MYSc_Myh2_insects_mollusks

cd14911

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...

97-745

5.49e-179

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: 549.20 E-value: 5.49e-179

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQ--LQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd14911    1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKgiKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFIL--------SSSVSNNTIGDCVVTSGVL----------LEAMGNARTTHNSNSSRFGKFIRIE 236
Cdd:cd14911   81 ESGAGKTENTKKVIQFLAyvaaskpkGSGAVPHPAVNPAVLIGELeqqllqanpiLEAFGNAKTVKNDNSSRFGKFIRIN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  237 FDENSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLKLSKKvnEYKYLRNDDSM---IDDAETAK 313
Cdd:cd14911  161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVK--SYAFLSNGSLPvpgVDDYAEFQ 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  314 MTDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKL 393
Cdd:cd14911  239 ATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDF 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  394 IRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDafSVDDTEStcRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKL 473
Cdd:cd14911  319 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINR--SLDRTKR--QGASFIGILDMAGFEIFELNSFEQLCINYTNEKL 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  474 QQFFNHFMFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKS 553
Cdd:cd14911  395 QQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKT 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  554 kqtqKCSTIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNL------------KTRR 621
Cdd:cd14911  475 ----DFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMaqqaltdtqfgaRTRK 550

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  622 GTItnSTVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFI 701
Cdd:cd14911  551 GMF--RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 628

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....
gi 32566156  702 ERYSLLMKNKEQSKGASEKEKCTLICQDAQVRKERYAVGKTKLF 745
Cdd:cd14911  629 QRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIF 672

MYSc_Myo7

cd01381

class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...

97-747

1.66e-178

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: 546.85 E-value: 1.66e-178

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQN--DLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd01381    1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKigELPPHIFAIADNAYTNMKRNKRDQCVVISG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFILSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYLLE 254
Cdd:cd01381   81 ESGAGKTESTKLILQYLAAISGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  255 KSRVVFQSDGDRNFHIFYQMLSNyFDNPHKSFLKLSKKvNEYKYLRNDDSM----IDDAETAKMTDEAFTRIGLSEEEkI 330
Cdd:cd01381  161 KSRIVSQAPDERNYHIFYCMLAG-LSAEEKKKLELGDA-SDYYYLTQGNCLtcegRDDAAEFADIRSAMKVLMFTDEE-I 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  331 W-IFQILSAVLWIGDIKF--GERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLSSA 407
Cdd:cd01381  238 WdIFKLLAAILHLGNIKFeaTVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVR 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  408 SAMAKILYERLFGWIVKRCNDAFSVDDTESTCRLSrfIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQS 487
Cdd:cd01381  318 DAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSRTS--IGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQE 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  488 DYLEEGIKWTQVNFANHlQPTIDLI-EKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKcstiRHFY 566
Cdd:cd01381  396 EYDKEGINWQHIEFVDN-QDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLN----TSFG 470

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  567 VQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNLKTRRGTItnsTVSFLYKNQLQCLLDTLNS 646
Cdd:cd01381  471 INHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKSP---TLSSQFRKSLDQLMKTLSA 547

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  647 SSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKGASEKEKCTLI 726
Cdd:cd01381  548 CQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKI 627

                        650       660
                 ....*....|....*....|.
gi 32566156  727 CQDAQVRKERYAVGKTKLFCK 747
Cdd:cd01381  628 CCAVLGGDADYQLGKTKIFLK 648

MYSc_Myh7b

cd14927

class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...

97-747

4.52e-178

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: 546.86 E-value: 4.52e-178

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQ--LQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd14927    1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKgkRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFI-----LSSSVSNNTIGDCVVTSGVL----------LEAMGNARTTHNSNSSRFGKFIRIEFDE 239
Cdd:cd14927   81 ESGAGKTVNTKRVIQYFaivaaLGDGPGKKAQFLATKTGGTLedqiieanpaMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  240 NSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNyfdnpHKSFLK--LSKKVNEYKY------LRNDDSMiDDAET 311
Cdd:cd14927  161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSG-----KKPELQdmLLVSMNPYDYhfcsqgVTTVDNM-DDGEE 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  312 AKMTDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHD 391
Cdd:cd14927  235 LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGN 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  392 KLIRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAFSVddtestcRLSR--FIAVLDIAGFEIIEKNSFEQFCINYT 469
Cdd:cd14927  315 EYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDT-------KLPRqfFIGVLDIAGFEIFEFNSFEQLCINFT 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  470 NEKLQQFFNHFMFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCSN-LSNDS 548
Cdd:cd14927  388 NEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNhLGKSP 467

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  549 SFKKSKQTQKCSTIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPV--------PVNNLKTR 620
Cdd:cd14927  468 NFQKPRPDKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYvgsdstedPKSGVKEK 547

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  621 RGTITN-STVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSE 699
Cdd:cd14927  548 RKKAASfQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAD 627

                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....
gi 32566156  700 FIERYSLLMKNK------EQSKGASEKEKCTLicqdaQVRKERYAVGKTKLFCK 747
Cdd:cd14927  628 FKQRYRILNPSAipddkfVDSRKATEKLLGSL-----DIDHTQYQFGHTKVFFK 676

MYSc_Myo1

cd01378

class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...

103-747

8.01e-177

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: 542.52 E-value: 8.01e-177

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  103 LKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQNDL--PPHVYSVAQNAFHGILKGGRNQSILITGESGAGK 180
Cdd:cd01378    7 LKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYevPPHVFALADSAYRNMKSEKENQCVIISGESGAGK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  181 TENTKKIIDFIlsSSVSNNT------IGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYLLE 254
Cdd:cd01378   87 TEASKRIMQYI--AAVSGGSeseverVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLE 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  255 KSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFlKLSKKVNEYKYLRN---DDSMIDDAETAKMTDEAFTRIGLSEEEKIW 331
Cdd:cd01378  165 KSRVVGQIKGERNFHIFYQLLKGASQEYLQEL-GLQRPEQYYYYSKSgcfDVDGIDDAADFKEVLNAMKVIGFTEEEQDS 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  332 IFQILSAVLWIGDIKFGERSGLDVSfVESMQEVDNIAELLEMKSSKLVDALTQPTIKV---HDKLIRKNQNLAKTLSSAS 408
Cdd:cd01378  244 IFRILAAILHLGNIQFAEDEEGNAA-ISDTSVLDFVAYLLGVDPDQLEKALTHRTIETgggGRSVYEVPLNVEQAAYARD 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  409 AMAKILYERLFGWIVKRCNDAFSVDDTEStcrlSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSD 488
Cdd:cd01378  323 ALAKAIYSRLFDWIVERINKSLAAKSGGK----KKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEE 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  489 YLEEGIKWTQVNFANHlQPTIDLIE-KPMGILSFLEEECV-VPNGSEKSLLEKLCSNLSNDSSFKKSKqTQKCSTIRHFY 566
Cdd:cd01378  399 YVREGIEWTPIKYFNN-KIICDLIEeKPPGIFAILDDACLtAGDATDQTFLQKLNQLFSNHPHFECPS-GHFELRRGEFR 476

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  567 VQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNLKTRRgtitnSTVSFLYKNQLQCLLDTLNS 646
Cdd:cd01378  477 IKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSKKRP-----PTAGTKFKNSANALVETLMK 551

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  647 SSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKGASEKEKCTLI 726
Cdd:cd01378  552 KQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESI 631

                        650       660
                 ....*....|....*....|.
gi 32566156  727 CQDAQVRKERYAVGKTKLFCK 747
Cdd:cd01378  632 LKDLNIPPEEYQMGKTKIFIR 652

MYSc_Myh15_mammals

cd14929

class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...

97-747

2.78e-175

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: 538.79 E-value: 2.78e-175

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQ--LQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd14929    1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKgkRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDF------ILSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKI 248
Cdd:cd14929   81 ESGAGKTVNTKHIIQYfatiaaMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  249 ECYLLEKSRVVFQSDGDRNFHIFYQMLSNyfDNPHKSFLKLSKKVNEYKYLRNDD---SMIDDAETAKMTDEAFTRIGLS 325
Cdd:cd14929  161 DIYLLEKSRVIFQQPGERNYHIFYQILSG--KKELRDLLLVSANPSDFHFCSCGAvavESLDDAEELLATEQAMDILGFL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  326 EEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLS 405
Cdd:cd14929  239 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTY 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  406 SASAMAKILYERLFGWIVKRCNDAFSVddtestcRLSR--FIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFA 483
Cdd:cd14929  319 AVGALSKSIYERMFKWLVARINRVLDA-------KLSRqfFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFV 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  484 KEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCsnlsnDSSFKKSKQTQKCSTIR 563
Cdd:cd14929  392 LEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLF-----DNHFGKSVHFQKPKPDK 466

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  564 -----HFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNL------KTRRGTITNSTVSFL 632
Cdd:cd14929  467 kkfeaHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSaiqfgeKKRKKGASFQTVASL 546

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  633 YKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLM-KNK 711
Cdd:cd14929  547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNpRTF 626

                        650       660       670
                 ....*....|....*....|....*....|....*.
gi 32566156  712 EQSKGASEKEKCTLICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14929  627 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662

MYSc_Myh10

cd14920

class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...

97-745

1.40e-174

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: 537.29 E-value: 1.40e-174

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd14920    1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFI--LSSSVSNNTIGDC-------VVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIG 245
Cdd:cd14920   81 ESGAGKTENTKKVIQYLahVASSHKGRKDHNIpgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  246 AKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLKlsKKVNEYKYLRNDDSMI---DDAETAKMTDEAFTRI 322
Cdd:cd14920  161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL--EGFNNYRFLSNGYIPIpgqQDKDNFQETMEAMHIM 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  323 GLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAK 402
Cdd:cd14920  239 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  403 TLSSASAMAKILYERLFGWIVKRCNDAfsVDDTEStcRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMF 482
Cdd:cd14920  319 ADFAVEALAKATYERLFRWLVHRINKA--LDRTKR--QGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  483 AKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPM---GILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKC 559
Cdd:cd14920  395 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDK 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  560 STirhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPV------------PV----NNLKTRRGT 623
Cdd:cd14920  475 AD---FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgldqvtgmTEtafgSAYKTKKGM 551

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  624 ItnSTVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIER 703
Cdd:cd14920  552 F--RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 629

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 32566156  704 YSLLMKNKEQSKGASEKEKCTLICQDAQVRKERYAVGKTKLF 745
Cdd:cd14920  630 YEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 671

MYSc_Myh3

cd14913

class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...

99-747

5.22e-173

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: 533.09 E-value: 5.22e-173

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   99 VLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILITGES 176
Cdd:cd14913    3 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  177 GAGKTENTKKIIDFILSSSVSNN-----------TIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIG 245
Cdd:cd14913   83 GAGKTVNTKRVIQYFATIAATGDlakkkdskmkgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  246 AKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNyfDNPHK-SFLKLSKKVNEYKYLRNDD---SMIDDAETAKMTDEAFTR 321
Cdd:cd14913  163 ADIETYLLEKSRVTFQLKAERSYHIFYQILSN--KKPELiELLLITTNPYDYPFISQGEilvASIDDAEELLATDSAIDI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  322 IGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLA 401
Cdd:cd14913  241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  402 KTLSSASAMAKILYERLFGWIVKRCNDAFsvdDTestcRLSR--FIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNH 479
Cdd:cd14913  321 QVHHAVNALSKSVYEKLFLWMVTRINQQL---DT----KLPRqhFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNH 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  480 FMFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCSN-LSNDSSFKKSKQTqK 558
Cdd:cd14913  394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNNFQKPKVV-K 472

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  559 CSTIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFP-------PVPVNNLKTRRGTiTNSTVSF 631
Cdd:cd14913  473 GRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAtfatadaDSGKKKVAKKKGS-SFQTVSA 551

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  632 LYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNK 711
Cdd:cd14913  552 LFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASA 631

                        650       660       670
                 ....*....|....*....|....*....|....*..
gi 32566156  712 -EQSKGASEKEKCTLICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14913  632 iPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668

MYSc_Myo11

cd01384

class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...

99-745

5.56e-169

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: 521.47 E-value: 5.56e-169

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   99 VLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLYQ--LQNDLPPHVYSVAQNAFHGILKGGRNQSILITGE 175
Cdd:cd01384    3 VLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKgaPLGELSPHVFAVADAAYRAMINEGKSQSILVSGE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  176 SGAGKTENTKKIIDFIL----SSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECY 251
Cdd:cd01384   83 SGAGKTETTKMLMQYLAymggRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTY 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  252 LLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFlKLsKKVNEYKYLRNDDSM----IDDAETAKMTDEAFTRIGLSEE 327
Cdd:cd01384  163 LLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKY-KL-KDPKQFHYLNQSKCFeldgVDDAEEYRATRRAMDVVGISEE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  328 EKIWIFQILSAVLWIGDIKFGERSGLDVSFV---ESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTL 404
Cdd:cd01384  241 EQDAIFRVVAAILHLGNIEFSKGEEDDSSVPkdeKSEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAAT 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  405 SSASAMAKILYERLFGWIVKRCNDAFSvDDTESTcrlsRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAK 484
Cdd:cd01384  321 LSRDALAKTIYSRLFDWLVDKINRSIG-QDPNSK----RLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKM 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  485 EQSDYLEEGIKWTQVNFANHlQPTIDLIE-KPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKcstir 563
Cdd:cd01384  396 EQEEYTKEEIDWSYIEFVDN-QDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLSRT----- 469

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  564 HFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNnlKTRRGTITNStVSFLYKNQLQCLLDT 643
Cdd:cd01384  470 DFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPRE--GTSSSSKFSS-IGSRFKQQLQELMET 546

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  644 LNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKgASEKEKC 723
Cdd:cd01384  547 LNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGS-DDEKAAC 625

                        650       660
                 ....*....|....*....|..
gi 32566156  724 TLICQDAQVrkERYAVGKTKLF 745
Cdd:cd01384  626 KKILEKAGL--KGYQIGKTKVF 645

MYSc_Myo40

cd14901

class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...

97-746

2.49e-167

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: 517.42 E-value: 2.49e-167

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYqLQND---------LPPHVYSVAQNAFHGILK---- 163
Cdd:cd14901    1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAY-YEHGerraagerkLPPHVYAVADKAFRAMLFasrg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  164 GGRNQSILITGESGAGKTENTKKIIDFILSSS---------VSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIR 234
Cdd:cd14901   80 QKCDQSILVSGESGAGKTETTKIIMNYLASVSsatthgqnaTERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  235 IEFDENSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSfLKLSkKVNEYKYL-------RNDDsmID 307
Cdd:cd14901  160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHA-LGLT-HVEEYKYLnssqcydRRDG--VD 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  308 DAETAKMTDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSF-VESMQEVDNIAELLEMKSSKLVDALTQPT 386
Cdd:cd14901  236 DSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFsMSSLANVRAACDLLGLDMDVLEKTLCTRE 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  387 IKVHDKLIRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTESTcrlSRFIAVLDIAGFEIIEKNSFEQFCI 466
Cdd:cd14901  316 IRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGA---SRFIGIVDIFGFEIFATNSLEQLCI 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  467 NYTNEKLQQFFNHFMFAKEQSDYLEEGIKWTQVNFANHlQPTIDLIE-KPMGILSFLEEECVVPNGSEKSLLEKLCSNLS 545
Cdd:cd14901  393 NFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDLLA 471

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  546 NDSSFKKSKQTQkcsTIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLkllfppvpvnnlktrrgtit 625
Cdd:cd14901  472 KHASFSVSKLQQ---GKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL-------------------- 528

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  626 NSTVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYS 705
Cdd:cd14901  529 SSTVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYS 608

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*.
gi 32566156  706 LLM----KNKEQSKGASEKEKCTLICQDAQVR-KERYAVGKTKLFC 746
Cdd:cd14901  609 CLApdgaSDTWKVNELAERLMSQLQHSELNIEhLPPFQVGKTKVFL 654

MYSc_Myh18

cd14932

class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...

97-745

1.23e-165

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: 513.81 E-value: 1.23e-165

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQ--LQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd14932    1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDF---ILSSSVSNNTIGDCVVTSGVL----------LEAMGNARTTHNSNSSRFGKFIRIEFDENS 241
Cdd:cd14932   81 ESGAGKTENTKKVIQYlayVASSFKTKKDQSSIALSHGELekqllqanpiLEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  242 KLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNpHKSFLKLsKKVNEYKYLRNDDSMI---DDAETAKMTDEA 318
Cdd:cd14932  161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDK-LRSELCL-EDYSKYRFLSNGNVTIpgqQDKELFAETMEA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  319 FTRIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQ 398
Cdd:cd14932  239 FRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  399 NLAKTLSSASAMAKILYERLFGWIVKRCNDAfsVDDTEStcRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFN 478
Cdd:cd14932  319 TQEQAEFAVEALAKASYERMFRWLVMRINKA--LDKTKR--QGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  479 HFMFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPM---GILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQ 555
Cdd:cd14932  395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKK 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  556 TQKCSTirhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPV---------------PVNNLKTR 620
Cdd:cd14932  475 LKDDAD---FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivgldkvagmgesLHGAFKTR 551

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  621 RGTItnSTVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEF 700
Cdd:cd14932  552 KGMF--RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 629

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*
gi 32566156  701 IERYSLLMKNKEQSKGASEKEKCTLICQDAQVRKERYAVGKTKLF 745
Cdd:cd14932  630 RQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVF 674

MYSc_Myh7

cd14917

class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...

99-747

1.28e-163

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: 508.10 E-value: 1.28e-163

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   99 VLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILITGES 176
Cdd:cd14917    3 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYrgKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  177 GAGKTENTKKIIDFIL-----------SSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIG 245
Cdd:cd14917   83 GAGKTVNTKRVIQYFAviaaigdrskkDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  246 AKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNyfDNPHK-SFLKLSKKVNEYKYLRNDDSM---IDDAETAKMTDEAFTR 321
Cdd:cd14917  163 ADIETYLLEKSRVIFQLKAERDYHIFYQILSN--KKPELlDMLLITNNPYDYAFISQGETTvasIDDAEELMATDNAFDV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  322 IGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLA 401
Cdd:cd14917  241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  402 KTLSSASAMAKILYERLFGWIVKRCNDAFsvddtESTCRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFM 481
Cdd:cd14917  321 QVIYATGALAKAVYEKMFNWMVTRINATL-----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  482 FAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCSN-LSNDSSFKKSKQTqKCS 560
Cdd:cd14917  396 FVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNhLGKSNNFQKPRNI-KGK 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  561 TIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLF-------PPVPVNNLKTRRGTiTNSTVSFLY 633
Cdd:cd14917  475 PEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFanyagadAPIEKGKGKAKKGS-SFQTVSALH 553

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  634 KNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNK-E 712
Cdd:cd14917  554 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAiP 633

                        650       660       670
                 ....*....|....*....|....*....|....*
gi 32566156  713 QSKGASEKEKCTLICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14917  634 EGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668

MYSc_Myo4

cd14872

class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...

97-744

2.46e-162

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: 503.92 E-value: 2.46e-162

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd14872    1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYmhKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFILSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYLLE 254
Cdd:cd14872   81 ESGAGKTEATKQCLSFFAEVAGSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYLLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  255 KSRVVFQSDGDRNFHIFYQMLS--------NYFDNPHKSFLKLSKKVneykylrnDDSMIDDAETAKMTDEAFTRIGLSE 326
Cdd:cd14872  161 KSRVVYQIKGERNFHIFYQLLAspdpasrgGWGSSAAYGYLSLSGCI--------EVEGVDDVADFEEVVLAMEQLGFDD 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  327 EEKIWIFQILSAVLWIGDIKFGE---RSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVhdklirKNQNL--- 400
Cdd:cd14872  233 ADINNVMSLIAAILKLGNIEFASgggKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEI------KGCDPtri 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  401 ----AKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTESTCrlsrFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQF 476
Cdd:cd14872  307 pltpAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTT----FIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQH 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  477 FNHFMFAKEQSDYLEEGIKWTQVNFANHlQPTIDLIEK-PMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQ 555
Cdd:cd14872  383 FNQYTFKLEEALYQSEGVKFEHIDFIDN-QPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEV 461

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  556 tqkCSTIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNlKTRRGTITNStvsflYKN 635
Cdd:cd14872  462 ---RTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQ-KTSKVTLGGQ-----FRK 532

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  636 QLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSK 715
Cdd:cd14872  533 QLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIAKRV 612

                        650       660
                 ....*....|....*....|....*....
gi 32566156  716 GASEKEKCTLICQDAQVRKERYAVGKTKL 744
Cdd:cd14872  613 GPDDRQRCDLLLKSLKQDFSKVQVGKTRV 641

MYSc_Myh11

cd14921

class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...

97-745

4.14e-156

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: 488.37 E-value: 4.14e-156

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQ--LQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd14921    1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKgkKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFILSSSVSNNTIGDCVVTSGV---------LLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIG 245
Cdd:cd14921   81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELekqllqanpILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  246 AKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLKlsKKVNEYKYLRNDDSMI---DDAETAKMTDEAFTRI 322
Cdd:cd14921  161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLL--EGFNNYTFLSNGFVPIpaaQDDEMFQETLEAMSIM 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  323 GLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAK 402
Cdd:cd14921  239 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  403 TLSSASAMAKILYERLFGWIVKRCNDAfsVDDTEStcRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMF 482
Cdd:cd14921  319 ADFAIEALAKATYERLFRWILTRVNKA--LDKTHR--QGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  483 AKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPM---GILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKC 559
Cdd:cd14921  395 ILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDK 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  560 STirhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVP----------------VNNLKTRRGT 623
Cdd:cd14921  475 TE---FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrivgldqmakmtesslPSASKTKKGM 551

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  624 ItnSTVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIER 703
Cdd:cd14921  552 F--RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 629

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 32566156  704 YSLLMKNKEQSKGASEKEKCTLICQDAQVRKERYAVGKTKLF 745
Cdd:cd14921  630 YEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIF 671

MYSc_Myh6

cd14916

class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...

99-747

4.90e-156

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: 488.41 E-value: 4.90e-156

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   99 VLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILITGES 176
Cdd:cd14916    3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYrgKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  177 GAGKTENTKKIIDFILS------------SSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLI 244
Cdd:cd14916   83 GAGKTVNTKRVIQYFASiaaigdrskkenPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  245 GAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNyfDNPHK-SFLKLSKKVNEYKYLRNDD---SMIDDAETAKMTDEAFT 320
Cdd:cd14916  163 SADIETYLLEKSRVIFQLKAERNYHIFYQILSN--KKPELlDMLLVTNNPYDYAFVSQGEvsvASIDDSEELLATDSAFD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  321 RIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNL 400
Cdd:cd14916  241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  401 AKTLSSASAMAKILYERLFGWIVKRCNDAFsvddtESTCRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHF 480
Cdd:cd14916  321 QQVYYSIGALAKSVYEKMFNWMVTRINATL-----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  481 MFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCSN-LSNDSSFKKSKQTqKC 559
Cdd:cd14916  396 MFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNhLGKSNNFQKPRNV-KG 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  560 STIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNL----KTRRGTITNS---TVSFL 632
Cdd:cd14916  475 KQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTgdsgKGKGGKKKGSsfqTVSAL 554

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  633 YKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNK- 711
Cdd:cd14916  555 HRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAi 634

                        650       660       670
                 ....*....|....*....|....*....|....*.
gi 32566156  712 EQSKGASEKEKCTLICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14916  635 PEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670

MYSc_Myh9

cd14919

class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...

97-745

6.75e-156

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: 488.06 E-value: 6.75e-156

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQ--LQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd14919    1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDF---ILSSSVSNNTIGDC---VVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKI 248
Cdd:cd14919   81 ESGAGKTENTKKVIQYlahVASSHKSKKDQGELerqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  249 ECYLLEKSRVVFQSDGDRNFHIFYQMLSNYfdNPHKSFLKLSKKVNEYKYLRNDDSMI---DDAETAKMTDEAFTRIGLS 325
Cdd:cd14919  161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGA--GEHLKTDLLLEPYNKYRFLSNGHVTIpgqQDKDMFQETMEAMRIMGIP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  326 EEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLS 405
Cdd:cd14919  239 EEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  406 SASAMAKILYERLFGWIVKRCNDAfsVDDTEStcRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKE 485
Cdd:cd14919  319 AIEALAKATYERMFRWLVLRINKA--LDKTKR--QGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  486 QSDYLEEGIKWTQVNFANHLQPTIDLIEKPMG---ILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKCSTi 562
Cdd:cd14919  395 QEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGppgILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKAD- 473

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  563 rhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVP----------------VNNLKTRRGTItn 626
Cdd:cd14919  474 --FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagmsetalPGAFKTRKGMF-- 549

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  627 STVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSL 706
Cdd:cd14919  550 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 629

                        650       660       670
                 ....*....|....*....|....*....|....*....
gi 32566156  707 LMKNKEQSKGASEKEKCTLICQDAQVRKERYAVGKTKLF 745
Cdd:cd14919  630 LTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVF 668

MYSc_Myh8

cd14918

class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...

99-747

5.86e-155

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: 485.39 E-value: 5.86e-155

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   99 VLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILITGES 176
Cdd:cd14918    3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  177 GAGKTENTKKIIDFILSSSVS-----------NNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIG 245
Cdd:cd14918   83 GAGKTVNTKRVIQYFATIAVTgekkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  246 AKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLkLSKKVNEYKYLRNDD---SMIDDAETAKMTDEAFTRI 322
Cdd:cd14918  163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLL-ITTNPYDYAFVSQGEitvPSIDDQEELMATDSAIDIL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  323 GLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAK 402
Cdd:cd14918  242 GFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  403 TLSSASAMAKILYERLFGWIVKRCNDAFsvdDTESTCRLsrFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMF 482
Cdd:cd14918  322 VYNAVGALAKAVYEKMFLWMVTRINQQL---DTKQPRQY--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  483 AKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLC-SNLSNDSSFKKSKqTQKCST 561
Cdd:cd14918  397 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPK-VVKGKA 475

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  562 IRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNLKT-------RRGTiTNSTVSFLYK 634
Cdd:cd14918  476 EAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSgakkgakKKGS-SFQTVSALFR 554

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  635 NQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNK--- 711
Cdd:cd14918  555 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAipe 634

                        650       660       670
                 ....*....|....*....|....*....|....*....
gi 32566156  712 ---EQSKGASEKekctlICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14918  635 gqfIDSKKASEK-----LLASIDIDHTQYKFGHTKVFFK 668

MYSc_Myh13

cd14923

class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...

99-747

9.29e-155

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: 484.96 E-value: 9.29e-155

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   99 VLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILITGES 176
Cdd:cd14923    3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYrgKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGES 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  177 GAGKTENTKKIIDFILSSSVSNN------------TIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLI 244
Cdd:cd14923   83 GAGKTVNTKRVIQYFATIAVTGDkkkeqqpgkmqgTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  245 GAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNyfDNPHK-SFLKLSKKVNEYKYLRNDD---SMIDDAETAKMTDEAFT 320
Cdd:cd14923  163 SADIETYLLEKSRVTFQLSSERSYHIFYQIMSN--KKPELiDLLLISTNPFDFPFVSQGEvtvASIDDSEELLATDNAID 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  321 RIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNL 400
Cdd:cd14923  241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  401 AKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTEStcrlsRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHF 480
Cdd:cd14923  321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQ-----YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  481 MFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLC-SNLSNDSSFKKSKQTqKC 559
Cdd:cd14923  396 MFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPA-KG 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  560 STIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNLKTRRGTITN--------STVSF 631
Cdd:cd14923  475 KAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGSKKGgkkkgssfQTVSA 554

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  632 LYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNK 711
Cdd:cd14923  555 VFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASA 634

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 32566156  712 ------EQSKGASEKekctlICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14923  635 ipegqfIDSKNASEK-----LLNSIDVDREQYRFGHTKVFFK 671

MYSc_Myh19

cd15896

class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...

97-745

9.81e-155

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: 484.95 E-value: 9.81e-155

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQ--LQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd15896    1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFILSSSVSNNTIGD---CVVTSGVL----------LEAMGNARTTHNSNSSRFGKFIRIEFDENS 241
Cdd:cd15896   81 ESGAGKTENTKKVIQYLAHVASSHKTKKDqnsLALSHGELekqllqanpiLEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  242 KLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLKlsKKVNEYKYLRNDDSMIDDAETAKM---TDEA 318
Cdd:cd15896  161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL--ENYNNYRFLSNGNVTIPGQQDKDLfteTMEA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  319 FTRIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQ 398
Cdd:cd15896  239 FRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  399 NLAKTLSSASAMAKILYERLFGWIVKRCNDAfsVDDTEStcRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFN 478
Cdd:cd15896  319 TQEQAEFAVEALAKATYERMFRWLVMRINKA--LDKTKR--QGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  479 HFMFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPM---GILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQ 555
Cdd:cd15896  395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKK 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  556 TQKCSTirhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPV--------------NNLKTRR 621
Cdd:cd15896  475 LKDEAD---FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRivgldkvsgmsempGAFKTRK 551

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  622 GTItnSTVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFI 701
Cdd:cd15896  552 GMF--RTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 629

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....
gi 32566156  702 ERYSLLMKNKEQSKGASEKEKCTLICQDAQVRKERYAVGKTKLF 745
Cdd:cd15896  630 QRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVF 673

MYSc_Myh1_mammals

cd14910

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...

99-747

1.23e-154

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: 484.62 E-value: 1.23e-154

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   99 VLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILITGES 176
Cdd:cd14910    3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  177 GAGKTENTKKIIDFILSSSVSNN-------------TIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKL 243
Cdd:cd14910   83 GAGKTVNTKRVIQYFATIAVTGEkkkeeatsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  244 IGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLkLSKKVNEYKYLRNDD---SMIDDAETAKMTDEAFT 320
Cdd:cd14910  163 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLL-ITTNPYDYAFVSQGEitvPSIDDQEELMATDSAIE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  321 RIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNL 400
Cdd:cd14910  242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  401 AKTLSSASAMAKILYERLFGWIVKRCNDAFsvdDTESTCRLsrFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHF 480
Cdd:cd14910  322 QQVYNAVGALAKAVYDKMFLWMVTRINQQL---DTKQPRQY--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  481 MFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLC-SNLSNDSSFKKSKQTqKC 559
Cdd:cd14910  397 MFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPA-KG 475

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  560 STIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNLKT--------RRGTiTNSTVSF 631
Cdd:cd14910  476 KVEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEgggkkggkKKGS-SFQTVSA 554

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  632 LYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNK 711
Cdd:cd14910  555 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 634

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 32566156  712 ------EQSKGASEKekctlICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14910  635 ipegqfIDSKKASEK-----LLGSIDIDHTQYKFGHTKVFFK 671

MYSc_Myh4

cd14915

class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...

99-747

1.52e-154

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: 484.23 E-value: 1.52e-154

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   99 VLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILITGES 176
Cdd:cd14915    3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  177 GAGKTENTKKIIDFILSSSVSNN-------------TIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKL 243
Cdd:cd14915   83 GAGKTVNTKRVIQYFATIAVTGEkkkeeaasgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  244 IGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNyfDNPHK-SFLKLSKKVNEYKYLRNDD---SMIDDAETAKMTDEAF 319
Cdd:cd14915  163 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN--KKPELiEMLLITTNPYDFAFVSQGEitvPSIDDQEELMATDSAV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  320 TRIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQN 399
Cdd:cd14915  241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  400 LAKTLSSASAMAKILYERLFGWIVKRCNDAFsvdDTESTCRLsrFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNH 479
Cdd:cd14915  321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQL---DTKQPRQY--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  480 FMFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLC-SNLSNDSSFKKSKQTqK 558
Cdd:cd14915  396 HMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPA-K 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  559 CSTIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNLK--------TRRGTiTNSTVS 630
Cdd:cd14915  475 GKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEggggkkggKKKGS-SFQTVS 553

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  631 FLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKN 710
Cdd:cd14915  554 ALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 633

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|...
gi 32566156  711 K------EQSKGASEKekctlICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14915  634 AipegqfIDSKKASEK-----LLGSIDIDHTQYKFGHTKVFFK 671

MYSc_Myh2_mammals

cd14912

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...

99-747

7.37e-154

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: 482.70 E-value: 7.37e-154

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   99 VLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILITGES 176
Cdd:cd14912    3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  177 GAGKTENTKKIIDFILSSSVS-------------NNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKL 243
Cdd:cd14912   83 GAGKTVNTKRVIQYFATIAVTgekkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  244 IGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNyfDNPHK-SFLKLSKKVNEYKYLRNDD---SMIDDAETAKMTDEAF 319
Cdd:cd14912  163 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSN--KKPELiEMLLITTNPYDYPFVSQGEisvASIDDQEELMATDSAI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  320 TRIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQN 399
Cdd:cd14912  241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  400 LAKTLSSASAMAKILYERLFGWIVKRCNDAFsvdDTESTCRLsrFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNH 479
Cdd:cd14912  321 VEQVTNAVGALAKAVYEKMFLWMVARINQQL---DTKQPRQY--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  480 FMFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLC-SNLSNDSSFKKSKqTQK 558
Cdd:cd14912  396 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPK-VVK 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  559 CSTIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNLK----------TRRGTiTNST 628
Cdd:cd14912  475 GKAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGAsagggakkggKKKGS-SFQT 553

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  629 VSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLM 708
Cdd:cd14912  554 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 633

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*
gi 32566156  709 KNK------EQSKGASEKekctlICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14912  634 ASAipegqfIDSKKASEK-----LLASIDIDHTQYKFGHTKVFFK 673

MYSc_Myo27

cd14888

class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...

97-747

1.56e-152

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: 478.80 E-value: 1.56e-152

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLY-QLQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd14888    1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFiQPSISKSPHVFSTASSAYQGMCNNKKSQTILISG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFI---LSSSVSN-NTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDEN---------S 241
Cdd:cd14888   81 ESGAGKTESTKYVMKFLacaGSEDIKKrSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskrmsgdrG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  242 KLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQM-----------LSNYFDNPH--------------KSFLKLSKKVNEY 296
Cdd:cd14888  161 RLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLcaaareakntgLSYEENDEKlakgadakpisidmSSFEPHLKFRYLT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  297 KYLRNDDSMIDDAETAKMTDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKF---GERSGLDVSFVESMQEVDNIAELLEM 373
Cdd:cd14888  241 KSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFennEACSEGAVVSASCTDDLEKVASLLGV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  374 KSSKLVDALTQPTIKVHDKLIRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDA--FSVDDTESTCrlsrfiAVLDIA 451
Cdd:cd14888  321 DAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESigYSKDNSLLFC------GVLDIF 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  452 GFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSDYLEEGIKWTQVNFANHlQPTIDLI-EKPMGILSFLEEECVVPN 530
Cdd:cd14888  395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDN-QDCVDLLqEKPLGIFCMLDEECFVPG 473

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  531 GSEKSLLEKLCSNLSNDSSFKKSKQTQKCstirhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFP 610
Cdd:cd14888  474 GKDQGLCNKLCQKHKGHKRFDVVKTDPNS-----FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFS 548

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  611 PvpvnnlKTRRGTITNS------TVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGI 684
Cdd:cd14888  549 A------YLRRGTDGNTkkkkfvTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAV 622

                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32566156  685 RICREGYPSRLSHSEFIERYSLLMkNKEQSKGASEkekctlicqdaqvrkerYAVGKTKLFCK 747
Cdd:cd14888  623 QVSRAGYPVRLSHAEFYNDYRILL-NGEGKKQLSI-----------------WAVGKTLCFFK 667

MYSc_Myo3

cd01379

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...

98-747

2.29e-148

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: 466.37 E-value: 2.29e-148

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   98 TVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQ--NDLPPHVYSVAQNAFHGILKGGRNQSILITGE 175
Cdd:cd01379    2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAkrSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  176 SGAGKTENTKKIIDFILSSSVSNN-TIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYLLE 254
Cdd:cd01379   82 SGAGKTESANLLVQQLTVLGKANNrTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  255 KSRVVFQSDGDRNFHIFYQMLSNYFDNP--HKSFLKLSKKVNEYKY--LRNDDSMIDDA--ETAKMTDEAFTRIGLSEEE 328
Cdd:cd01379  162 KSRVVHQAIGERNFHIFYYIYAGLAEDKklAKYKLPENKPPRYLQNdgLTVQDIVNNSGnrEKFEEIEQCFKVIGFTKEE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  329 KIWIFQILSAVLWIGDIKFGERSG----LDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTL 404
Cdd:cd01379  242 VDSVYSILAAILHIGDIEFTEVESnhqtDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEEAT 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  405 SSASAMAKILYERLFGWIVKRCNDAFSVDDTESTCRLSrfIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAK 484
Cdd:cd01379  322 DARDAMAKALYGRLFSWIVNRINSLLKPDRSASDEPLS--IGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFAW 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  485 EQSDYLEEGIKWTQVNFANHlQPTID-LIEKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNdSSFKKSKQTQKCstir 563
Cdd:cd01379  400 EQQEYLNEGIDVDLIEYEDN-RPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIKS-KYYWRPKSNALS---- 473

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  564 hFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLlfppvpvnnlktrrgtitnsTVSFLYKNQLQCLLDT 643
Cdd:cd01379  474 -FGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ--------------------TVATYFRYSLMDLLSK 532

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  644 LNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKGASeKEKC 723
Cdd:cd01379  533 MVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVAN-RENC 611

                        650       660
                 ....*....|....*....|....
gi 32566156  724 TLICQdaQVRKERYAVGKTKLFCK 747
Cdd:cd01379  612 RLILE--RLKLDNWALGKTKVFLK 633

MYSc_Myh14_mammals

cd14930

class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...

97-745

1.95e-147

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: 465.34 E-value: 1.95e-147

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd14930    1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYrgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFILSSSVSNN---------TIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIG 245
Cdd:cd14930   81 ESGAGKTENTKKVIQYLAHVASSPKgrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  246 AKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLKlsKKVNEYKYLRNDDSMI--DDAETAKMTDEAFTRIG 323
Cdd:cd14930  161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL--EPCSHYRFLTNGPSSSpgQERELFQETLESLRVLG 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  324 LSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKT 403
Cdd:cd14930  239 FSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  404 LSSASAMAKILYERLFGWIVKRCNDAFSvddtESTCRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFA 483
Cdd:cd14930  319 DFALEALAKATYERLFRWLVLRLNRALD----RSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  484 KEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPM---GILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKCS 560
Cdd:cd14930  395 LEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQA 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  561 TirhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVP-------VNNL-------KTRRGTItn 626
Cdd:cd14930  475 D---FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgivgleqVSSLgdgppggRPRRGMF-- 549

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  627 STVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSL 706
Cdd:cd14930  550 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 629

                        650       660       670
                 ....*....|....*....|....*....|....*....
gi 32566156  707 LMKNKEQSKGASEKEKCTLICQDAQVRKERYAVGKTKLF 745
Cdd:cd14930  630 LTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIF 668

MYSc_Myo36

cd14897

class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...

97-747

2.05e-146

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: 461.08 E-value: 2.05e-146

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQ---LQNDLPPHVYSVAQNAFHGILKGGRNQSILIT 173
Cdd:cd14897    1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSnlsVRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  174 GESGAGKTENTKKIIDFILSSSVSNNT-IGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYL 252
Cdd:cd14897   81 GESGAGKTESTKYMIKHLMKLSPSDDSdLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  253 LEKSRVVFQSDGDRNFHIFYQMlsnyFDNPHKSFLK--LSKKVNEYKYLRNDD---SMIDDAETAKMTDEAFTR------ 321
Cdd:cd14897  161 LEKSRVVHRGNGEKNFHIFYAL----FAGMSRDRLLyyFLEDPDCHRILRDDNrnrPVFNDSEELEYYRQMFHDltnimk 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  322 -IGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNL 400
Cdd:cd14897  237 lIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  401 AKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTESTCRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHF 480
Cdd:cd14897  317 RQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDY 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  481 MFAKEQSDYLEEGIKWTQVNFANHlQPTIDLI-EKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKC 559
Cdd:cd14897  397 VFPRERSEYEIEGIEWRDIEYHDN-DDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASPGNRVA 475

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  560 stirhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFppvpvnnlktrrgtitnstvSFLYKNQLQC 639
Cdd:cd14897  476 -----FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF--------------------TSYFKRSLSD 530

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  640 LLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKGASE 719
Cdd:cd14897  531 LMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKVRSDDL 610

                        650       660
                 ....*....|....*....|....*...
gi 32566156  720 kEKCTLICQDAQVrkERYAVGKTKLFCK 747
Cdd:cd14897  611 -GKCQKILKTAGI--KGYQFGKTKVFLK 635

MYSc_Myo29

cd14890

class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...

97-747

2.84e-144

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: 456.54 E-value: 2.84e-144

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGG----RNQS 169
Cdd:cd14890    1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYhgTTAGELPPHVFAIADHAYTQLIQSGvldpSNQS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  170 ILITGESGAGKTENTKKIIDFI----------------LSSSVSNNTIG---DCVVTSGVLLEAMGNARTTHNSNSSRFG 230
Cdd:cd14890   81 IIISGESGAGKTEATKIIMQYLaritsgfaqgasgegeAASEAIEQTLGsleDRVLSSNPLLESFGNAKTLRNDNSSRFG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  231 KFIRIEFDENSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYfDNPHKSFLKLSKKVnEYKYLRNDDSMI---D 307
Cdd:cd14890  161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGA-DEALRERLKLQTPV-EYFYLRGECSSIpscD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  308 DAETAKMTDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKFG----ERSGLDVSFVESMQEVdniAELLEMKSSKLVDALT 383
Cdd:cd14890  239 DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFEsendTTVLEDATTLQSLKLA---AELLGVNEDALEKALL 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  384 QPTIKVHDKLIRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAFSvddteSTCRLSRFIAVLDIAGFEIIEKNSFEQ 463
Cdd:cd14890  316 TRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTIS-----SPDDKWGFIGVLDIYGFEKFEWNTFEQ 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  464 FCINYTNEKLQQFFNHFMFAKEQSDYLEEGIKWTQVNFaNHLQPTIDLIE-----KPmGILSFLeEECVVPNGSEKSLle 538
Cdd:cd14890  391 LCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITL-DDCWRFKGEEANK-- 465

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  539 KLCSNL---------SNDSSFKKSKQ----TQKCSTIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSThpll 605
Cdd:cd14890  466 KFVSQLhasfgrksgSGGTRRGSSQHphfvHPKFDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR---- 541

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  606 kllfppvpvnnlKTRRGTitnsTVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIR 685
Cdd:cd14890  542 ------------RSIREV----SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQ 605

                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32566156  686 ICREGYPSRLSHSEFIERYSLLMKNKEqskgaSEKEKCTLICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14890  606 IRQQGFALREEHDSFFYDFQVLLPTAE-----NIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662

MYSc_Myo6

cd01382

class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...

97-711

8.70e-144

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: 454.78 E-value: 8.70e-144

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLYQLQN--DLPPHVYSVAQNAFHGILKGGRNQSILIT 173
Cdd:cd01382    1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSlgTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  174 GESGAGKTENTKKIIDFILSSSVSN-NTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYL 252
Cdd:cd01382   81 GESGAGKTESTKYILRYLTESWGSGaGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  253 LEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLKlskkvneykylrndDSMIDDAETAKMTDEAFTRIGLSEEEKIWI 332
Cdd:cd01382  161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK--------------DPLLDDVGDFIRMDKAMKKIGLSDEEKLDI 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  333 FQILSAVLWIGDIKFGE-----RSGLDVSfVESMQEVDNIAELLEMKSSKLVDALT----QPT--------IKVhdKLIR 395
Cdd:cd01382  227 FRVVAAVLHLGNIEFEEngsdsGGGCNVK-PKSEQSLEYAAELLGLDQDELRVSLTtrvmQTTrggakgtvIKV--PLKV 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  396 KNQNLAKtlssaSAMAKILYERLFGWIVKRCNDAFSVDDTEStcrlsrFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQ 475
Cdd:cd01382  304 EEANNAR-----DALAKAIYSKLFDHIVNRINQCIPFETSSY------FIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  476 FFNHFMFAKEQSDYLEEGIKWTQVNFANHlQPTIDLIE-KPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSF---K 551
Cdd:cd01382  373 FFNERILKEEQELYEKEGLGVKEVEYVDN-QDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLsipR 451

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  552 KSKQTQKcSTIRH---FYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNL--KTRRGTITN 626
Cdd:cd01382  452 KSKLKIH-RNLRDdegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKdsKQKAGKLSF 530

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  627 STVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSL 706
Cdd:cd01382  531 ISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKK 610


                 ....*
gi 32566156  707 LMKNK 711
Cdd:cd01382  611 YLPPK 615

MYSc_Myo15

cd01387

class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...

97-747

1.25e-142

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: 451.90 E-value: 1.25e-142

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd01387    1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYsgRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFILSSSVS-NNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSkLIGAKIECYLL 253
Cdd:cd01387   81 ESGSGKTEATKLIMQYLAAVNQRrNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEGGV-IVGAITSQYLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  254 EKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLKLSkkVNEYKYLR---NDDSM-IDDAETAKMTDEAFTRIGLSEEEK 329
Cdd:cd01387  160 EKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQE--AEKYFYLNqggNCEIAgKSDADDFRRLLAAMQVLGFSSEEQ 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  330 IWIFQILSAVLWIGDIKFGE---RSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLSS 406
Cdd:cd01387  238 DSIFRILASVLHLGNVYFHKrqlRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDA 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  407 ASAMAKILYERLFGWIVKRCNdAFSVDDTESTCRlsrfIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQ 486
Cdd:cd01387  318 RDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLS----IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQ 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  487 SDYLEEGIKWTQVNFANHlQPTIDLI-EKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQtqkcsTIRHF 565
Cdd:cd01387  393 EEYIREQIDWTEIAFADN-QPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM-----PLPEF 466

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  566 YVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPV-PVNNLKTRRGTITNS--------TVSFLYKNQ 636
Cdd:cd01387  467 TIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHrAQTDKAPPRLGKGRFvtmkprtpTVAARFQDS 546

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  637 LQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEqSKG 716
Cdd:cd01387  547 LLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKL-PRP 625

                        650       660       670
                 ....*....|....*....|....*....|..
gi 32566156  717 ASEKEKCTLICQ-DAQVRKERYAVGKTKLFCK 747
Cdd:cd01387  626 APGDMCVSLLSRlCTVTPKDMYRLGATKVFLR 657

MYSc_Myo31

cd14892

class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...

97-747

3.03e-142

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: 450.75 E-value: 3.03e-142

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSD--EVKQLYQLQNDL---PPHVYSVAQNAFHGILKGG----RN 167
Cdd:cd14892    1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDvpGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  168 QSILITGESGAGKTENTKKIIDFILSSSVSNN-------------TIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIR 234
Cdd:cd14892   81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKgastskgaanaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  235 IEFDENSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNyFDNPHKSFLKLsKKVNEYKYLRNDDSM----IDDAE 310
Cdd:cd14892  161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAG-LDANENAALEL-TPAESFLFLNQGNCVevdgVDDAT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  311 TAKMTDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVES--MQEVDNIAELLEMKSSKLVDAL-TQPTI 387
Cdd:cd14892  239 EFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSadGVNVAKAAGLLGVDAAELMFKLvTQTTS 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  388 KVHDKLIRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTESTCR-----LSRFIAVLDIAGFEIIEKNSFE 462
Cdd:cd14892  319 TARGSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGVTGGaasptFSPFIGILDIFGFEIMPTNSFE 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  463 QFCINYTNEKLQQFFNHFMFAKEQSDYLEEGIKWTQVNFANHlQPTIDLIEK-PMGILSFLEEECVVP-NGSEKSLLEKL 540
Cdd:cd14892  399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDN-QDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTIY 477

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  541 CSN-LSNDSSFKKSKQtqKCStirHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILsqsthpllkllfppvpvnnLKT 619
Cdd:cd14892  478 HQThLDKHPHYAKPRF--ECD---EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLL-------------------RSS 533

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  620 RRgtitnstvsflYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSE 699
Cdd:cd14892  534 SK-----------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEE 602

                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 32566156  700 FIERYSLLMKNK-------EQSKGASEKEKCTLICQDAqVRKERYAVGKTKLFCK 747
Cdd:cd14892  603 FYEKFWPLARNKagvaaspDACDATTARKKCEEIVARA-LERENFQLGRTKVFLR 656

MYSc_Myo28

cd14889

class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...

99-747

1.21e-141

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: 449.36 E-value: 1.21e-141

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   99 VLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQ--NDLPPHVYSVAQNAFHGIL----KGGRNQSILI 172
Cdd:cd14889    3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEkkSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  173 TGESGAGKTENTKKIIDFILSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFdENSKLIGAKIECYL 252
Cdd:cd14889   83 SGESGAGKTESTKLLLRQIMELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKINEYL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  253 LEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLKLSKKVneYKYLRNDDSMIDDAETAKMT-DE---AFTRIGLSEEE 328
Cdd:cd14889  162 LEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGK--YRYLNNGAGCKREVQYWKKKyDEvcnAMDMVGFTEQE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  329 KIWIFQILSAVLWIGDIKFgERSGLDVSFVESMQE--VDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLSS 406
Cdd:cd14889  240 EVDMFTILAGILSLGNITF-EMDDDEALKVENDSNgwLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDA 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  407 ASAMAKILYERLFGWIVKRCN------DAFSVDDTEstcrlsrfIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHF 480
Cdd:cd14889  319 RDSIAKVAYGRVFGWIVSKINqllapkDDSSVELRE--------IGILDIFGFENFAVNRFEQACINLANEQLQYFFNHH 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  481 MFAKEQSDYLEEGIKWTQVNFANHlQPTIDL-IEKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKqtqkc 559
Cdd:cd14889  391 IFLMEQKEYKKEGIDWKEITYKDN-KPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSR----- 464

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  560 STIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLF----------------PPVPVNNLKTRRgt 623
Cdd:cd14889  465 SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFtatrsrtgtlmpraklPQAGSDNFNSTR-- 542

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  624 itNSTVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIER 703
Cdd:cd14889  543 --KQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAER 620

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....
gi 32566156  704 YSLLMKNKEQSkgaSEKEKCTLICQDAQVRKerYAVGKTKLFCK 747
Cdd:cd14889  621 YKILLCEPALP---GTKQSCLRILKATKLVG--WKCGKTRLFFK 659

MYSc_Myo9

cd01385

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...

97-747

2.01e-140

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: 447.21 E-value: 2.01e-140

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQN--DLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd01385    1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRlgKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFI--LSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYL 252
Cdd:cd01385   81 ESGSGKTESTNFLLHHLtaLSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  253 LEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFlkLSKKVNEYKYLRNDDSMIDDAETAK----MTDEAFTRIGLSEEE 328
Cdd:cd01385  161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERKEL--HLKQPEDYHYLNQSDCYTLEGEDEKyefeRLKQAMEMVGFLPET 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  329 KIWIFQILSAVLWIGDIKFGERS--GLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLSS 406
Cdd:cd01385  239 QRQIFSVLSAVLHLGNIEYKKKAyhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIAT 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  407 ASAMAKILYERLFGWIVKRCNDAF-SVDDTESTCRLSrfIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKE 485
Cdd:cd01385  319 RDAMAKCLYSALFDWIVLRINHALlNKKDLEEAKGLS--IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLE 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  486 QSDYLEEGIKWTQVNFANHLQpTIDLIE-KPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKskqTQKCSTirH 564
Cdd:cd01385  397 QEEYKKEGISWHNIEYTDNTG-CLQLISkKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEK---PQVMEP--A 470

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  565 FYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPV------------------------------ 614
Cdd:cd01385  471 FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVavfrwavlrafframaafreagrrraqrta 550

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  615 NNLKTRRGTITNS-----------TVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEG 683
Cdd:cd01385  551 GHSLTLHDRTTKSllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLET 630

                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32566156  684 IRICREGYPSRLSHSEFIERYSLLMKNKEQSkgaSEKEKCTLICQdAQVRKERYAVGKTKLFCK 747
Cdd:cd01385  631 VRIRRSGYSVRYTFQEFITQFQVLLPKGLIS---SKEDIKDFLEK-LNLDRDNYQIGKTKVFLK 690

MYSc_Myo42

cd14903

class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...

97-745

1.56e-139

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: 443.83 E-value: 1.56e-139

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILIT 173
Cdd:cd14903    1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYlnKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  174 GESGAGKTENTKKIIDFI--LSSSVSNNTIGDCVVTSGvLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECY 251
Cdd:cd14903   81 GESGAGKTETTKILMNHLatIAGGLNDSTIKKIIEVNP-LLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  252 LLEKSRVVFQSDGDRNFHIFYQMLSNYfDNPHKSFLKLSkkvNEYKYL-RNDDSMID---DAETAKMTDEAFTRIGLSEE 327
Cdd:cd14903  160 LLEKTRVISHERPERNYHIFYQLLASP-DVEERLFLDSA---NECAYTgANKTIKIEgmsDRKHFARTKEALSLIGVSEE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  328 EKIWIFQILSAVLWIGDIKFGERSGLDVS--FVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLS 405
Cdd:cd14903  236 KQEVLFEVLAGILHLGQLQIQSKPNDDEKsaIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAED 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  406 SASAMAKILYERLFGWIVKRCNDAFSVDDtestcRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKE 485
Cdd:cd14903  316 CRDALAKAIYSNVFDWLVATINASLGNDA-----KMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTV 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  486 QSDYLEEGIKWTQVNFANHlQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSS---FKKSKQTQkcsti 562
Cdd:cd14903  391 QIEYEEEGIRWAHIDFADN-QDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDvieFPRTSRTQ----- 464

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  563 rhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPV----NNLKTRR-------GTITNSTVSF 631
Cdd:cd14903  465 --FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVEspaaASTSLARgarrrrgGALTTTTVGT 542

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  632 LYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNK 711
Cdd:cd14903  543 QFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG 622

                        650       660       670
                 ....*....|....*....|....*....|....*
gi 32566156  712 EQSKgASEKEKCTLICQDAQVRK-ERYAVGKTKLF 745
Cdd:cd14903  623 RNTD-VPVAERCEALMKKLKLESpEQYQMGLTRIY 656

MYSc_Myo10

cd14873

class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...

97-747

3.83e-138

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: 439.62 E-value: 3.83e-138

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLYQLQN--DLPPHVYSVAQNAFHGILKGGRNQSILIT 173
Cdd:cd14873    1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHlgELPPHIFAIANECYRCLWKRHDNQCILIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  174 GESGAGKTENTKKIIDFIlsSSVSNNTIG-----------DCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSK 242
Cdd:cd14873   81 GESGAGKTESTKLILKFL--SVISQQSLElslkektscveQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  243 LIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNyfDNPHKSFLKLSKKVNEYKYLRN----DDSMIDDAETAKMTDEA 318
Cdd:cd14873  159 IQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAG--LEHEEREEFYLSTPENYHYLNQsgcvEDKTISDQESFREVITA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  319 FTRIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQevdNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQ 398
Cdd:cd14873  237 MEVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALG---RSAELLGLDPTQLTDALTQRSMFLRGEEILTPL 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  399 NLAKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTestcrlSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFN 478
Cdd:cd14873  314 NVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKED------FKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  479 HFMFAKEQSDYLEEGIKWTQVNFANHLQpTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKqtqk 558
Cdd:cd14873  388 KHIFSLEQLEYSREGLVWEDIDWIDNGE-CLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPR---- 462

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  559 cSTIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNLKTRRGTITN---STVSFLYKN 635
Cdd:cd14873  463 -VAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKhrrPTVSSQFKD 541

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  636 QLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSK 715
Cdd:cd14873  542 SLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPE 621

                        650       660       670
                 ....*....|....*....|....*....|..
gi 32566156  716 GAseKEKCTLICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14873  622 DV--RGKCTSLLQLYDASNSEWQLGKTKVFLR 651

MYSc_Myo34

cd14895

class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...

103-747

9.65e-133

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: 427.06 E-value: 9.65e-133

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  103 LKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQN--DLPPHVYSVAQNAF-------HGILKGGRNQSILIT 173
Cdd:cd14895    7 LAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYDLHKYREEMPGwtALPPHVFSIAEGAYrslrrrlHEPGASKKNQTILVS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  174 GESGAGKTENTKKIIDFI----------LSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRI-----EFD 238
Cdd:cd14895   87 GESGAGKTETTKFIMNYLaesskhttatSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVRMffeghELD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  239 ENSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLKLSKKVNEYKYL-------RNDDsmIDDAET 311
Cdd:cd14895  167 TSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQEFQYIsggqcyqRNDG--VRDDKQ 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  312 AKMTDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKFGERSG------------------LDVSFVESMQEVDNIAELLEM 373
Cdd:cd14895  245 FQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEdegeedngaasapcrlasASPSSLTVQQHLDIVSKLFAV 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  374 KSSKLVDALTQPTIKVHDKLIRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDA-----FSVDDTESTCR-LSRFIAV 447
Cdd:cd14895  325 DQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAspqrqFALNPNKAANKdTTPCIAV 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  448 LDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSDYLEEGIKWTQVNFANHlQPTIDLIE-KPMGILSFLEEEC 526
Cdd:cd14895  405 LDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqRPSGIFSLLDEEC 483

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  527 VVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKCSTirhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLK 606
Cdd:cd14895  484 VVPKGSDAGFARKLYQRLQEHSNFSASRTDQADVA---FQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDAHLR 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  607 LLFPPVPVN--------NLKTRRGTITNSTVSF--LYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLK 676
Cdd:cd14895  561 ELFEFFKASesaelslgQPKLRRRSSVLSSVGIgsQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLR 640

                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32566156  677 CNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKGASEKEKCTLicqdaqvRKERYAVGKTKLFCK 747
Cdd:cd14895  641 YGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETL-------KVDHAELGKTRVFLR 704

PTZ00014

myosin-A; Provisional

87-800

4.85e-130

myosin-A; Provisional

Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 423.29 E-value: 4.85e-130

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    87 DLCTLTQPNAATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQND---LPPHVYSVAQNAFHGILK 163
Cdd:PTZ00014  100 DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDsdkLPPHVFTTARRALENLHG 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   164 GGRNQSILITGESGAGKTENTKKIIDFILSSSVSNN--TIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENS 241
Cdd:PTZ00014  180 VKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMdlKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEG 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   242 KLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNyFDNPHKSFLKLsKKVNEYKYLRN---DDSMIDDAETAKMTDEA 318
Cdd:PTZ00014  260 GIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKG-ANDEMKEKYKL-KSLEEYKYINPkclDVPGIDDVKDFEEVMES 337

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   319 FTRIGLSEEEKIWIFQILSAVLWIGDIKFGERS---GLDVSFV--ESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKL 393
Cdd:PTZ00014  338 FDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEeggLTDAAAIsdESLEVFNEACELLFLDYESLKKELTVKVTYAGNQK 417

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   394 IRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDafsvdDTESTCRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKL 473
Cdd:PTZ00014  418 IEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNA-----TIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEML 492

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   474 QQFFNHFMFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKS 553
Cdd:PTZ00014  493 QKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPA 572

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   554 KQTQKCStirhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNLKTRRGTItnstVSFLY 633
Cdd:PTZ00014  573 KVDSNKN----FVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLAKGQL----IGSQF 644

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   634 KNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQ 713
Cdd:PTZ00014  645 LNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSN 724

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   714 SKGASEKEKCTLICQDAQVRKERYAVGKTKLFCKVGVISELETKRNNYISSF---IILIQANIRYLNIQKDLierRKKLE 790
Cdd:PTZ00014  725 DSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAWeplVSVLEALILKIKKKRKV---RKNIK 801

                         730
                  ....*....|
gi 32566156   791 AVVTIQDNVR 800
Cdd:PTZ00014  802 SLVRIQAHLR 811

MYSc_Myo46

cd14907

class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...

97-710

9.55e-130

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: 417.51 E-value: 9.55e-130

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLYQ----------LQNDLPPHVYSVAQNAFHGILKGG 165
Cdd:cd14907    1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKeqiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  166 RNQSILITGESGAGKTENTKKIIDFILSSS--------------------VSNNTIGDCVVTSGVLLEAMGNARTTHNSN 225
Cdd:cd14907   81 KKQAIVISGESGAGKTENAKYAMKFLTQLSqqeqnseevltltssiratsKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  226 SSRFGKFIRIEFDENSKLI-GAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYfDNPHKSFLKLSKKVNEYKYLRNDDS 304
Cdd:cd14907  161 SSRFGKYVSILVDKKKRKIlGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGA-DQQLLQQLGLKNQLSGDRYDYLKKS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  305 ------MIDDAETAKMTDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSF--VESMQEVDNIAELLEMKSS 376
Cdd:cd14907  240 ncyevdTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSPccVKNKETLQIIAKLLGIDEE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  377 KLVDALTQPTIKVHDKLIRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAF---SVDDTESTCRLSRFIAVLDIAGF 453
Cdd:cd14907  320 ELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkDEKDQQLFQNKYLSIGLLDIFGF 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  454 EIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSDYLEEGIK--WTQVNFANHlQPTIDLIEK-PMGILSFLEEECVVPN 530
Cdd:cd14907  400 EVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSYTDN-QDVIDLLDKpPIGIFNLLDDSCKLAT 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  531 GSEKSLLEKLCSNLSNDSSFKKSKQTQKCStirhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFP 610
Cdd:cd14907  479 GTDEKLLNKIKKQHKNNSKLIFPNKINKDT----FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFS 554

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  611 PVpVNNLKTRRGTITNSTVS--FL---YKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIR 685
Cdd:cd14907  555 GE-DGSQQQNQSKQKKSQKKdkFLgskFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIR 633

                        650       660
                 ....*....|....*....|....*
gi 32566156  686 ICREGYPSRLSHSEFIERYSLLMKN 710
Cdd:cd14907  634 VRKQGYPYRKSYEDFYKQYSLLKKN 658

MYSc_Myo43

cd14904

class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...

97-747

1.45e-129

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: 416.65 E-value: 1.45e-129

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLY--QLQNDLPPHVYSVAQNAFHGILKGGRNQSILIT 173
Cdd:cd14904    1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYlkKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  174 GESGAGKTENTKKIIDFILS--SSVSNNTIgDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECY 251
Cdd:cd14904   81 GESGAGKTETTKIVMNHLASvaGGRKDKTI-AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  252 LLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLKLSKKvnEYKYLRND-DSM----IDDAETAKMTDEAFTRIGLSE 326
Cdd:cd14904  160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNC--QYQYLGDSlAQMqipgLDDAKLFASTQKSLSLIGLDN 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  327 EEKIWIFQILSAVLWIGDIKFGErSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIkvhdklIRKNQNLAKTLSS 406
Cdd:cd14904  238 DAQRTLFKILSGVLHLGEVMFDK-SDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSV------VTRNESVTVPLAP 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  407 ASA------MAKILYERLFGWIVKRCNDAFSVDDTestcRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHF 480
Cdd:cd14904  311 VEAeenrdaLAKAIYSKLFDWMVVKINAAISTDDD----RIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTD 386

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  481 MFAKEQSDYLEEGIKWTQVNFANHlQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSS-----FKKSKQ 555
Cdd:cd14904  387 VFKTVEEEYIREGLQWDHIEYQDN-QGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKKDnesidFPKVKR 465

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  556 TQkcstirhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPV--PVNNLKTRRGTITNSTVSF-- 631
Cdd:cd14904  466 TQ-------FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSeaPSETKEGKSGKGTKAPKSLgs 538

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  632 LYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNK 711
Cdd:cd14904  539 QFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPS 618

                        650       660       670
                 ....*....|....*....|....*....|....*...
gi 32566156  712 EQSKgaSEKEKCTLIcQDAQVRKE--RYAVGKTKLFCK 747
Cdd:cd14904  619 MHSK--DVRRTCSVF-MTAIGRKSplEYQIGKSLIYFK 653

MYSc_Myo39

cd14900

class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...

98-719

2.88e-129

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: 415.09 E-value: 2.88e-129

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   98 TVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLYQL-------------QNDLPPHVYSVAQNAFHGILK 163
Cdd:cd14900    2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYLLsfearssstrnkgSDPMPPHIYQVAGEAYKAMML 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  164 G--GR--NQSILITGESGAGKTENTKKIIDFI-----------LSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSR 228
Cdd:cd14900   82 GlnGVmsDQSILVSGESGSGKTESTKFLMEYLaqagdnnlaasVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  229 FGKFIRIEFDENSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSflklskkvNEYKylrnddsmidd 308
Cdd:cd14900  162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR--------DMYR----------- 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  309 aetaKMTDeAFTRIGLSEEEKIWIFQILSAVLWIGDIKF-----GERSGLDVSFV--ESMQEVDNIAELLEMKSSKLVDA 381
Cdd:cd14900  223 ----RVMD-AMDIIGFTPHERAGIFDLLAALLHIGNLTFehdenSDRLGQLKSDLapSSIWSRDAAATLLSVDATKLEKA 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  382 LTQPTIKVHDKLIRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTESTCRLSRFIAVLDIAGFEIIEKNSF 461
Cdd:cd14900  298 LSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHGGLHFIGILDIFGFEVFPKNSF 377

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  462 EQFCINYTNEKLQQFFNHFMFAKEQSDYLEEGIKWTQVNFANHlQPTIDLI-EKPMGILSFLEEECVVPNGSEKSLLEKL 540
Cdd:cd14900  378 EQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDN-QDCVNLIsQRPTGILSLIDEECVMPKGSDTTLASKL 456

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  541 CSNLSNDSSFKKSKqTQKCSTIrhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILsqsthpllkllfppvpVNNLKtr 620
Cdd:cd14900  457 YRACGSHPRFSASR-IQRARGL--FTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLF----------------VYGLQ-- 515

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  621 rgtitnstvsflYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEF 700
Cdd:cd14900  516 ------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEF 583

                        650
                 ....*....|....*....
gi 32566156  701 IERYSLLMKNKEQSKGASE 719
Cdd:cd14900  584 VARYFSLARAKNRLLAKKQ 602

MYSc_Myo41

cd14902

class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...

97-747

5.78e-127

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: 411.59 E-value: 5.78e-127

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLYQ----------LQNDLPPHVYSVAQNAFHGILKGG 165
Cdd:cd14902    1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspvsQLSELPPHVFAIGGKAFGGLLKPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  166 R-NQSILITGESGAGKTENTKKIIDFI------LSSSVSNNT----IGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIR 234
Cdd:cd14902   81 RrNQSILVSGESGSGKTESTKFLMQFLtsvgrdQSSTEQEGSdaveIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  235 IEFDENSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYfDNPHKSFLKLSKK-----VNEY--KYLRNDDSMID 307
Cdd:cd14902  161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGA-DKTLLDLLGLQKGgkyelLNSYgpSFARKRAVADK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  308 DAETAKMTDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKF-GERSGLDVSFV--ESMQEVDNIAELLEMKSSKLVDALTQ 384
Cdd:cd14902  240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFtAENGQEDATAVtaASRFHLAKCAELMGVDVDKLETLLSS 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  385 PTIKVHDKLIRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTESTCRLSR----FIAVLDIAGFEIIEKNS 460
Cdd:cd14902  320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSISDEDeelaTIGILDIFGFESLNRNG 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  461 FEQFCINYTNEKLQQFFNHFMFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKL 540
Cdd:cd14902  400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALSTKF 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  541 CsnlsndSSFKKSKQtqkcstirhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLF-------PPVP 613
Cdd:cd14902  480 Y------RYHGGLGQ---------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGadenrdsPGAD 544

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  614 VNNLKTRR-GTITNSTVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYP 692
Cdd:cd14902  545 NGAAGRRRySMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYS 624

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  693 SRLSHSEFIERYSLL------------MKNKEQSKGASEKEKCTLICQDAQVRKER------------------------ 736
Cdd:cd14902  625 VRLAHASFIELFSGFkcflstrdraakMNNHDLAQALVTVLMDRVLLEDGVEREEKnpgaltavtgdgsgtafendcrrk 704

                        730
                 ....*....|..
gi 32566156  737 -YAVGKTKLFCK 747
Cdd:cd14902  705 dVQVGRTLVFCK 716

MYSc_Myo14

cd14876

class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...

97-747

6.29e-123

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: 398.59 E-value: 6.29e-123

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQND---LPPHVYSVAQNAF---HGILKggrNQSI 170
Cdd:cd14876    1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDltkLPPHVFYTARRALenlHGVNK---SQTI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  171 LITGESGAGKTENTKKIIDFILSSS--VSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKI 248
Cdd:cd14876   78 IVSGESGAGKTEATKQIMRYFASAKsgNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  249 ECYLLEKSRVVFQSDGDRNFHIFYQMLSNYfDNPHKSFLKLsKKVNEYKYLRN---DDSMIDDAETAKMTDEAFTRIGLS 325
Cdd:cd14876  158 VAFLLEKSRIVTQDDNERSYHIFYQLLKGA-DSEMKSKYHL-LGLKEYKFLNPkclDVPGIDDVADFEEVLESLKSMGLT 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  326 EEEKIWIFQILSAVLWIGDIKFG--ERSGLDVSFV---ESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLI--RKNQ 398
Cdd:cd14876  236 EEQIDTVFSIVSGVLLLGNVKITgkTEQGVDDAAAisnESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIegRWTK 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  399 NLAKTLssASAMAKILYERLFGWIVKRCNDafsvdDTESTCRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFN 478
Cdd:cd14876  316 DDAEML--KLSLAKAMYDKLFLWIIRNLNS-----TIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFI 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  479 HFMFAKEQSDYLEEGIKWTQVNFANHLqPTID-LIEKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQ 557
Cdd:cd14876  389 DIVFERESKLYKDEGIPTAELEYTSNA-EVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDS 467

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  558 KcstiRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNLKTRRGTITNStvSFLykNQL 637
Cdd:cd14876  468 N----INFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKGSLIGS--QFL--KQL 539

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  638 QCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKGA 717
Cdd:cd14876  540 ESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSL 619

                        650       660       670
                 ....*....|....*....|....*....|
gi 32566156  718 SEKEKCTLICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14876  620 DPKVAALKLLESSGLSEDEYAIGKTMVFLK 649

MYSc_Myo30

cd14891

class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...

113-747

1.06e-120

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: 392.10 E-value: 1.06e-120

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  113 HTFCGLFCVVINPWRNI--PIYSDEVKQlyQLqNDLPPHVYSVAQNAFHG-ILKGGR--NQSILITGESGAGKTENTKKI 187
Cdd:cd14891   19 YTFMANVLIAVNPLRRLpePDKSDYINT--PL-DPCPPHPYAIAEMAYQQmCLGSGRmqNQSIVISGESGAGKTETSKII 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  188 IDFILSSSV-------------------SNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENS-KLIGAK 247
Cdd:cd14891   96 LRFLTTRAVggkkasgqdieqsskkrklSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFGKFMKLQFTKDKfKLAGAF 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  248 IECYLLEKSRVVFQSDGDRNFHIFYQMLSNYfDNPHKSFLKLSKKVNEYKYLRND---DSMIDDAETAKMTDEAFTRIGL 324
Cdd:cd14891  176 IETYLLEKSRLVAQPPGERNFHIFYQLLAGA-SAELLKELLLLSPEDFIYLNQSGcvsDDNIDDAANFDNVVSALDTVGI 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  325 SEEEKIWIFQILSAVLWIGDIKFGER---SGLDVSFVESMQE-VDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNL 400
Cdd:cd14891  255 DEDLQLQIWRILAGLLHLGNIEFDEEdtsEGEAEIASESDKEaLATAAELLGVDEEALEKVITQREIVTRGETFTIKRNA 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  401 AKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTESTcrlsrFIAVLDIAGFEIIE-KNSFEQFCINYTNEKLQQFFNH 479
Cdd:cd14891  335 REAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLP-----YIGVLDIFGFESFEtKNDFEQLLINYANEALQATFNQ 409

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  480 FMFAKEQSDYLEEGIKWTQVNFANHlQPTIDLI-EKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQK 558
Cdd:cd14891  410 QVFIAEQELYKSEGIDVGVITWPDN-RECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTHKRHPCFPRPHPKDM 488

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  559 cstiRH-FYVQHYAGEVHYNIDGWLDKNRDnvetsvldILSQSTHPLLKllfppvpvnnlktrrgtitnSTVSFLykNQL 637
Cdd:cd14891  489 ----REmFIVKHYAGTVSYTIGSFIDKNND--------IIPEDFEDLLA--------------------SSAKFS--DQM 534

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  638 QCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSK-G 716
Cdd:cd14891  535 QELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLfA 614

                        650       660       670
                 ....*....|....*....|....*....|.
gi 32566156  717 ASEKEKCTLICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14891  615 ENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645

MYSc_Myo45

cd14906

class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...

97-743

2.73e-115

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: 379.71 E-value: 2.73e-115

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLYQLQNDL---PPHVYSVAQNAFHGILKGGRNQSILI 172
Cdd:cd14906    1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNkspIPHIYAVALRAYQSMVSEKKNQSIII 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  173 TGESGAGKTENTKKIIDFILSSSVS-----------NNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENS 241
Cdd:cd14906   81 SGESGSGKTEASKTILQYLINTSSSnqqqnnnnnnnNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  242 KLI-GAKIECYLLEKSRVVFQSD-GDRNFHIFYQMLSNYfDNPHKSFLKLSKKVNEYKYLRNDDSMIDDAETAKM----- 314
Cdd:cd14906  161 GKIdGASIETYLLEKSRISHRPDnINLSYHIFYYLVYGA-SKDERSKWGLNNDPSKYRYLDARDDVISSFKSQSSnknsn 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  315 ------TDEAFT-------RIGLSEEEKIWIFQILSAVLWIGDIKFGERS-GLDVSFV--ESMQEVDNIAELLEMKSSKL 378
Cdd:cd14906  240 hnnkteSIESFQllkqsmeSMSINKEQCDAIFLSLAAILHLGNIEFEEDSdFSKYAYQkdKVTASLESVSKLLGYIESVF 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  379 VDALTQPTIKVHDK--LIRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTE------STCRLSRFIAVLDI 450
Cdd:cd14906  320 KQALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSndlaggSNKKNNLFIGVLDI 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  451 AGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSDYLEEGIKWTQVNFANHlQPTIDLIE-KPMGILSFLEEECVVP 529
Cdd:cd14906  400 FGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDN-KECIELIEkKSDGILSLLDDECIMP 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  530 NGSEKSLLEKLCSNLSNDSSFkkskqTQKCSTIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLF 609
Cdd:cd14906  479 KGSEQSLLEKYNKQYHNTNQY-----YQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF 553

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  610 PPVPVNNLKTRRGTITNSTVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICRE 689
Cdd:cd14906  554 QQQITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKM 633

                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....
gi 32566156  690 GYPSRLSHSEFIERYSLLMKNKEQSKGASEKEKCTLICQDAQVRKERYAVGKTK 743
Cdd:cd14906  634 GYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687

MYSc_Myo35

cd14896

class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...

97-747

4.30e-114

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: 374.12 E-value: 4.30e-114

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQ--LQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd14896    1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHprKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFiLSSSVSNNTIGDCVVTSGVL--LEAMGNARTTHNSNSSRFGKFIRIEFdENSKLIGAKIECYL 252
Cdd:cd14896   81 HSGSGKTEAAKKIVQF-LSSLYQDQTEDRLRQPEDVLpiLESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVSHYL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  253 LEKSRVVFQSDGDRNFHIFYQMLSNyFDNPHKSFLKLsKKVNEYKYLRN----DDSMIDDAETAKMTDEAFTRIGLSEEE 328
Cdd:cd14896  159 LETSRVVFQAQAERSFHVFYELLAG-LDPEEREQLSL-QGPETYYYLNQggacRLQGKEDAQDFEGLLKALQGLGLCAEE 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  329 KIWIFQILSAVLWIGDIKFG--ERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLSS 406
Cdd:cd14896  237 LTAIWAVLAAILQLGNICFSssERESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAIDA 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  407 ASAMAKILYERLFGWIVKRCNDAFS-VDDTESTCRlsrfIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKE 485
Cdd:cd14896  317 RDALAKTLYSRLFTWLLKRINAWLApPGEAESDAT----IGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQE 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  486 QSDYLEEGIKWTQVNFANHlQPTIDLI-EKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKqtqkcSTIRH 564
Cdd:cd14896  393 EEECQRELLPWVPIPQPPR-ESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQ-----LPLPV 466

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  565 FYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFppvpvNNLKTRRGTITN-STVSFLYKNQLQCLLDT 643
Cdd:cd14896  467 FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF-----QEAEPQYGLGQGkPTLASRFQQSLGDLTAR 541

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  644 LNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLmkNKEQSKGASEKEKC 723
Cdd:cd14896  542 LGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL--GSERQEALSDRERC 619

                        650       660
                 ....*....|....*....|....*
gi 32566156  724 -TLICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14896  620 gAILSQVLGAESPLYHLGATKVLLK 644

MYSc_Myo25

cd14886

class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...

97-747

1.40e-113

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: 373.07 E-value: 1.40e-113

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLYQ-------LQNDLPPHVYSVAQNAFHGILKGGRNQ 168
Cdd:cd14886    1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRqadtsrgFPSDLPPHSYAVAQSALNGLISDGISQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  169 SILITGESGAGKTENTKKIIDFI-LSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAK 247
Cdd:cd14886   81 SCIVSGESGAGKTETAKQLMNFFaYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  248 IECYLLEKSRVVFQSDGDRNFHIFYQMLSNyFDNPHKSFLKLsKKVNEYKYLRN----DDSMIDD-AETAKMTDEafTRI 322
Cdd:cd14886  161 ITSYMLELSRIEFQSTNERNYHIFYQCIKG-LSPEEKKSLGF-KSLESYNFLNAskcyDAPGIDDqKEFAPVRSQ--LEK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  323 GLSEEEKIWIFQILSAVLWIGDIKFGERSGLDV---SFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQN 399
Cdd:cd14886  237 LFSKNEIDSFYKCISGILLAGNIEFSEEGDMGVinaAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVT 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  400 LAKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTEstcrlSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNH 479
Cdd:cd14886  317 QAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADA-----RPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFIN 391

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  480 FMFAKEQSDYLEEGIKWTQVNFANHLQpTIDLIEKP-MGILSFLEEECVVPNGSEKSLLEKlCSNLSNDSSFKKSKQTQk 558
Cdd:cd14886  392 QVFKSEIQEYEIEGIDHSMITFTDNSN-VLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSS-CKSKIKNNSFIPGKGSQ- 468

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  559 CStirhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNlktrrGTITNSTVSFLYKNQLQ 638
Cdd:cd14886  469 CN----FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNED-----GNMKGKFLGSTFQLSID 539

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  639 CLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMK--NKEQSKG 716
Cdd:cd14886  540 QLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIShnSSSQNAG 619

                        650       660       670
                 ....*....|....*....|....*....|.
gi 32566156  717 ASEKEKCTLICQDAQVRKERYAVGKTKLFCK 747
Cdd:cd14886  620 EDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650

MYSc_Myo47

cd14908

class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...

97-708

1.43e-107

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: 357.30 E-value: 1.43e-107

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY-----------QLQNDLPPHVYSVAQNAFHGILKGG 165
Cdd:cd14908    1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllrsqgiESPQALGPHVFAIADRSYRQMMSEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  166 R-NQSILITGESGAGKTENTKKIIDFILSSSVSNN------------TIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKF 232
Cdd:cd14908   81 RaSQSILISGESGAGKTESTKIVMLYLTTLGNGEEgapnegeelgklSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  233 IRIEFDENSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSF------LKLSKKVNEYKYLRNDDS-- 304
Cdd:cd14908  161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYefhdgiTGGLQLPNEFHYTGQGGApd 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  305 --MIDDAETAKMTDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKF--GERSGLDVSFVESMQE-VDNIAELLEMKSSKLV 379
Cdd:cd14908  241 lrEFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFesKEEDGAAEIAEEGNEKcLARVAKLLGVDVDKLL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  380 DALTQPTIKVHDKLIRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAFSVD---DTESTCrlsrfiAVLDIAGFEII 456
Cdd:cd14908  321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWEndkDIRSSV------GVLDIFGFECF 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  457 EKNSFEQFCINYTNEKLQQFFNHFMFAKEQSDYLEEGIKWTQVNFANHlQPTIDLIE-KPMGILSFLEEECVVP-NGSEK 534
Cdd:cd14908  395 AHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDN-QDCLDTIQaKKKGILTMLDDECRLGiRGSDA 473

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  535 SLLEKLCSNLSNDSSFKKSKQT-------QKCSTIrhFYVQHYAGEVHYNID-GWLDKNRDNVETSVLDILSQSTHpllk 606
Cdd:cd14908  474 NYASRLYETYLPEKNQTHSENTrfeatsiQKTKLI--FAVRHFAGQVQYTVEtTFCEKNKDEIPLTADSLFESGQQ---- 547

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  607 llfppvpvnnlktrrgtitnstvsflYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRI 686
Cdd:cd14908  548 --------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRV 601

                        650       660
                 ....*....|....*....|..
gi 32566156  687 CREGYPSRLSHSEFIERYSLLM 708
Cdd:cd14908  602 ARSGYPVRLPHKDFFKRYRMLL 623

MYSc_Myo19

cd14880

class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...

97-745

1.93e-107

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: 356.08 E-value: 1.93e-107

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLYQLQ---NDLPPHVYSVAQNAFHGI--LKGGRNQSI 170
Cdd:cd14880    1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAApqpQKLKPHIFTVGEQTYRNVksLIEPVNQSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  171 LITGESGAGKTENTKKIIDF--ILSSSVSNNT-------IGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENS 241
Cdd:cd14880   81 VVSGESGAGKTWTSRCLMKFyaVVAASPTSWEshkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  242 KLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFlKLSKKVNeYKYLRNDDSMIDDaETAKMTDEAFTR 321
Cdd:cd14880  161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQW-HLPEGAA-FSWLPNPERNLEE-DCFEVTREAMLH 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  322 IGLSEEEKIWIFQILSAVLWIGDIKFGErSGLDVSFVESMQE----VDNIAELLEMKSSKLVDALTQPTIKV--HDKLIR 395
Cdd:cd14880  238 LGIDTPTQNNIFKVLAGLLHLGNIQFAD-SEDEAQPCQPMDDtkesVRTSALLLKLPEDHLLETLQIRTIRAgkQQQVFK 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  396 KNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAFSVDdtesTCRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQ 475
Cdd:cd14880  317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICAD----TDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQ 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  476 -FFNHFMFAkEQSDYLEEGIKWTQVNFANHlQPTIDLIE-KPMGILSFLEEECVVPNGSEKSLLE-KLCSNLSNDSSFKK 552
Cdd:cd14880  393 hFVAHYLRA-QQEEYAVEGLEWSFINYQDN-QTCLDLIEgSPISICSLINEECRLNRPSSAAQLQtRIESALAGNPCLGH 470

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  553 SKQTQKCStirhFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNnlKTRRGTITNS----- 627
Cdd:cd14880  471 NKLSREPS----FIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEE--KTQEEPSGQSrapvl 544

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  628 TVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLL 707
Cdd:cd14880  545 TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL 624

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....
gi 32566156  708 ------MKNKEQSKGASEKEKCTLICqdaqvrkeryavGKTKLF 745
Cdd:cd14880  625 rrlrphTSSGPHSPYPAKGLSEPVHC------------GRTKVF 656

MYSc_Myo13

cd14875

class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...

97-745

3.76e-105

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: 349.88 E-value: 3.76e-105

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTS-NVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQND---LPPHVYSVAQNAFHGILKGG-RNQSIL 171
Cdd:cd14875    1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDprlLPPHIWQVAHKAFNAIFVQGlGNQSVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  172 ITGESGAGKTENTKKIIDFI--LSSSVSNNT--------IGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENS 241
Cdd:cd14875   81 ISGESGSGKTENAKMLIAYLgqLSYMHSSNTsqrsiadkIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  242 K-LIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNyFDNPHKSFLKLSKKVNEYKYLRN---------DDSMIDDAET 311
Cdd:cd14875  161 GvMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAG-LSPEEKKELGGLKTAQDYKCLNGgntfvrrgvDGKTLDDAHE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  312 AKMTDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKFgERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALtqptikvhd 391
Cdd:cd14875  240 FQNVRHALSMIGVELETQNSIFRVLASILHLMEVEF-ESDQNDKAQIADETPFLTACRLLQLDPAKLRECF--------- 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  392 kLIRKNQNLAKTLSSAS-------AMAKILYERLFGWIVKRCNDAFSVDDTESTCRlsrFIAVLDIAGFEIIEKNSFEQF 464
Cdd:cd14875  310 -LVKSKTSLVTILANKTeaegfrnAFCKAIYVGLFDRLVEFVNASITPQGDCSGCK---YIGLLDIFGFENFTRNSFEQL 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  465 CINYTNEKLQQFFNHFMFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEksllEKLCSNL 544
Cdd:cd14875  386 CINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTT----ERFTTNL 461

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  545 SNDSSFKKSKQTQKCSTI-RHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNlktRRgt 623
Cdd:cd14875  462 WDQWANKSPYFVLPKSTIpNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLA---RR-- 536

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  624 itNSTVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIER 703
Cdd:cd14875  537 --KQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRY 614

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*...
gi 32566156  704 YSLLMKNKEQS--KGASEKEKCTLICQDAQV----RKERYAVGKTKLF 745
Cdd:cd14875  615 FYLIMPRSTASlfKQEKYSEAAKDFLAYYQRlygwAKPNYAVGKTKVF 662

MYSc_Myo16

cd14878

class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...

97-747

2.56e-104

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: 347.57 E-value: 2.56e-104

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLY-----QLQNDLPPHVYSVAQNAFHGILKGGRNQSIL 171
Cdd:cd14878    1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlsssgQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  172 ITGESGAGKTENTKKIIDFILSSSVSNNTIGDCVVT-SGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSK-LIGAKIE 249
Cdd:cd14878   81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFKhVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERKKhLTGARIY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  250 CYLLEKSRVVFQSDGDRNFHIFYQMLSNyFDNPHKSFLKLSKkVNEYKYLRNddSMIDDAETAKMT---------DEAFT 320
Cdd:cd14878  161 TYMLEKSRLVSQPPGQSNFLIFYLLMDG-LSAEEKYGLHLNN-LCAHRYLNQ--TMREDVSTAERSlnreklavlKQALN 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  321 RIGLSEEEKIWIFQILSAVLWIGDIKFGERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNL 400
Cdd:cd14878  237 VVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  401 AKTLSSASAMAKILYERLFGWIVKRCNDAF-SVDDTESTCRLSrfIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNH 479
Cdd:cd14878  317 QIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqSQDEQKSMQTLD--IGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINE 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  480 FMFAKEQSDYLEEGIKW-TQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCSNL--SN-DSSFKKSKQ 555
Cdd:cd14878  395 VLFLQEQTECVQEGVTMeTAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLesSNtNAVYSPMKD 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  556 TQKCSTIRH----FYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVnnlktrrgtitnsTVSF 631
Cdd:cd14878  475 GNGNVALKDqgtaFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLV-------------TIAS 541

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  632 LYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKN- 710
Cdd:cd14878  542 QLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTl 621

                        650       660       670
                 ....*....|....*....|....*....|....*..
gi 32566156  711 KEQSKGASEKEKCTLICQdaQVRKERYAVGKTKLFCK 747
Cdd:cd14878  622 LGEKKKQSAEERCRLVLQ--QCKLQGWQMGVRKVFLK 656

MYSc_Myo38

cd14899

class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...

97-704

6.55e-104

class XXXVIII myosin; The class XXXVIII 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: 276864 [Multi-domain] Cd Length: 717 Bit Score: 348.24 E-value: 6.55e-104

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLYQLQNDLP------------PHVYSVAQNAFHGILK 163
Cdd:cd14899    1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAYDHNSQfgdrvtstdprePHLFAVARAAYIDIVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  164 GGRNQSILITGESGAGKTENTKKIIDFI------------------LSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSN 225
Cdd:cd14899   81 NGRSQSILISGESGAGKTEATKIIMTYFavhcgtgnnnltnsesisPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  226 SSRFGKFIRIEF-DENSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLS---NYFDNPHKSFLKLSKKVNEYKYL-- 299
Cdd:cd14899  161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSadnNCVSKEQKQVLALSGGPQSFRLLnq 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  300 -----RNDDsmIDDAETAKMTDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKFGERS--GLDVSFVESMQ---------- 362
Cdd:cd14899  241 slcskRRDG--VKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPhkGDDTVFADEARvmssttgafd 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  363 EVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAF------------ 430
Cdd:cd14899  319 HFTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgade 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  431 -SVDDTESTcrlSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSDYLEEGIKWTQVNFANHlQPTI 509
Cdd:cd14899  399 sDVDDEEDA---TDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACL 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  510 DLIE-KPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKCSTIRHFYVQHYAGEVHYNIDGWLDKNRDN 588
Cdd:cd14899  475 ELFEhRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDS 554

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  589 VETSVLDILSQSTHPLLKLL--------------FPPVPVNNLKTRRGTITNSTVSFLYKNQLQCLLDTLNSSSAHFIRC 654
Cdd:cd14899  555 FCESAAQLLAGSSNPLIQALaagsndedangdseLDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRC 634

                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|
gi 32566156  655 VVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERY 704
Cdd:cd14899  635 IKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684

MYSc_Myo37

cd14898

class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...

98-707

4.55e-96

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: 321.85 E-value: 4.55e-96

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   98 TVLNALKIRYTSNVIHTFCGLFCVVINPWRNIpiYSDEVKQLYQLQND-LPPHVYSVAQNAFHGILKGGrNQSILITGES 176
Cdd:cd14898    2 ATLEILEKRYASGKIYTKSGLVFLALNPYETI--YGAGAMKAYLKNYShVEPHVYDVAEASVQDLLVHG-NQTIVISGES 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  177 GAGKTENTKKIIDFILSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDenSKLIGAKIECYLLEKS 256
Cdd:cd14898   79 GSGKTENAKLVIKYLVERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLLEKS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  257 RVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLKLSKkvneykYLRNDDSMIDDAETAKMTDEAFTRIGLSEEEKIWifQIL 336
Cdd:cd14898  157 RVTHHEKGERNFHIFYQFCASKRLNIKNDFIDTSS------TAGNKESIVQLSEKYKMTCSAMKSLGIANFKSIE--DCL 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  337 SAVLWIGDIKFGERSGLDVSFVESMQEVDNiaeLLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLSSASAMAKILYE 416
Cdd:cd14898  229 LGILYLGSIQFVNDGILKLQRNESFTEFCK---LHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNSMARLLYS 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  417 RLFGWIVKRCNDAFSvddtestCRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSDYLEEGIKW 496
Cdd:cd14898  306 NVFNYITASINNCLE-------GSGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGIEW 378

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  497 TQVNFANHLQPTIDlIEKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNdssFKKSKQTQKcstirhFYVQHYAGEVHY 576
Cdd:cd14898  379 PDVEFFDNNQCIRD-FEKPCGLMDLISEESFNAWGNVKNLLVKIKKYLNG---FINTKARDK------IKVSHYAGDVEY 448

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  577 NIDGWLDKNRDNVETsvldilsqsthpllkLLFPPVPVNNLKTRRGTITnstvsfLYKNQLQCLLDTLNSSSAHFIRCVV 656
Cdd:cd14898  449 DLRDFLDKNREKGQL---------------LIFKNLLINDEGSKEDLVK------YFKDSMNKLLNSINETQAKYIKCIR 507

                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|.
gi 32566156  657 SNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLL 707
Cdd:cd14898  508 PNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558

MYSc_Myo18

cd01386

class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...

97-745

2.05e-93

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: 317.71 E-value: 2.05e-93

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQ--LQNDLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd01386    1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKgcRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFILSS--SVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYL 252
Cdd:cd01386   81 RSGSGKTTNCRHILEYLVTAagSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  253 LEKSRVVFQSDGDRNFHIFYQMLS------------NYFDNPHKSFLKLSKKVNEykylRNDDSmiddAETAKMTdEAFT 320
Cdd:cd01386  161 LERSRVARRPEGESNFNVFYYLLAgadaalrtelhlNQLAESNSFGIVPLQKPED----KQKAA----AAFSKLQ-AAMK 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  321 RIGLSEEEKIWIFQILSAVL---WIGDIKfgERSGLDVSFV--ESMQEVdniAELL-----EMKS----SKLVDALTQPT 386
Cdd:cd01386  232 TLGISEEEQRAIWSILAAIYhlgAAGATK--AASAGRKQFArpEWAQRA---AYLLgctleELSSaifkHHLSGGPQQST 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  387 IKVHDKLIRKNQNLAKTLSSASA---MAKILYERLFGWIVKRCNDAFSvddteSTCRLSRFIAVLDIAGFEIIEKN---- 459
Cdd:cd01386  307 TSSGQESPARSSSGGPKLTGVEAlegFAAGLYSELFAAVVSLINRSLS-----SSHHSTSSITIVDTPGFQNPAHSgsqr 381

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  460 --SFEQFCINYTNEKLQQFFNHFMFAKEQSDYLEEGIkwtQVNFA---NHLQPTIDLIEK---------------PMGIL 519
Cdd:cd01386  382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENV---EVDFDlpeLSPGALVALIDQapqqalvrsdlrdedRRGLL 458

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  520 SFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKCSTIRHFYVQHYAG--EVHYNIDGWLDKNRDNVET-SVLDI 596
Cdd:cd01386  459 WLLDEEALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSEGPLQFVLGHLLGtnPVEYDVSGWLKAAKENPSAqNATQL 538

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  597 LSQSTHPLlkllfppvpvnnlktrrGTITNSTVSFLYKNQLQCLLDTLNSSSAHFIRCVV--SNYEKLPGK--------- 665
Cdd:cd01386  539 LQESQKET-----------------AAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLpqHNAGKDERStsspaagde 601

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  666 -IDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLM-----KNKEQSKGASEKEKCTLICQDAQVRKERYAV 739
Cdd:cd01386  602 lLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAppltkKLGLNSEVADERKAVEELLEELDLEKSSYRI 681


                 ....*.
gi 32566156  740 GKTKLF 745
Cdd:cd01386  682 GLSQVF 687

MYSc_Myo24A

cd14937

class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...

97-747

5.41e-91

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: 309.25 E-value: 5.41e-91

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQlyQLQNDLPPHVYSVAQNAFHGILKGGRNQSILITGES 176
Cdd:cd14937    1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINEYKN--KNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  177 GAGKTENTKKIIDFILSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYLLEKS 256
Cdd:cd14937   79 GSGKTEASKLVIKYYLSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLENI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  257 RVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLKLSKkvNEYKYLRNDDSMIDDAETAKMTDE---AFTRIGLSeEEKIWIF 333
Cdd:cd14937  159 RVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSE--NEYKYIVNKNVVIPEIDDAKDFGNlmiSFDKMNMH-DMKDDLF 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  334 QILSAVLWIGDIKF-----GERSGLDVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLSSAS 408
Cdd:cd14937  236 LTLSGLLLLGNVEYqeiekGGKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSICK 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  409 AMAKILYERLFGWIVKRCNDaFSVDDTEstcrLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSD 488
Cdd:cd14937  316 SISKDLYNKIFSYITKRINN-FLNNNKE----LNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETEL 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  489 YLEEGIKWTQVNFANHlQPTIDLIEKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKcstiRHFYVQ 568
Cdd:cd14937  391 YKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDIN----KNFVIK 465

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  569 HYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNLKTRRGTITnstvsFLYKNQLQCLLDTLNSSS 648
Cdd:cd14937  466 HTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRKNLIT-----FKYLKNLNNIISYLKSTN 540

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  649 AHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRIcREGYPSRLSHSEFIERYSLLMKNKEQSKGASEKEKCTLICQ 728
Cdd:cd14937  541 IYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQ 619

                        650
                 ....*....|....*....
gi 32566156  729 DaQVRKERYAVGKTKLFCK 747
Cdd:cd14937  620 N-TVDPDLYKVGKTMVFLK 637

MYSc_Myo17

cd14879

class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...

94-746

2.11e-83

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: 287.91 E-value: 2.11e-83

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   94 PNAATVLNALKIRYTSNVIHTFCGLFC-VVINPWRNIPIYSDEV---------KQLYQLQNDLPPHVYSVAQNAFHGILK 163
Cdd:cd14879    1 PSDDAITSHLASRFRSDLPYTRLGSSAlVAVNPYKYLSSNSDASlgeygseyyDTTSGSKEPLPPHAYDLAARAYLRMRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  164 GGRNQSILITGESGAGKTENTKKIIDFILSSSVSNNT---IGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDEN 240
Cdd:cd14879   81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKgtkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNER 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  241 SKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNpHKSFLKLSKKVNeYKYL-------RNDDSMIDDAEtaK 313
Cdd:cd14879  161 GRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPE-ERQHLGLDDPSD-YALLasygchpLPLGPGSDDAE--G 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  314 MTD--EAFTRIGLSEEEKIWIFQILSAVLWIGDIKFG-ERSGLDVS-FVESMQEVDNIAELLEMKSSKLVDALTQPTikv 389
Cdd:cd14879  237 FQElkTALKTLGFKRKHVAQICQLLAAILHLGNLEFTyDHEGGEESaVVKNTDVLDIVAAFLGVSPEDLETSLTYKT--- 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  390 hdKLIRKN------------QN---LAKTLssasamakilYERLFGWIV-----KRCndafSVDDTESTcrlsrFIAVLD 449
Cdd:cd14879  314 --KLVRKElctvfldpegaaAQrdeLARTL----------YSLLFAWVVetinqKLC----APEDDFAT-----FISLLD 372

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  450 IAGFEII---EKNSFEQFCINYTNEKLQQFFNHFMFAKeQSDYLE-EGIKWTQVnfanhlqPTID-------LIEKPMGI 518
Cdd:cd14879  373 FPGFQNRsstGGNSLDQFCVNFANERLHNYVLRSFFER-KAEELEaEGVSVPAT-------SYFDnsdcvrlLRGKPGGL 444

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  519 LSFLEEEC-VVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKCSTIRHFYVQHYAGEVHYNIDGWLDKNRDNVETsvlDIL 597
Cdd:cd14879  445 LGILDDQTrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSP---DFV 521

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  598 SqsthpllkLLfppvpvnnlktrrgtitNSTVSFLYKnqLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKC 677
Cdd:cd14879  522 N--------LL-----------------RGATQLNAA--LSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRS 574

                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  678 NGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKGASEkekctliCQDAQVRKER-YAVGKTKLFC 746
Cdd:cd14879  575 LGLPELAARLRVEYVVSLEHAEFCERYKSTLRGSAAERIRQC-------ARANGWWEGRdYVLGNTKVFL 637

MYSc_Myo44

cd14905

class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...

98-747

2.27e-76

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: 268.11 E-value: 2.27e-76

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   98 TVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLYQLQNDLPPHVYSVAQNAFHGILKGGRNQSILITGES 176
Cdd:cd14905    2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGES 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  177 GAGKTENTKKIIDFILSSSVSNNT-IGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYLLEK 255
Cdd:cd14905   82 GSGKSENTKIIIQYLLTTDLSRSKyLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  256 SRVVFQSDGDRNFHIFYQMLSNYFDNpHKSFLKLSkKVNEYKYLRNDDSM----IDDAETAKMTDEAFTRIGLSEEEKIW 331
Cdd:cd14905  162 NRVTYQNKGERNFHIFYQFLKGITDE-EKAAYQLG-DINSYHYLNQGGSIsvesIDDNRVFDRLKMSFVFFDFPSEKIDL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  332 IFQILSAVLWIGDIKFGERSGldVSFVESMQEVDNIAELLEMKSSKLVDALtqptikVHDKLIRKNQnlakTLSSASAMA 411
Cdd:cd14905  240 IFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENIL------ISDRSMPVNE----AVENRDSLA 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  412 KILYERLFGWIVKRCNDAFsvddteSTCRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSDYLE 491
Cdd:cd14905  308 RSLYSALFHWIIDFLNSKL------KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQT 381

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  492 EGIKW-TQVNFANHlQPTIDLIEKpmgILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTqkcstirhFYVQHY 570
Cdd:cd14905  382 ERIPWmTPISFKDN-EESVEMMEK---IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKPNK--------FGIEHY 449

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  571 AGEVHYNIDGWLDKNRDNV--ETSVL--------------------------------DILSQSTHPLLKLLFP-----P 611
Cdd:cd14905  450 FGQFYYDVRGFIIKNRDEIlqRTNVLhknsitkylfsrdgvfninatvaelnqmfdakNTAKKSPLSIVKVLLScgsnnP 529

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  612 VPVNNLKTR-------------RGTITNSTVSFLYKNQlqclldTLNSSSA--HFIRCVVSNYEKLPGKIDAPLVLAQLK 676
Cdd:cd14905  530 NNVNNPNNNsgggggggnsgggSGSGGSTYTTYSSTNK------AINNSNCdfHFIRCIKPNSKKTHLTFDVKSVNEQIK 603

                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32566156  677 CNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKGASEKEKCTLICQDAqVRKERYAVGKTKLFCK 747
Cdd:cd14905  604 SLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQRNFQNLFEKLKENDINIDS-ILPPPIQVGNTKIFLR 673

MYSc_Myo26

cd14887

class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...

110-745

1.79e-75

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: 266.90 E-value: 1.79e-75

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  110 NVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQND--LPPHVYSVAQNAFHGILKGGRNQSILITGESGAGKTENTKKI 187
Cdd:cd14887   22 NCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANsrLVPHPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSKHV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  188 IDFILSSS-----VSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYLLEKSRVVFQS 262
Cdd:cd14887  102 LTYLAAVSdrrhgADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIP 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  263 DGDRNFHIFYQMLSNYfdnphksflKLSKKVN-----EYKYLRNDDSMIddaetakmtdEAFTRIGLSEEEKIWIFQILS 337
Cdd:cd14887  182 SDEFSFHIFYALCNAA---------VAAATQKssageGDPESTDLRRIT----------AAMKTVGIGGGEQADIFKLLA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  338 AVLWIGDIKFGERSGLDVSFVESMQEVD--------NIAELLEMKS--------------SKLVDAL--TQPTIKVHDKL 393
Cdd:cd14887  243 AILHLGNVEFTTDQEPETSKKRKLTSVSvgceetaaDRSHSSEVKClssglkvteasrkhLKTVARLlgLPPGVEGEEML 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  394 I-----------RKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAF----------SVDDTESTCRlSRFIAVLDIAG 452
Cdd:cd14887  323 RlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLqrsakpsesdSDEDTPSTTG-TQTIGILDLFG 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  453 FEIIE---KNSFEQFCINYTNEKLQQFFNHFMFAKEQSDYLEEGIKWTQV--NFANHLQPTIDLIEKPMGILSFL---EE 524
Cdd:cd14887  402 FEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFPLASTLTSSPSSTSPFSptpSF 481

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  525 ECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKCSTI--------------------------RHFYVQHYAGEVHYNI 578
Cdd:cd14887  482 RSSSAFATSPSLPSSLSSLSSSLSSSPPVWEGRDNSDLfyeklnkniinsakyknitpalsrenLEFTVSHFACDVTYDA 561

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  579 DGWLDKNRDNVETSVLDILSQ-STHPLLKLLFPPVPVNNLKTRRGTITNStvsflYKNQLQCLLDTLNSSSAHFIRCVVS 657
Cdd:cd14887  562 RDFCRANREATSDELERLFLAcSTYTRLVGSKKNSGVRAISSRRSTLSAQ-----FASQLQQVLKALQETSCHFIRCVKP 636

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  658 NYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKnKEQSKGASEKEKCTLICQDAQVRKERY 737
Cdd:cd14887  637 NRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLP-MALREALTPKMFCKIVLMFLEINSNSY 715


                 ....*...
gi 32566156  738 AVGKTKLF 745
Cdd:cd14887  716 TFGKTKIF 723

MYSc_Myo12

cd14874

class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...

97-747

1.72e-72

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: 255.57 E-value: 1.72e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYqlqndlppHVYSVAQNAFHGILKGGRN-QSILITGE 175
Cdd:cd14874    1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC--------HISGVAENALDRIKSMSSNaESIVFGGE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  176 SGAGKTENTKKIIDFILSSSVSNNTIGDCVVTSGVLlEAMGNARTTHNSNSSRFGKFIRIEFDENSkLIGAKIECYL-LE 254
Cdd:cd14874   73 SGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIESVF-KSFGCAKTLKNDEATRFGCSIDLLYKRNV-LTGLNLKYTVpLE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  255 KSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSF-LKLSKKVNEYKYLRNDDSMIDDAETAKMTDEAFTRIGLSEEEKIWIF 333
Cdd:cd14874  151 VPRVISQKPGERNFNVFYEVYHGLNDEMKAKFgIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDDHCISIY 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  334 QILSAVLWIGDIKFGERSG----LDVSFVESMQEVDNIAELLEMKSSKLVDALTqPTIKVHDKLirknqNLAKTLSSASA 409
Cdd:cd14874  231 KIISTILHIGNIYFRTKRNpnveQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLL-PKSEDGTTI-----DLNAALDNRDS 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  410 MAKILYERLFGWIVKRCNDAFSvddtestCRL-SRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSD 488
Cdd:cd14874  305 FAMLIYEELFKWVLNRIGLHLK-------CPLhTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQLVD 377

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  489 YLEEGIKWT-QVNFANHLQPTIDLI-EKPMGILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKCstirHFY 566
Cdd:cd14874  378 YAKDGISVDyKVPNSIENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKERL----EFG 453

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  567 VQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFppvpvnnlktrRGTITNSTVSFLYKNQL-----QCLL 641
Cdd:cd14874  454 VRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLF-----------ESYSSNTSDMIVSQAQFilrgaQEIA 522

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  642 DTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNkEQSKGASEKE 721
Cdd:cd14874  523 DKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPG-DIAMCQNEKE 601

                        650       660
                 ....*....|....*....|....*..
gi 32566156  722 KCTLICQDAQVRKER-YAVGKTKLFCK 747
Cdd:cd14874  602 IIQDILQGQGVKYENdFKIGTEYVFLR 628

MYSc_Myo20

cd14881

class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...

98-745

3.25e-72

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: 255.04 E-value: 3.25e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   98 TVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-----IYSDEVKQLYQLQNdlpphvysVAQNAFHGILKGGRNQSILI 172
Cdd:cd14881    2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVGnpltlTSTRSSPLAPQLLK--------VVQEAVRQQSETGYPQAIIL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  173 TGESGAGKTENTKKIID--FILSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDEnSKLIGAKIEC 250
Cdd:cd14881   74 SGTSGSGKTYASMLLLRqlFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GALYRTKIHC 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  251 YLLEKSRVVFQSDGDRNFHIFYQMLSNyFDNPHKSFLKLSK-KVNEYKYLRNDDSMIDDAETAKMTDEAFTRIGLSEEEK 329
Cdd:cd14881  153 YFLDQTRVIRPLPGEKNYHIFYQMLAG-LSQEERVKLHLDGySPANLRYLSHGDTRQNEAEDAARFQAWKACLGILGIPF 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  330 IWIFQILSAVLWIGDIKFGERSGLDVSfVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLSSASA 409
Cdd:cd14881  232 LDVVRVLAAVLLLGNVQFIDGGGLEVD-VKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMSNMTRDA 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  410 MAKILYERLFGWIVKRCNDAFSVDDTESTCRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSDY 489
Cdd:cd14881  311 LAKALYCRTVATIVRRANSLKRLGSTLGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSSIESC 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  490 LEEGIKW-TQVNFANHLqPTIDLIEK-PMGILSFLEEECvVPNGSEKSLLEKLCSNLSNDSSFKKSKQtqkcSTIRHFYV 567
Cdd:cd14881  391 RDEGIQCeVEVDYVDNV-PCIDLISSlRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQNPRLFEAKP----QDDRMFGI 464

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  568 QHYAGEVHYNIDGWLDKNRDNVETSVLDILSQsthpllkllfppvpvnnlktrrgtiTNSTVSFL-----YKNQLQCLLD 642
Cdd:cd14881  465 RHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK-------------------------QNCNFGFAthtqdFHTRLDNLLR 519

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  643 TLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKG-ASEKE 721
Cdd:cd14881  520 TLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVeEKALE 599

                        650       660       670
                 ....*....|....*....|....*....|..
gi 32566156  722 KCTLICQDAQVRKE--------RYAVGKTKLF 745
Cdd:cd14881  600 DCALILQFLEAQPPsklssvstSWALGKRHIF 631

MYSc_Myo23

cd14884

class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...

97-705

4.00e-72

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: 255.99 E-value: 4.00e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   97 ATVLNALKIRYTSNVIHTFCGLFCVVINPWRNIP-IYSDEVKQLY---------QLQNDLPPHVYSVAQNAFHGILKGGR 166
Cdd:cd14884    1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYlhkksnsaaSAAPFPKAHIYDIANMAYKNMRGKLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  167 NQSILITGESGAGKTENTK---KIIDFILSSSVSNNTIgDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDE---- 239
Cdd:cd14884   81 RQTIVVSGHSGSGKTENCKflfKYFHYIQTDSQMTERI-DKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEvent 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  240 -----NSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSfLKLSKKVNEYKYLRNDDS---------- 304
Cdd:cd14884  160 qknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLAR-RNLVRNCGVYGLLNPDEShqkrsvkgtl 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  305 -----MIDDAETAKMTDE--------AFTRIGLSEEEKIWIFQILSAVLWIGDIKFgersgldvsfvesmqevDNIAELL 371
Cdd:cd14884  239 rlgsdSLDPSEEEKAKDEknfvallhGLHYIKYDERQINEFFDIIAGILHLGNRAY-----------------KAAAECL 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  372 EMKSSKLVDALTQPTIKVHDKLIRKNQNLAKTLSSASAMAKILYERLFGWI-------VKRCNDAFSVDDTESTCRLSRF 444
Cdd:cd14884  302 QIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIiedinrnVLKCKEKDESDNEDIYSINEAI 381

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  445 IAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSDYLEEGIKWTQVNFANHlQPTIDLIEKpmgILSFLEE 524
Cdd:cd14884  382 ISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSY-SDTLIFIAK---IFRRLDD 457

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  525 ECVVPN-GSEKS---------------LLEKL-----CSNLSNDSSFKKSKQTQKcstirHFYVQHYAGEVHYNIDGWLD 583
Cdd:cd14884  458 ITKLKNqGQKKTddhffryllnnerqqQLEGKvsygfVLNHDADGTAKKQNIKKN-----IFFIRHYAGLVTYRINNWID 532

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  584 KNRDNVETSVLDILSQSTHPLLKllfppvpVNNLKTRRGTItnSTVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNYEKLP 663
Cdd:cd14884  533 KNSDKIETSIETLISCSSNRFLR-------EANNGGNKGNF--LSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLP 603

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 32566156  664 GKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYS 705
Cdd:cd14884  604 NTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALK 645

MYSc_Myo21

cd14882

class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...

98-747

9.06e-70

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: 247.73 E-value: 9.06e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   98 TVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQN--DLPPHVYSVAQNAFHGILKGGRNQSILITGE 175
Cdd:cd14882    2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSrsDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  176 SGAGKTENTKKIIDFILSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIRIEFDENSKLIGAKIECYLLEK 255
Cdd:cd14882   82 SYSGKTTNARLLIKHLCYLGDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQLEK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  256 SRVVFQSDGDRNFHIFY---------QMLSNYF--DNPHKSFLKLSKKV--NEYKYLRNDDSmiDDAETAKMTDEAFTRI 322
Cdd:cd14882  162 LRVSTTDGNQSNFHIFYyfydfieaqNRLKEYNlkAGRNYRYLRIPPEVppSKLKYRRDDPE--GNVERYKEFEEILKDL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  323 GLSEEEKIWIFQILSAVLWIGDIKFGERSGldVSFVESMQEVDNIAELLEMKSSKLVDALTQPTIKVHDKLIRKNQNLAK 402
Cdd:cd14882  240 DFNEEQLETVRKVLAAILNLGEIRFRQNGG--YAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEE 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  403 TLSSASAMAKILYERLFGWIVKRCNDAFSV-----DDTEStcrlsrfIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFF 477
Cdd:cd14882  318 ARDARDVLASTLYSRLVDWIINRINMKMSFpravfGDKYS-------ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHY 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  478 NHFMFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVPNGSEKSLleklcsnlsnDSSFKKSKQTQ 557
Cdd:cd14882  391 NQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDASRSCQDQNYIM----------DRIKEKHSQFV 460

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  558 KCSTIRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNLKTRRGTITNSTVSFLyKNql 637
Cdd:cd14882  461 KKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQVRNMRTLAATFRATSLELL-KM-- 537

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  638 qcLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKGA 717
Cdd:cd14882  538 --LSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDFDETVEM 615

                        650       660       670
                 ....*....|....*....|....*....|
gi 32566156  718 SeKEKCTLICqdAQVRKERYAVGKTKLFCK 747
Cdd:cd14882  616 T-KDNCRLLL--IRLKMEGWAIGKTKVFLK 642

MYSc_Myo32

cd14893

class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...

100-745

7.65e-64

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: 232.94 E-value: 7.65e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  100 LNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQ------------NDLPPHVYSVAQNAFHGILKGGRN 167
Cdd:cd14893    4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSreqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  168 QSILITGESGAGKTENTKKIIDFI-------------LSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFGKFIR 234
Cdd:cd14893   84 QAVILLGGMGAGKSEAAKLIVQYLceigdeteprpdsEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  235 IEFDENSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPH-KSFLKLSKKVNEYKYLRNDDSMID----DA 309
Cdd:cd14893  164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPTlRDSLEMNKCVNEFVMLKQADPLATnfalDA 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  310 ETAKMTDEAFTRIGLSEEEKIWIFQILSAVLWIGDIKF-------GERSGLDVSFVESMQE--VDNIAELLemKSSKLVD 380
Cdd:cd14893  244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQScaLKDPAQIL--LAAKLLE 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  381 alTQPTikVHDKLIRKNQNLAKTLSSASAMAKI----------------LYERLFGWIVKRCNDAF-SVDDTESTCRL-- 441
Cdd:cd14893  322 --VEPV--VLDNYFRTRQFFSKDGNKTVSSLKVvtvhqarkardtfvrsLYESLFNFLVETLNGILgGIFDRYEKSNIvi 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  442 -SRFIAVLDIAGFEIIE--KNSFEQFCINYTNEKLQQFF------NHFMFAKEQSDYLEEGIK-WTQVNFANHLQPTIDL 511
Cdd:cd14893  398 nSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvqntlaINFSFLEDESQQVENRLTvNSNVDITSEQEKCLQL 477

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  512 IE-KPMGILSFLEEECVVPNGSEKSLLEKLCSnlSNDSSFKKSKQTQKCSTIRH-----------FYVQHYAGEVHYNID 579
Cdd:cd14893  478 FEdKPFGIFDLLTENCKVRLPNDEDFVNKLFS--GNEAVGGLSRPNMGADTTNEylapskdwrllFIVQHHCGKVTYNGK 555

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  580 GWLDKNRDNVETSVLDILSQSTHPLLKLLFPPVPVNNLK-------TRRGT-----------------ITNSTVSFLYkN 635
Cdd:cd14893  556 GLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSekaakqtEERGStsskfrksassaresknITDSAATDVY-N 634

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  636 QLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYsllmKNKEQSK 715
Cdd:cd14893  635 QADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY----KNVCGHR 710

                        730       740       750
                 ....*....|....*....|....*....|
gi 32566156  716 GASEKEKCTLiCQDAQVRKERYAVGKTKLF 745
Cdd:cd14893  711 GTLESLLRSL-SAIGVLEEEKFVVGKTKVY 739

MYSc_Myo24B

cd14938

class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...

98-745

4.80e-45

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: 175.41 E-value: 4.80e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   98 TVLNALKIRYTSNVIHTFCGLFCVVINPWRNIPIYSDEVKQLYQLQN---DLPPHVYSVAQNAFHGILKGGRNQSILITG 174
Cdd:cd14938    2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDcieDLSLNEYHVVHNALKNLNELKRNQSIIISG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  175 ESGAGKTENTKKIIDFI------------------------LSSSVSNNTIGDCVVTSGVLLEAMGNARTTHNSNSSRFG 230
Cdd:cd14938   82 ESGSGKSEIAKNIINFIayqvkgsrrlptnlndqeednihnEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  231 KFIRIEFDeNSKLIGAKIECYLLEKSRVVFQSDGDRNFHIFYQMLSNYFDNPHKSFLKlsKKVNEYKYLRND---DSMID 307
Cdd:cd14938  162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFL--KNIENYSMLNNEkgfEKFSD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  308 DAETAKMTDEAFTRIGLSEEEKIWIFQILSAVLWIGD---IKFGERSGLDVSFVESMQEVDNIAELLEMKSS-------- 376
Cdd:cd14938  239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteiVKAFRKKSLLMGKNQCGQNINYETILSELENSediglden 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  377 --------KLVDALTQPTIK-------VHDKLIRKNQNLAKTLSSASAMAKILYERLFGWIVKRCNDAFSVDDTESTcrL 441
Cdd:cd14938  319 vknlllacKLLSFDIETFVKyfttnyiFNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNINI--N 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  442 SRFIAVLDIAGFEIIEKNSFEQFCINYTNEKLQQFFNHFMFAKEQSDYLEEGI--KWTQVNFANhlQPTIDLIEKPM--G 517
Cdd:cd14938  397 TNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIfcEYNSENIDN--EPLYNLLVGPTegS 474

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  518 ILSFLEEECVVPNGSEKSLLEKLCSNLSNDSSFKKSKQTQKCStiRHFYVQHYAGEVHYNIDGWLDKNRDNVETSVLDIL 597
Cdd:cd14938  475 LFSLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNK--KTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMV 552

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  598 SQSTHPLLKLLFPPVPVNN------------------LKTRRGTITNSTVSFLYKNQLQCLLDTLNSSSAHFIRCVVSNY 659
Cdd:cd14938  553 KQSENEYMRQFCMFYNYDNsgniveekrrysiqsalkLFKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNE 632

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  660 EK-LPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYsllmknkeQSKGASEKEKCTLICQDAQVRKERYA 738
Cdd:cd14938  633 SKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIF--------DIKNEDLKEKVEALIKSYQISNYEWM 704


                 ....*..
gi 32566156  739 VGKTKLF 745
Cdd:cd14938  705 IGNNMIF 711

Motor_domain

cd01363

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...

119-238

4.95e-30

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: 117.45 E-value: 4.95e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  119 FCVVINPWRNIPIYSDE-VKQLYQL--QNDLPPHVYSVAQNAFHGILKGGRNQSILITGESGAGKTENTKKIIDFILSSS 195
Cdd:cd01363    1 VLVRVNPFKELPIYRDSkIIVFYRGfrRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32566156  196 VSNNTIGDCVVTSGV----------------LLEAMGNARTTHNSNSSRFGKFIRIEFD 238
Cdd:cd01363   81 FNGINKGETEGWVYLteitvtledqilqanpILEAFGNAKTTRNENSSRFGKFIEILLD 139

MYSc_Myo33

cd14894

class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...

205-709

3.09e-27

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: 120.23 E-value: 3.09e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  205 VVTSGVLLEAMGNARTTHNSNSSRFGKF--IRIEFDENS---KLIGAKIECYLLEKSRVVFQ---SDGDRN---FHIFYQ 273
Cdd:cd14894  249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSErgrESGDQNelnFHILYA 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  274 MLSNYFDNPhksFLKLSKKV----------------NEYK---YLRNDDSMIDDAETAKMTDEAFTRIGLSEEEKIWIFQ 334
Cdd:cd14894  329 MVAGVNAFP---FMRLLAKElhldgidcsaltylgrSDHKlagFVSKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFK 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  335 ILSAVLWIGDIK--FGERSG-LDVSFVESMQEVDNIAELLEMKSsklVDALTQPTIKVHDKLIRKNQNLAKTLSSAS--- 408
Cdd:cd14894  406 VLSAVLWLGNIEldYREVSGkLVMSSTGALNAPQKVVELLELGS---VEKLERMLMTKSVSLQSTSETFEVTLEKGQvnh 482

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  409 ---AMAKILYERLFGWIVKRCNDA------------FSVDDTESTCRLSRFIAVLDIAGFEIIEKNSFEQFCINYTNEKL 473
Cdd:cd14894  483 vrdTLARLLYQLAFNYVVFVMNEAtkmsalstdgnkHQMDSNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL 562

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  474 qqffnhfmFAKEQSDYLEEGIKWTQVNFANHLQPTIDLIEKPMGILSFLEEECVVP-----NGSEKSLLEKL-CSNLSND 547
Cdd:cd14894  563 --------YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHqsenmNAQQEEKRNKLfVRNIYDR 634

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  548 SSFKKSKQTQKCSTI-RH---------FYVQHYAGEVHYNIDGWLDKNRDNVETSVLDIL--SQSTH------PLLKLLF 609
Cdd:cd14894  635 NSSRLPEPPRVLSNAkRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLktSNSSHfcrmlnESSQLGW 714

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  610 PPVPVNNLKTRRGTITNSTVSFL--YKNQLQCLLDTLNSSSAHFIRCVVSNYEKLPGKIDAPLVLAQLKCNGVLEGIRIC 687
Cdd:cd14894  715 SPNTNRSMLGSAESRLSGTKSFVgqFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEIC 794

                        570       580
                 ....*....|....*....|....*.
gi 32566156  688 REGYPS----RLSHSEFIERYSLLMK 709
Cdd:cd14894  795 RNSSSSysaiDISKSTLLTRYGSLLR 820

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

848-1463

4.29e-20

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 97.43 E-value: 4.29e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    848 EIKNEEalkENLKLSMLLDREKSEKVKVQkELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIFNVLERKYNEQHKKVMK 927
Cdd:TIGR02168  217 ELKAEL---RELELALLVLRLEELREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    928 MNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLET 1007
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1008 ALEDEKARF--------------ARQNNTIGDMQKLISELNEKIARF--------DNIALNERNSTR----KIEREKEKL 1061
Cdd:TIGR02168  373 RLEELEEQLetlrskvaqlelqiASLNNEIERLEARLERLEDRRERLqqeieellKKLEEAELKELQaeleELEEELEEL 452

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1062 NEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMM------ADCVKELKDsHKERL------------- 1122
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQenlegfSEGVKALLK-NQSGLsgilgvlselisv 531

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1123 -KEMEQKVEDV--KRKNSKLENENSTQKSQIEtFQRESSVdsdyGRSS-------SGRLSTLGRQYSLTSIGSFSSIrTV 1192
Cdd:TIGR02168  532 dEGYEAAIEAAlgGRLQAVVVENLNAAKKAIA-FLKQNEL----GRVTflpldsiKGTEIQGNDREILKNIEGFLGV-AK 605

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1193 GLGSRKDSISDMTSSMYSL------------RRRDSTYDMTSST-----------IGLQRSPSTSQVMEKERRILELEKE 1249
Cdd:TIGR02168  606 DLVKFDPKLRKALSYLLGGvlvvddldnaleLAKKLRPGYRIVTldgdlvrpggvITGGSAKTNSSILERRREIEELEEK 685

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1250 KAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKNADNLALR---LKKALADCDEWKKK 1326
Cdd:TIGR02168  686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqLSKELTELEAEIEE 765

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1327 HEESIVESKTEIL-MERKRAMDRAEACEKETELKQSRmATIESARMELG-----------------GELARTQSELDRCR 1388
Cdd:TIGR02168  766 LEERLEEAEEELAeAEAEIEELEAQIEQLKEELKALR-EALDELRAELTllneeaanlrerlesleRRIAATERRLEDLE 844

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1389 QIIIQLEENLKSQESLGNSFGRHQTNLNFEIE---NLRDENCALKAKIRRQY------------KQIELLTQQDETNDEL 1453
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEallNERASLEEALALLRSELeelseelrelesKRSELRRELEELREKL 924

                          730
                   ....*....|
gi 32566156   1454 NHFENKVERL 1463
Cdd:TIGR02168  925 AQLELRLEGL 934

PRK03918

DNA double-strand break repair ATPase Rad50;

824-1370

1.07e-17

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 89.35 E-value: 1.07e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   824 NRDKERIEELENEKLKLEEEIQEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQgREKLLEKEREFRKTMEE 903
Cdd:PRK03918  175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL-KEEIEELEKELESLEGS 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   904 MEQNEEIFNVLERKYNEQHKKvmkmndvLREYERKIEQLNmEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDE 983
Cdd:PRK03918  254 KRKLEEKIRELEERIEELKKE-------IEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   984 LQNQIQKLSDENNEQRlTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNE-RNSTRKIEREKEKLN 1062
Cdd:PRK03918  326 IEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEIE 404

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1063 EELTTAKEIIQKQAKKIDELK---EECRKRKNEASRLERKL--EDKEAMMADCVKELKDSHKErLKEMEQKVEDVKRKNS 1137
Cdd:PRK03918  405 EEISKITARIGELKKEIKELKkaiEELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEKE-LKEIEEKERKLRKELR 483

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1138 KLENENSTQK---SQIETFQRESSVDSDYGRSSSGRLSTLGRQYSLT---SIGSFSSIRtvGLGSRKDSISDMTSSMYSL 1211
Cdd:PRK03918  484 ELEKVLKKESeliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLkekLIKLKGEIK--SLKKELEKLEELKKKLAEL 561

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1212 RRR-DSTYDMTSSTIGLQRSPSTSQVMEKERRILELEK------EKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTA 1284
Cdd:PRK03918  562 EKKlDELEEELAELLKELEELGFESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1285 NRKQSNQLQETTRQLNSAQ-KNADNLALRLKKALADCDEWKKKHEESI--VESKTEILMERKRAMDRAeacEKETELKQS 1361
Cdd:PRK03918  642 LEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRReeIKKTLEKLKEELEEREKA---KKELEKLEK 718


                  ....*....
gi 32566156  1362 RMATIESAR 1370
Cdd:PRK03918  719 ALERVEELR 727

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

827-1463

2.26e-17

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: 88.59 E-value: 2.26e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    827 KERIEELENEKLKLEEEIQEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLLEKEREFRKTMEEMEQ 906
Cdd:TIGR02169  183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    907 NEEIFNVLERKYNEQHKKVMKMNDV---------------LREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLE 971
Cdd:TIGR02169  263 LEKRLEEIEQLLEELNKKIKDLGEEeqlrvkekigeleaeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    972 KEVMEKSSLIDELQNQIQKLSDENNEqrltiakLETALEDEKARFARQNNTIGDMQKLISELNEKIARFdnialnERNST 1051
Cdd:TIGR02169  343 REIEEERKRRDKLTEEYAELKEELED-------LRAELEEVDKEFAETRDELKDYREKLEKLKREINEL------KRELD 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1052 RKIErEKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELKDShKERLKEMEQKVED 1131
Cdd:TIGR02169  410 RLQE-ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL-KEEYDRVEKELSK 487

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1132 VKRKNSKLENENSTQKSQIETFQRESSVDSDYGRSSSGRLSTLGR---QYSLTSigsfssirTVGLGSRKDSI-----SD 1203
Cdd:TIGR02169  488 LQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSvgeRYATAI--------EVAAGNRLNNVvveddAV 559

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1204 MTSSMYSLRR------------------RDSTYDMTSSTIGL---------QRSPSTSQV---------MEKERRIL--- 1244
Cdd:TIGR02169  560 AKEAIELLKRrkagratflplnkmrderRDLSILSEDGVIGFavdlvefdpKYEPAFKYVfgdtlvvedIEAARRLMgky 639

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1245 ---ELEKE---------------------KAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLN 1300
Cdd:TIGR02169  640 rmvTLEGElfeksgamtggsraprggilfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG 719

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1301 SAQKNADNLALRLKKA---LADCDEWKKKHEESIVESKTEIlmerkrAMDRAEACEKETELKQSRMATIESARMELGGEL 1377
Cdd:TIGR02169  720 EIEKEIEQLEQEEEKLkerLEELEEDLSSLEQEIENVKSEL------KELEARIEELEEDLHKLEEALNDLEARLSHSRI 793

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1378 ARTQSELDRCRQIIIQLEENLKSQESLGNSFGRHQTNLNFEIENLRDENCALKAKIRRQYKQIELL-TQQDETNDELNHF 1456
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLnGKKEELEEELEEL 873


                   ....*..
gi 32566156   1457 ENKVERL 1463
Cdd:TIGR02169  874 EAALRDL 880

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

868-1463

7.37e-17

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.03 E-value: 7.37e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    868 EKSEKVK-VQKELEEVEKQgrekLLEKEREFRKtmEEMEQNEEIFNVLERKYNEQHKKvmkmndvLREYERKIEQLNMEK 946
Cdd:TIGR02168  210 EKAERYKeLKAELRELELA----LLVLRLEELR--EELEELQEELKEAEEELEELTAE-------LQELEEKLEELRLEV 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    947 TDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSD--ENNEQRLTI-----AKLETALEDEKARFARQ 1019
Cdd:TIGR02168  277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAqlEELESKLDElaeelAELEEKLEELKEELESL 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1020 NNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERK 1099
Cdd:TIGR02168  357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1100 -----LEDKEAMMADCVKELkDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQI----------ETFQRES------- 1157
Cdd:TIGR02168  437 elqaeLEELEEELEELQEEL-ERLEEALEELREELEEAEQALDAAERELAQLQARLdslerlqenlEGFSEGVkallknq 515

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1158 --------------SVDSDYG------------------------------RSSSGRLSTL------------GRQYSLT 1181
Cdd:TIGR02168  516 sglsgilgvlseliSVDEGYEaaieaalggrlqavvvenlnaakkaiaflkQNELGRVTFLpldsikgteiqgNDREILK 595

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1182 SIGSFSSIrTVGLGSRKDSISDMTSSMYSL------------RRRDSTYDMTSST-----------IGLQRSPSTSQVME 1238
Cdd:TIGR02168  596 NIEGFLGV-AKDLVKFDPKLRKALSYLLGGvlvvddldnaleLAKKLRPGYRIVTldgdlvrpggvITGGSAKTNSSILE 674

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1239 KERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKNADNLALR---LKK 1315
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqLSK 754

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1316 ALADCDEWKKKHEESIVESKTEIlmerKRAMDRAEACEKETELKQSRMATIESARMELGGELARTQSELDRCRQIIIQLE 1395
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEEL----AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32566156   1396 ENLKSQEslgnsfgRHQTNLNFEIENLRDENCALKAKIRrqykqiELLTQQDETNDELNHFENKVERL 1463
Cdd:TIGR02168  831 RRIAATE-------RRLEDLEEQIEELSEDIESLAAEIE------ELEELIEELESELEALLNERASL 885

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

844-1399

8.66e-15

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 80.22 E-value: 8.66e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    844 IQEMEIKNEEALKENLKLsmlldreKSEKVKVQKELEEVEKQ------GREKL-LEK---EREFRKTMEEMEQNEEIFNV 913
Cdd:pfam01576   77 LHELESRLEEEEERSQQL-------QNEKKKMQQHIQDLEEQldeeeaARQKLqLEKvttEAKIKKLEEDILLLEDQNSK 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    914 LERKYNEQHKKVMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSD 993
Cdd:pfam01576  150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQA 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    994 ENNEQRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQ 1073
Cdd:pfam01576  230 QIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE 309

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1074 KQAKKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETF 1153
Cdd:pfam01576  310 DTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAEL 389

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1154 QRE-SSVDSDYGRSSSGRLSTLGRQYSLTSIGSFSSIRTVGLGSRkdsISDMTSSMYSLrrrdstydmtsstiglqrsps 1232
Cdd:pfam01576  390 QAElRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEK---LSKLQSELESV--------------------- 445

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1233 TSQVMEKERRILELEKEKAAINTDLQLVKRELD-------VYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQkn 1305
Cdd:pfam01576  446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQeetrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQ-- 523

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1306 adnlalrlkkalADCDEWKKKHEE--SIVESKTEilmERKRAMDRAEACEKETELKQSRMATIESARMELGGELARTQSE 1383
Cdd:pfam01576  524 ------------AQLSDMKKKLEEdaGTLEALEE---GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVD 588

                          570
                   ....*....|....*.
gi 32566156   1384 LDRCRQIIIQLEENLK 1399
Cdd:pfam01576  589 LDHQRQLVSNLEKKQK 604

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

876-1150

1.74e-14

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.95 E-value: 1.74e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    876 QKELEEVEKQgREKLLEKEREFRKTMEEME-QNEEIFNVLE---RKYNEQHKKVMKMNDVLREYERKIEQLNMEKTDLEN 951
Cdd:TIGR02168  676 RREIEELEEK-IEELEEKIAELEKALAELRkELEELEEELEqlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    952 ENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQNNTIGDMQKLIS 1031
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1032 ELNEKIARFDnialnerNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMADCV 1111
Cdd:TIGR02168  835 ATERRLEDLE-------EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 32566156   1112 KELKDShKERLKEMEQKVEDVKRKNSKLENENSTQKSQI 1150
Cdd:TIGR02168  908 SKRSEL-RRELEELREKLAQLELRLEGLEVRIDNLQERL 945

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

889-1168

3.26e-14

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.19 E-value: 3.26e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    889 KLLEKEREFRKTMEEMEQNEEIfnvLERKYNEQHKKVMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYS 968
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSS---LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    969 NLEKEVMEKSSLIDELQNQIQklsdennEQRLTIAKLETALEDEKARFARQNntIGDMQKLISELNEKIARFDNIALNER 1048
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIE-------ELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1049 NSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELKDSHKER------L 1122
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERdeleaqL 898

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 32566156   1123 KEMEQKVEDVKRKNSKLENENSTQKSQIET-FQRESSVDSDYGRSSS 1168
Cdd:TIGR02169  899 RELERKIEELEAQIEKKRKRLSELKAKLEAlEEELSEIEDPKGEDEE 945

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

823-1140

4.22e-14

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.79 E-value: 4.22e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    823 RNRDKERIEELENEKLKLEEEIQEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQ---GREKLLEKEREFRK 899
Cdd:TIGR02168  707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERleeAEEELAEAEAEIEE 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    900 TMEEMEQNEEIFNVLERKYNEQHKKVMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSS 979
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    980 LIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNialnERNSTR-KIEREK 1058
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL----RLEGLEvRIDNLQ 942

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1059 EKLNEELTTAKEIIQKQAKKIDELKEECRKRkneASRLERKLEDKEAMMADCVKELKDShKERLKEMEQKVEDVKRKNSK 1138
Cdd:TIGR02168  943 ERLSEEYSLTLEEAEALENKIEDDEEEARRR---LKRLENKIKELGPVNLAAIEEYEEL-KERYDFLTAQKEDLTEAKET 1018


                   ..
gi 32566156   1139 LE 1140
Cdd:TIGR02168 1019 LE 1020

Smc

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

889-1156

6.18e-13

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 6.18e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  889 KLLEKEREFRKTMEEMEQNeeifnvLERkyneqhkkvmkMNDVLREYERKIEQLNMEKTDLEnENQKLRETQNRQDSHYS 968
Cdd:COG1196  169 KYKERKEEAERKLEATEEN------LER-----------LEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELL 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  969 NLEKEVMEKSslIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNER 1048
Cdd:COG1196  231 LLKLRELEAE--LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1049 NSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMAdcvkELKDSHKERLKEMEQK 1128
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL----EAEAELAEAEEELEEL 384

                        250       260
                 ....*....|....*....|....*...
gi 32566156 1129 VEDVKRKNSKLENENSTQKSQIETFQRE 1156
Cdd:COG1196  385 AEELLEALRAAAELAAQLEELEEAEEAL 412

Smc

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

825-1109

1.05e-12

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 1.05e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  825 RDKERIEELENEKLKLEEEIQEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEkQGREKLLEKEREFRKTMEEM 904
Cdd:COG1196  243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-QDIARLEERRRELEERLEEL 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  905 EQNEEifnVLERKyneqhkkvmkmndvLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDEL 984
Cdd:COG1196  322 EEELA---ELEEE--------------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  985 QNQIQKLSDENNEQRLTIAKLETALEDEKARFARQnntigdmQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEE 1064
Cdd:COG1196  385 AEELLEALRAAAELAAQLEELEEAEEALLERLERL-------EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 32566156 1065 LTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMAD 1109
Cdd:COG1196  458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502

MAD

pfam05557

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...

844-1321

1.24e-12

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: 72.47 E-value: 1.24e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    844 IQEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIFNVLERKYNEQHK 923
Cdd:pfam05557   18 KKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKES 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    924 KVMKMNDV-------LREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVME---KSSLIDELQNQIQKLSD 993
Cdd:pfam05557   98 QLADAREVisclkneLSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNlekQQSSLAEAEQRIKELEF 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    994 ENNEQRLTIAKLETAledeKARFARqnntIGDMQKLISELNEKIARF-----DNIALNER--NSTRKIER---------- 1056
Cdd:pfam05557  178 EIQSQEQDSEIVKNS----KSELAR----IPELEKELERLREHNKHLnenieNKLLLKEEveDLKRKLEReekyreeaat 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1057 ---EKEKLNEELTTAKEIIQKQ----------AKKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELKDSHKE--- 1120
Cdd:pfam05557  250 lelEKEKLEQELQSWVKLAQDTglnlrspedlSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKied 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1121 ---RLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSvDSDYGRSSSGRLSTLGR-----QYSLTSIGSFSSIRTV 1192
Cdd:pfam05557  330 lnkKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELT-MSNYSPQLLERIEEAEDmtqkmQAHNEEMEAQLSVAEE 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1193 GLGSRKDSISDMTSSMYSLRRRDSTYDMTSSTIG-------LQRSPSTSQVMEKERRILELEKEKAAINTDLQLVKREL- 1264
Cdd:pfam05557  409 ELGGYKQQAQTLERELQALRQQESLADPSYSKEEvdslrrkLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVl 488

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32566156   1265 -----------DVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKNADNLALRLKKALADCD 1321
Cdd:pfam05557  489 hlsmnpaaeayQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAE 556

CwlO1

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

936-1207

2.30e-12

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 70.63 E-value: 2.30e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  936 ERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKAR 1015
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1016 FARQNNTIGDMQKL-----ISELNEKIARFDNIALNERNSTRKIEREKEKLNE---ELTTAKEIIQKQAKKIDELKEECR 1087
Cdd:COG3883   95 LYRSGGSVSYLDVLlgsesFSDFLDRLSALSKIADADADLLEELKADKAELEAkkaELEAKLAELEALKAELEAAKAELE 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1088 KRKNEASRLERKLEDKEAMMADCVKELKDSHKERLKEMEQKVEDVKRKNSKL--------ENENSTQKSQIETFQRESSV 1159
Cdd:COG3883  175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAaaaaaaaaAAAAAAAAAASAAGAGAAGA 254

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 32566156 1160 DSDYGRSSSGRLSTLGRQYSLTSIGSFSSIRTVGLGSRKDSISDMTSS 1207
Cdd:COG3883  255 AGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGG 302

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

845-1461

2.76e-12

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: 71.93 E-value: 2.76e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    845 QEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIFNVLERKYNEQHKK 924
Cdd:pfam02463  208 KALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    925 VMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAK 1004
Cdd:pfam02463  288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1005 LETALEDEKARFARQnntiGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKK-IDELK 1083
Cdd:pfam02463  368 LEQLEEELLAKKKLE----SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEEsIELKQ 443

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1084 EECRKRKNEASRLERKLEDKEAMMADCVKELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSVDSDY 1163
Cdd:pfam02463  444 GKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR 523

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1164 GRSSSGRLSTLGRQ------YSLTSIGSFSSIRTVGLGSRKDSISDMTSS---MYSLRRRDSTYDMTSSTIGLQRSPSTS 1234
Cdd:pfam02463  524 IISAHGRLGDLGVAvenykvAISTAVIVEVSATADEVEERQKLVRALTELplgARKLRLLIPKLKLPLKSIAVLEIDPIL 603

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1235 QVMEKERRILE--------LEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKNA 1306
Cdd:pfam02463  604 NLAQLDKATLEadeddkraKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE 683

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1307 DNLALRLKKALADCDEWKKKHEESI--VESKTEILMERKRAMDRAEACEKETELKQSRMATIESARMELG---GELARTQ 1381
Cdd:pfam02463  684 KAESELAKEEILRRQLEIKKKEQREkeELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEksrLKKEEKE 763

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1382 SELDRCRQIIIQLEENLKSQESLGNSfGRHQTNLNFEIENLRDENCALKAKIRRQYKQIELLTQQDETNDELNHFENKVE 1461
Cdd:pfam02463  764 EEKSELSLKEKELAEEREKTEKLKVE-EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALEL 842

Smc

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

866-1156

3.07e-12

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 3.07e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  866 DREKSEKVK-VQKELEEVEKQGR-EKLLEKEREFRKTMEEMEQNEEIFNVLERKyneqhkkvmkmndvLREYERKIEQLN 943
Cdd:COG1196  208 QAEKAERYReLKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAE--------------LAELEAELEELR 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  944 MEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQnnti 1023
Cdd:COG1196  274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA---- 349

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1024 gdmQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDK 1103
Cdd:COG1196  350 ---EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 32566156 1104 EAMMADcVKELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRE 1156
Cdd:COG1196  427 EEALAE-LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

824-1151

6.97e-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: 70.43 E-value: 6.97e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    824 NRDKERIEELENEKLKLEEEIQEMEIK----NEEALKENLKLSML---------LDREKSEKVKVQKELEEVEKQGREKL 890
Cdd:TIGR04523  162 NDLKKQKEELENELNLLEKEKLNIQKNidkiKNKLLKLELLLSNLkkkiqknksLESQISELKKQNNQLKDNIEKKQQEI 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    891 LEKEREFRKTMEEMEQ----NEEIFNVLERKYNE---QHKKVMKMNDVLREYERKIEQLNMEKTdlENENQKLRETQNRQ 963
Cdd:TIGR04523  242 NEKTTEISNTQTQLNQlkdeQNKIKKQLSEKQKEleqNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQ 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    964 DSHYSNLEKEVMEKSSLIDELQNQIQKL-------SDENNEQRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEK 1036
Cdd:TIGR04523  320 EKKLEEIQNQISQNNKIISQLNEQISQLkkeltnsESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1037 IARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMmadcVKELKD 1116
Cdd:TIGR04523  400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ----LKVLSR 475

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 32566156   1117 SHKERLKEMEQKVEDVKRKNSKLENENStQKSQIE 1151
Cdd:TIGR04523  476 SINKIKQNLEQKQKELKSKEKELKKLNE-EKKELE 509

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

892-1151

8.85e-12

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.10 E-value: 8.85e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    892 EKEREFRKtMEEMEQNEEIFNVLERKYNEQHKKVMKMNDVLREY-ERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNL 970
Cdd:TIGR02169  171 KKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRREREKAERYqALLKEKREYEGYELLKEKEALERQKEAIERQLASL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    971 EKEvmeksslIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQnntigdMQKLISELNEKIARF-DNIALNER- 1048
Cdd:TIGR02169  250 EEE-------LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR------VKEKIGELEAEIASLeRSIAEKERe 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1049 -----NSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELKDsHKERLK 1123
Cdd:TIGR02169  317 ledaeERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD-YREKLE 395

                          250       260
                   ....*....|....*....|....*...
gi 32566156   1124 EMEQKVEDVKRKNSKLENENSTQKSQIE 1151
Cdd:TIGR02169  396 KLKREINELKRELDRLQEELQRLSEELA 423

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

929-1149

1.43e-11

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: 67.87 E-value: 1.43e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  929 NDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETA 1008
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1009 LEDEKARFARQNNTI---GDMQKLISELN-EKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKE 1084
Cdd:COG4942   99 LEAQKEELAELLRALyrlGRQPPLALLLSpEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32566156 1085 ECRKRKNEASRLERKLEDKEAMMADCVKELKdSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQ 1149
Cdd:COG4942  179 LLAELEEERAALEALKAERQKLLARLEKELA-ELAAELAELQQEAEELEALIARLEAEAAAAAER 242

DUF5401

pfam17380

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

783-1126

2.30e-11

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: 68.61 E-value: 2.30e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    783 IERRKKLEAvvtiQDNVRQFAELSQWPWYRIYHltRGLIPRNRDKERIEELENEKLKLEeeIQEMEIKNEEALKENLKLS 862
Cdd:pfam17380  312 VERRRKLEE----AEKARQAEMDRQAAIYAEQE--RMAMERERELERIRQEERKRELER--IRQEEIAMEISRMRELERL 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    863 MLLDREKSEKVKvqKELEEVEKQgreKLLEKEREfRKTMEEMEQNEEIfnvleRKYNEQHKKVmKMNDVLREYERKIEQL 942
Cdd:pfam17380  384 QMERQQKNERVR--QELEAARKV---KILEEERQ-RKIQQQKVEMEQI-----RAEQEEARQR-EVRRLEEERAREMERV 451

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    943 NMEKTDLENENQKLRETQNRQDSHYSNLEKEvMEKSSLIDELQNQIQKLSDENNEQRLtiakletaLEDEKARfarqnnt 1022
Cdd:pfam17380  452 RLEEQERQQQVERLRQQEEERKRKKLELEKE-KRDRKRAEEQRRKILEKELEERKQAM--------IEEERKR------- 515

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1023 igdmqklisELNEKiarfdniALNERNSTRKIEREKEKLNEELTTAKEIIQKQakkidELKEECRKRKNEASRLERKLED 1102
Cdd:pfam17380  516 ---------KLLEK-------EMEERQKAIYEEERRREAEEERRKQQEMEERR-----RIQEQMRKATEERSRLEAMERE 574

                          330       340
                   ....*....|....*....|....
gi 32566156   1103 KEAMmadcvKELKDSHKERlKEME 1126
Cdd:pfam17380  575 REMM-----RQIVESEKAR-AEYE 592

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

844-1106

7.21e-11

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 7.21e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    844 IQEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVE-KQGREKLLEKEREFRKTMEEMEQNEEIFNVLERKYNEQH 922
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    923 -----------KKVMKMNDV---LREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQI 988
Cdd:TIGR02169  826 lekeylekeiqELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    989 QKLSDENNEQRLTIAKLETALEDEKarfaRQNNTIGDMQKLISELNEKIARFDNIALNernsTRKIEREKEKLNEELTTA 1068
Cdd:TIGR02169  906 EELEAQIEKKRKRLSELKAKLEALE----EELSEIEDPKGEDEEIPEEELSLEDVQAE----LQRVEEEIRALEPVNMLA 977

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 32566156   1069 KEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAM 1106
Cdd:TIGR02169  978 IQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

850-1294

1.99e-10

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: 65.51 E-value: 1.99e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    850 KNEEALKenlKLSMLLDREKSEKVKVQK-------ELEEVEK--QGREKLLEKEREFRKTMEEMEQNE-EIFNVLERKYN 919
Cdd:pfam05483  374 KNEDQLK---IITMELQKKSSELEEMTKfknnkevELEELKKilAEDEKLLDEKKQFEKIAEELKGKEqELIFLLQAREK 450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    920 EQHKKVMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQR 999
Cdd:pfam05483  451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEE 530

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1000 LTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKI 1079
Cdd:pfam05483  531 RMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI 610

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1080 DELKEECRKRKNEASRLERKLEDKEAMMADCVKELkDSHKERLKEM----EQKVEDVKRKNSKLENENSTQKSQI-ETFQ 1154
Cdd:pfam05483  611 EELHQENKALKKKGSAENKQLNAYEIKVNKLELEL-ASAKQKFEEIidnyQKEIEDKKISEEKLLEEVEKAKAIAdEAVK 689

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1155 RESSVDSDYgrsssgrlstlgrqysltsigsfssirtvglgsrKDSISDMTSSMYSLRRR-DSTYDMTSSTIGLQRSPST 1233
Cdd:pfam05483  690 LQKEIDKRC----------------------------------QHKIAEMVALMEKHKHQyDKIIEERDSELGLYKNKEQ 735

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32566156   1234 SQvmekerrilelEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQE 1294
Cdd:pfam05483  736 EQ-----------SSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

850-1315

2.33e-10

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.43 E-value: 2.33e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    850 KNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLLekerefrkTMEEMEQNEEIFNVLERKYNEQHKKVMKMN 929
Cdd:TIGR04523  160 KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL--------LLSNLKKKIQKNKSLESQISELKKQNNQLK 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    930 DVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQ----KLSDENNE-QRLTIAK 1004
Cdd:TIGR04523  232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlksEISDLNNQkEQDWNKE 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1005 LETALEDEKARFARQNNTIGDMQKLISELNEKIArfdnialNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKE 1084
Cdd:TIGR04523  312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS-------QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ 384

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1085 ECRKRKNEASRLERKLEDKEAMMADCVKELKDSHKERLKeMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSVDSDYG 1164
Cdd:TIGR04523  385 EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL-LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1165 RSSSGRLSTLGRQYSltSIGSFSSIRTVGLGSRKDSISDMTSSMYSLRRRDSTYdmtsstiglqrspsTSQVMEKERRIL 1244
Cdd:TIGR04523  464 ESLETQLKVLSRSIN--KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL--------------TKKISSLKEKIE 527

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32566156   1245 ELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQtaNRKQSNQLQETTRQLNSAQKNADNLALRLKK 1315
Cdd:TIGR04523  528 KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDE--KNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596

CCDC158

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

845-1247

4.47e-10

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: 64.75 E-value: 4.47e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    845 QEMEIKNEEALKENLKLSMlldrekSEKVKVQKELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIFNvlERKYNEQHKK 924
Cdd:pfam15921  539 EGDHLRNVQTECEALKLQM------AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIN--DRRLELQEFK 610

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    925 VMK--MNDVLREYERKIEQLNMEKTDLENENQK----LRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQ 998
Cdd:pfam15921  611 ILKdkKDAKIRELEARVSDLELEKVKLVNAGSErlraVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEM 690

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    999 RLTIAKLETALEDEKARFARQNNTIGDM--------------QKLISE-------LNEKIARFDNIALNERNSTRKIERE 1057
Cdd:pfam15921  691 ETTTNKLKMQLKSAQSELEQTRNTLKSMegsdghamkvamgmQKQITAkrgqidaLQSKIQFLEEAMTNANKEKHFLKEE 770

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1058 KEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELKDSHKERLKEMEQKVEDVKRKNS 1137
Cdd:pfam15921  771 KNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQG 850

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1138 KLENENSTQKSQIETfqressvDSDYGRSSSGRLSTlgrqYSLTSIGSFSSIRTVGLgsRKDSISDMTSSMYSLRR--RD 1215
Cdd:pfam15921  851 PGYTSNSSMKPRLLQ-------PASFTRTHSNVPSS----QSTASFLSHHSRKTNAL--KEDPTRDLKQLLQELRSviNE 917

                          410       420       430
                   ....*....|....*....|....*....|...
gi 32566156   1216 STYDMTSSTIGLQRSPSTSQVMEKERR-ILELE 1247
Cdd:pfam15921  918 EPTVQLSKAEDKGRAPSLGALDDRVRDcIIESS 950

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

826-1341

5.19e-10

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.27 E-value: 5.19e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    826 DKERIEELENEKLKLEEEIQEMEIKNEEALKENLKLSMLLDR--EKSEKVKVQKE-LEEVEKQGREKLLEKEREFRKTME 902
Cdd:TIGR04523  115 DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKlnNKYNDLKKQKEeLENELNLLEKEKLNIQKNIDKIKN 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    903 EMEQNEEIFNVLErKYNEQHK----KVMKMNDVLREYERKIEQLNMEKTDLENENQK-------LRETQNRQDSHYSNLE 971
Cdd:TIGR04523  195 KLLKLELLLSNLK-KKIQKNKslesQISELKKQNNQLKDNIEKKQQEINEKTTEISNtqtqlnqLKDEQNKIKKQLSEKQ 273

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    972 KEVMEKSSLIDELQNQIQ----KLSDENNE-QRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIArfdnialN 1046
Cdd:TIGR04523  274 KELEQNNKKIKELEKQLNqlksEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS-------Q 346

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1047 ERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELKDSHKERLKeME 1126
Cdd:TIGR04523  347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL-LE 425

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1127 QKVEDVKRKNSKLENENSTQKSQIETFQRESSVDSDYGRSSSGRLSTLGRQYSltSIGSFSSIRTVGLGSRKDSISDMTS 1206
Cdd:TIGR04523  426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN--KIKQNLEQKQKELKSKEKELKKLNE 503

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1207 SMYSLRRRDSTYDMTSSTIGLQRSPSTSQVMEKERRILELEKEKAAINTDL--QLVKRELDVYKSQLSAVESEKESLQTA 1284
Cdd:TIGR04523  504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKK 583

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32566156   1285 NRKQSNQLQETTRQ---LNSAQKNADNLALRLKKALADCDEWKKKHEESI--VESKTEILME 1341
Cdd:TIGR04523  584 QEEKQELIDQKEKEkkdLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIknIKSKKNKLKQ 645

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

845-1153

5.60e-10

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.89 E-value: 5.60e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    845 QEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLLEKErEFRKTMEEMEQNEEifnVLERKYNEQHKK 924
Cdd:TIGR04523  408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK-NLDNTRESLETQLK---VLSRSINKIKQN 483

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    925 VMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRL---- 1000
Cdd:TIGR04523  484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLekei 563

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1001 -----TIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTT---AKEII 1072
Cdd:TIGR04523  564 deknkEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNiksKKNKL 643

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1073 QKQAKKIDELKEECRKRKNE----ASRLERKLEDKEAMMADCVKELKDSHKERLKEM---------EQKVEDVKRKNSKL 1139
Cdd:TIGR04523  644 KQEVKQIKETIKEIRNKWPEiikkIKESKTKIDDIIELMKDWLKELSLHYKKYITRMirikdlpklEEKYKEIEKELKKL 723

                          330
                   ....*....|....
gi 32566156   1140 ENENSTQKSQIETF 1153
Cdd:TIGR04523  724 DEFSKELENIIKNF 737

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

882-1464

8.22e-10

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.50 E-value: 8.22e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    882 VEKQGREKLLEKEreFRKTMEEMEQNEEIFNVLERKYNEQHKKVMKMNDVLREYERKIEQLNmekTDLENENQKLretqN 961
Cdd:TIGR04523   29 NKQDTEEKQLEKK--LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN---DKLKKNKDKI----N 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    962 RQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFD 1041
Cdd:TIGR04523  100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1042 NIALNERNSTRKIEREKEKLNEELTTAKEIIQKQ---AKKIDELKEECRKRKNEASRLERKLEDKEAMMADC------VK 1112
Cdd:TIGR04523  180 KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNkslESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTqtqlnqLK 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1113 ELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSVDSDYGRSSsgrlstlgrqySLTSIGSFSSIRTV 1192
Cdd:TIGR04523  260 DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKS-----------ELKNQEKKLEEIQN 328

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1193 GLGSRKDSISDMTSSMYSLRRrdstydmtsstiglQRSPSTSQVMEKERRILELEKEkaaintdLQLVKRELDVYKSQLS 1272
Cdd:TIGR04523  329 QISQNNKIISQLNEQISQLKK--------------ELTNSESENSEKQRELEEKQNE-------IEKLKKENQSYKQEIK 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1273 AVESEKESLQTANRKQSNQLQETTRQLNSAQKNADNLALRLKKALADcDEWKKKHEESIVESKTEILMERKRAMDRAEAC 1352
Cdd:TIGR04523  388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET-IIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1353 EKETELKQSRMATIESARMELGGELARTQSELDRCRQIIIQLEENLKSQESLGNSFGRHQTNLNFEIENLRDENCALKAK 1432
Cdd:TIGR04523  467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546

                          570       580       590
                   ....*....|....*....|....*....|....*
gi 32566156   1433 IRR---QYKQIELLTQQDETNDELNHFENKVERLL 1464
Cdd:TIGR04523  547 LNKddfELKKENLEKEIDEKNKEIEELKQTQKSLK 581

DUF3584

pfam12128

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...

876-1463

9.93e-10

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: 63.70 E-value: 9.93e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    876 QKELEEVEKQGREKLLEKEREFRKTMEEMeqNEEIFNVLERKYNEQHKKvmkmnDVLREYERKIEQLNME--KTDLENEN 953
Cdd:pfam12128  278 QEERQETSAELNQLLRTLDDQWKEKRDEL--NGELSAADAAVAKDRSEL-----EALEDQHGAFLDADIEtaAADQEQLP 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    954 QKLRETQNRQDSHYSNLEKEvmekSSLIDELQNQIQKLSDENNEQrltIAKLETALEDEKARFARQNNTI-GDMQKLISE 1032
Cdd:pfam12128  351 SWQSELENLEERLKALTGKH----QDVTAKYNRRRSKIKEQNNRD---IAGIKDKLAKIREARDRQLAVAeDDLQALESE 423

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1033 LNEKI-ARFDNIALNERNSTRKIEREKEKLN-----EELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLedkeam 1106
Cdd:pfam12128  424 LREQLeAGKLEFNEEEYRLKSRLGELKLRLNqatatPELLLQLENFDERIERAREEQEAANAEVERLQSELRQA------ 497

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1107 madcvKELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSVDsdyGRSSSGRL---STLGR-----QY 1178
Cdd:pfam12128  498 -----RKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPD---WEQSIGKVispELLHRtdldpEV 569

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1179 SLTSIGSFSSIRTVGLGSRKDSISDMTSSMYSLRRRdstYDMTSSTIGLQRSpstsqvmekerRILELEKEKAAINTDLQ 1258
Cdd:pfam12128  570 WDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRER---LDKAEEALQSARE-----------KQAAAEEQLVQANGELE 635

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1259 LVKRELDVYKSQLSAVE-------SEKESLQTA-NRKQSNQLQETTRQLNSAQKNADNLALRLKKALADCDEWKKKHEES 1330
Cdd:pfam12128  636 KASREETFARTALKNARldlrrlfDEKQSEKDKkNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTE 715

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1331 ------IVES---------KTEILMERKRAMDRAEACEKE--TELKQSRMATIESARMELG-GELARTQSELDRCRQIII 1392
Cdd:pfam12128  716 kqaywqVVEGaldaqlallKAAIAARRSGAKAELKALETWykRDLASLGVDPDVIAKLKREiRTLERKIERIAVRRQEVL 795

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32566156   1393 QLEENLKSQESLGNSfgRHQT---NLNFEIENLRDENCALKAKIRRQYKQIE-----LLTQQDETNDELNHFENKVERL 1463
Cdd:pfam12128  796 RYFDWYQETWLQRRP--RLATqlsNIERAISELQQQLARLIADTKLRRAKLEmerkaSEKQQVRLSENLRGLRCEMSKL 872

PRK02224

DNA double-strand break repair Rad50 ATPase;

864-1436

1.02e-09

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 1.02e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   864 LLDREKSEKVKVQKELEEVEKQG-REKLLEKEREFRKTMEEMEQNEEifnvlERKYNEQHKKvmKMNDVLREYERKIEQL 942
Cdd:PRK02224  181 VLSDQRGSLDQLKAQIEEKEEKDlHERLNGLESELAELDEEIERYEE-----QREQARETRD--EADEVLEEHEERREEL 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   943 nmekTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQNNT 1022
Cdd:PRK02224  254 ----ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1023 IGDMQKLISELNEKIARF-DNIALNERNSTRKIEREKEkLNEELTTAKEIIQKQAKKIDELKEECR-----------KRK 1090
Cdd:PRK02224  330 LEECRVAAQAHNEEAESLrEDADDLEERAEELREEAAE-LESELEEAREAVEDRREEIEELEEEIEelrerfgdapvDLG 408

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1091 NEASRLERKLEDKEAMMAD-----------------------------CVKELKDS-HKERLKEMEQKVEDVKRKNSKLE 1140
Cdd:PRK02224  409 NAEDFLEELREERDELREReaeleatlrtarerveeaealleagkcpeCGQPVEGSpHVETIEEDRERVEELEAELEDLE 488

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1141 NENSTQKSQIETFQRESSVDSdygrsssgRLSTLGRQYSLtsIGSFSSIRTVGLGSRKDSISdmtssmySLRRRDSTYDM 1220
Cdd:PRK02224  489 EEVEEVEERLERAEDLVEAED--------RIERLEERRED--LEELIAERRETIEEKRERAE-------ELRERAAELEA 551

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1221 TSSTIGLQRSPSTSQVMEKERRILELEKEKAAINTDLQlvkrELDVYKSQLSAVESEKESLQTANRKQSnQLQETTRQln 1300
Cdd:PRK02224  552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE----SLERIRTLLAAIADAEDEIERLREKRE-ALAELNDE-- 624

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1301 saqknadnlalrLKKALADCDEWKKKHEESIVESKTEILMERKramDRAEACEKETELKqsrMATIESARMELGGELART 1380
Cdd:PRK02224  625 ------------RRERLAEKRERKRELEAEFDEARIEEAREDK---ERAEEYLEQVEEK---LDELREERDDLQAEIGAV 686

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 32566156  1381 QSELDRcrqiiiqLEENLKSQESLGNSFGRHQTnLNFEIENLRDENCALKAKIRRQ 1436
Cdd:PRK02224  687 ENELEE-------LEELRERREALENRVEALEA-LYDEAEELESMYGDLRAELRQR 734

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

825-1142

1.18e-09

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 1.18e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    825 RDKERIEEleneklkleeeiqeMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQgREKLLEKEREFRktmEEM 904
Cdd:TIGR02169  678 RLRERLEG--------------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE-IEQLEQEEEKLK---ERL 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    905 EQNEEIFNVLERKYNEQHKKVMKMNDVLREYERKIEQLNMEKTDLEnenQKLRETQNRQ-DSHYSNLEKEVMEKSSLIDE 983
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEiQAELSKLEEEVSRIEARLRE 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    984 LQNQIQKLSDENNEQRLTIAKLETALEDEKARfarqnntIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNE 1063
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ-------IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1064 ELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEammaDCVKELKDSHKERLKEMEQK--VEDVKRKNSKLEN 1141
Cdd:TIGR02169  890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE----EELSEIEDPKGEDEEIPEEElsLEDVQAELQRVEE 965


                   .
gi 32566156   1142 E 1142
Cdd:TIGR02169  966 E 966

PRK03918

DNA double-strand break repair ATPase Rad50;

844-1127

1.19e-09

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.19e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   844 IQEMEIKNEEALKENLKLSMLLDREK--SEKVKVQKELEEVEKQ----GREKLLEKEREFRKTMEEMEQNEEIFNVLERK 917
Cdd:PRK03918  468 LKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKlkkyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   918 YNEqhkkvmkmndvLREYERKIEQLNMEKTDLENENQKL-RETQNRQDSHYSNLEKEVMEksslIDELQNQIQKLSDENN 996
Cdd:PRK03918  548 LEK-----------LEELKKKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKE----LEPFYNEYLELKDAEK 612

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   997 EQRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNE-RNSTRKIEREKEKLNEELTTAKEIIQKQ 1075
Cdd:PRK03918  613 ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEElREEYLELSRELAGLRAELEELEKRREEI 692

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 32566156  1076 AKKIDELKEECRKR---KNEASRLERKLEDKEAMMADcVKELKDSHKER-LKEMEQ 1127
Cdd:PRK03918  693 KKTLEKLKEELEERekaKKELEKLEKALERVEELREK-VKKYKALLKERaLSKVGE 747

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

876-1108

1.29e-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: 62.09 E-value: 1.29e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  876 QKELEEVEKQgrekLLEKEREFRKTMEEMEQNEEIFNVLERKYNEQHKKvmkmndvLREYERKIEQLNMEKTDLENENQK 955
Cdd:COG4942   26 EAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARR-------IRALEQELAALEAELAELEKEIAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  956 LRETQNRQDSHYSNLEKeVMEKSSLIDELQNqiqKLSDENNEQRLTIAK-LETALEDEKARFARQNNTIGDMQKLISELN 1034
Cdd:COG4942   95 LRAELEAQKEELAELLR-ALYRLGRQPPLAL---LLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELE 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32566156 1035 EKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMA 1108
Cdd:COG4942  171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

1055-1420

1.66e-09

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 1.66e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1055 EREKEKLNEELTTAKEIIQKQAKKIDELkeecrkrKNEASRLERKLEDKEAMmadcvKELKDSHKE-RLKEMEQKVEDVK 1133
Cdd:TIGR02169  169 DRKKEKALEELEEVEENIERLDLIIDEK-------RQQLERLRREREKAERY-----QALLKEKREyEGYELLKEKEALE 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1134 RKNSKLENENSTQKSQIETFQRESSVDSDYGRSSSGRLSTLGRQYSLTSIGSFSSIRTvGLGSRKDSISDMTSSMYSLRR 1213
Cdd:TIGR02169  237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKE-KIGELEAEIASLERSIAEKER 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1214 RDSTYDMTSSTIGLQRSPSTSQVMEKERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQ 1293
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1294 ETTRQLNSAQKNADNLALRLKKALADCDEWKKKhEESIVESKTEILMERKRAmdRAEACEKETELKQSR--MATIESARM 1371
Cdd:TIGR02169  396 KLKREINELKRELDRLQEELQRLSEELADLNAA-IAGIEAKINELEEEKEDK--ALEIKKQEWKLEQLAadLSKYEQELY 472

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 32566156   1372 ELGGELARTQSELDRCRQIIIQLEENLKSQESLGNSFGRHQTNLNFEIE 1420
Cdd:TIGR02169  473 DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521

PTZ00121

MAEBL; Provisional

845-1165

4.70e-09

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 4.70e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   845 QEMEIKNEEALK-ENLKLSMLLDREKSE---KVKVQKELEEVEKQGrEKLLEKEREFRKTMEEMEQNEEIFNVLERKYNE 920
Cdd:PTZ00121 1447 DEAKKKAEEAKKaEEAKKKAEEAKKADEakkKAEEAKKADEAKKKA-EEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD 1525

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   921 QHKKVmkmndvlrEYERKIEQL-NMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQR 999
Cdd:PTZ00121 1526 EAKKA--------EEAKKADEAkKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1000 LTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKI 1079
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1080 DELK--EECRKRKNEASRLE----------RKLEDKEAMMADCVKELKDSHKERLKEMEQKVEDVKRKNSKLENENStQK 1147
Cdd:PTZ00121 1678 EEAKkaEEDEKKAAEALKKEaeeakkaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE-EK 1756

                         330
                  ....*....|....*...
gi 32566156  1148 SQIETFQRESSVDSDYGR 1165
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIR 1774

PRK03918

DNA double-strand break repair ATPase Rad50;

923-1452

5.22e-09

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 5.22e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   923 KKVMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTI 1002
Cdd:PRK03918  168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKEL 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1003 AKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNI--------ALNE-RNSTRKIEREKEKLNEELTTAKEIIQ 1073
Cdd:PRK03918  248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekaeeyiKLSEfYEEYLDELREIEKRLSRLEEEINGIE 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1074 KQAKKIDELKEECRKRKNEASRLERKLED-----KEAMMADCVKELKDSHKERLK-----EMEQKVEDVKRKNSKLENEN 1143
Cdd:PRK03918  328 ERIKELEEKEERLEELKKKLKELEKRLEEleerhELYEEAKAKKEELERLKKRLTgltpeKLEKELEELEKAKEEIEEEI 407

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1144 ST---QKSQIETFQRESSVDSDYGRSSSGRLSTLGRQYSLTSIGSFSSIRTVGLGSRKDSISDMTSSMYSLRRRDSTYDM 1220
Cdd:PRK03918  408 SKitaRIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1221 TsstigLQRSPSTSQVMEKERRILELEKEKAAIN--------TDLQLVKRELDVYKSQLSAVESEKESLQTANRKqsnqL 1292
Cdd:PRK03918  488 V-----LKKESELIKLKELAEQLKELEEKLKKYNleelekkaEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK----L 558

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1293 QETTRQLNSAQKNADNLALRLKKALADCDEWkkkheesiVESKTEILMERKRAMDRAEACEKETELKQSRMATIESARME 1372
Cdd:PRK03918  559 AELEKKLDELEEELAELLKELEELGFESVEE--------LEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK 630

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1373 LGGELARTQSELDRCRQIIIQLEENLkSQESLGNSFGRHqTNLNFEIENLRDENCALKAKIRRQYKQIELLTQQDETNDE 1452
Cdd:PRK03918  631 AFEELAETEKRLEELRKELEELEKKY-SEEEYEELREEY-LELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

856-1463

5.90e-09

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.89 E-value: 5.90e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    856 KENLKLSMLLDREKSEKV--KVQKELEEVEKQGreklLEKEREFRKTMEEMEQNEEIFNVlerkyneQHKKVMKMNDVLR 933
Cdd:pfam05483   62 QEGLKDSDFENSEGLSRLysKLYKEAEKIKKWK----VSIEAELKQKENKLQENRKIIEA-------QRKAIQELQFENE 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    934 EYERKIEQLNMEKTDLENENQK-------LRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTI--AK 1004
Cdd:pfam05483  131 KVSLKLEEEIQENKDLIKENNAtrhlcnlLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAenAR 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1005 LETAL---ED-EKARFARQ------NNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQK 1074
Cdd:pfam05483  211 LEMHFklkEDhEKIQHLEEeykkeiNDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEK 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1075 Q---AKKIDELKEECRKRKNEASRLERKL-----------EDKEAMMADCVKElKDSHKERLKEMEQKV----EDVKRKN 1136
Cdd:pfam05483  291 KdhlTKELEDIKMSLQRSMSTQKALEEDLqiatkticqltEEKEAQMEELNKA-KAAHSFVVTEFEATTcsleELLRTEQ 369

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1137 SKLENENSTQKSQIETFQRESSvdsdygrsssgrlstlgrqySLTSIGSFSSIRTVGLGSRKDSISDMTSSMYSLRRrds 1216
Cdd:pfam05483  370 QRLEKNEDQLKIITMELQKKSS--------------------ELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ--- 426

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1217 tYDMTSSTIGLQRSPSTSQVMEKERRILELEKEKAAINTDLQLVKRELDVYKSQLsavesEKESLQTAN-RKQSNQLQET 1295
Cdd:pfam05483  427 -FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL-----EKEKLKNIElTAHCDKLLLE 500

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1296 TRQLNsaqKNADNLALRLKKALADCDEWKKKHEESIVESKTeilMERKRAMDRAEACEKETELKQSRMatiesarmELGG 1375
Cdd:pfam05483  501 NKELT---QEASDMTLELKKHQEDIINCKKQEERMLKQIEN---LEEKEMNLRDELESVREEFIQKGD--------EVKC 566

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1376 ELARTQSELDRCRQIIIQLEENLKSQESLGNSFGRHQTNLNFEIENLRDENCALKAKIRRQYKQielltqqdetndeLNH 1455
Cdd:pfam05483  567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQ-------------LNA 633


                   ....*...
gi 32566156   1456 FENKVERL 1463
Cdd:pfam05483  634 YEIKVNKL 641

CCDC158

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

869-1395

7.74e-09

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: 60.52 E-value: 7.74e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    869 KSEKVKVQKELEEVEKQGREK-------LLEKEREFRKTMEEMEQNEEIFnvlERKYNEQHKKVMKMNDVLREYERKIEQ 941
Cdd:pfam15921  291 RSQANSIQSQLEIIQEQARNQnsmymrqLSDLESTVSQLRSELREAKRMY---EDKIEELEKQLVLANSELTEARTERDQ 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    942 LNMEKTDLENENQKLRETQNRQDSHYSnLEKEvmeksslidelqnQIQKLSDENNEQRLTIAKLETALEDEKARFAR--- 1018
Cdd:pfam15921  368 FSQESGNLDDQLQKLLADLHKREKELS-LEKE-------------QNKRLWDRDTGNSITIDHLRRELDDRNMEVQRlea 433

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1019 -----QNNTIGDMQKLISELNEKiarfdNIALNERNS-TRKIEREKE---KLNEELTTAKEIIQKQAKKIDELkeecrkr 1089
Cdd:pfam15921  434 llkamKSECQGQMERQMAAIQGK-----NESLEKVSSlTAQLESTKEmlrKVVEELTAKKMTLESSERTVSDL------- 501

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1090 kneASRLERKLEDKEAMMADCVK-----ELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSvdsdyg 1164
Cdd:pfam15921  502 ---TASLQEKERAIEATNAEITKlrsrvDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIE------ 572

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1165 rsssgRLSTLGRQYSltsigsfssiRTVGLgsrkdsisdMTSSMYSLRRRDSTYDMTSSTIGLQRSPSTSQVMEKERRIL 1244
Cdd:pfam15921  573 -----NMTQLVGQHG----------RTAGA---------MQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVS 628

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1245 ELEKEKAAI----NTDLQLVK----------RELDVYKSQLSAVESEKESLQTANRKQSNQLQETTR----QLNSAQ--- 1303
Cdd:pfam15921  629 DLELEKVKLvnagSERLRAVKdikqerdqllNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNklkmQLKSAQsel 708

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1304 ----------KNADNLALRLKKALADCDEWKKKHEESIvESKTEILMERKRAMDRAEACEKETELKQSR-MATIESARME 1372
Cdd:pfam15921  709 eqtrntlksmEGSDGHAMKVAMGMQKQITAKRGQIDAL-QSKIQFLEEAMTNANKEKHFLKEEKNKLSQeLSTVATEKNK 787

                          570       580
                   ....*....|....*....|...
gi 32566156   1373 LGGELARTQSELDRCRQIIIQLE 1395
Cdd:pfam15921  788 MAGELEVLRSQERRLKEKVANME 810

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

844-1039

8.00e-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: 59.39 E-value: 8.00e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  844 IQEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQ---GREKLLEKEREFRKTMEEMEQNEEIFNVLERKYNE 920
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaaLARRIRALEQELAALEAELAELEKEIAELRAELEA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  921 QHKKVMKMNDVL------------------REYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLID 982
Cdd:COG4942  102 QKEELAELLRALyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 32566156  983 ELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIAR 1039
Cdd:COG4942  182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

842-1404

8.66e-09

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.12 E-value: 8.66e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    842 EEIQEmeikNEEALKEN---------LKLSMLLDREKS----------------------------EKVKVQKELEEVE- 883
Cdd:pfam05483  138 EEIQE----NKDLIKENnatrhlcnlLKETCARSAEKTkkyeyereetrqvymdlnnniekmilafEELRVQAENARLEm 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    884 ----KQGREKLLEKEREFRKtmeEMEQNEEIFNVLERKYNEQHKKVMKMNDVLREYERKIEQLNmEKTDLENENqkLRET 959
Cdd:pfam05483  214 hfklKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE-EKTKLQDEN--LKEL 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    960 QNRQDSHYSNLE-------KEVMEKSSLIDELQ---NQIQKLSDENNEQ------------------RLTIAKLETALED 1011
Cdd:pfam05483  288 IEKKDHLTKELEdikmslqRSMSTQKALEEDLQiatKTICQLTEEKEAQmeelnkakaahsfvvtefEATTCSLEELLRT 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1012 EKARFARQNNTIG----DMQKLISELnEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECR 1087
Cdd:pfam05483  368 EQQRLEKNEDQLKiitmELQKKSSEL-EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1088 KRKNEASRLERKL---EDKEAMMADCVKELK-DSHKERLK--EMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSVDS 1161
Cdd:pfam05483  447 AREKEIHDLEIQLtaiKTSEEHYLKEVEDLKtELEKEKLKniELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCK 526

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1162 DYGRSSSGRLSTLgRQYSLTSIGSFSSIRTVGLGSRKDSISDMTSSMYSLRRRDSTYDMTSSTIGLQRSPSTS---QVME 1238
Cdd:pfam05483  527 KQEERMLKQIENL-EEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNlkkQIEN 605

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1239 KERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQettRQLNSAQKNADNLALRLKKALA 1318
Cdd:pfam05483  606 KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQ---KEIEDKKISEEKLLEEVEKAKA 682

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1319 DCDEWKKKHEESIVESKTEI-----LMER-KRAMDR-AEACEKETELKQSRMATIESARMELGGELARTQSELDRCRQii 1391
Cdd:pfam05483  683 IADEAVKLQKEIDKRCQHKIaemvaLMEKhKHQYDKiIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKK-- 760

                          650
                   ....*....|...
gi 32566156   1392 iQLEENLKSQESL 1404
Cdd:pfam05483  761 -QLEIEKEEKEKL 772

PTZ00121

MAEBL; Provisional

850-1168

1.81e-08

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 1.81e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   850 KNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIfnvleRKYNEQHKKVMKMN 929
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL-----KKAEEEKKKVEQLK 1639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   930 DVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQnqiQKLSDENNEQRLTIAKLETAL 1009
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK---KEAEEAKKAEELKKKEAEEKK 1716

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1010 EDEKARFARQNNTIGDMQ-KLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQakkidELKEECRK 1088
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEaKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE-----ELDEEDEK 1791

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1089 RKNEASRLERKLEDKEAMMADCVKElKDSHKERLKEMEQKV--EDVKRKNSKLENENSTQKSQIETfQRESSVDSDYGRS 1166
Cdd:PTZ00121 1792 RRMEVDKKIKDIFDNFANIIEGGKE-GNLVINDSKEMEDSAikEVADSKNMQLEEADAFEKHKFNK-NNENGEDGNKEAD 1869


                  ..
gi 32566156  1167 SS 1168
Cdd:PTZ00121 1870 FN 1871

CCDC158

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

935-1453

2.87e-08

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: 58.59 E-value: 2.87e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    935 YERKIEQLNMEKTDLE---NENQKLRETQN---RQD--SHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLE 1006
Cdd:pfam15921   76 IERVLEEYSHQVKDLQrrlNESNELHEKQKfylRQSviDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELE 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1007 TALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALN-ERNSTRKIErekEKLNEELTTAKEIIQKQAKKIDELKEE 1085
Cdd:pfam15921  156 AAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDfEEASGKKIY---EHDSMSTMHFRSLGSAISKILRELDTE 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1086 CRKRKNEASRLERKLEDKEAMMADCVKELKDSHKERLkemEQKVEDVKRKNSKLENENSTQKSQIETFQRESSVDSDYGR 1165
Cdd:pfam15921  233 ISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRI---EQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQAR 309

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1166 SSsgrlstlgrqysltsigsfSSIRTVGLGSRKDSISDMTSsmySLRRRDSTYDMTSSTIGLQRSPSTSQVMEKERRILE 1245
Cdd:pfam15921  310 NQ-------------------NSMYMRQLSDLESTVSQLRS---ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ 367

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1246 LEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKNADNLALRLKKALADCdEWKK 1325
Cdd:pfam15921  368 FSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEC-QGQM 446

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1326 KHEESIVESKTEIL---------MERKRAMDRA---EACEKETELKQSR--MATIESARMELGGELARTQSELDRCRQII 1391
Cdd:pfam15921  447 ERQMAAIQGKNESLekvssltaqLESTKEMLRKvveELTAKKMTLESSErtVSDLTASLQEKERAIEATNAEITKLRSRV 526

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32566156   1392 iqleeNLKSQESlgnsfgRHQTNLNFEIENLRDENCALKAKIRRQYKQIELLTQQDETNDEL 1453
Cdd:pfam15921  527 -----DLKLQEL------QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQL 577

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

845-1449

4.81e-08

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: 58.06 E-value: 4.81e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    845 QEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEK---------QGREKLLEKEREFRKTMEEMEQNEEIFNVLE 915
Cdd:TIGR00618  268 RIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQqaqrihtelQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    916 RKYNEQHKKVMKMNDVLREYErkiEQLNMEKTDLenenQKLReTQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDEN 995
Cdd:TIGR00618  348 QTLHSQEIHIRDAHEVATSIR---EISCQQHTLT----QHIH-TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    996 NEQRLTIAKLETALEDEKARFArqnntigdMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELT-TAKEIIQK 1074
Cdd:TIGR00618  420 RDLQGQLAHAKKQQELQQRYAE--------LCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHlQETRKKAV 491

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1075 QAKKIDELKEECRKRKNEASRLERKLEDKEAMMADC--VKELKDSHkerlKEMEQKVEDVKRKNSKLENENSTQKSQIE- 1151
Cdd:TIGR00618  492 VLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTrrMQRGEQTY----AQLETSEEDVYHQLTSERKQRASLKEQMQe 567

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1152 ---TFQRESSVDSDYGRSSSGRLSTLGRQYSLTSIGSFSSIRTVGLGSR-----KDSISDMTSSMYSLRRRDSTYDMTSS 1223
Cdd:TIGR00618  568 iqqSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAllrklQPEQDLQDVRLHLQQCSQELALKLTA 647

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1224 TIGLQRSPSTSQVMEKERRILELEKEKAAIN----TDLQLVKRELDVYKSQL----SAVESEKESLQTaNRKQSNQLQET 1295
Cdd:TIGR00618  648 LHALQLTLTQERVREHALSIRVLPKELLASRqlalQKMQSEKEQLTYWKEMLaqcqTLLRELETHIEE-YDREFNEIENA 726

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1296 TRQLNSAQKNADNLALRLKKALADCDEWKKKHEESIVESKTEILMERKRAMDRAEACEKETELKQsrmatieSARMELGG 1375
Cdd:TIGR00618  727 SSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFN-------RLREEDTH 799

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32566156   1376 ELARTQSELDRCR---QIIIQLEENLKSQEslgnsfgRHQTnlnfeiENLRDENCALKAKIRRQYKQIELLTQQDET 1449
Cdd:TIGR00618  800 LLKTLEAEIGQEIpsdEDILNLQCETLVQE-------EEQF------LSRLEEKSATLGEITHQLLKYEECSKQLAQ 863

PTZ00121

MAEBL; Provisional

848-1461

5.79e-08

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 5.79e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   848 EIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLLEKEREFRKTmEEMEQNEEIFNVLERKYNEQHKKVmk 927
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA-DELKKAEEKKKADEAKKAEEKKKA-- 1304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   928 mndvlREYERKIEqlnmEKTDLENENQKLRETQNRQDShysnLEKEVMEKSSLIDELQNQIQKLSDE--NNEQRLTIAKL 1005
Cdd:PTZ00121 1305 -----DEAKKKAE----EAKKADEAKKKAEEAKKKADA----AKKKAEEAKKAAEAAKAEAEAAADEaeAAEEKAEAAEK 1371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1006 ETALEDEKARFARQNntiGDMQKLISELNEKIARFDNIA--LNERNSTRKIEREKEKLNEELTTAKEIIQK--QAKKIDE 1081
Cdd:PTZ00121 1372 KKEEAKKKADAAKKK---AEEKKKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAKKKAEEKKKADEAKKKaeEAKKADE 1448

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1082 LKEECRKRKnEASRLERKLEdkEAMMADCVKElKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSVDS 1161
Cdd:PTZ00121 1449 AKKKAEEAK-KAEEAKKKAE--EAKKADEAKK-KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1162 DYGRSS--SGRLSTLGRQYSLTSIGSFSSIRTVGLGSRKDSISDMtssmyslRRRDSTYDMTSSTIGLQRSPSTSQVMEK 1239
Cdd:PTZ00121 1525 DEAKKAeeAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA-------KKAEEDKNMALRKAEEAKKAEEARIEEV 1597

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1240 ERRILELEKEKAAintdlQLVKRELDVYKS-QLSAVESEKESLQTANRKQsnqlQETTRQLNSAQKNADNLALRLKKALA 1318
Cdd:PTZ00121 1598 MKLYEEEKKMKAE-----EAKKAEEAKIKAeELKKAEEEKKKVEQLKKKE----AEEKKKAEELKKAEEENKIKAAEEAK 1668

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1319 DCDEWKKKHEESIVES-----KTEILMERKRAMDRAEACEK--ETELKQSRMATIESARMELGGELARTQSELDRCRQii 1391
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEedekkAAEALKKEAEEAKKAEELKKkeAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA-- 1746

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1392 iqleENLKSQESLGNSFGRHQTNLNFEIENLRDENCALKAKIRRQYKQIELLTQQDETNDELNHFENKVE 1461
Cdd:PTZ00121 1747 ----EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812

COG4913

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

877-1464

6.28e-08

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 6.28e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  877 KELEEVEKQgreklLEKEREFRKTMEEMEQNEEIFNVLERKYNEQhKKVMKMNDVLREyERKIEQLNMEKTDLENENQKL 956
Cdd:COG4913  235 DDLERAHEA-----LEDAREQIELLEPIRELAERYAAARERLAEL-EYLRAALRLWFA-QRRLELLEAELEELRAELARL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  957 RETQNRQDSHYSNLEKEvmeksslIDELQNQIQKLSDENneqrltIAKLETALEDEKARFARQNNTIGDMQKLISELNEK 1036
Cdd:COG4913  308 EAELERLEARLDALREE-------LDELEAQIRGNGGDR------LEQLEREIERLERELEERERRRARLEALLAALGLP 374

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1037 I----ARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMAdcvk 1112
Cdd:COG4913  375 LpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA---- 450

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1113 elkdshkERLKEMEQKVE------DVKRKNSKLEN--E------------------------NSTQKSQIETFQRESSVD 1160
Cdd:COG4913  451 -------EALGLDEAELPfvgeliEVRPEEERWRGaiErvlggfaltllvppehyaaalrwvNRLHLRGRLVYERVRTGL 523

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1161 SDYGRSS------SGRLSTLG---RQYSLTSIGSFSSIRTVglgsrkDSISD------------MTSSMYSLRRRDSTYD 1219
Cdd:COG4913  524 PDPERPRldpdslAGKLDFKPhpfRAWLEAELGRRFDYVCV------DSPEElrrhpraitragQVKGNGTRHEKDDRRR 597

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1220 MTSS-TIGLQrspSTSQVMEKERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVEsekeslqtanrkQSNQLQETTRQ 1298
Cdd:COG4913  598 IRSRyVLGFD---NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ------------RLAEYSWDEID 662

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1299 LNSAQKNADNLALRLKKALADCDEwkkkheesiveskteiLMERKRAMDRAEAceketelkqsRMATIESARMELGGELA 1378
Cdd:COG4913  663 VASAEREIAELEAELERLDASSDD----------------LAALEEQLEELEA----------ELEELEEELDELKGEIG 716

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1379 RTQSELDRCRQIIIQLEENLKSQESLGnsfgrhQTNLNFEIENLRDEncALKAKIRRQYKQiELLTQQDETNDELNHFEN 1458
Cdd:COG4913  717 RLEKELEQAEEELDELQDRLEAAEDLA------RLELRALLEERFAA--ALGDAVERELRE-NLEERIDALRARLNRAEE 787


                 ....*.
gi 32566156 1459 KVERLL 1464
Cdd:COG4913  788 ELERAM 793

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

902-1446

8.62e-08

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.11 E-value: 8.62e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    902 EEMEQNEEIFnvleRKYNEQHKKVMKMndvLREYERKIEQLNMEKTDLENENQ-------KLRETQNRQDSHYSNLEKEV 974
Cdd:pfam01576    5 EEMQAKEEEL----QKVKERQQKAESE---LKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEEIL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    975 MEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKArfARQNNtigDMQKLISELNEKIARFDNIALNERNStrKI 1054
Cdd:pfam01576   78 HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEA--ARQKL---QLEKVTTEAKIKKLEEDILLLEDQNS--KL 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1055 EREKEKLNEELttakeiiqkqAKKIDELKEECRKRKNEAsrlerKLEDK-EAMMADCVKELKDSHKERLkEMEQKVEDVK 1133
Cdd:pfam01576  151 SKERKLLEERI----------SEFTSNLAEEEEKAKSLS-----KLKNKhEAMISDLEERLKKEEKGRQ-ELEKAKRKLE 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1134 RKNSKLENENSTQKSQIETFQRESSVDSDYGRSSSGRLSTLGRQYSLtsigSFSSIRTVglgsrKDSISDMTSSMYSLRr 1213
Cdd:pfam01576  215 GESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNN----ALKKIREL-----EAQISELQEDLESER- 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1214 rdstydmtsstigLQRSPStsqvmEKERRilELEKEKAAINTDLQ------------LVKRELDVYKSQlSAVESEKES- 1280
Cdd:pfam01576  285 -------------AARNKA-----EKQRR--DLGEELEALKTELEdtldttaaqqelRSKREQEVTELK-KALEEETRSh 343

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1281 ---LQTANRKQSNQLQETTRQLNSAQKNADNLAlRLKKALAdcDEWKKKHEE--SIVESKTEILMERKRAmdraeacEKE 1355
Cdd:pfam01576  344 eaqLQEMRQKHTQALEELTEQLEQAKRNKANLE-KAKQALE--SENAELQAElrTLQQAKQDSEHKRKKL-------EGQ 413

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1356 TELKQSRMATIESARMELGGELARTQSELD--------------RCRQIIIQLEENLKSQESLGNSFGRHQTNLNFEIEN 1421
Cdd:pfam01576  414 LQELQARLSESERQRAELAEKLSKLQSELEsvssllneaegkniKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQ 493

                          570       580       590
                   ....*....|....*....|....*....|..
gi 32566156   1422 LRDENCALKAKI-------RRQYKQIELLTQQ 1446
Cdd:pfam01576  494 LEDERNSLQEQLeeeeeakRNVERQLSTLQAQ 525

PHA02562

endonuclease subunit; Provisional

844-1092

1.03e-07

endonuclease subunit; Provisional

Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 56.56 E-value: 1.03e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   844 IQEMEIKNEEALKENLKLSMLLDREKS---EKVKVQKEL-EEVEKQGREKLLEKEREFRKTMEEMEQNeeifnvlerkyn 919
Cdd:PHA02562  165 LSEMDKLNKDKIRELNQQIQTLDMKIDhiqQQIKTYNKNiEEQRKKNGENIARKQNKYDELVEEAKTI------------ 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   920 eqHKKVMKMNDvlreyerKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEV--MEK-------SSLIDELQNQIQK 990
Cdd:PHA02562  233 --KAEIEELTD-------ELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmYEKggvcptcTQQISEGPDRITK 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   991 LSDENNEQRLTIAKLETALEDEKARFarqnNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKE 1070
Cdd:PHA02562  304 IKDKLKELQHSLEKLDTAIDELEEIM----DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379

                         250       260
                  ....*....|....*....|..
gi 32566156  1071 IIQKQAKKIDELKEECRKRKNE 1092
Cdd:PHA02562  380 ELAKLQDELDKIVKTKSELVKE 401

PTZ00121

MAEBL; Provisional

844-1121

1.53e-07

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.53e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   844 IQEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIFNVLE---RKYNE 920
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAealKKEAE 1699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   921 QHKKVMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSlIDELQNQIQKLSDENNEQRL 1000
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK-IAHLKKEEEKKAEEIRKEKE 1778

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1001 TIAKLETALEDEKARFARQNNT--IGDMQKLISELNEKiarfDNIALNERNST--RKIEREKEKLNEELTTAKEIIQKQA 1076
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVDKKIkdIFDNFANIIEGGKE----GNLVINDSKEMedSAIKEVADSKNMQLEEADAFEKHKF 1854

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 32566156  1077 KKIDELKEECRKRKNEASRLERKLEDKEAMM-ADCVKELKDSHKER 1121
Cdd:PTZ00121 1855 NKNNENGEDGNKEADFNKEKDLKEDDEEEIEeADEIEKIDKDDIER 1900

YhaN

COG4717

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

977-1396

1.84e-07

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.84e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  977 KSSLIDELQNQIQKLS------DENNEQRLTIAKLE-TALEDEKARFARQNNTIGDMQKLISELNEKIARFDNI--ALNE 1047
Cdd:COG4717   44 RAMLLERLEKEADELFkpqgrkPELNLKELKELEEElKEAEEKEEEYAELQEELEELEEELEELEAELEELREEleKLEK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1048 RNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEecrkRKNEASRLERKLEDKEAMMADCVKELKDSHKERLKEMEQ 1127
Cdd:COG4717  124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1128 KVEDVKRKN-------SKLENENSTQKSQIETFQRESSVDSDYGRSS---------SGRLSTLGRQYSLTS--------I 1183
Cdd:COG4717  200 ELEELQQRLaeleeelEEAQEELEELEEELEQLENELEAAALEERLKearlllliaAALLALLGLGGSLLSliltiagvL 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1184 GSFSSIRTVGLGSRKDSISDMTSSMYSLRRRDSTYDMTS-------STIGLQRSPSTSQVMEKERRILELEKEKAAINTD 1256
Cdd:COG4717  280 FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEeeleellAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1257 LQlvKRELDVYKSQLSA------VESEKESLQTANRKQsnQLQETTRQLNSAQKNADNLALRLKKALADCDEwkkkhees 1330
Cdd:COG4717  360 EE--ELQLEELEQEIAAllaeagVEDEEELRAALEQAE--EYQELKEELEELEEQLEELLGELEELLEALDE-------- 427

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32566156 1331 iveskTEILMERKRAMDRAEACEKETELKQSRMATIES--ARMELGGELARTQSELDRCRQIIIQLEE 1396
Cdd:COG4717  428 -----EELEEELEELEEELEELEEELEELREELAELEAelEQLEEDGELAELLQELEELKAELRELAE 490

CCDC158

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

873-1457

1.91e-07

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: 55.89 E-value: 1.91e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    873 VKVQKELEEVEKQgREKLLEKEREfrktmeEMEQNEEIFNVLERKYNEQHKKVMKMNDVLREYERKIEQLnmEKTDLENE 952
Cdd:pfam15921  113 IDLQTKLQEMQME-RDAMADIRRR------ESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQL--RKMMLSHE 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    953 -----------------NQKLRETQNRQDSHYSNLEKEVmekSSLIDELQNQIQKLSDE--NNEQRLTIAKLETALEDEK 1013
Cdd:pfam15921  184 gvlqeirsilvdfeeasGKKIYEHDSMSTMHFRSLGSAI---SKILRELDTEISYLKGRifPVEDQLEALKSESQNKIEL 260

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1014 ARFARQNNtigdMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEA 1093
Cdd:pfam15921  261 LLQQHQDR----IEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREA 336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1094 SRL-ERKLEDKEAMMADCVKELKDSHKER--------------------LKEMEQKVEDVKRKNSKLENENSTQKSQIET 1152
Cdd:pfam15921  337 KRMyEDKIEELEKQLVLANSELTEARTERdqfsqesgnlddqlqklladLHKREKELSLEKEQNKRLWDRDTGNSITIDH 416

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1153 FQRESSVDSDYGRSSSGRLSTLGRQYSLTSIGSFSSIRtvGLGSRKDSISDMTSSMYSLRR--RDSTYDMTSSTIGLQRS 1230
Cdd:pfam15921  417 LRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQ--GKNESLEKVSSLTAQLESTKEmlRKVVEELTAKKMTLESS 494

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1231 PS-----TSQVMEKERRIlelekekAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRK-QSNQLQETTRQ-----L 1299
Cdd:pfam15921  495 ERtvsdlTASLQEKERAI-------EATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcEALKLQMAEKDkvieiL 567

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1300 NSAQKNADNLALRLKKALADCDEWKKKHEESIVESKTEiLMERKRAMDRAEACEKETELKQSRMATIESARMELGGELAR 1379
Cdd:pfam15921  568 RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE-LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLR 646

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32566156   1380 TQSELDRCRQiiiQLEENLKSQESLGNSFGRHQTNLNFEIENLRDENCALKAKIRRQYKQIEllTQQDETNDELNHFE 1457
Cdd:pfam15921  647 AVKDIKQERD---QLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQ--SELEQTRNTLKSME 719

COG2433

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

973-1130

2.20e-07

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

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 55.63 E-value: 2.20e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  973 EVMEKssLIDELQNqiqklsDENNEQRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDnialnernstR 1052
Cdd:COG2433  380 EALEE--LIEKELP------EEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKD----------E 441

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32566156 1053 KIEREKEKLNEELTTAKEIIQKQakkidelkEECRKRKNEASRLERKLEDKEAMmadcVKELKdSHKERLKEMEQKVE 1130
Cdd:COG2433  442 RIERLERELSEARSEERREIRKD--------REISRLDREIERLERELEEERER----IEELK-RKLERLKELWKLEH 506

DR0291

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

981-1140

2.50e-07

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: 53.39 E-value: 2.50e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  981 IDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARfdniaLNERNSTRKIEREKEK 1060
Cdd:COG1579   19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-----YEEQLGNVRNNKEYEA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1061 LNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAmmadCVKELKDSHKERLKEMEQKVEDVKRKNSKLE 1140
Cdd:COG1579   94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA----ELEEKKAELDEELAELEAELEELEAEREELA 169

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

933-1156

3.12e-07

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 3.12e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    933 REYERKIEQLNMEKTDLENENQKLRETQNRQDSHysnlekevmeksslIDEL--------------QNQIQKLSDENNEQ 998
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENR--------------LDELsqelsdasrkigeiEKEIEQLEQEEEKL 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    999 RLTIAKLET-------ALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNERnsTRKIEREKEKLNEELTTAKEI 1071
Cdd:TIGR02169  736 KERLEELEEdlssleqEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEAR 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1072 IQKQAKKIDEL---KEECRKRKNEASRLERKLEDKEAMMADCVKEL---KDSHKERLKEMEQKVEDVKRKNSKLENENST 1145
Cdd:TIGR02169  814 LREIEQKLNRLtleKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLngkKEELEEELEELEAALRDLESRLGDLKKERDE 893

                          250
                   ....*....|.
gi 32566156   1146 QKSQIETFQRE 1156
Cdd:TIGR02169  894 LEAQLRELERK 904

Smc

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

1238-1452

3.16e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 3.16e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1238 EKERRI--LELEKEKA----AINTDLQLVKREL-----DVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKNA 1306
Cdd:COG1196  197 ELERQLepLERQAEKAeryrELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1307 DNLALRLKKALADCDEWKKKHEEsiVESKTEILMERKRAM-DRAEACEKETELKQSRMATIESARMELGGELARTQSELD 1385
Cdd:COG1196  277 EELELELEEAQAEEYELLAELAR--LEQDIARLEERRRELeERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32566156 1386 RCRQIIIQLEENLKSQESLGNSFGRHQTNLNFEIENLRDENCALKAKIRRQYKQIELLTQQDETNDE 1452
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

PRK01156

chromosome segregation protein; Provisional

840-1347

3.24e-07

chromosome segregation protein; Provisional

Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.29 E-value: 3.24e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   840 LEEEIQEMEIKNEEALKENLKLSmlldreksekvKVQKELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIFNVLE---R 916
Cdd:PRK01156  254 YESEIKTAESDLSMELEKNNYYK-----------ELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDaeiN 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   917 KYNEQHKKVMKMNDVLREYERKieqlNMEKTDLENENQKLRETQnrqdSHYSNLEKEVMEKSSLIDELQNQIQKLSDENN 996
Cdd:PRK01156  323 KYHAIIKKLSVLQKDYNDYIKK----KSRYDDLNNQILELEGYE----MDYNSYLKSIESLKKKIEEYSKNIERMSAFIS 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   997 EqrlTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKI-ARFDNIALNERN-----------------STRKIEREK 1058
Cdd:PRK01156  395 E---ILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIrALRENLDELSRNmemlngqsvcpvcgttlGEEKSNHII 471

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1059 EKLNEELTTAKEIIQK---QAKKIDELKEECRKRK--------NEASRLERKLEDKEAMMADC---VKELKDSH------ 1118
Cdd:PRK01156  472 NHYNEKKSRLEEKIREieiEVKDIDEKIVDLKKRKeyleseeiNKSINEYNKIESARADLEDIkikINELKDKHdkyeei 551

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1119 KERLKEMeqKVEDVKRKNSKLENENSTQKS-QIETFQRESSVDSDYGRSSSGRLSTLGRQYSLTSIGSFSSIRTV----- 1192
Cdd:PRK01156  552 KNRYKSL--KLEDLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIenean 629

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1193 GLGSRKDSISDMTSSMYSLRRRDSTYDMTSSTIGlqrspstsqvmEKERRILELEKEKAAINTDLQLVKRELDVYKSQLS 1272
Cdd:PRK01156  630 NLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-----------SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA 698

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32566156  1273 AVESEKESLQTANRKQSNQLQETTRQLNSAQKnadnlalrLKKALADCDEWKKKHEESIVESkteilMERKRAMD 1347
Cdd:PRK01156  699 RLESTIEILRTRINELSDRINDINETLESMKK--------IKKAIGDLKRLREAFDKSGVPA-----MIRKSASQ 760

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

1242-1453

4.73e-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: 4.73e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1242 RILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKNADNLALRLKKALADCD 1321
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1322 EWKKKHEESIVESKTEILMERKRAMDRAEACEkETELKQSRMATIESARMELGGELARTQSELDRCRQiiiQLEENLKSQ 1401
Cdd:COG4942  101 AQKEELAELLRALYRLGRQPPLALLLSPEDFL-DAVRRLQYLKYLAPARREQAEELRADLAELAALRA---ELEAERAEL 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 32566156 1402 ESLGNSFGRHQTNLNFEIENLRDENCALKAKIRRQYKQIELLTQQDETNDEL 1453
Cdd:COG4942  177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228

HMMR_N

pfam15905

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...

868-1150

5.21e-07

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: 53.28 E-value: 5.21e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    868 EKSEKVKVQKELEEVEKQGREK------------LLEKEREFRKTMEEM----EQNEEIFN-VLERkyNEQHKKVMKMND 930
Cdd:pfam15905   24 EKSQRFRKQKAAESQPNLNNSKdastpatarkvkSLELKKKSQKNLKESkdqkELEKEIRAlVQER--GEQDKRLQALEE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    931 VLREYERKIEQLNMEKTDLENENQklretqnrqdshysNLEKEVMEKSSLIDELQNqiqKLSDENNEQRLTIAKLE---- 1006
Cdd:pfam15905  102 ELEKVEAKLNAAVREKTSLSASVA--------------SLEKQLLELTRVNELLKA---KFSEDGTQKKMSSLSMElmkl 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1007 --TALEDEKARFARQNNTIGDMQKLISELNEKIARFDNiaLNERNSTRKIEREKEKL--------NEELTTAKEIIQKQA 1076
Cdd:pfam15905  165 rnKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQ--LEEKLVSTEKEKIEEKSeteklleyITELSCVSEQVEKYK 242

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32566156   1077 KKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQI 1150
Cdd:pfam15905  243 LDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKL 316

CCDC158

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

813-1154

6.03e-07

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: 54.35 E-value: 6.03e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    813 IYHLTRGLIPRNRDKERIeeleneklkleeeiqemeikneEALKENLKlSMLLDREKSEKVKVQKELEEVEK-QGREKLL 891
Cdd:pfam15921  414 IDHLRRELDDRNMEVQRL----------------------EALLKAMK-SECQGQMERQMAAIQGKNESLEKvSSLTAQL 470

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    892 EKERE-FRKTMEEMEQNEEIFNVLERkyneqhkKVMKMNDVLREYERKIEQLNMEKTDLENE-NQKLRETQN--RQDSHY 967
Cdd:pfam15921  471 ESTKEmLRKVVEELTAKKMTLESSER-------TVSDLTASLQEKERAIEATNAEITKLRSRvDLKLQELQHlkNEGDHL 543

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    968 SNLEKE-------VMEKSSLIDELQNQIQKLSDENNEQRLTI-------AKLETALEDEKARFA-------RQNNTIGDM 1026
Cdd:pfam15921  544 RNVQTEcealklqMAEKDKVIEILRQQIENMTQLVGQHGRTAgamqvekAQLEKEINDRRLELQefkilkdKKDAKIREL 623

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1027 QKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEdkeaM 1106
Cdd:pfam15921  624 EARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLK----M 699

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 32566156   1107 MADCVKELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQ 1154
Cdd:pfam15921  700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQ 747

Smc

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

1233-1464

1.09e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.09e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1233 TSQVMEKERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQ---TANRKQSNQLQETTRQLNSAQKNADNL 1309
Cdd:COG1196  259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEerrRELEERLEELEEELAELEEELEELEEE 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1310 ALRLKKALADCD---EWKKKHEESIVESKTEILMERKRAMDRAEACEKETELKQSRMATIESARMELGGELARTQSELDR 1386
Cdd:COG1196  339 LEELEEELEEAEeelEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32566156 1387 CRQIIIQLEENLKSQESLGNSFGRHQTNLNFEIENLRDENCALKAKIRRQYKQIELLTQQDETNDELNHFENKVERLL 1464
Cdd:COG1196  419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496

PTZ00121

MAEBL; Provisional

845-1142

1.45e-06

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.45e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   845 QEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLLEKEREFRKTmeemeqnEEIFNVLERKYNEQHKk 924
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA-------EEKKKAEEAKKAEEDK- 1576

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   925 vmkmNDVLREYE--RKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTI 1002
Cdd:PTZ00121 1577 ----NMALRKAEeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1003 AKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQ---AKKI 1079
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEeenKIKA 1732

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32566156  1080 DELKEECRKRKNEASRLeRKLEDKEAMMADCVKELKDSHKERLKEMEQKV-EDVKRKNSKLENE 1142
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEA-KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIeEELDEEDEKRRME 1795

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

845-1378

1.81e-06

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 1.81e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    845 QEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIfNVLERKYNEQHKK 924
Cdd:TIGR02169  364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI-AGIEAKINELEEE 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    925 VMKMNDVLREYERKIEQLnmeKTDLENENQKLRETQNRqdshYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRL---- 1000
Cdd:TIGR02169  443 KEDKALEIKKQEWKLEQL---AADLSKYEQELYDLKEE----YDRVEKELSKLQRELAEAEAQARASEERVRGGRAveev 515

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1001 ----------TIAKL-----ETALEDEKARFARQNNTI----GDMQKLISELNE-KIARFDNIALNErnsTRKIEREKEK 1060
Cdd:TIGR02169  516 lkasiqgvhgTVAQLgsvgeRYATAIEVAAGNRLNNVVveddAVAKEAIELLKRrKAGRATFLPLNK---MRDERRDLSI 592

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1061 LNEE---------------------------------------------LTTAKEIIQKQ------AKKIDELKEECRKR 1089
Cdd:TIGR02169  593 LSEDgvigfavdlvefdpkyepafkyvfgdtlvvedieaarrlmgkyrmVTLEGELFEKSgamtggSRAPRGGILFSRSE 672

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1090 KNEASRLERKLEDKEAMMADCVKELkDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQREssvdsdygrsssg 1169
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSEL-RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER------------- 738

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1170 rlstlgrqysLTSIGSFSSIRTVGLGSRKDSISDMTSSMYSLRRRDSTYDMTSSTIglQRSPSTSQVMEKERRILELEKE 1249
Cdd:TIGR02169  739 ----------LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEE 806

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1250 KAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKNADNLALRLKKALADCDEWKKKHEE 1329
Cdd:TIGR02169  807 VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|
gi 32566156   1330 siVESKTEILMERKRAMDRA-EACEKETELKQSRMATIESARMELGGELA 1378
Cdd:TIGR02169  887 --LKKERDELEAQLRELERKiEELEAQIEKKRKRLSELKAKLEALEEELS 934

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

850-1093

1.84e-06

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.84e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    850 KNEEALKEnlkLSMLLDREKSEKVKVQKELEEVEKQGREK---LLEKEREFRKTMEEMEQNEEIFNVLERKYNEQHKKVM 926
Cdd:TIGR02168  800 ALREALDE---LRAELTLLNEEAANLRERLESLERRIAATerrLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    927 KMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQklsdeNNEQRLTiAKLE 1006
Cdd:TIGR02168  877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID-----NLQERLS-EEYS 950

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1007 TALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALN-----ERNSTRKIEREKEKlnEELTTAKEIIQkqaKKIDE 1081
Cdd:TIGR02168  951 LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAaieeyEELKERYDFLTAQK--EDLTEAKETLE---EAIEE 1025

                          250
                   ....*....|..
gi 32566156   1082 LKEECRKRKNEA 1093
Cdd:TIGR02168 1026 IDREARERFKDT 1037

PTZ00121

MAEBL; Provisional

850-1402

2.15e-06

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 2.15e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   850 KNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLLE--KEREFRKTMEEMEQNEEIFNVLERKYNEQHKKVMk 927
Cdd:PTZ00121 1071 GLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEarKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE- 1149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   928 mNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQN-----QIQKLSDENNEQRL-T 1001
Cdd:PTZ00121 1150 -DAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKaeeerKAEEARKAEDAKKAeA 1228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1002 IAKLETALED-EKARFARQNNTIGDMQKLISELNEKIARFDNIALNE--------RNSTRKIEREKEKLNEELTTAKEII 1072
Cdd:PTZ00121 1229 VKKAEEAKKDaEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEearkadelKKAEEKKKADEAKKAEEKKKADEAK 1308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1073 QK--QAKKIDELKEECRKRKNEASRLERKLEDKEAmMADCVKELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQI 1150
Cdd:PTZ00121 1309 KKaeEAKKADEAKKKAEEAKKKADAAKKKAEEAKK-AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1151 ETFQRessvdSDYGRSSSGRLSTLGRQYSLTSIGSFSSIRTVGLGSRKDSISDMTSSMYSLRRRDSTYDMTSSTiglQRS 1230
Cdd:PTZ00121 1388 EEKKK-----ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA---KKA 1459

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1231 PSTSQVMEKERRILELEK--EKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKnADN 1308
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK-ADE 1538

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1309 L--ALRLKKAladcDEWKKKHEESIVESKTEILMERKRAMDRAEACEKETELKQSRMATIESARMELGGELARTQSELDR 1386
Cdd:PTZ00121 1539 AkkAEEKKKA----DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614

                         570
                  ....*....|....*.
gi 32566156  1387 CRQIIIQLEENLKSQE 1402
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEE 1630

Smc

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

1235-1448

2.83e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 2.83e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1235 QVMEKERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKNADNLALRLK 1314
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1315 KALADCDEWKKKhEESIVESKTEILMERKRAMDRAEACEKETELKQSRMATIESARMELGGELARTQSELDRCRQIIIQL 1394
Cdd:COG1196  369 EAEAELAEAEEE-LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 32566156 1395 EENLKSQESLGNSFGRHQTNLNFEIENLRDENCALKAKIRRQYKQIELLTQQDE 1448
Cdd:COG1196  448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

660-1158

3.95e-06

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.90 E-value: 3.95e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    660 EKLPGKIDAPLVLAQLKCNGVLEGIRICREGYPSRLSHSEFIERYSLLMKNKEQSKGASEKEKCTLICQDAQVRKERYAV 739
Cdd:pfam02463  587 LKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA 666

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    740 GKTKLFCKVGVISELETKRNNYISSFIILIQANIRYLNIQK-DLIERRKKLEAVVTIQDNVRQFAELSQwpwyriyhltr 818
Cdd:pfam02463  667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQReKEELKKLKLEAEELLADRVQEAQDKIN----------- 735

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    819 gliprnrdkerieeleneklkLEEEIQEMEIKNEEALKENLKLSmLLDREKSEKVKVQKELEEVEKQGREKLLEKEREFR 898
Cdd:pfam02463  736 ---------------------EELKLLKQKIDEEEEEEEKSRLK-KEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE 793

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    899 KTMEEMEQNEEIfNVLERKYNEQHKKvMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKS 978
Cdd:pfam02463  794 EKLKAQEEELRA-LEEELKEEAELLE-EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    979 SLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQNntigdmqKLISELNEKIARFDNIALNERNSTRKIEREK 1058
Cdd:pfam02463  872 LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE-------EKENEIEERIKEEAEILLKYEEEPEELLLEE 944

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1059 EKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEAsRLERKLEDKEAMMADCVKELKDSHKERLKEMEQKvEDVKRKNSK 1138
Cdd:pfam02463  945 ADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMA-IEEFEEKEERYNKDELEKERLEEEKKKLIRAIIE-ETCQRLKEF 1022

                          490       500
                   ....*....|....*....|
gi 32566156   1139 LENENSTQKSQIETFQRESS 1158
Cdd:pfam02463 1023 LELFVSINKGWNKVFFYLEL 1042

PRK03918

DNA double-strand break repair ATPase Rad50;

1037-1463

4.14e-06

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 4.14e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1037 IARFDNIALNERNSTRKIEREKEKLnEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELkD 1116
Cdd:PRK03918  157 LDDYENAYKNLGEVIKEIKRRIERL-EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-E 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1117 SHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSVDSDYGRSSSgRLSTLGRQYSltSIGSFSSIRTVGLGS 1196
Cdd:PRK03918  235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYI--KLSEFYEEYLDELRE 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1197 RKDSISDMTSSMYSLRRRDStydmtsstiglQRSPSTSQVMEKERRILELEKEKAAINTDLQL------VKRELDVYKSQ 1270
Cdd:PRK03918  312 IEKRLSRLEEEINGIEERIK-----------ELEEKEERLEELKKKLKELEKRLEELEERHELyeeakaKKEELERLKKR 380

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1271 LSAVESEK-----ESLQTANRKQSNQLQETTRQLNSAQKNADNLAL---RLKKALADCDEWKKKHEEsivESKTEILMER 1342
Cdd:PRK03918  381 LTGLTPEKlekelEELEKAKEEIEEEISKITARIGELKKEIKELKKaieELKKAKGKCPVCGRELTE---EHRKELLEEY 457

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1343 KRAMDRAEaceketelkqSRMATIESARMELGGELARTQSELDRCRQIIIQLE--ENLKSQESLGNSFGRHQTNLNF-EI 1419
Cdd:PRK03918  458 TAELKRIE----------KELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAeEY 527

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 32566156  1420 ENLRDENCALKAKIRRQYKQIELLtqqDETNDELNHFENKVERL 1463
Cdd:PRK03918  528 EKLKEKLIKLKGEIKSLKKELEKL---EELKKKLAELEKKLDEL 568

HOOK

pfam05622

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...

933-1156

4.38e-06

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: 51.23 E-value: 4.38e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    933 REYERKIEQLNMEKTDLENENQKLRETQNRqdshYSNLEKEVMEKSSLIDELQNQIQKLSDENneqrltiAKLETALEDE 1012
Cdd:pfam05622   17 HELDQQVSLLQEEKNSLQQENKKLQERLDQ----LESGDDSGTPGGKKYLLLQKQLEQLQEEN-------FRLETARDDY 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1013 KARFARQNNTIGDMQKLISELNekiarfdnialnernstrKIEREKEKLNEELTTAKEIIQKqAKKIDELKEECRKRKNE 1092
Cdd:pfam05622   86 RIKCEELEKEVLELQHRNEELT------------------SLAEEAQALKDEMDILRESSDK-VKKLEATVETYKKKLED 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1093 ASRLERK---LEDKEAMM----ADCVKELK---------DSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRE 1156
Cdd:pfam05622  147 LGDLRRQvklLEERNAEYmqrtLQLEEELKkanalrgqlETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKE 226

DR0291

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

932-1100

5.11e-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: 5.11e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  932 LREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKlsdenNEQRLTIAKLE---TA 1008
Cdd:COG1579   19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-----YEEQLGNVRNNkeyEA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1009 LEDEKARFARQnntIGDMQKLISELNEKIarfDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEEcrk 1088
Cdd:COG1579   94 LQKEIESLKRR---ISDLEDEILELMERI---EELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE--- 164

                        170
                 ....*....|..
gi 32566156 1089 RKNEASRLERKL 1100
Cdd:COG1579  165 REELAAKIPPEL 176

rad50

TIGR00606

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

1046-1350

6.76e-06

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: 50.82 E-value: 6.76e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1046 NERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECR-------KRKNEASRLERKLEDKEAMMADCVKELKDSH 1118
Cdd:TIGR00606  231 AQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKalksrkkQMEKDNSELELKMEKVFQGTDEQLNDLYHNH 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1119 KERLKEMEQKVEDVKRKNSKLENEN---STQKSQIETFQRESSVDSDygrsssgRLSTLGRQYSLTSIGSFSSIRTVGLG 1195
Cdd:TIGR00606  311 QRTVREKERELVDCQRELEKLNKERrllNQEKTELLVEQGRLQLQAD-------RHQEHIRARDSLIQSLATRLELDGFE 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1196 SRKDSISDMTSSMYSLRRRDSTydmTSSTIGLQRSPSTSQVMEKERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVE 1275
Cdd:TIGR00606  384 RGPFSERQIKNFHTLVIERQED---EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVI 460

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1276 SEKESLQTANR---KQSNQLQETTRQLNSAQKNADNLALR-----LKKALADCDEWKKKHEESIVE------SKTEILME 1341
Cdd:TIGR00606  461 KELQQLEGSSDrilELDQELRKAERELSKAEKNSLTETLKkevksLQNEKADLDRKLRKLDQEMEQlnhhttTRTQMEML 540


                   ....*....
gi 32566156   1342 RKRAMDRAE 1350
Cdd:TIGR00606  541 TKDKMDKDE 549

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

844-1404

8.15e-06

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: 50.59 E-value: 8.15e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    844 IQEMEIKNEEALKENLKLSMLLDR--EKSEKVKVQKELEEVEKQGREKLLEKEREFRKTMEE-----------MEQNEEI 910
Cdd:pfam10174  194 LGHLEVLLDQKEKENIHLREELHRrnQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEvqmlktngllhTEDREEE 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    911 FNVLERKYNeqHKKVM--KMNDVLREYERK----------IEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEV---- 974
Cdd:pfam10174  274 IKQMEVYKS--HSKFMknKIDQLKQELSKKesellalqtkLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVdalr 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    975 ---MEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALeDEKARfarqnnTIGDMQKLISELNEKIARFDNIALNERNST 1051
Cdd:pfam10174  352 lrlEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML-DVKER------KINVLQKKIENLQEQLRDKDKQLAGLKERV 424

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1052 RKIEREKEKLNEELTTAKEIIQKQAKKIDELKEecrkrkneasrlERKLEDKEAMmadcvKELKDSHKErLKEMEQKVEd 1131
Cdd:pfam10174  425 KSLQTDSSNTDTALTTLEEALSEKERIIERLKE------------QREREDRERL-----EELESLKKE-NKDLKEKVS- 485

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1132 vkrknsklenenstqKSQIETFQRESSVDSDYGRSSSGRLSTLGRQYSLTSIgsfssirTVGLGSRKDSISDMTSSMYSL 1211
Cdd:pfam10174  486 ---------------ALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL-------EIAVEQKKEECSKLENQLKKA 543

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1212 RRRDSTYDMTSstiglqrspstsqvmEKERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESlqtANRKQSNQ 1291
Cdd:pfam10174  544 HNAEEAVRTNP---------------EINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKND---KDKKIAEL 605

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1292 LQETTRQLNSAQKNADNLALR---LKKALADCDEWKKKHEESIVESKTEILMErkRAMDRAEACEKETELKQSRMATIES 1368
Cdd:pfam10174  606 ESLTLRQMKEQNKKVANIKHGqqeMKKKGAQLLEEARRREDNLADNSQQLQLE--ELMGALEKTRQELDATKARLSSTQQ 683

                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 32566156   1369 ARMELGGELARTQSELDRcrqiiiQLEENLK-SQESL 1404
Cdd:pfam10174  684 SLAEKDGHLTNLRAERRK------QLEEILEmKQEAL 714

PspC_subgroup_1

NF033838

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...

951-1350

8.32e-06

Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 50.40 E-value: 8.32e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   951 NENQKlrETQNRQDSHYSNLEKEVMEKSSLIDELQNQ--IQKLSDENNEQRLTIAKLETALEDEKarfarqnntigdMQK 1028
Cdd:NF033838   53 NESQK--EHAKEVESHLEKILSEIQKSLDKRKHTQNValNKKLSDIKTEYLYELNVLKEKSEAEL------------TSK 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1029 LISELNEKIARFdnialnernstrkiEREKEKLNEELTTAKEIIQKQAKKIDELKEECRK-------RKNEASRLERKLE 1101
Cdd:NF033838  119 TKKELDAAFEQF--------------KKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRnyptntyKTLELEIAESDVE 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1102 DKEAMMADCVKELKDSH-KERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSVDSDYGRSSSGRLSTLGRQYSL 1180
Cdd:NF033838  185 VKKAELELVKEEAKEPRdEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRR 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1181 TSIGSfssirtVGLGSRKD-SISDMTSSmyslrrrdstydmtSSTIGLQRSPSTSQ-----VMEKERRILELEKeKA--- 1251
Cdd:NF033838  265 AKRGV------LGEPATPDkKENDAKSS--------------DSSVGEETLPSPSLkpekkVAEAEKKVEEAKK-KAkdq 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1252 --------AINT----DLQLVKRELDVYKSQLSAVESEKEslQTANRKQSNQLQETTRqlnsaQKNADnlALRLKKALAD 1319
Cdd:NF033838  324 keedrrnyPTNTyktlELEIAESDVKVKEAELELVKEEAK--EPRNEEKIKQAKAKVE-----SKKAE--ATRLEKIKTD 394

                         410       420       430
                  ....*....|....*....|....*....|.
gi 32566156  1320 cdewKKKHEEsivESKTEILMERKRAMDRAE 1350
Cdd:NF033838  395 ----RKKAEE---EAKRKAAEEDKVKEKPAE 418

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

1055-1462

9.18e-06

Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.21 E-value: 9.18e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1055 EREKEKLNEELTTAKEIIQKQAKkIDELKEECRKRKNEASRLERKLEDKEammaDCVKELK-------DSHKERLKEME- 1126
Cdd:pfam10174  205 EKENIHLREELHRRNQLQPDPAK-TKALQTVIEMKDTKISSLERNIRDLE----DEVQMLKtngllhtEDREEEIKQMEv 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1127 --QKVEDVKRKNSKLENENSTQKSQIETFQRessvdsdygrsssgRLSTLGRQYSltsigsfssirtvglgSRKDSISDM 1204
Cdd:pfam10174  280 ykSHSKFMKNKIDQLKQELSKKESELLALQT--------------KLETLTNQNS----------------DCKQHIEVL 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1205 TSSMYSLRRRDSTYDMTSSTIGLQRSPSTSQVMEKERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTA 1284
Cdd:pfam10174  330 KESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQ 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1285 NRKQSNQLQETTRQLNSAQK---NADNLALRLKKALADcdewkkkhEESIVESkteiLMERKRAMDRAEACEKETELKQS 1361
Cdd:pfam10174  410 LRDKDKQLAGLKERVKSLQTdssNTDTALTTLEEALSE--------KERIIER----LKEQREREDRERLEELESLKKEN 477

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1362 RmatiesarmELGGELARTQSELDRCRQIIIQLEENLKSQESLGNSFGRHQTNLNFEIENLRDENCALKAKIRRQYKQIE 1441
Cdd:pfam10174  478 K---------DLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548

                          410       420
                   ....*....|....*....|.
gi 32566156   1442 LLTQQDETNDELNHFENKVER 1462
Cdd:pfam10174  549 AVRTNPEINDRIRLLEQEVAR 569

DUF3584

pfam12128

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...

874-1463

9.39e-06

Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.61 E-value: 9.39e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    874 KVQKELEEVEKQGR-------EKL---LEKEREFRKTMEEMEQN-----------EEIFNVLERKYNEQHKKVMKMNDVL 932
Cdd:pfam12128  319 KDRSELEALEDQHGafldadiETAaadQEQLPSWQSELENLEERlkaltgkhqdvTAKYNRRRSKIKEQNNRDIAGIKDK 398

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    933 RE--YERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALE 1010
Cdd:pfam12128  399 LAkiREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERARE 478

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1011 DEKARFARQnntigdmQKLISELNEKIARFDnialnerNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRK 1090
Cdd:pfam12128  479 EQEAANAEV-------ERLQSELRQARKRRD-------QASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEA 544

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1091 NEASRLERKLEDKEAMmadCVKELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQiETFQRESSVDSDYGrSSSGR 1170
Cdd:pfam12128  545 PDWEQSIGKVISPELL---HRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEE-ELRERLDKAEEALQ-SAREK 619

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1171 LSTLGRQYSLTSIgsfssirTVGLGSRKDSISDMTSSMYSLRRRDSTYDMTSSTIGLQRSpSTSQVMEKERRILELEKEK 1250
Cdd:pfam12128  620 QAAAEEQLVQANG-------ELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKA-LAERKDSANERLNSLEAQL 691

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1251 AAINTDLQLVKRELDVYKSQLSAVESEKesLQTANRKQSNQLQETTRQLNSAQKNAdnlalrlKKALADCDEWKKKH--- 1327
Cdd:pfam12128  692 KQLDKKHQAWLEEQKEQKREARTEKQAY--WQVVEGALDAQLALLKAAIAARRSGA-------KAELKALETWYKRDlas 762

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1328 ----EESIVESKTEIL-MERK---RAMDRAEACE-----KETELKQ-----SRMATIESARMELGGELARTQSELDRCRQ 1389
Cdd:pfam12128  763 lgvdPDVIAKLKREIRtLERKierIAVRRQEVLRyfdwyQETWLQRrprlaTQLSNIERAISELQQQLARLIADTKLRRA 842

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32566156   1390 iiiQLEENLKSQESLgnsfgrhQTNLNFEIENLRDENCALkAKIRRQYKQIELLTQQDETNDELNHFENKVERL 1463
Cdd:pfam12128  843 ---KLEMERKASEKQ-------QVRLSENLRGLRCEMSKL-ATLKEDANSEQAQGSIGERLAQLEDLKLKRDYL 905

COG1340

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

851-1135

9.67e-06

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 9.67e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  851 NEEALKENLK-LSMLLDREKSEKVKVQKELEEVEKQgREKLLEKEREFR----KTMEEMEQNEEIFNVLERKYNEQHKKV 925
Cdd:COG1340    9 SLEELEEKIEeLREEIEELKEKRDELNEELKELAEK-RDELNAQVKELReeaqELREKRDELNEKVKELKEERDELNEKL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  926 MKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQD--SHYSNLEKEVMEKsslIDELQNQIQKLSDEnNEQRLTIA 1003
Cdd:COG1340   88 NELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQteVLSPEEEKELVEK---IKELEKELEKAKKA-LEKNEKLK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1004 KLETALEDEKarfarqnntigdmqKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELK 1083
Cdd:COG1340  164 ELRAELKELR--------------KEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELH 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 32566156 1084 EECRKRKNEASRLERKLEDKEAmmadcvKELKDSHKERLKEMEQKVEDVKRK 1135
Cdd:COG1340  230 EEIIELQKELRELRKELKKLRK------KQRALKREKEKEELEEKAEEIFEK 275

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

1049-1302

1.05e-05

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: 49.38 E-value: 1.05e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1049 NSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAmmadcvkelkdshkeRLKEMEQK 1128
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ---------------ELAALEAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1129 VEDVKRKNSKLENENSTQKSQIETFqressVDSDYGRSSSGRLSTLGRQYSLTSIGSFSSIRTVGLGSRKDSISDMTSSM 1208
Cdd:COG4942   85 LAELEKEIAELRAELEAQKEELAEL-----LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1209 YSLRRrdstydmTSSTIGLQRSPSTSQVMEKERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQ 1288
Cdd:COG4942  160 AELAA-------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232

                        250
                 ....*....|....
gi 32566156 1289 SNQLQETTRQLNSA 1302
Cdd:COG4942  233 EAEAAAAAERTPAA 246

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

866-1151

1.15e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.15e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  866 DREKSEKVKVQKELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIFNVLERKYNEQHKKVMKMNDVLREYERKIEQLNME 945
Cdd:COG4372    2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  946 KTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQNNTIGD 1025
Cdd:COG4372   82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1026 MQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEA 1105
Cdd:COG4372  162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 32566156 1106 MMADCVKELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIE 1151
Cdd:COG4372  242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287

CwlO1

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

1067-1306

1.18e-05

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.18e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1067 TAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELKDSHKErlkeMEQKVEDVKRKNSKLENENSTQ 1146
Cdd:COG3883   13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEAEIEERREEL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1147 KSQIETFQRESSvdsdygrsSSGRLSTLgrqysltsigsfssirtvgLGSrkDSISDMTSSMYSLRR-RDSTYDMTSSTI 1225
Cdd:COG3883   89 GERARALYRSGG--------SVSYLDVL-------------------LGS--ESFSDFLDRLSALSKiADADADLLEELK 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1226 GLQRSPST--SQVMEKERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQ 1303
Cdd:COG3883  140 ADKAELEAkkAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219


                 ...
gi 32566156 1304 KNA 1306
Cdd:COG3883  220 AAA 222

CwlO1

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

844-1028

1.23e-05

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.23e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  844 IQEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEkqgrEKLLEKEREFRKTMEEMEQNEEIFNVLE-------- 915
Cdd:COG3883   39 LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE----AEIEERREELGERARALYRSGGSVSYLDvllgsesf 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  916 ----------RKYNEQHkkvmkmNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQ 985
Cdd:COG3883  115 sdfldrlsalSKIADAD------ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 32566156  986 NQIQKLSDENNEQRLTIAKLETALEDEKARFARQNNTIGDMQK 1028
Cdd:COG3883  189 AEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231

PRK01156

chromosome segregation protein; Provisional

747-1182

1.37e-05

chromosome segregation protein; Provisional

Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 1.37e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   747 KVGVISELETKRNNYISSFIILIQANIR-YLNIQKDLIERRKKLEA----VVTIQDNVRQFAEL-SQWPWYRIYHLTRGL 820
Cdd:PRK01156  271 KNNYYKELEERHMKIINDPVYKNRNYINdYFKYKNDIENKKQILSNidaeINKYHAIIKKLSVLqKDYNDYIKKKSRYDD 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   821 IPRNRDKERIEELENEKLKLEEEIQEMEIKNEEALKENL--KLSMLLDREKSEKVKVQKELEEVEKQGRE------KLLE 892
Cdd:PRK01156  351 LNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsaFISEILKIQEIDPDAIKKELNEINVKLQDisskvsSLNQ 430

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   893 KEREFRKTMEEMEQNEEIFNVLER-KYNEQHKKVMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLE 971
Cdd:PRK01156  431 RIRALRENLDELSRNMEMLNGQSVcPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLE 510

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   972 KEVMEKS----SLIDELQNQIQKLSDENNEqrltIAKLETALEDEKARFarQNNTIGDMQKLISELNEKIARFDNIALnE 1047
Cdd:PRK01156  511 SEEINKSineyNKIESARADLEDIKIKINE----LKDKHDKYEEIKNRY--KSLKLEDLDSKRTSWLNALAVISLIDI-E 583

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1048 RNSTRKIEREKeKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMmadcvkelkdshKERLKEMEQ 1127
Cdd:PRK01156  584 TNRSRSNEIKK-QLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQEN------------KILIEKLRG 650

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 32566156  1128 KVEDVKRKNSKLEnenSTQKSQIETFQRESSVDSDYGRSSSGRLSTLGRQYSLTS 1182
Cdd:PRK01156  651 KIDNYKKQIAEID---SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLES 702

DUF3584

pfam12128

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...

852-1133

1.41e-05

Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.84 E-value: 1.41e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    852 EEALKENL-KLSMLLDREKSekvkVQKELEEVEKQGREKLLEKEREFRKTMEEMEQNEEifnVLERKYNEQHKKVMKMND 930
Cdd:pfam12128  599 EEELRERLdKAEEALQSARE----KQAAAEEQLVQANGELEKASREETFARTALKNARL---DLRRLFDEKQSEKDKKNK 671

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    931 VLREYERK----IEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEksSLIDELQNQIQKLSDENNEQRLTIAKLE 1006
Cdd:pfam12128  672 ALAERKDSanerLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQ--VVEGALDAQLALLKAAIAARRSGAKAEL 749

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1007 TALEDEKARFARQNNTIGD-MQKLISELNEKIARFDNIALNERNSTR---------------------KIEREKEKLNEE 1064
Cdd:pfam12128  750 KALETWYKRDLASLGVDPDvIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwlqrrprlatqlsNIERAISELQQQ 829

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1065 LTTAKEIIQKQAKKI-----------DELKEECRKRKNEASRLERKLEDKEAMMAD--------CVKELKDSHKERLKEM 1125
Cdd:pfam12128  830 LARLIADTKLRRAKLemerkasekqqVRLSENLRGLRCEMSKLATLKEDANSEQAQgsigerlaQLEDLKLKRDYLSESV 909


                   ....*...
gi 32566156   1126 EQKVEDVK 1133
Cdd:pfam12128  910 KKYVEHFK 917

CwlO1

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

1097-1318

1.60e-05

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.60e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1097 ERKLEDKEAMMADCVKELKDShKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQREssvdsdygrsssgrLSTLGR 1176
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAA-QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE--------------IAEAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1177 QYSltsigsfssirtvglgSRKDSISDMTSSMYSLRRRDSTYDM--TSSTIG--LQRSPSTSQVMEKERRIL-------- 1244
Cdd:COG3883   80 EIE----------------ERREELGERARALYRSGGSVSYLDVllGSESFSdfLDRLSALSKIADADADLLeelkadka 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32566156 1245 ELEKEKAAINT---DLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKNADNLALRLKKALA 1318
Cdd:COG3883  144 ELEAKKAELEAklaELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220

DR0291

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

1241-1398

1.91e-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: 47.61 E-value: 1.91e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1241 RRILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQE--TTRQLNSAQKNADNLALRLKKAla 1318
Cdd:COG1579   31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIESLKRRISDL-- 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1319 dcdewkkkhEESIVEskteilmerkrAMDRAEACEKETELKQSRMA----TIESARMELGGELARTQSELDRCRQIIIQL 1394
Cdd:COG1579  109 ---------EDEILE-----------LMERIEELEEELAELEAELAeleaELEEKKAELDEELAELEAELEELEAEREEL 168


                 ....
gi 32566156 1395 EENL 1398
Cdd:COG1579  169 AAKI 172

rad50

TIGR00606

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

845-1460

1.94e-05

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.66 E-value: 1.94e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    845 QEMEIKNEEalKENLKLSMLLDREKSEKvkvQKELEEVEKQGREKLLEKEREFRKTmeemEQNEEIFNVLERKYNEQHKK 924
Cdd:TIGR00606  522 QEMEQLNHH--TTTRTQMEMLTKDKMDK---DEQIRKIKSRHSDELTSLLGYFPNK----KQLEDWLHSKSKEINQTRDR 592

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    925 VMKMNDVLREYERKIEQLNMEKTDLENENQKLRE------TQNRQDSHYSNLEKEVmEKSSlidelqNQIQKLSDENNEQ 998
Cdd:TIGR00606  593 LAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcGSQDEESDLERLKEEI-EKSS------KQRAMLAGATAVY 665

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    999 RLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKK 1078
Cdd:TIGR00606  666 SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE 745

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1079 IDELKEECRKRKNEASRLERKLEDKEAMMADCVKELKDSH------------KERLKEMEQKVEDVKRKNSKLENENSTQ 1146
Cdd:TIGR00606  746 IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvtimerfQMELKDVERKIAQQAAKLQGSDLDRTVQ 825

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1147 KSQIETFQRESSVDSDYGRSSSGRLSTLGRQYSLTSIGSfssiRTVGLGSRKDSISdmtssmyslrrrdstydmtsstig 1226
Cdd:TIGR00606  826 QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKS----KTNELKSEKLQIG------------------------ 877

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1227 lqrspstsqvmEKERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANrkqsnqlQETTRQLNSAQKNA 1306
Cdd:TIGR00606  878 -----------TNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK-------EELISSKETSNKKA 939

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1307 DNLALRLKKALADCDEWKKKHEESIVESKTEILMERKRAMDRAEACEKETELKQSRMatieSARMELGGELARTQSELDR 1386
Cdd:TIGR00606  940 QDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKI----NEDMRLMRQDIDTQKIQER 1015

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32566156   1387 CRQIIIQLEENLKSQESLGNSFGRHQTNLN-FEIENLRDENCALKAKIRR-QYKQIELLTQQDETNDELNHFENKV 1460
Cdd:TIGR00606 1016 WLQDNLTLRKRENELKEVEEELKQHLKEMGqMQVLQMKQEHQKLEENIDLiKRNHVLALGRQKGYEKEIKHFKKEL 1091

Rab5-bind

pfam09311

Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ...

851-1112

2.10e-05

Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.

Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 48.43 E-value: 2.10e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    851 NEEALKENLKLSMLLDREKSEKV----KVQKELEEVEKQGREKLLEKEREFRKTMEEMEQneeIFNVLERKYNEQHKKVM 926
Cdd:pfam09311   17 QEAETRDQVKKLQEMLRQANDQLektmKDKKELEDKMNQLSEETSNQVSTLAKRNQKSET---LLDELQQAFSQAKRNFQ 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    927 KMNDVLREyerKIEQLNMEKTDLENENQKLretQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLE 1006
Cdd:pfam09311   94 DQLAVLMD---SREQVSDELVRLQKDNESL---QGKHSLHVSLQQAEKFDMPDTVQELQELVLKYREELIEVRTAADHME 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1007 TALEDE--------KARFARQNNTIGDMQKLISELNEKIARFDNIALN------ERNSTRKIEREKEKLNEELTTAKEII 1072
Cdd:pfam09311  168 EKLKAEilflkeqiQAEQCLKENLEETLQAEIENCKEEIASISSLKVElerikaEKEQLENGLTEKIRQLEDLQTTKGSL 247

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 32566156   1073 QKQAKKIDE----LKEECRKRKNEASRLERKLEDKEAMMADCVK 1112
Cdd:pfam09311  248 ETQLKKETNekaaVEQLVFEEKNKAQRLQTELDVSEQVQRDFVK 291

rad50

TIGR00606

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

848-1162

2.22e-05

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 2.22e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    848 EIKN-EEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLlekEREFRKTMEEMEQNEEIFNVLERKYNEQhkkvm 926
Cdd:TIGR00606  249 PLKNrLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKM---EKVFQGTDEQLNDLYHNHQRTVREKERE----- 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    927 kmndvLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNE----QRLTI 1002
Cdd:TIGR00606  321 -----LVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPfserQIKNF 395

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1003 AKLETALEDEKARFARQNntigdMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQK------QA 1076
Cdd:TIGR00606  396 HTLVIERQEDEAKTAAQL-----CADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKElqqlegSS 470

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1077 KKIDELKEECRKRKNEASRLERkledkeammadcvKELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRE 1156
Cdd:TIGR00606  471 DRILELDQELRKAERELSKAEK-------------NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQM 537


                   ....*.
gi 32566156   1157 SSVDSD 1162
Cdd:TIGR00606  538 EMLTKD 543

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

865-1124

2.28e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 2.28e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  865 LDREKSEKVKVQKELEEVEKQ---GREKLLEKEREFRKTMEEMEQNEEIFNVLERKYNEQHKKVMKMNDVLREYERKIEQ 941
Cdd:COG4372   40 LDKLQEELEQLREELEQAREEleqLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  942 LNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLsdENNEQRLTIAKLETALEDEKARFARQNN 1021
Cdd:COG4372  120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL--EQELQALSEAEAEQALDELLKEANRNAE 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1022 TIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNeeLTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLE 1101
Cdd:COG4372  198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL--LDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275

                        250       260
                 ....*....|....*....|...
gi 32566156 1102 DKEAMMADCVKELKDSHKERLKE 1124
Cdd:COG4372  276 EELEIAALELEALEEAALELKLL 298

CagA_N

pfam18971

CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ...

858-1150

3.02e-05

CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.

Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 48.62 E-value: 3.02e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    858 NLKLSMLLDREKSEKVKVQK-ELEEVEK------QGREKLLEKEREFRKTMEEMEQNEEiFNVLERKYNEQHKKVMKMND 930
Cdd:pfam18971  550 NLAITSFVRRNLENKLTAKGlSLQEANKlikdflSSNKELAGKALNFNKAVAEAKSTGN-YDEVKKAQKDLEKSLRKREH 628

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    931 VLREYERKIEQLNMEKTDLENENQklreTQNRQDSHYSNLEKEVMEKSSLIDELQNQI---QKLSDENNEQRLTIAKLET 1007
Cdd:pfam18971  629 LEKEVEKKLESKSGNKNKMEAKAQ----ANSQKDEIFALINKEANRDARAIAYTQNLKgikRELSDKLEKISKDLKDFSK 704

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1008 ALEDEK----ARFARQNNTIGDMQKLISELN---EKIARFDNI--ALNE-RNSTRKIEREKEKLNEEL-TTAKEII--QK 1074
Cdd:pfam18971  705 SFDEFKngknKDFSKAEETLKALKGSVKDLGinpEWISKVENLnaALNEfKNGKNKDFSKVTQAKSDLeNSVKDVIinQK 784

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1075 QAKKIDELKE--ECRKRKNEASRLERKLEDkeammadcvkeLKDSHKERLKEMEQKVEDVKR-KNSKLEN--ENSTQKSQ 1149
Cdd:pfam18971  785 VTDKVDNLNQavSVAKAMGDFSRVEQVLAD-----------LKNFSKEQLAQQAQKNEDFNTgKNSELYQsvKNSVNKTL 853


                   .
gi 32566156   1150 I 1150
Cdd:pfam18971  854 V 854

PTZ00121

MAEBL; Provisional

846-1151

3.29e-05

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 3.29e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   846 EMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLLEKEREFRKtMEEMEQNEEIFNVLERKYNEQHKK- 924
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK-AEEARKAEDAKKAEAARKAEEVRKa 1190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   925 --VMKMNDVLR-------EYERKIEQL-------NMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQI 988
Cdd:PTZ00121 1191 eeLRKAEDARKaeaarkaEEERKAEEArkaedakKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   989 QKLSDENNEQRltiaKLETALEDEKARFARQNNTIGDMQKLISELNEKiARFDNIALNERNSTRKIEREKEKLNEELTTA 1068
Cdd:PTZ00121 1271 AIKAEEARKAD----ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1069 KEIIQKQAKKIDELKEEcrKRKNEASRLERKLEDKEAMMADCVKELK---DSHKERLKEMEQKVEDVKRKNSKLENENST 1145
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAA--EEKAEAAEKKKEEAKKKADAAKKKAEEKkkaDEAKKKAEEDKKKADELKKAAAAKKKADEA 1423


                  ....*.
gi 32566156  1146 QKSQIE 1151
Cdd:PTZ00121 1424 KKKAEE 1429

CwlO1

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

1240-1452

3.35e-05

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 3.35e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1240 ERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKNADNLALRLKKALAD 1319
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1320 cdewkkKHEESIVESKTEILMERK---RAMDRAEACEKETELKQSRMATIESARmelgGELARTQSELDRCRQIIIQLEE 1396
Cdd:COG3883   95 ------LYRSGGSVSYLDVLLGSEsfsDFLDRLSALSKIADADADLLEELKADK----AELEAKKAELEAKLAELEALKA 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 32566156 1397 NLKSQeslgnsfgrhQTNLNFEIENLRDENCALKAKIRRQYKQIELLTQQDETNDE 1452
Cdd:COG3883  165 ELEAA----------KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210

PRK12704

phosphodiesterase; Provisional

1043-1156

4.58e-05

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 4.58e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1043 IALNERNSTRKIEREKEKLNEElttAKEIIQKQAKKIDELKE----ECRKRKNEASRLERKLEDKEammadcvkELKDSH 1118
Cdd:PRK12704   33 IKEAEEEAKRILEEAKKEAEAI---KKEALLEAKEEIHKLRNefekELRERRNELQKLEKRLLQKE--------ENLDRK 101

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 32566156  1119 KERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRE 1156
Cdd:PRK12704  102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139

COG1340

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

900-1151

4.88e-05

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 4.88e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  900 TMEEMEQNEEIfNVLERKYNEQHKKVMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQ---NRQDSHYSNLEKEVME 976
Cdd:COG1340    7 SSSLEELEEKI-EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRdelNEKVKELKEERDELNE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  977 KSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNI--ALNERNSTRKI 1054
Cdd:COG1340   86 KLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAkkALEKNEKLKEL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1055 EREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELkDSHKERLKEMEQKVEDVKR 1134
Cdd:COG1340  166 RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKA-DELHEEIIELQKELRELRK 244

                        250
                 ....*....|....*..
gi 32566156 1135 KNSKLENENSTQKSQIE 1151
Cdd:COG1340  245 ELKKLRKKQRALKREKE 261

PRK11637

AmiB activator; Provisional

936-1078

5.53e-05

AmiB activator; Provisional

Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.38 E-value: 5.53e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   936 ERKIEQLNMEKTDLENENQKLRETQNRQdshysnlekevmekSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKAR 1015
Cdd:PRK11637  169 QETIAELKQTREELAAQKAELEEKQSQQ--------------KTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQ 234

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32566156  1016 FA--RQNNTigdmqklisELNEKIARfdnialNERNSTRKIE---REKEKLNEElttakeiiQKQAKK 1078
Cdd:PRK11637  235 LSelRANES---------RLRDSIAR------AEREAKARAEreaREAARVRDK--------QKQAKR 279

235kDa-fam

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...

888-1156

6.19e-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: 48.12 E-value: 6.19e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    888 EKLLEKEREFRKT--MEEMEQNEEIFNVLERKYneqhkKVMKMNDVLREYERK-IEQLNMEKTDLENENQKLretqnrqD 964
Cdd:TIGR01612 1061 EKEIGKNIELLNKeiLEEAEINITNFNEIKEKL-----KHYNFDDFGKEENIKyADEINKIKDDIKNLDQKI-------D 1128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    965 SHYSNLEKEVMEKSSLIDELQNQIQKLSDENNE--QRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNE------K 1036
Cdd:TIGR01612 1129 HHIKALEEIKKKSENYIDEIKAQINDLEDVADKaiSNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEiekdktS 1208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1037 IARFDNIALNERNSTRKIERekEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELKD 1116
Cdd:TIGR01612 1209 LEEVKGINLSYGKNLGKLFL--EKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDD 1286

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 32566156   1117 S-HKERLKEMEQKVEDVKRKNSKLENENStQKSQIETFQRE 1156
Cdd:TIGR01612 1287 KdHHIISKKHDENISDIREKSLKIIEDFS-EESDINDIKKE 1326

ERM_helical

pfam20492

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...

892-1012

7.22e-05

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

Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 43.75 E-value: 7.22e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    892 EKEREFRKTMEEMEQNEEIFNVLERKYNEQHKKVMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLE 971
Cdd:pfam20492    3 EAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 32566156    972 KEVMEKSSLIDELQNQIQKLSDENNEQRltiAKLETALEDE 1012
Cdd:pfam20492   83 AELAEAQEEIARLEEEVERKEEEARRLQ---EELEEAREEE 120

COG2433

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

944-1086

7.36e-05

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

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 7.36e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  944 MEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARfarqnnti 1023
Cdd:COG2433  385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE-------- 456

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1024 gdmQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQ-------AKKIDELKEEC 1086
Cdd:COG2433  457 ---ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEhsgelvpVKVVEKFTKEA 523

Smc

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

778-1027

7.43e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 7.43e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  778 IQKDLIERRKKLEAV-VTIQDNVRQFAELSQwpwyRIYHLTRGLIP----RNRDKERIEELENEKLKLEEEIQEMEIKNE 852
Cdd:COG1196  265 LEAELEELRLELEELeLELEEAQAEEYELLA----ELARLEQDIARleerRRELEERLEELEEELAELEEELEELEEELE 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  853 EALKenlklsmlldrEKSEKVKVQKELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIFNVLERKYNEQHKKVMKMNDVL 932
Cdd:COG1196  341 ELEE-----------ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  933 REYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDE 1012
Cdd:COG1196  410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489

                        250
                 ....*....|....*
gi 32566156 1013 KARFARQNNTIGDMQ 1027
Cdd:COG1196  490 AARLLLLLEAEADYE 504

235kDa-fam

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...

867-1142

8.39e-05

Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.35 E-value: 8.39e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    867 REKSEKV----KVQKELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIFNVLerKYNeqhkKVMKMNDVLREYERKIEQL 942
Cdd:TIGR01612 1304 REKSLKIiedfSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNIL--KLN----KIKKIIDEVKEYTKEIEEN 1377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    943 NME-KTDLEN---------ENQKLRETQNRQDSHYSNleKEVMEKSSLIDELQNQIQ----------KLSDENNEQRLTI 1002
Cdd:TIGR01612 1378 NKNiKDELDKseklikkikDDINLEECKSKIESTLDD--KDIDECIKKIKELKNHILseesnidtyfKNADENNENVLLL 1455

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1003 AKlETALEDEKARFA---RQNNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKi 1079
Cdd:TIGR01612 1456 FK-NIEMADNKSQHIlkiKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSAL- 1533

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32566156   1080 dELKEECRKRKNEASRLerkledkeammadcVKELKDSHKERLKEM---EQKVEDVKRKNSKLENE 1142
Cdd:TIGR01612 1534 -AIKNKFAKTKKDSEII--------------IKEIKDAHKKFILEAeksEQKIKEIKKEKFRIEDD 1584

HAP1_N

pfam04849

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...

1047-1155

1.25e-04

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.

Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 45.79 E-value: 1.25e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1047 ERNSTRKIEREKEKLNEELTTAKEIIQKQA--KKIDELKEECRKRKNEASRLERK---LEDKEAM-MADCVKELKDSHK- 1119
Cdd:pfam04849  139 EESETESSCSTPLRRNESFSSLHGCVQLDAlqEKLRGLEEENLKLRSEASHLKTEtdtYEEKEQQlMSDCVEQLSEANQq 218

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 32566156   1120 --ERLKEMEQKVEDvkrkNSKLENENSTQKSQIETFQR 1155
Cdd:pfam04849  219 maELSEELARKMEE----NLRQQEEITSLLAQIVDLQH 252

Mitofilin

pfam09731

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...

954-1147

1.30e-04

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

Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 46.67 E-value: 1.30e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    954 QKLRETQNRQDSHYSNLEKEVMEK-SSLIDELQNQIQKLSDENNEQRLTI-AKLETALEDEKARFARQNNtigdmqKLIS 1031
Cdd:pfam09731  261 QELVSIFPDIIPVLKEDNLLSNDDlNSLIAHAHREIDQLSKKLAELKKREeKHIERALEKQKEELDKLAE------ELSA 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1032 ELNEKIARF--DNIALNERNSTRKIEREKEKLNEELTTAKEIIQkqakkiDELKEECRKRKNEASR-LERKLEDKeamma 1108
Cdd:pfam09731  335 RLEEVRAADeaQLRLEFEREREEIRESYEEKLRTELERQAEAHE------EHLKDVLVEQEIELQReFLQDIKEK----- 403

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 32566156   1109 dcVKELKDSHKERLKEMEQKVEDVKR---KNSKLENEN-STQK 1147
Cdd:pfam09731  404 --VEEERAGRLLKLNELLANLKGLEKatsSHSEVEDENrKAQQ 444

YhaN

COG4717

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

842-1157

1.31e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.31e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  842 EEIQEMEIKNEEALKENLKLSMLLDREK--SEKVKVQKELEEVEKQgREKLLEKEREFRKTMEEMEQ-NEEIFNVLERKY 918
Cdd:COG4717  102 EELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPER-LEELEERLEELRELEEELEElEAELAELQEELE 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  919 NEQHKKVMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDShysnlEKEVMEKSSLIDELQNQIQKLsdennEQ 998
Cdd:COG4717  181 ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE-----ELEQLENELEAAALEERLKEA-----RL 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  999 RLTIAKLETALEDEKARFARQNNTIGDMQKLI---------------SELNEKIARFDNIALNERNSTRKIEREKEKLNE 1063
Cdd:COG4717  251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllallflllarekASLGKEAEELQALPALEELEEEELEELLAALGL 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1064 ELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERK--LEDKEAMMADC-VKELKD--SHKERLKEMEQKVEDVKRKNSK 1138
Cdd:COG4717  331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLAEAgVEDEEElrAALEQAEEYQELKEELEELEEQ 410

                        330
                 ....*....|....*....
gi 32566156 1139 LENENSTQKSQIETFQRES 1157
Cdd:COG4717  411 LEELLGELEELLEALDEEE 429

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

1019-1156

1.36e-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: 45.91 E-value: 1.36e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1019 QNNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLER 1098
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1099 KLEDKEAMMADCV-------------------------------KELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQK 1147
Cdd:COG4942   98 ELEAQKEELAELLralyrlgrqpplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELE 177


                 ....*....
gi 32566156 1148 SQIETFQRE 1156
Cdd:COG4942  178 ALLAELEEE 186

DR0291

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

1234-1354

1.46e-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: 44.92 E-value: 1.46e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1234 SQVMEKERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKE---------SLQTANRKQSNQLQETTRQLNSAQK 1304
Cdd:COG1579   45 ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealqkeieSLKRRISDLEDEILELMERIEELEE 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 32566156 1305 NADNLALRLKKALADCDEWKKKHEESIVESKTEILMERKRamdRAEACEK 1354
Cdd:COG1579  125 ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE---REELAAK 171

Lebercilin

pfam15619

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...

940-1104

1.47e-04

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: 44.51 E-value: 1.47e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    940 EQLNMEKTDLENENQKLRETQNRqdshYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRL-TIAKLETALEDEKARFAR 1018
Cdd:pfam15619   60 QLIARHNEEVRVLRERLRRLQEK----ERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLaEREELQKKLEQLEAKLED 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1019 QNNTIGDMQKliselnekiarfdNIALNERNSTRKIEREKeklneelttakeiiqkqaKKIDELKEECRKRKNEASRLER 1098
Cdd:pfam15619  136 KDEKIQDLER-------------KLELENKSFRRQLAAEK------------------KKHKEAQEEVKILQEEIERLQQ 184


                   ....*.
gi 32566156   1099 KLEDKE 1104
Cdd:pfam15619  185 KLKEKE 190

PRK12704

phosphodiesterase; Provisional

872-1079

1.52e-04

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.52e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   872 KVKVQKELEEVEKQGREKLLEKEREFRKTMEE--MEQNEEIFNV---LERKYNEQHKKVMKMNDVLREYErkiEQLNMEK 946
Cdd:PRK12704   26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEalLEAKEEIHKLrneFEKELRERRNELQKLEKRLLQKE---ENLDRKL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   947 TDLENENQKLREtqnrqdshysnLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLeTAlEDEKARFarqnntigdM 1026
Cdd:PRK12704  103 ELLEKREEELEK-----------KEKELEQKQQELEKKEEELEELIEEQLQELERISGL-TA-EEAKEIL---------L 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 32566156  1027 QKLISELNEKIARFdnialnernsTRKIEREkeklneelttAKEIIQKQAKKI 1079
Cdd:PRK12704  161 EKVEEEARHEAAVL----------IKEIEEE----------AKEEADKKAKEI 193

EzrA

pfam06160

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...

914-1135

2.02e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.

Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 45.62 E-value: 2.02e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    914 LERKYNEQHKKVMKmndVLREYERKIEQL--NMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSL---IDELQNQI 988
Cdd:pfam06160  224 EEEGYALEHLNVDK---EIQQLEEQLEENlaLLENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVeknLPEIEDYL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    989 QKLSDENNEqrltiakLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNERNST---RKIEREKEKLNEEL 1065
Cdd:pfam06160  301 EHAEEQNKE-------LKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEvaySELQEELEEILEQL 373

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32566156   1066 TTAKEIIQKQAKKIDELKEECRKRKNEASRLERKL-EDKEAMMADCVKELKDSHKERLKEMEQKVEDVKRK 1135
Cdd:pfam06160  374 EEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELrEIKRLVEKSNLPGLPESYLDYFFDVSDEIEDLADE 444

PLN03229

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional

844-1148

2.04e-04

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional

Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 46.00 E-value: 2.04e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   844 IQEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELE---EVEKQG-REKLLEKEREFRKT-----------MEEMEQNE 908
Cdd:PLN03229  438 VEKLKEQILKAKESSSKPSELALNEMIEKLKKEIDLEyteAVIAMGlQERLENLREEFSKAnsqdqlmhpvlMEKIEKLK 517

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   909 EIFNV-LERKYNeqHKKVMKMNDVLREYERK--IEQLNMEKTDLENE-NQKLRETQNRQDShysnleKEVMEksSLIDEL 984
Cdd:PLN03229  518 DEFNKrLSRAPN--YLSLKYKLDMLNEFSRAkaLSEKKSKAEKLKAEiNKKFKEVMDRPEI------KEKME--ALKAEV 587

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   985 QNQ-IQKLSDENNEQRLTIAKLETALEDEKARFARQnntigdmqkliSELNEKIARFDNIALNERNSTRKIEREKEKLNE 1063
Cdd:PLN03229  588 ASSgASSGDELDDDLKEKVEKMKKEIELELAGVLKS-----------MGLEVIGVTKKNKDTAEQTPPPNLQEKIESLNE 656

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1064 ELTTAKEIIQKQA---KKIDELKEECRK--------RKNEASRLERKLEDKEAMMADcVKELKDSHKERLKEMEQKVEDV 1132
Cdd:PLN03229  657 EINKKIERVIRSSdlkSKIELLKLEVAKasktpdvtEKEKIEALEQQIKQKIAEALN-SSELKEKFEELEAELAAARETA 735

                         330
                  ....*....|....*.
gi 32566156  1133 KRKNSKLENENSTQKS 1148
Cdd:PLN03229  736 AESNGSLKNDDDKEED 751

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

1238-1463

2.34e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 2.34e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1238 EKERRI--LELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKEslqtanrkqsnqLQETTRQLNSAQKNADNLALRLKK 1315
Cdd:TIGR02168  197 ELERQLksLERQAEKAERYKELKAELRELELALLVLRLEELREE------------LEELQEELKEAEEELEELTAELQE 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1316 ALADCDEWKKKHEEsiVESKTEILMER-KRAMDRAEACEKETELKQSRMATIESARMELGGELARTQSELDRCRQIIIQL 1394
Cdd:TIGR02168  265 LEEKLEELRLEVSE--LEEEIEELQKElYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1395 EENLKSQESLGNSFGRHQTNLNFEIENLRDENCALKAKIRRQY-KQIELLTQQDETNDELNHFENKVERL 1463
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRsKVAQLELQIASLNNEIERLEARLERL 412

PRK04778

septation ring formation regulator EzrA; Provisional

914-1143

2.40e-04

septation ring formation regulator EzrA; Provisional

Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 2.40e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   914 LERKYNEQHKKVMKMndvLREYERKIEQL--NMEKTDLENENQKLRETQNRQDSHYSNLEKEV-----MEKssLIDELQN 986
Cdd:PRK04778  243 VEEGYHLDHLDIEKE---IQDLKEQIDENlaLLEELDLDEAEEKNEEIQERIDQLYDILEREVkarkyVEK--NSDTLPD 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   987 QIQKLSDENNEqrltiakLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIalnernsTRKIErEKEKLNEELt 1066
Cdd:PRK04778  318 FLEHAKEQNKE-------LKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEI-------TERIA-EQEIAYSEL- 381

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32566156  1067 taKEIIQKQAKKIDELKEECRKRKNEASRLERklEDKEAmmadcvkelkdshKERLKEMEQKVEDVKRknsKLENEN 1143
Cdd:PRK04778  382 --QEELEEILKQLEEIEKEQEKLSEMLQGLRK--DELEA-------------REKLERYRNKLHEIKR---YLEKSN 438

PRK05771

V-type ATP synthase subunit I; Validated

909-1123

2.65e-04

V-type ATP synthase subunit I; Validated

Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 2.65e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   909 EIFNVLERKYNEQHKKVMKMNDVLREYERKIEQ-LNMEKTDLENEN----QKLRETQNRQDSHYSNLEKEVMEKSSLIDE 983
Cdd:PRK05771   32 HIEDLKEELSNERLRKLRSLLTKLSEALDKLRSyLPKLNPLREEKKkvsvKSLEELIKDVEEELEKIEKEIKELEEEISE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   984 LQNQIQKLsdENNEQRLTI-AKLETALEDE------KARFARQNNTIGDMQKLISEL-NEKIARFDN-----IALNERNS 1050
Cdd:PRK05771  112 LENEIKEL--EQEIERLEPwGNFDLDLSLLlgfkyvSVFVGTVPEDKLEELKLESDVeNVEYISTDKgyvyvVVVVLKEL 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32566156  1051 TRKIEREKEKLN------EELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMmadcVKELKDSHKERLK 1123
Cdd:PRK05771  190 SDEVEEELKKLGferlelEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLA----LYEYLEIELERAE 264

COG2433

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

1054-1156

3.13e-04

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

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 3.13e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1054 IEREKEK-LNEELTTAKEIIQKQAKKIDELKEECRKRKN-------EASRLERKLEDKEAMMADCVKELKDSHKERLKEM 1125
Cdd:COG2433  382 LEELIEKeLPEEEPEAEREKEHEERELTEEEEEIRRLEEqverleaEVEELEAELEEKDERIERLERELSEARSEERREI 461

                         90       100       110
                 ....*....|....*....|....*....|...
gi 32566156 1126 --EQKVEDVKRKNSKLENENSTQKSQIETFQRE 1156
Cdd:COG2433  462 rkDREISRLDREIERLERELEEERERIEELKRK 494

PHA02562

endonuclease subunit; Provisional

939-1142

3.23e-04

endonuclease subunit; Provisional

Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 3.23e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   939 IEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETA---------- 1008
Cdd:PHA02562  194 QQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAaakikskieq 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1009 --------------------LEDEKARFARQNNTIGDMQKLISELNEkiarfdnialnernstrKIEREKEKLNEeltta 1068
Cdd:PHA02562  274 fqkvikmyekggvcptctqqISEGPDRITKIKDKLKELQHSLEKLDT-----------------AIDELEEIMDE----- 331

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32566156  1069 keiIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELKDsHKERLKEMEQKVEDVKRKNSKLENE 1142
Cdd:PHA02562  332 ---FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD-NAEELAKLQDELDKIVKTKSELVKE 401

Myosin_tail_1

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

852-1150

3.37e-04

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 3.37e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    852 EEALKENLKLSMLLDreksekvKVQKELEEVeKQGREKLLEKEREFRKTMEEME----QNEEIFNVLER--KYNEQHKKV 925
Cdd:pfam01576  794 EEAVKQLKKLQAQMK-------DLQRELEEA-RASRDEILAQSKESEKKLKNLEaellQLQEDLAASERarRQAQQERDE 865

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    926 MK------------MNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSD 993
Cdd:pfam01576  866 LAdeiasgasgksaLQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLER 945

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    994 ENNEQRLTIAKLETALEdekarfARQNNTIGDMQKLISELNEKIarfdNIALNERNSTRKIEREKEKLNEELTTAKEIIQ 1073
Cdd:pfam01576  946 QNKELKAKLQEMEGTVK------SKFKSSIAALEAKIAQLEEQL----EQESRERQAANKLVRRTEKKLKEVLLQVEDER 1015

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32566156   1074 KQAkkiDELKEECRKRKNEASRLERKLEDKEammadcvKELKDSHKERLKeMEQKVEDVKRKNSKLENENSTQKSQI 1150
Cdd:pfam01576 1016 RHA---DQYKDQAEKGNSRMKQLKRQLEEAE-------EEASRANAARRK-LQRELDDATESNESMNREVSTLKSKL 1081

HCR

pfam07111

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...

861-1125

3.46e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.

Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.13 E-value: 3.46e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    861 LSMLLDREKSEKVKVQKELEEVEKQGR---EKLLEKEREFRKTMEEMEQNEEIFNVLERKYNEQHKKVMKMNDVLreyER 937
Cdd:pfam07111  378 LQMELSRAQEARRRQQQQTASAEEQLKfvvNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLM---AR 454

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    938 KIE--QLNMEK-----------TDLENENQKLRETQNRQDSHYS---------------NLEKEVMEKSSLIDELQNQIQ 989
Cdd:pfam07111  455 KVAlaQLRQEScpppppappvdADLSLELEQLREERNRLDAELQlsahliqqevgrareQGEAERQQLSEVAQQLEQELQ 534

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    990 KLSDE--NNEQRLTIAKLETALEDEKARFARQNNTigDMQKLISE-LNEKIARFDNIALNERNSTRKIEREKEKLNEELT 1066
Cdd:pfam07111  535 RAQESlaSVGQQLEVARQGQQESTEEAASLRQELT--QQQEIYGQaLQEKVAEVETRLREQLSDTKRRLNEARREQAKAV 612

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1067 TAKEIIQKQAKKIDELKEECRK-----RKNEASRLERKLE----DKEAMMADCVKE--LKDSHKERLKEM 1125
Cdd:pfam07111  613 VSLRQIQHRATQEKERNQELRRlqdeaRKEEGQRLARRVQelerDKNLMLATLQQEglLSRYKQQRLLAV 682

PHA02562

endonuclease subunit; Provisional

1022-1284

3.74e-04

endonuclease subunit; Provisional

Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 3.74e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1022 TIGDMQKL----ISELNEKIARFDNIAlneRNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLe 1097
Cdd:PHA02562  164 VLSEMDKLnkdkIRELNQQIQTLDMKI---DHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEEL- 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1098 rkledkeammadcvkelkdshKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRE--------------SSVDSDY 1163
Cdd:PHA02562  240 ---------------------TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcptctQQISEGP 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1164 GRSSSGRLSTLGRQYSLTSIgsfsSIRTVGLGSRKDSISDMTSSMYSLRRRDSTYDMTSSTIglqrspsTSQVMEKERRI 1243
Cdd:PHA02562  299 DRITKIKDKLKELQHSLEKL----DTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITL-------VDKAKKVKAAI 367

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 32566156  1244 LELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTA 1284
Cdd:PHA02562  368 EELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIV 408

Taxilin

pfam09728

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...

845-1087

3.78e-04

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.

Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 44.17 E-value: 3.78e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    845 QEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGRE------KLLEKEREFRKTMEEMEQNE--EIFNVLER 916
Cdd:pfam09728   42 KKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNKKlkeeskKLAKEEEEKRKELSEKFQSTlkDIQDKMEE 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    917 KyNEQHKKVMKMNDVLRE--------YERKIEQLN--MEKTDLENENQKLRETQNRQDSHYSNLEKEVMEksslIDELQN 986
Cdd:pfam09728  122 K-SEKNNKLREENEELREklkslieqYELRELHFEklLKTKELEVQLAEAKLQQATEEEEKKAQEKEVAK----ARELKA 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    987 QIQKLSDENNEQRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARF--DNIALnernsTRKIEREKEKL--- 1061
Cdd:pfam09728  197 QVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLekENLTW-----KRKWEKSNKALlem 271

                          250       260
                   ....*....|....*....|....*.
gi 32566156   1062 NEELTTAKEIIQKQAKKIDELKEECR 1087
Cdd:pfam09728  272 AEERQKLKEELEKLQKKLEKLENLCR 297

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

1034-1418

3.78e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 3.78e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1034 NEKIARFDNIaLNERN-STRKIEREKEKLNE--ELTTAKEIIQKQ--AKKIDELKEECRKRKNEASRLERKLEDKEAMMA 1108
Cdd:TIGR02168  185 RENLDRLEDI-LNELErQLKSLERQAEKAERykELKAELRELELAllVLRLEELREELEELQEELKEAEEELEELTAELQ 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1109 DCVKELkDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSVDSDYGRSSSGRLSTLGRQ-----YSLTSI 1183
Cdd:TIGR02168  264 ELEEKL-EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKldelaEELAEL 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1184 gsfssirtvglgsrKDSISDMTSSMYSLRRRdstydmtsstigLQRSPSTSQVMEkeRRILELEKEKAAINTDLQLVKRE 1263
Cdd:TIGR02168  343 --------------EEKLEELKEELESLEAE------------LEELEAELEELE--SRLEELEEQLETLRSKVAQLELQ 394

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1264 LDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQknadnlalrlkkaladcdewKKKHEESIVESKTEIlmerK 1343
Cdd:TIGR02168  395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--------------------LKELQAELEELEEEL----E 450

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1344 RAMDRAEACEKETELKQSRMATIESARMELGGELARTQSELDRCRQIIIQLE-------ENLKSQESLGNSFGRHQTNLN 1416
Cdd:TIGR02168  451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvkALLKNQSGLSGILGVLSELIS 530


                   ..
gi 32566156   1417 FE 1418
Cdd:TIGR02168  531 VD 532

Crescentin

pfam19220

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...

880-1126

3.90e-04

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: 44.67 E-value: 3.90e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    880 EEVEKQGREKLLEKERE-FRKTMEEMEQNEEIFNVLERKYNEQHKKVMKMNDVLREYERKIEQLNMEKTDLEN-----EN 953
Cdd:pfam19220   46 AKSRLLELEALLAQERAaYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAqaealER 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    954 QKLRETQNRQ---------DSHYSNLEKEVMEKSSLIDELQNQIQKLSDEN-------NEQRLTIAKL-------ETALE 1010
Cdd:pfam19220  126 QLAAETEQNRaleeenkalREEAQAAEKALQRAEGELATARERLALLEQENrrlqalsEEQAAELAELtrrlaelETQLD 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1011 DEKARfarqnntIGDMQKLISELNEKIARFDNiALNERNSTRKIER-----EKEKLNEELTTAKEIIQKQAKKIDELKEE 1085
Cdd:pfam19220  206 ATRAR-------LRALEGQLAAEQAERERAEA-QLEEAVEAHRAERaslrmKLEALTARAAATEQLLAEARNQLRDRDEA 277

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 32566156   1086 CRK--RKN-EAS----RLERKLEDKEAMMADCVKELKDSHKERLKEME 1126
Cdd:pfam19220  278 IRAaeRRLkEASierdTLERRLAGLEADLERRTQQFQEMQRARAELEE 325

CALCOCO1

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

827-1127

5.66e-04

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: 44.12 E-value: 5.66e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    827 KERIEELENEKLKLEEEIQEMEIKNEEALKENLKLSM---LLDREKSEKVKVQKELEEVEKQGREKLLEKEREFRKTMEE 903
Cdd:pfam07888   79 ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEekdALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKER 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    904 MEQneeifNVLERKYNEQHKKvmkmndvlrEYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDE 983
Cdd:pfam07888  159 AKK-----AGAQRKEEEAERK---------QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    984 LQNQIQKLSDENNE-----QRLTIA--KLETALEDEKARFARQNNTIGDMQKL---ISELNEKIARFdNIALNERNSTRK 1053
Cdd:pfam07888  225 AHRKEAENEALLEElrslqERLNASerKVEGLGEELSSMAAQRDRTQAELHQArlqAAQLTLQLADA-SLALREGRARWA 303

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1054 IEREKEKLNEELTtaKEIIQKQAKKIDELKEECRKRKNEASRLERKLedkeAMMADC-----------VKELKDSHKERL 1122
Cdd:pfam07888  304 QERETLQQSAEAD--KDRIEKLSAELQRLEERLQEERMEREKLEVEL----GREKDCnrvqlsesrreLQELKASLRVAQ 377


                   ....*
gi 32566156   1123 KEMEQ 1127
Cdd:pfam07888  378 KEKEQ 382

235kDa-fam

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...

865-1143

7.47e-04

Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.27 E-value: 7.47e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    865 LDREKSEKVKVQKELEEVEKQGREKL-LEKEREFrktmeEMEQNEEIFNVLERKYNEQHKKVMKMNDVLREYERKIEQLN 943
Cdd:TIGR01612 1182 IDKKKNIYDEIKKLLNEIAEIEKDKTsLEEVKGI-----NLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIK 1256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    944 MEKTDLENEN------QKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRlTIAKLETALEDEKARFA 1017
Cdd:TIGR01612 1257 EKSPEIENEMgiemdiKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIEDFSEES-DINDIKKELQKNLLDAQ 1335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1018 RQNNTIGDMQKLISELNE--KIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKqaKKIDELKEECRkrkneaSR 1095
Cdd:TIGR01612 1336 KHNSDINLYLNEIANIYNilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKK--IKDDINLEECK------SK 1407

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 32566156   1096 LERKLEDKEamMADCVKELKDSHKERLKemEQKVEDVKRKNSKLENEN 1143
Cdd:TIGR01612 1408 IESTLDDKD--IDECIKKIKELKNHILS--EESNIDTYFKNADENNEN 1451

TACC_C

pfam05010

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...

876-1104

9.83e-04

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.

Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 41.97 E-value: 9.83e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    876 QKELEEVEKQGREKLLEKEREFRKtmeemeqneeifnvLERKYNEQHKKVMKMNDVLREYERKIEQLnmektdlenenqk 955
Cdd:pfam05010    3 QKDMDAALEKARNEIEEKELEINE--------------LKAKYEELRRENLEMRKIVAEFEKTIAQM------------- 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    956 LRETQNRQDSHYSNLEKEVMEKSSLIDELQNqiqklsdenneqrltiakLETALEDEKARFARQNNTIGDMQKLISELNE 1035
Cdd:pfam05010   56 IEEKQKQKELEHAEIQKVLEEKDQALADLNS------------------VEKSFSDLFKRYEKQKEVISGYKKNEESLKK 117

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32566156   1036 KIARF-DNIALNE-RNSTRKIEREK--EKLNEELTTAKEIIQKQAKKideLKEECRKRKNEASRLERKLEDKE 1104
Cdd:pfam05010  118 CAQDYlARIKKEEqRYQALKAHAEEklDQANEEIAQVRSKAKAETAA---LQASLRKEQMKVQSLERQLEQKT 187

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

1075-1345

1.04e-03

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 1.04e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1075 QAKKIDELKEECRKRKNEASRLERKLEDkeammadcVKELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQ 1154
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAA--------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1155 REssvdsdygrsssgrLSTLGRQysltsigsfssirtvgLGSRKDSISDMTSSMYSLRRRDStydmtsstIGLQRSPSTS 1234
Cdd:COG4942   90 KE--------------IAELRAE----------------LEAQKEELAELLRALYRLGRQPP--------LALLLSPEDF 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1235 QVMEKERRILE-LEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQLNSAQKNADNLALRL 1313
Cdd:COG4942  132 LDAVRRLQYLKyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211

                        250       260       270
                 ....*....|....*....|....*....|..
gi 32566156 1314 KKALADCDEWKKKHEESIVESKTEILMERKRA 1345
Cdd:COG4942  212 AAELAELQQEAEELEALIARLEAEAAAAAERT 243

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

846-1131

1.09e-03

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 1.09e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    846 EMEIKNEEALKENLKLSmlLDREKSEKVKVQKELEEVEKQgrekLLEKEREFRKTMEEMEQNEEIFNVLERKYNEQHKKV 925
Cdd:TIGR04523  453 ELIIKNLDNTRESLETQ--LKVLSRSINKIKQNLEQKQKE----LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI 526

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    926 MKMNDVLREYERKIEQLNME---------KTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENN 996
Cdd:TIGR04523  527 EKLESEKKEKESKISDLEDElnkddfelkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    997 EQRLTIAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNERNSTRKIErekEKLNEELTTAKEIIQKQA 1076
Cdd:TIGR04523  607 EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII---KKIKESKTKIDDIIELMK 683

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32566156   1077 KKIDELKEECRK------RKNEASRLERKLEDKEAMMADcVKELKDSHKERLKEMEQKVED 1131
Cdd:TIGR04523  684 DWLKELSLHYKKyitrmiRIKDLPKLEEKYKEIEKELKK-LDEFSKELENIIKNFNKKFDD 743

GumC

COG3206

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

1119-1316

1.15e-03

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.15e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1119 KERLKEMEQKVEDVKRKNS--KLENENSTQKSQIETFQRE-SSVDSDYgRSSSGRLSTLGRQYSLTSIGSFSSIRTVGLG 1195
Cdd:COG3206  188 RKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQlAEARAEL-AEAEARLAALRAQLGSGPDALPELLQSPVIQ 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1196 SRKDSISDMTSSMYSLRRRdstYdmtsstiglqrSPSTSQVMEKERRILELEKE-KAAINTDLQLVKRELDVYKSQLSAV 1274
Cdd:COG3206  267 QLRAQLAELEAELAELSAR---Y-----------TPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALQAREASL 332

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 32566156 1275 ESEKESLQTANR---KQSNQLQETTRQLNSAQKNADNLALRLKKA 1316
Cdd:COG3206  333 QAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEA 377

PTZ00121

MAEBL; Provisional

848-1361

1.37e-03

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.37e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   848 EIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIfnvleRKYNEQHKKvmk 927
Cdd:PTZ00121 1065 HVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDA-----RKAEEARKA--- 1136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   928 mndvlrEYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLET 1007
Cdd:PTZ00121 1137 ------EDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEE 1210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1008 ALEDEKARFARQNNTIGDMQKliSELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECR 1087
Cdd:PTZ00121 1211 ERKAEEARKAEDAKKAEAVKK--AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1088 KRKNEASRlerKLEDKEAmmadcVKELKDSHKERLK--EMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSVDSDYGR 1165
Cdd:PTZ00121 1289 KKKADEAK---KAEEKKK-----ADEAKKKAEEAKKadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1166 SSSGRLSTLGRQYSltsigsfssirtvglgSRKDSISDMTSSMYSLRRRDStydmtsstiglqrspSTSQVMEKERRILE 1245
Cdd:PTZ00121 1361 AAEEKAEAAEKKKE----------------EAKKKADAAKKKAEEKKKADE---------------AKKKAEEDKKKADE 1409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1246 LEKEKAAINTDLQLVKRELDVYKSQlsavESEKESLQTANRKQSNQLQETTRQLNSAQKNADNL--ALRLKKALAD---C 1320
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKAD----EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEakkA 1485

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 32566156  1321 DEWKKKHEESivESKTEILMERKRAMDRAEACEKETELKQS 1361
Cdd:PTZ00121 1486 DEAKKKAEEA--KKKADEAKKAAEAKKKADEAKKAEEAKKA 1524

HMMR_N

pfam15905

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...

852-1099

1.38e-03

Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.49 E-value: 1.38e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    852 EEALKENLKLSMLLdrekSEKVKVQKELEEVEKQGREklLEKEREFRKTMEEMEQNEEIFNVLERKYNEQHKKV-MKMND 930
Cdd:pfam15905  101 EELEKVEAKLNAAV----REKTSLSASVASLEKQLLE--LTRVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLeAKMKE 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    931 VLREYERKIEQLNMEKTDLENENQKLRETQNRQdshySNLEKEVMEKSSLIDELQNQIQKLS---DENNEQRLTIAKLET 1007
Cdd:pfam15905  175 VMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKL----VSTEKEKIEEKSETEKLLEYITELScvsEQVEKYKLDIAQLEE 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1008 ALEdEKARfarqnntigDMQKLISELNEKIARFDNIAlNERNSTRK-IEREKEKLneeLTTAKEIIQKQAKKIDELKEEC 1086
Cdd:pfam15905  251 LLK-EKND---------EIESLKQSLEEKEQELSKQI-KDLNEKCKlLESEKEEL---LREYEEKEQTLNAELEELKEKL 316

                          250
                   ....*....|...
gi 32566156   1087 RKRKNEASRLERK 1099
Cdd:pfam15905  317 TLEEQEHQKLQQK 329

HEC1

COG5185

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...

871-1162

1.80e-03

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: 42.64 E-value: 1.80e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  871 EKVKVQKELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIFNVL-ERKYNEQHKKVMKMNDVLREYERKIEQLNMEK-TD 948
Cdd:COG5185   91 EKKLDTKILQEYVNSLIKLPNYEWSADILISLLYLYKSEIVALKdELIKVEKLDEIADIEASYGEVETGIIKDIFGKlTQ 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  949 LENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQNNTIGDMQK 1028
Cdd:COG5185  171 ELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQ 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1029 LISELNEKIARFDNIAL----NERNSTRKIEREKEKLNEELTTAKEIIQKQAKKID-----ELKEECRKRKNEASRLERK 1099
Cdd:COG5185  251 TSDKLEKLVEQNTDLRLeklgENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDikkatESLEEQLAAAEAEQELEES 330

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32566156 1100 LEDKEAMMADCVKELKDSHKERLKEMEQKVEDVKRKNSKLENENSTQKSQIETFQRESSVDSD 1162
Cdd:COG5185  331 KRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESL 393

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

828-1020

2.40e-03

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.40e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  828 ERIEELENEKLKLEEEIQEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGREKLLEKEREFRKTMEEMEQN 907
Cdd:COG4942   62 RRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  908 EEIFNVLERKYNEQHKKVMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQ 987
Cdd:COG4942  142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221

                        170       180       190
                 ....*....|....*....|....*....|...
gi 32566156  988 IQKLSDEnneqrltIAKLETALEDEKARFARQN 1020
Cdd:COG4942  222 AEELEAL-------IARLEAEAAAAAERTPAAG 247

235kDa-fam

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...

901-1130

2.45e-03

Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 2.45e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    901 MEEMEQNEEIFNVLERKYNEQHKKVMKMNDVLREYERKIEQLNMEKTDLENENqKLRETQNrqdshysnlEKEVMEKSsl 980
Cdd:TIGR01612 1485 INELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKN-KFAKTKK---------DSEIIIKE-- 1552

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    981 IDELQNQIqKLSDENNEQRLT-IAKLETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNI------------ALNE 1047
Cdd:TIGR01612 1553 IKDAHKKF-ILEAEKSEQKIKeIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIkkkindclketeSIEK 1631

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1048 RNSTRKIEREKEKLN-------------EELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERkleDKEAMMADCVKEL 1114
Cdd:TIGR01612 1632 KISSFSIDSQDTELKengdnlnslqeflESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKK---NYEIGIIEKIKEI 1708

                          250
                   ....*....|....*.
gi 32566156   1115 KDSHKERLKEMEQKVE 1130
Cdd:TIGR01612 1709 AIANKEEIESIKELIE 1724

CALCOCO1

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

1228-1406

2.49e-03

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 2.49e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1228 QRSPSTSQVMEKERRILELEKEKAAINTDLQLVKRELDVYK-------SQLSAVESEKESLQT---ANRKQSNQLQETTR 1297
Cdd:pfam07888  116 EKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKerakkagAQRKEEEAERKQLQAklqQTEEELRSLSKEFQ 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1298 QLNSAQKNADNLALRLKKALADCDEWKKKHEESIVESktEILMERKRAM-DRAEACEKETELKQSRMATIESARmelgge 1376
Cdd:pfam07888  196 ELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN--EALLEELRSLqERLNASERKVEGLGEELSSMAAQR------ 267

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 32566156   1377 lARTQSELDRCR----QIIIQLEE-NLKSQESLGN 1406
Cdd:pfam07888  268 -DRTQAELHQARlqaaQLTLQLADaSLALREGRAR 301

CALCOCO1

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

876-1299

2.51e-03

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 2.51e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    876 QKELEEVEKQGREKLLEKEREFRKTMEEMEQNEEIFNVLERKYNEQHKKVMKMNDVLREYERKIEQLNMEKTDLENENQK 955
Cdd:pfam07888   33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    956 LRETQNrqdshysNLEKEVMEKSSLIDELQNQIQKLSDENNEQrltiaklETALEDEKARFARQNNTIGDMQKLISELNE 1035
Cdd:pfam07888  113 LSEEKD-------ALLAQRAAHEARIRELEEDIKTLTQRVLER-------ETELERMKERAKKAGAQRKEEEAERKQLQA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1036 KIarfdnialnernstRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMadcvKELK 1115
Cdd:pfam07888  179 KL--------------QQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALL----EELR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1116 dSHKERLKEMEQKVEDVKRKNSKLenenSTQKSQIETFQRESSVDSdygRSSSGRLSTLGRQYSlTSIGSFSSIRTVGLG 1195
Cdd:pfam07888  241 -SLQERLNASERKVEGLGEELSSM----AAQRDRTQAELHQARLQA---AQLTLQLADASLALR-EGRARWAQERETLQQ 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1196 S---RKDSISDMTSSMYSLRRRdstydmtsstigLQRspstsQVMEKERRILELEKEKAAINTDLQLVKRELDVYKSQLS 1272
Cdd:pfam07888  312 SaeaDKDRIEKLSAELQRLEER------------LQE-----ERMEREKLEVELGREKDCNRVQLSESRRELQELKASLR 374

                          410       420
                   ....*....|....*....|....*..
gi 32566156   1273 AVESEKESLQTanrkQSNQLQETTRQL 1299
Cdd:pfam07888  375 VAQKEKEQLQA----EKQELLEYIRQL 397

PRK12704

phosphodiesterase; Provisional

846-1015

2.69e-03

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.69e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   846 EMEIKNEEAL----KENLKLSMLLDREKSEKvkvQKELEEVEK--QGREKLLEKERE-FRKTMEEMEQNEEIFNVLERKY 918
Cdd:PRK12704   50 EAEAIKKEALleakEEIHKLRNEFEKELRER---RNELQKLEKrlLQKEENLDRKLElLEKREEELEKKEKELEQKQQEL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   919 NEQHKkvmkmndvlrEYERKIEQlnmektdlenENQKLretqnrqdSHYSNLEKE-----VMEKssLIDELQNQIQKLSD 993
Cdd:PRK12704  127 EKKEE----------ELEELIEE----------QLQEL--------ERISGLTAEeakeiLLEK--VEEEARHEAAVLIK 176

                         170       180
                  ....*....|....*....|..
gi 32566156   994 ENNEQrltiAKLETaleDEKAR 1015
Cdd:PRK12704  177 EIEEE----AKEEA---DKKAK 191

DUF5401

pfam17380

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

894-1147

2.79e-03

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

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 2.79e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    894 EREFRKTMEEMEQNEEIFNvlERKYNEQHKKvMKMNDVLREYERKIEQlnMEKTDLENENQKLRETQ-NRQDSHYSNLEK 972
Cdd:pfam17380  267 ENEFLNQLLHIVQHQKAVS--ERQQQEKFEK-MEQERLRQEKEEKARE--VERRRKLEEAEKARQAEmDRQAAIYAEQER 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    973 EVMEKSSLIDELQNQIQKLSDENNEQRltiaklETALEDEKARfarqnntigDMQKLISELNEKiarfdnialNERNSTR 1052
Cdd:pfam17380  342 MAMERERELERIRQEERKRELERIRQE------EIAMEISRMR---------ELERLQMERQQK---------NERVRQE 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1053 KIEREKEKLNEELTtakeiiQKQAKKIDELKEECRKRKNEASRLE-RKLEDKEAmmadcvKELkdshkERLKEME----- 1126
Cdd:pfam17380  398 LEAARKVKILEEER------QRKIQQQKVEMEQIRAEQEEARQREvRRLEEERA------REM-----ERVRLEEqerqq 460

                          250       260
                   ....*....|....*....|....*..
gi 32566156   1127 ------QKVEDVKRKNSKLENENSTQK 1147
Cdd:pfam17380  461 qverlrQQEEERKRKKLELEKEKRDRK 487

PRK11637

AmiB activator; Provisional

939-1109

2.81e-03

AmiB activator; Provisional

Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 2.81e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   939 IEQLNMEKTDLENENQKLRETQNRqdshYSNLEKEVMEKSSLIDELQNQiqklsdENNEQRLTIAKLETALedekarfaR 1018
Cdd:PRK11637   74 LAQLKKQEEAISQASRKLRETQNT----LNQLNKQIDELNASIAKLEQQ------QAAQERLLAAQLDAAF--------R 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1019 QNNTIGdMQKLIS----ELNEKI---------ARFDNIalNERNSTRK-IEREKEKLNEELTTAKEIIQKQAKKIDELKE 1084
Cdd:PRK11637  136 QGEHTG-LQLILSgeesQRGERIlayfgylnqARQETI--AELKQTREeLAAQKAELEEKQSQQKTLLYEQQAQQQKLEQ 212

                         170       180
                  ....*....|....*....|....*
gi 32566156  1085 ECRKRKNEASRLERKLEDKEAMMAD 1109
Cdd:PRK11637  213 ARNERKKTLTGLESSLQKDQQQLSE 237

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

1228-1404

3.67e-03

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 3.67e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1228 QRSPSTSQVMEKERRILELEKEKAAINTDLQLVKRELDVYKSQLSAVESEKESLQTANRKQSNQLQETTRQ------LNS 1301
Cdd:COG4942   49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplallLSP 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1302 AQKNADNLALRLKKALADCDewkKKHEESIVESKTEILMERKRAMDRAEACEKETELKQSRMATIESARMELGGELARTQ 1381
Cdd:COG4942  129 EDFLDAVRRLQYLKYLAPAR---REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE 205

                        170       180
                 ....*....|....*....|...
gi 32566156 1382 SELDRCRQIIIQLEENLKSQESL 1404
Cdd:COG4942  206 KELAELAAELAELQQEAEELEAL 228

Tropomyosin

pfam00261

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...

954-1145

4.08e-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: 40.40 E-value: 4.08e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    954 QKLRETQNRQDSHYSNLEKEVMEKSSLIDE---LQNQIQKLSDE--NNEQRLTIA--KLETAL----EDEKARFARQNNT 1022
Cdd:pfam00261    8 EELDEAEERLKEAMKKLEEAEKRAEKAEAEvaaLNRRIQLLEEEleRTEERLAEAleKLEEAEkaadESERGRKVLENRA 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1023 IGDMQKLiSELNEKIARFDNIALNERNSTRKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLE- 1101
Cdd:pfam00261   88 LKDEEKM-EILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEk 166

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 32566156   1102 --DKEAMMADCVKELKDshkeRLKEMEQKVEDVKRKNSKLENENST 1145
Cdd:pfam00261  167 asEREDKYEEQIRFLTE----KLKEAETRAEFAERSVQKLEKEVDR 208

235kDa-fam

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...

876-1347

4.23e-03

Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 4.23e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    876 QKELEEVEKQGREKLLEKEREFRKTMEEMEqnEEIFNVLerkyNEQhkKVMKmNDVLREYERKIEQLNMEKTDLENENQK 955
Cdd:TIGR01612  798 QINIDNIKDEDAKQNYDKSKEYIKTISIKE--DEIFKII----NEM--KFMK-DDFLNKVDKFINFENNCKEKIDSEHEQ 868

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    956 LRETQNR-----QDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNeqrlTIAKLETALEDEKARFARQNNTIGDMQKLI 1030
Cdd:TIGR01612  869 FAELTNKikaeiSDDKLNDYEKKFNDSKSLINEINKSIEEEYQNIN----TLKKVDEYIKICENTKESIEKFHNKQNILK 944

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1031 SELNEKIA--------------RFDNIALNERNSTRKIEREKEkLNEELTTAKEIIQkqakKIDELKEECrkRKNEASRL 1096
Cdd:TIGR01612  945 EILNKNIDtikesnlieksykdKFDNTLIDKINELDKAFKDAS-LNDYEAKNNELIK----YFNDLKANL--GKNKENML 1017

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1097 ERKLEDKEAMMADCVKELKDSHKE----------RLKEMEQKVEDVKRKNSKLENENSTQKSQ--IETFQRESSVDSDYG 1164
Cdd:TIGR01612 1018 YHQFDEKEKATNDIEQKIEDANKNipnieiaihtSIYNIIDEIEKEIGKNIELLNKEILEEAEinITNFNEIKEKLKHYN 1097

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1165 RSSSGRLSTLGRQYSLTSIGsfSSIRTVglgsrKDSISDMTSSMYSLRRRDSTY--DMTSSTIGLQRSPSTSQVMEKERr 1242
Cdd:TIGR01612 1098 FDDFGKEENIKYADEINKIK--DDIKNL-----DQKIDHHIKALEEIKKKSENYidEIKAQINDLEDVADKAISNDDPE- 1169

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1243 ilELEKEKAAINTDLQLVK---RELDVYKSQLSAVESEKESLQTANRKQSNQLQETTR----QLNSAQKNADNLALRLKK 1315
Cdd:TIGR01612 1170 --EIEKKIENIVTKIDKKKniyDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKlfleKIDEEKKKSEHMIKAMEA 1247

                          490       500       510
                   ....*....|....*....|....*....|..
gi 32566156   1316 ALADCDEWKKKHEEsiVESKTEILMERKRAMD 1347
Cdd:TIGR01612 1248 YIEDLDEIKEKSPE--IENEMGIEMDIKAEME 1277

Nuf2_DHR10-like

pfam18595

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...

940-1063

4.32e-03

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.

Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 38.72 E-value: 4.32e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    940 EQLNMEKTDLENENQKLRETQNRQDShYSNLEKEVMEKSSLIDELQNQIQKLsdenNEQRLTIAKLETALEDEKARFARQ 1019
Cdd:pfam18595    2 STLAEEKEELAELERKARELQAKIDA-LQVVEKDLRSCIKLLEEIEAELAKL----EEAKKKLKELRDALEEKEIELREL 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 32566156   1020 NNTIGDMQKLISELNEKIARFdnialnERNSTRKIEREKEKLNE 1063
Cdd:pfam18595   77 ERREERLQRQLENAQEKLERL------REQAEEKREAAQARLEE 114

PRK12705

hypothetical protein; Provisional

884-1131

4.43e-03

hypothetical protein; Provisional

Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.23 E-value: 4.43e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   884 KQGREKLLEKEREFRKTMEEMEQNEEIFNVLERKYNEQHKKVMKmNDVLREYER---KIEQLNMEKTDLENEN------- 953
Cdd:PRK12705   33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRER-EELQREEERlvqKEEQLDARAEKLDNLEnqleere 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   954 QKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQ--IQKLSDENNEQRLTIAKLETALEDEKARFARQNNTIGDMQKLIS 1031
Cdd:PRK12705  112 KALSARELELEELEKQLDNELYRVAGLTPEQARKllLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQAMQRIAS 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  1032 ELNEKIARFDNIALNERNSTRKIERE---KEKLnEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAmma 1108
Cdd:PRK12705  192 ETASDLSVSVVPIPSDAMKGRIIGREgrnIRAF-EGLTGVDLIIDDTPEAVVISSFNPIRREIARLTLEKLLADGRI--- 267

                         250       260
                  ....*....|....*....|...
gi 32566156  1109 dcvkelkdsHKERLKEMEQKVED 1131
Cdd:PRK12705  268 ---------HPARIEEYVQKANE 281

DUF5401

pfam17380

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

1053-1394

4.49e-03

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

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 4.49e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1053 KIEREKEKLN--EELTT--AKEIIQKQAKKIDE---LKEECRKRKNEASRLERKLEDKEAMMadcvkelkdsHKERLK-E 1124
Cdd:pfam17380  235 KMERRKESFNlaEDVTTmtPEYTVRYNGQTMTEnefLNQLLHIVQHQKAVSERQQQEKFEKM----------EQERLRqE 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1125 MEQKVEDVKRKNsKLENENSTQKSQIEtfqRESSVDSDYGRSSSGRLSTLGRQYSLTSIGSFSSIRtvglgsrKDSISDM 1204
Cdd:pfam17380  305 KEEKAREVERRR-KLEEAEKARQAEMD---RQAAIYAEQERMAMERERELERIRQEERKRELERIR-------QEEIAME 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1205 TSSMYSLRRRDSTYDmtsstiglQRSPSTSQVMEKERRILELEKEKaaiNTDLQLVKRELD-VYKSQLSAVESEKESLQT 1283
Cdd:pfam17380  374 ISRMRELERLQMERQ--------QKNERVRQELEAARKVKILEEER---QRKIQQQKVEMEqIRAEQEEARQREVRRLEE 442

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1284 ANRKQSNQ--LQETTRQLNSAQKNADNLALRLKKALADCDEWKKKHEES----IVESKTEilmERKRAMDRAEACEK--E 1355
Cdd:pfam17380  443 ERAREMERvrLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEqrrkILEKELE---ERKQAMIEEERKRKllE 519

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 32566156   1356 TELKQSRMATIESARMELGGELARTQSELDRCRQIIIQL 1394
Cdd:pfam17380  520 KEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQM 558

Spc7

smart00787

Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...

887-1018

4.58e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.

Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 4.58e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156     887 REKLLEKERE-FRKTMEEMEQNEEIFNVLERKYNEQHKKVMKMNDVLreyERKIEQLNMEKTDLENENQKLretQNRQDS 965
Cdd:smart00787  138 RMKLLEGLKEgLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDAL---EEELRQLKQLEDELEDCDPTE---LDRAKE 211

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|...
gi 32566156     966 HYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFAR 1018
Cdd:smart00787  212 KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264

TPH

pfam13868

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

844-1135

4.66e-03

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

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 4.66e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    844 IQEMEIKNEEALKENLKlsmlldreksEKVKVQKELEEVEKQGREKLLEKEREFRKTMEEMEQneeiFNVLERKYNEQHK 923
Cdd:pfam13868   82 IEEREQKRQEEYEEKLQ----------EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDE----FNEEQAEWKELEK 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    924 KVMkmndvlREYERKIEQLNMEKTDLENENQKLRETQNRqdshysnlekevmEKSSLIDELQNQIQKLSDENNEQRLTIA 1003
Cdd:pfam13868  148 EEE------REEDERILEYLKEKAEREEEREAEREEIEE-------------EKEREIARLRAQQEKAQDEKAERDELRA 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156   1004 KL--ETALEDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREK--EKLNEELTTAKEIIQKQAKKI 1079
Cdd:pfam13868  209 KLyqEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERmlRKQAEDEEIEQEEAEKRRMKR 288

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 32566156   1080 DELKEECRKRKNEasRLERKLEDKEAMMADCVKElkdshKERLKEMEQKVEDVKRK 1135
Cdd:pfam13868  289 LEHRRELEKQIEE--REEQRAAEREEELEEGERL-----REEEAERRERIEEERQK 337

COG4913

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

865-1040

5.55e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.55e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  865 LDREKSEKVKVQKELEEVEKQGREklLEKEREFRKTMEEMEQNEEIFNVLERKY---NEQHKKVMKMNDVLREYERKIEQ 941
Cdd:COG4913  619 LAELEEELAEAEERLEALEAELDA--LQERREALQRLAEYSWDEIDVASAEREIaelEAELERLDASSDDLAALEEQLEE 696

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156  942 LNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSSLIDELQNQIQKLSDENNEQRLTIAKLETALEDEKARFARQNN 1021
Cdd:COG4913  697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID 776

                        170       180
                 ....*....|....*....|
gi 32566156 1022 TI-GDMQKLISELNEKIARF 1040
Cdd:COG4913  777 ALrARLNRAEEELERAMRAF 796

CALCOCO1

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

827-1110

5.87e-03

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 5.87e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    827 KERIEELENEKLKLEEEIQEMEIKNEEALKENLKLSMLLDREKSEKVKVQKELEEVEKQGReKLLEKEREFRKTMEEME- 905
Cdd:pfam07888  128 EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR-SLSKEFQELRNSLAQRDt 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    906 ---QNEEIFNVLERKYNEQHKKVMKMNDVLREYERKIEQLNMEKTDLENENQKLRETQNRQDSHYSNLEKEVMEKSslid 982
Cdd:pfam07888  207 qvlQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAA---- 282

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156    983 ELQNQIQKLSDENNEQRLTIAKLETAL----EDEKARFARQNNTIGDMQKLISELNEKIARFDNIALNERNSTRKIEREK 1058
Cdd:pfam07888  283 QLTLQLADASLALREGRARWAQERETLqqsaEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSES 362

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 32566156   1059 EKLNEELTTAKEIIQKQakkidelKEECRKRKNEASRLERKLEDKEAMMADC 1110
Cdd:pfam07888  363 RRELQELKASLRVAQKE-------KEQLQAEKQELLEYIRQLEQRLETVADA 407

DR0291

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

1052-1156

8.36e-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: 39.52 E-value: 8.36e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566156 1052 RKIEREKEKLNEELTTAKEIIQKQAKKIDELKEECRKRKNEASRLERKLEDKEAMMADCVKELKDSHKER-LKEMEQKVE 1130
Cdd:COG1579   20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeYEALQKEIE 99

                         90       100
                 ....*....|....*....|....*.
gi 32566156 1131 DVKRKNSKLENENSTQKSQIETFQRE 1156
Cdd:COG1579  100 SLKRRISDLEDEILELMERIEELEEE 125

Myosin_tail_1