NCBI Conserved Domain Search

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

606-1089

1.55e-17

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 1.55e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  606 RLEFERQQREELE-KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:COG1196   303 DIARLEERRRELEeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  685 AEKEKFEEERLReqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEE 764
Cdd:COG1196   383 ELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  765 QEKEQVMLVAHLEEQLREKQEMIQLLR-RGEVQWVEEEKRDLEGIRESLLR-VKEARAGGDEDGEELEKAQLRFFEFKRR 842
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEeLAEAAARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYE 537

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  843 QLV----------KLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDfekikPVEYR 912
Cdd:COG1196   538 AALeaalaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD-----LREAD 612

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  913 LQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLdnTLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeftANIAR 992
Cdd:COG1196   613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV--TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL----EELAE 686

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  993 QEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLAslnsgsrEQSGLQASLEAEQEALE 1072
Cdd:COG1196   687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL-------EEEELLEEEALEELPEP 759

                         490
                  ....*....|....*..
gi 530425792 1073 KDQERLEYEIQQLKQKI 1089
Cdd:COG1196   760 PDLEELERELERLEREI 776

DUF5401

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

624-937

1.37e-14

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: 79.40 E-value: 1.37e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   624 RKLIEEMEEKQKSDKAELERMQQEVETQRKETEivqlQIRKQEESLKRRSFHIEnKLKDLLAEKEKFEEERLReqqeiEL 703
Cdd:pfam17380  281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERER-----EL 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   704 QKKRQEEEtflrvQEELQRLKElnnNEKAEKFQIFQELDQLQKEKDEQYAKL--ELEKKR----LEEQEKEQVMLVAHLE 777
Cdd:pfam17380  351 ERIRQEER-----KRELERIRQ---EEIAMEISRMRELERLQMERQQKNERVrqELEAARkvkiLEEERQRKIQQQKVEM 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   778 EQLREKQEMIqllRRGEVQWVEEEK-RDLEGIREsllrvkearaggdedgEELEKAQ----LRFFEFKRRQlvKLVNLEK 852
Cdd:pfam17380  423 EQIRAEQEEA---RQREVRRLEEERaREMERVRL----------------EEQERQQqverLRQQEEERKR--KKLELEK 481

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   853 DLVQQKD-------ILKKEVQEEQEILeclkCEHDKESRLLEKHDESVTdvTEVPQDFEKIKPVEYRLQYKERQLQYLLQ 925
Cdd:pfam17380  482 EKRDRKRaeeqrrkILEKELEERKQAM----IEEERKRKLLEKEMEERQ--KAIYEEERRREAEEERRKQQEMEERRRIQ 555

                          330
                   ....*....|..
gi 530425792   926 NHLPTLLEEKQR 937
Cdd:pfam17380  556 EQMRKATEERSR 567

PTZ00121

MAEBL; Provisional

610-902

5.84e-14

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.87 E-value: 5.84e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  610 ERQQREELEKLESKRKLIE--EMEEKQKSD---KAELERMQQE---VETQRKETEIVQLQIRKQEESLKRRSFHIENKLK 681
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEakKAEEKKKADelkKAEELKKAEEkkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  682 dLLAEKEKFEEerlreqqeiELQKKRQEE----ETFLRVQEELQRLKELNNNEKAEKfqifQELDQLQKEKDEQYAKLEL 757
Cdd:PTZ00121 1600 -LYEEEKKMKA---------EEAKKAEEAkikaEELKKAEEEKKKVEQLKKKEAEEK----KKAEELKKAEEENKIKAAE 1665

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  758 EKKRlEEQEKEQVMLVAHLEEQLREKQEmiQLLRRGE--------VQWVEEEKRDLEGIR----ESLLRVKEARAGGDED 825
Cdd:PTZ00121 1666 EAKK-AEEDKKKAEEAKKAEEDEKKAAE--ALKKEAEeakkaeelKKKEAEEKKKAEELKkaeeENKIKAEEAKKEAEED 1742

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530425792  826 GEELEKAQLRFFEFKrrqlvKLVNLEKDLVQQKDILKKEvqEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQD 902
Cdd:PTZ00121 1743 KKKAEEAKKDEEEKK-----KIAHLKKEEEKKAEEIRKE--KEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

614-1147

5.83e-13

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: 74.72 E-value: 5.83e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   614 REELEKLESKrklIEEMEEKQKSDKAELERMQQEVE-TQRKETEIVQLQIRKQEESLKRRS--FHIENKLKDLLAEKEKF 690
Cdd:TIGR02169  363 KEELEDLRAE---LEEVDKEFAETRDELKDYREKLEkLKREINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINEL 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   691 EEERLREQQEIELQkkrqeeetflrvQEELQRLKELNNNEKAEKFQIFQELDQLQKE---KDEQYAKLELEKKRLEEQEK 767
Cdd:TIGR02169  440 EEEKEDKALEIKKQ------------EWKLEQLAADLSKYEQELYDLKEEYDRVEKElskLQRELAEAEAQARASEERVR 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   768 EQVMLVAHLEEQLREKQEMIQLLRRGEVQW----------------VEEEKRDLEGIrESLLRVKEARAG---------- 821
Cdd:TIGR02169  508 GGRAVEEVLKASIQGVHGTVAQLGSVGERYataievaagnrlnnvvVEDDAVAKEAI-ELLKRRKAGRATflplnkmrde 586

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   822 ------GDEDG------------EELEKA---------QLRFFEFKRRQL--VKLVNLEKDLVQQ--------------- 857
Cdd:TIGR02169  587 rrdlsiLSEDGvigfavdlvefdPKYEPAfkyvfgdtlVVEDIEAARRLMgkYRMVTLEGELFEKsgamtggsraprggi 666

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   858 --KDILKKEVQEEQEILECLKCEhdkESRLLEKHDESVTdvtEVPQDFEKIKPVEYRLQYKERQLQYLLQNH--LPTLLE 933
Cdd:TIGR02169  667 lfSRSEPAELQRLRERLEGLKRE---LSSLQSELRRIEN---RLDELSQELSDASRKIGEIEKEIEQLEQEEekLKERLE 740

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   934 EKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQL---------QKLQATFEFTANIARQEEKVRKKEKEI 1004
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsriPEIQAELSKLEEEVSRIEARLREIEQK 820

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  1005 LESREkQQREALERALARLERRHSALQ-RHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQ 1083
Cdd:TIGR02169  821 LNRLT-LEKEYLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530425792  1084 QLKQKIYEV----------DGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDLHRV 1147
Cdd:TIGR02169  900 ELERKIEELeaqiekkrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973

Kinesin_assoc

pfam16183

Kinesin-associated;

364-476

1.11e-11

Kinesin-associated;

Pssm-ID: 465047 [Multi-domain] Cd Length: 177 Bit Score: 65.25 E-value: 1.11e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   395 ---LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183   83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162

                          170
                   ....*....|....
gi 530425792   463 LLSTGIILYHLKEG 476
Cdd:pfam16183  163 PLMSECLLYYIKDG 176

FHA

COG1716

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];

471-551

5.00e-07

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];

Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 49.57 E-value: 5.00e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  471 YHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLsGSQ--CSVNGVQIVEATHLNQGAVILLGRTnM 548
Cdd:COG1716    16 FPLDGGPLTIGRAPDN---DIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90


                  ...
gi 530425792  549 FRF 551
Cdd:COG1716    91 LRF 93

Yop-YscD_cpl

pfam16697

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...

471-555

1.78e-05

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.

Pssm-ID: 465238 [Multi-domain] Cd Length: 94 Bit Score: 44.94 E-value: 1.78e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   471 YHLKEGQTYVGRDDastEQDIVLHGLDLESEHCIFENIGGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILLGRTnM 548
Cdd:pfam16697   12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLgSGNGTLVNGQRVTELGIaLRPGDRIELGQT-E 87


                   ....*..
gi 530425792   549 FRFNHPK 555
Cdd:pfam16697   88 FCLVPAD 94

GBP_C

cd16269

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...

618-818

6.09e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.

Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.11 E-value: 6.09e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  618 EKLESKRKLIEEMEEKqksdKAELERMQQEVETQRKETEIVQLqIRKQEESLKRRSFHIENKLKDLLAEKEKFeeerlre 697
Cdd:cd16269    87 EDQKFQKKLMEQLEEK----KEEFCKQNEEASSKRCQALLQEL-SAPLEEKISQGSYSVPGGYQLYLEDREKL------- 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  698 qqeieLQKKRQEEETFLRVQEELQR-LKELNNNEKAEKfQIFQELDQLQKEKDEQYAK---LELEKKRLEEQEKEQVMLv 773
Cdd:cd16269   155 -----VEKYRQVPRKGVKAEEVLQEfLQSKEAEAEAIL-QADQALTEKEKEIEAERAKaeaAEQERKLLEEQQRELEQK- 227

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 530425792  774 ahLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEA 818
Cdd:cd16269   228 --LEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEA 270

Name

Accession

Description

Interval

E-value

KISc_KIF1A_KIF1B

cd01365

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...

2-365

0e+00

Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 564.29 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE- 239
Cdd:cd01365   159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqDAANTLAKKKQVFVPYRDSVLTWL 318
Cdd:cd01365   239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALA----DMSSGKSKKKSSFIPYRDSVLTWL 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 530425792  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365   315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361

KISc

smart00129

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...

3-365

1.81e-149

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.

Pssm-ID: 214526 [Multi-domain] Cd Length: 335 Bit Score: 463.97 E-value: 1.81e-149

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792      3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTL 82
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEET 67

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792     83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129   68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLL 145

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    163 RRKSSKtfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:smart00129  146 NPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaantlakkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129  223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292

                           330       340       350       360
                    ....*....|....*....|....*....|....*....|...
gi 530425792    323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129  293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335

Kinesin

pfam00225

Kinesin motor domain;

9-358

4.97e-148

Kinesin motor domain;

Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 459.73 E-value: 4.97e-148

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792     9 RVRPMNRREKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVK 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    89 SAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:pfam00225   68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKN 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   169 TFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPCE-TVSK 247
Cdd:pfam00225  146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   248 IHLVDLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKDSLGGN 326
Cdd:pfam00225  226 LNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGN 294

                          330       340       350
                   ....*....|....*....|....*....|..
gi 530425792   327 SKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:pfam00225  295 SKTLMIANISPSSSNYEETLSTLRFASRAKNI 326

KISc

cd00106

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...

3-356

7.48e-139

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

Pssm-ID: 276812 [Multi-domain] Cd Length: 326 Bit Score: 434.38 E-value: 7.48e-139

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTgdsgrertKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:cd00106     1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPP--------KTFAFDAVFDSTST-------QEEVYEGT 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS-GLIPRICEGLFSRINETtRWDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd00106    66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPEQrGIIPRALEDIFERIDKR-KETKSSFSVSASYLEIYNEKIYDL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  162 LRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMP 241
Cdd:cd00106   145 LSPVPKK--PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKD 321
Cdd:cd00106   223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----------GQNKHIPYRDSKLTRLLQD 291

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 530425792  322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd00106   292 SLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326

KISc_KIF3

cd01371

Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...

3-358

2.84e-118

Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 377.19 E-value: 2.84e-118

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnLKIPEGGTGdsgrERTKTFTYDfSFYSADTKspdyvsQEMVFKTL 82
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVS-VRNPKATAN----EPPKTFTFD-AVFDPNSK------QLDVYDET 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVR 159
Cdd:cd01371    70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQ--NNQQFLVRVSYLEIYNEEIR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  160 DLLRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF--D 237
Cdd:cd01371   148 DLLGKDQTK--RLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeD 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  238 SEMPCeTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTW 317
Cdd:cd01371   226 GENHI-RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----------GKSTHIPYRDSKLTR 293

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 530425792  318 LLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01371   294 LLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334

KISc_KIF4

cd01372

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...

3-358

3.85e-114

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

Pssm-ID: 276823 [Multi-domain] Cd Length: 341 Bit Score: 365.89 E-value: 3.85e-114

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkipeggtgdsgRERTKTFTYDFSFysaDTKSPdyvsQEMVFKTL 82
Cdd:cd01372     2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVT-------------VGTDKSFTFDYVF---DPSTE----QEEVYNTC 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS------GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01372    62 VAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAEedeeqvGIIPRAIQHIFKKIEKKK--DTFEFQLKVSFLEIYNE 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  157 RVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF 236
Cdd:cd01372   140 EIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKK 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  237 DSEMPC--------ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAntlakkkqvFV 308
Cdd:cd01372   220 NGPIAPmsaddknsTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGA---------HV 290

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 530425792  309 PYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01372   291 PYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340

KISc_KIP3_like

cd01370

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...

3-358

1.39e-104

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 338.94 E-value: 1.39e-104

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    3 SVKVAVRVRPMNRREKDLEAKFIIQ-MEKS------KTTITNLKIPEGGTGDSGRERTKTFTYDFsfysaDTKSPDYVSQ 75
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGFRRIVKvMDNHmlvfdpKDEEDGFFHGGSNNRDRRKRRNKELKYVF-----DRVFDETSTQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   76 EMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYN 155
Cdd:cd01370    76 EEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK--DEKEFEVSMSYLEIYN 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  156 ERVRDLLRrKSSKTfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ-A 234
Cdd:cd01370   154 ETIRDLLN-PSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQqD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  235 KFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLsqdaantlaKKKQVFVPYRDSV 314
Cdd:cd01370   231 KTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADP---------GKKNKHIPYRDSK 301

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 530425792  315 LTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01370   302 LTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345

KISc_CENP_E

cd01374

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...

3-358

4.55e-102

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

Pssm-ID: 276825 [Multi-domain] Cd Length: 321 Bit Score: 330.45 E-value: 4.55e-102

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    3 SVKVAVRVRPMNRREKDLEAKFIiqMEKSKTTITNLKIPEGgtgdsgrertkTFTYDFSFysaDTKSPDYVsqemVFKTL 82
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVA--WEIDNDTIYLVEPPST-----------SFTFDHVF---GGDSTNRE----VYELI 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWDeasFRTEVSYLEIYNERVRDLL 162
Cdd:cd01374    61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDRE---FLLRVSYLEIYNEKINDLL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  163 rrkSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIK-FTQAKFDSEMP 241
Cdd:cd01374   138 ---SPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITiESSERGELEEG 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKD 321
Cdd:cd01374   215 TVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----------GKVGGHIPYRDSKLTRILQP 284

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 530425792  322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01374   285 SLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321

KISc_KLP2_like

cd01373

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...

4-367

1.10e-101

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

Pssm-ID: 276824 [Multi-domain] Cd Length: 347 Bit Score: 330.62 E-value: 1.10e-101

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    4 VKVAVRVRPMNRREKDLEAKFIIQMEkSKTTITNLKIPEggtgdsgrertKTFTYDfSFYSADTkspdyvSQEMVFKTLG 83
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKL-SSDTLVLHSKPP-----------KTFTFD-HVADSNT------NQESVFQSVG 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNS--------GDSGLIPRICEGLFSRIN--ETTRWDEASFRTEVSYLEI 153
Cdd:cd01373    64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSesdnesphGLRGVIPRIFEYLFSLIQreKEKAGEGKSFLCKCSFLEI 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  154 YNERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ 233
Cdd:cd01373   144 YNEQIYDLLDPASR---NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  234 AKFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDaantlakkKQVFVPYRDS 313
Cdd:cd01373   221 WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDS 292

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530425792  314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01373   293 KLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346

KISc_KHC_KIF5

cd01369

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...

1-358

2.27e-99

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 323.13 E-value: 2.27e-99

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    1 MASVKVAVRVRPMNRREKDLEAKFIIqmekskttitnlKIPEGGTGD-SGRERTKTFTYDFSFYsADTkspdyvSQEMVF 79
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIV------------KFDPEDTVViATSETGKTFSFDRVFD-PNT------TQEDVY 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   80 KTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01369    62 NFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMD--ENLEFHVKVSYFEIYME 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  157 RVRDLLrrKSSKTfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAkf 236
Cdd:cd01369   140 KIRDLL--DVSKT-NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE-- 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  237 DSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLT 316
Cdd:cd01369   215 NVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----------GKKTHIPYRDSKLT 283

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 530425792  317 WLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01369   284 RILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325

KISc_C_terminal

cd01366

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...

9-360

1.74e-98

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

Pssm-ID: 276817 [Multi-domain] Cd Length: 329 Bit Score: 320.70 E-value: 1.74e-98

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    9 RVRPMNRREKDLEAKFI-IQMEKSKTTITNlkipeggtgdSGRERTKTFTYDFSFysadtkSPDyVSQEMVFKTLGTdVV 87
Cdd:cd01366     9 RVRPLLPSEENEDTSHItFPDEDGQTIELT----------SIGAKQKEFSFDKVF------DPE-ASQEDVFEEVSP-LV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   88 KSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINE--TTRWdeaSFRTEVSYLEIYNERVRDLLRRK 165
Cdd:cd01366    71 QSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElkEKGW---SYTIKASMLEIYNETIRDLLAPG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  166 SSKTFNLRVREHPKEGP-YVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKF------TQAKfds 238
Cdd:cd01366   148 NAPQKKLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnlqTGEI--- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  239 empceTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaantlakKKQVFVPYRDSVLTWL 318
Cdd:cd01366   225 -----SVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYL 287

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 530425792  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIIN 360
Cdd:cd01366   288 LQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329

KISc_BimC_Eg5

cd01364

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...

1-367

2.50e-89

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

Pssm-ID: 276815 [Multi-domain] Cd Length: 353 Bit Score: 295.39 E-value: 2.50e-89

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    1 MASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkIPEGGTGDSGRerTKTFTYDFSFYSAdtkspdyVSQEMVFK 80
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVS---VRTGGLADKSS--TKTYTFDMVFGPE-------AKQIDVYR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   81 TLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN-----------SGDSGLIPRICEGLFSRINETtrwdEASFRTEVS 149
Cdd:cd01364    69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwelDPLAGIIPRTLHQLFEKLEDN----GTEYSVKVS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  150 YLEIYNERVRDLLRRKSSKTFNLRVREHP--KEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:cd01364   145 YLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  228 TIKFTQAKFDSEMpcETV---SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakkK 304
Cdd:cd01364   225 SITIHIKETTIDG--EELvkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------------R 290

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530425792  305 QVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01364   291 APHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353

KIP1

COG5059

Kinesin-like protein [Cytoskeleton];

27-508

9.51e-85

Kinesin-like protein [Cytoskeleton];

Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 290.10 E-value: 9.51e-85

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   27 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 95
Cdd:COG5059    18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   96 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 175
Cdd:COG5059    91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  176 EHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDSEMPCETVSKIHLVDLAG 255
Cdd:COG5059   166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  256 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 335
Cdd:COG5059   244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  336 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQ--------------- 392
Cdd:COG5059   314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSqsslsgifaymqslk 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  393 --IALLDSPTALSMEEKLQQNEARVQEL-TKEWTNKwnETQNILKEQTLALrkegiGVVLDSELPHLIGIDDDLLSTGII 469
Cdd:COG5059   394 keTETLKSRIDLIMKSIISGTFERKKLLkEEGWKYK--STLQFLRIEIDRL-----LLLREEELSKKKTKIHKLNKLRHD 466

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 530425792  470 LYHLKEGQT-----YVGRDDASTEQDIVLHGLDLES--EHCIFENI 508
Cdd:COG5059   467 LSSLLSSIPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRDH 512

FHA_KIF16B

cd22732

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...

446-562

6.90e-79

Pssm-ID: 438784 [Multi-domain] Cd Length: 117 Bit Score: 255.63 E-value: 6.90e-79

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22732     1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 530425792  526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732    81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117

PLN03188

kinesin-12 family protein; Provisional

4-392

1.83e-74

kinesin-12 family protein; Provisional

Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 274.12 E-value: 1.83e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    4 VKVAVRVRPMNrreKDLEAKFIIQ-MEKSKTTITNlkipeggtgdsgrertKTFTYDfsfYSADTKSpdyvSQEMVFKTL 82
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQkMSNDSLTING----------------QTFTFD---SIADPES----TQEDIFQLV 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEGLFSRINE-----TTRwdEASFRTE 147
Cdd:PLN03188  154 GAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCR 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  148 VSYLEIYNERVRDLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:PLN03188  232 CSFLEIYNEQITDLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVF 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  228 TIKFtqakfdsEMPCETV---------SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAan 298
Cdd:PLN03188  309 TCVV-------ESRCKSVadglssfktSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-- 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  299 tlakkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KL 372
Cdd:PLN03188  380 -----KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEV 454

                         410       420
                  ....*....|....*....|
gi 530425792  373 IRELRAEIARLKtllAQGNQ 392
Cdd:PLN03188  455 IRQLRDELQRVK---ANGNN 471

KISc_KIF23_like

cd01368

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...

4-356

5.71e-73

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 248.08 E-value: 5.71e-73

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSkTTITnLKIPEGGTGDSGRERTKTFTYDFSFYSadTKSPDYvSQEMVFKTLG 83
Cdd:cd01368     3 VKVYLRVRPLSKDELESEDEGCIEVINS-TTVV-LHPPKGSAANKSERNGGQKETKFSFSK--VFGPNT-TQKEFFQGTA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWdeasfrteVSYLEIYNERVRDLLR 163
Cdd:cd01368    78 LPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGGYSVF--------VSYIEIYNEYIYDLLE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  164 RKSSKTF----NLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE 239
Cdd:cd01368   150 PSPSSPTkkrqSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  240 MPCE------TVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaaNTLAKKKQVfVPYRDS 313
Cdd:cd01368   230 GDVDqdkdqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE------NQLQGTNKM-VPFRDS 302

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 530425792  314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01368   303 KLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345

KISc_KIF9_like

cd01375

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...

3-356

4.33e-72

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 245.18 E-value: 4.33e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    3 SVKVAVRVRPMNRrekdlEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTK-TFTYDFSFYSAdtkspdyvSQEMVFKT 81
Cdd:cd01375     1 KVQAFVRVRPTDD-----FAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDwSFKFDGVLHNA--------SQELVYET 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG---NSGDSGLIPRICEGLFSRINEttRWDEAsFRTEVSYLEIYNERV 158
Cdd:cd01375    68 VAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEE--RPTKA-YTVHVSYLEIYNEQL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  159 RDLL--RRKSSKTFN-LRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAK 235
Cdd:cd01375   145 YDLLstLPYVGPSVTpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHS 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  236 FDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVL 315
Cdd:cd01375   225 RTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----------KDRTHVPFRQSKL 293

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 530425792  316 TWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01375   294 THVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334

KISc_KID_like

cd01376

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...

4-356

3.08e-68

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

Pssm-ID: 276827 [Multi-domain] Cd Length: 319 Bit Score: 233.16 E-value: 3.08e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTItnLKIPeggtgdsgRERTKTFTYDF-SFYSADTkspdyvSQEMVFKTL 82
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVE--LADP--------RNHGETLKYQFdAFYGEES------TQEDIYARE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFsRINETTRWdeaSFRTEVSYLEIYNERVRDLL 162
Cdd:cd01376    66 VQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-QMTRKEAW---ALSFTMSYLEIYQEKILDLL 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  163 RRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:cd01376   142 EPASK---ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQ 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  243 ETvSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALadlsqdaantlaKKKQVFVPYRDSVLTWLLKDS 322
Cdd:cd01376   219 RT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------------NKNLPRIPYRDSKLTRLLQDS 285

                         330       340       350
                  ....*....|....*....|....*....|....
gi 530425792  323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01376   286 LGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319

KISc_KIF2_like

cd01367

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...

4-356

4.16e-68

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

Pssm-ID: 276818 [Multi-domain] Cd Length: 328 Bit Score: 233.34 E-value: 4.16e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLkipeggtgdsgrERTK----------TFTYDFSFYSAdtkspdyV 73
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHE------------PKLKvdltkyienhTFRFDYVFDES-------S 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   74 SQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEG----LFSRINETTRWDEasFRTEVS 149
Cdd:cd01367    63 SNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALaardVFRLLNKLPYKDN--LGVTVS 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  150 YLEIYNERVRDLLRRKSSktfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTI 229
Cdd:cd01367   141 FFEIYGGKVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  230 KFTQAKFDsempcETVSKIHLVDLAGSER-ADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaantlakKKQVFV 308
Cdd:cd01367   217 ILRDRGTN-----KLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG------------QNKAHI 279

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 530425792  309 PYRDSVLTWLLKDSL-GGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01367   280 PFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328

FHA_KIF16

cd22708

forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...

446-554

5.17e-65

forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438760 [Multi-domain] Cd Length: 109 Bit Score: 215.60 E-value: 5.17e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22708     1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80

                          90       100
                  ....*....|....*....|....*....
gi 530425792  526 GVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22708    81 GQVITQPTRLTQGDVILLGKTNMFRFNHP 109

FHA_KIF16A_STARD9

cd22731

forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...

446-564

3.73e-49

forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438783 [Multi-domain] Cd Length: 119 Bit Score: 170.73 E-value: 3.73e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22731     1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 530425792  526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22731    81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQRR 119

FHA_PHLB1

cd22713

forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...

438-561

2.53e-34

forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438765 Cd Length: 120 Bit Score: 128.21 E-value: 2.53e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  438 LALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTeqdIVLHGLDLESEHCIFENIGGTVTLIPL 517
Cdd:cd22713     1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDI---ISLQGPGVEPEHCYIENINGTVTLYPC 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 530425792  518 sGSQCSVNGVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLR 561
Cdd:cd22713    78 -GNLCSVDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120

FHA_KIF1

cd22705

forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...

453-553

9.50e-32

forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438757 [Multi-domain] Cd Length: 101 Bit Score: 120.03 E-value: 9.50e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  453 LPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQIVEA 532
Cdd:cd22705     1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80

                          90       100
                  ....*....|....*....|.
gi 530425792  533 THLNQGAVILLGRTNMFRFNH 553
Cdd:cd22705    81 TRLKTGSRVILGKNHVFRFNH 101

FHA_KIF14

cd22707

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...

450-554

1.15e-26

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438759 [Multi-domain] Cd Length: 108 Bit Score: 105.81 E-value: 1.15e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  450 DSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQI 529
Cdd:cd22707     4 DNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGELI 83

                          90       100
                  ....*....|....*....|....*
gi 530425792  530 VEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22707    84 SEPTVLHHGDRVILGGDHYFRFNHP 108

FHA_KIF1A

cd22726

forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...

454-562

3.83e-26

forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438778 [Multi-domain] Cd Length: 115 Bit Score: 104.63 E-value: 3.83e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGT-----VTLIPLSGSQCSVNGVQ 528
Cdd:cd22726     2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 530425792  529 IVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22726    82 VTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 115

FHA_KIF1B

cd22727

forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...

454-556

2.07e-25

forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438779 [Multi-domain] Cd Length: 110 Bit Score: 102.42 E-value: 2.07e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIF-----ENIGGTVTLIPLSGSQCSVNGVQ 528
Cdd:cd22727     3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrsernNNGEVIVTLEPCERSETYVNGKR 82

                          90       100
                  ....*....|....*....|....*...
gi 530425792  529 IVEATHLNQGAVILLGRTNMFRFNHPKE 556
Cdd:cd22727    83 VVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110

FHA_KIF28P

cd22709

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...

454-554

3.53e-25

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438761 [Multi-domain] Cd Length: 102 Bit Score: 101.52 E-value: 3.53e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLS-GSQCSVNGVQIVEA 532
Cdd:cd22709     1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTGE 80

                          90       100
                  ....*....|....*....|..
gi 530425792  533 THLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22709    81 TELHHLDRVILGSNHLYVFVGP 102

Motor_domain

cd01363

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

6-288

7.63e-24

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: 100.11 E-value: 7.63e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    6 VAVRVRPMNRREkdleakfIIQMEKSKTTitnlkipeggtgDSGRERtktftydfsfysadtkspdYVSQEMVFKTLGtD 85
Cdd:cd01363     1 VLVRVNPFKELP-------IYRDSKIIVF------------YRGFRR-------------------SESQPHVFAIAD-P 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   86 VVKSAFEGYN-ACVFAYGQTGSGKSYTMMgnsgdsGLIPRICEGLFSRIN--ETTRWDEASFRTevsyleiynervrdll 162
Cdd:cd01363    42 AYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVAFNGINkgETEGWVYLTEIT---------------- 99

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  163 rrkssktfnlrvrehpkegpyvedlskhlVQNYGDVEELMDAGNINRtTAATGMNDVSSRSHAIFTIkftqakfdsempc 242
Cdd:cd01363   100 -----------------------------VTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------- 136

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 530425792  243 etvskihLVDLAGSERadatgatgvrlkeggnINKSLVTLGNVISA 288
Cdd:cd01363   137 -------LLDIAGFEI----------------INESLNTLMNVLRA 159

FHA_KIF13

cd22706

forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...

471-554

2.36e-20

forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438758 [Multi-domain] Cd Length: 101 Bit Score: 87.73 E-value: 2.36e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  471 YHLKEgQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQIVEATHLNQGAVILLGRTNMFR 550
Cdd:cd22706    19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97


                  ....
gi 530425792  551 FNHP 554
Cdd:cd22706    98 LNCP 101

FHA_KIF1C

cd22728

forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...

454-553

3.08e-18

forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438780 [Multi-domain] Cd Length: 102 Bit Score: 81.84 E-value: 3.08e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDAsteqDIVLHGLDLESEHCIFENIGG-----TVTLIPLSGSQCSVNGVQ 528
Cdd:cd22728     2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFRSIPNpsgevVVTLEPCEGAETYVNGKQ 77

                          90       100
                  ....*....|....*....|....*
gi 530425792  529 IVEATHLNQGAVILLGRTNMFRFNH 553
Cdd:cd22728    78 VTEPLVLKSGNRIVMGKNHVFRFNH 102

Smc

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

606-1089

1.55e-17

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 1.55e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  606 RLEFERQQREELE-KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:COG1196   303 DIARLEERRRELEeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  685 AEKEKFEEERLReqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEE 764
Cdd:COG1196   383 ELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  765 QEKEQVMLVAHLEEQLREKQEMIQLLR-RGEVQWVEEEKRDLEGIRESLLR-VKEARAGGDEDGEELEKAQLRFFEFKRR 842
Cdd:COG1196   458 EEALLELLAELLEEAALLEAALAELLEeLAEAAARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYE 537

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  843 QLV----------KLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDfekikPVEYR 912
Cdd:COG1196   538 AALeaalaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD-----LREAD 612

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  913 LQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLdnTLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeftANIAR 992
Cdd:COG1196   613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV--TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL----EELAE 686

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  993 QEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLAslnsgsrEQSGLQASLEAEQEALE 1072
Cdd:COG1196   687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL-------EEEELLEEEALEELPEP 759

                         490
                  ....*....|....*..
gi 530425792 1073 KDQERLEYEIQQLKQKI 1089
Cdd:COG1196   760 PDLEELERELERLEREI 776

Smc

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

611-1088

9.39e-17

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.91 E-value: 9.39e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  611 RQQREELEKLESKRKL--IEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLlaeke 688
Cdd:COG1196   216 RELKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE----- 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  689 kfeeerlreqqeielqkkRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKE 768
Cdd:COG1196   291 ------------------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  769 QVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESL-LRVKEARAGGDEDGEELEKAQLRffEFKRRQLVKL 847
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAeLAAQLEELEEAEEALLERLERLE--EELEELEEAL 430

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  848 VNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNH 927
Cdd:COG1196   431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  928 LPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQ---------LAQYQANANQLQKLQATFEFTANIARQEEKVR 998
Cdd:COG1196   511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnivveddevAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  999 KKEKEI--------------LESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASL 1064
Cdd:COG1196   591 ALARGAigaavdlvasdlreADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670

                         490       500
                  ....*....|....*....|....
gi 530425792 1065 EAEQEALEKDQERLEYEIQQLKQK 1088
Cdd:COG1196   671 LAALLEAEAELEELAERLAEEELE 694

Microtub_bd

pfam16796

Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...

3-162

2.01e-15

Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.

Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 74.95 E-value: 2.01e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792     3 SVKVAVRVRPMNRREkdleakfiIQMEKSKTTITNLKIpeggtgdsgRERTKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:pfam16796   21 NIRVFARVRPELLSE--------AQIDYPDETSSDGKI---------GSKNKSFSFDRVFPPESE-------QEDVFQEI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792    83 GTdVVKSAFEGYNACVFAYGQTGSGksytmmgnsGDSGLIPRICEGLFSRINETTRwdEASFRTEVSYLEIYNERVRDLL 162
Cdd:pfam16796   77 SQ-LVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKK--GWKYTIELQFVEIYNESSQDLL 144

FHA_AFDN

cd22711

forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...

453-554

8.43e-15

forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438763 [Multi-domain] Cd Length: 106 Bit Score: 71.97 E-value: 8.43e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  453 LPHLI-----GIDDDLLstgiILYHLKEGQTYVG--RDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSG-SQCSV 524
Cdd:cd22711     1 LPYLLelspdGSDRDKP----RRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYV 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 530425792  525 NGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22711    77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106

DUF5401

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

624-937

1.37e-14

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: 79.40 E-value: 1.37e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   624 RKLIEEMEEKQKSDKAELERMQQEVETQRKETEivqlQIRKQEESLKRRSFHIEnKLKDLLAEKEKFEEERLReqqeiEL 703
Cdd:pfam17380  281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERER-----EL 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   704 QKKRQEEEtflrvQEELQRLKElnnNEKAEKFQIFQELDQLQKEKDEQYAKL--ELEKKR----LEEQEKEQVMLVAHLE 777
Cdd:pfam17380  351 ERIRQEER-----KRELERIRQ---EEIAMEISRMRELERLQMERQQKNERVrqELEAARkvkiLEEERQRKIQQQKVEM 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   778 EQLREKQEMIqllRRGEVQWVEEEK-RDLEGIREsllrvkearaggdedgEELEKAQ----LRFFEFKRRQlvKLVNLEK 852
Cdd:pfam17380  423 EQIRAEQEEA---RQREVRRLEEERaREMERVRL----------------EEQERQQqverLRQQEEERKR--KKLELEK 481

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   853 DLVQQKD-------ILKKEVQEEQEILeclkCEHDKESRLLEKHDESVTdvTEVPQDFEKIKPVEYRLQYKERQLQYLLQ 925
Cdd:pfam17380  482 EKRDRKRaeeqrrkILEKELEERKQAM----IEEERKRKLLEKEMEERQ--KAIYEEERRREAEEERRKQQEMEERRRIQ 555

                          330
                   ....*....|..
gi 530425792   926 NHLPTLLEEKQR 937
Cdd:pfam17380  556 EQMRKATEERSR 567

PTZ00121

MAEBL; Provisional

610-902

5.84e-14

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.87 E-value: 5.84e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  610 ERQQREELEKLESKRKLIE--EMEEKQKSD---KAELERMQQE---VETQRKETEIVQLQIRKQEESLKRRSFHIENKLK 681
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEakKAEEKKKADelkKAEELKKAEEkkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  682 dLLAEKEKFEEerlreqqeiELQKKRQEE----ETFLRVQEELQRLKELNNNEKAEKfqifQELDQLQKEKDEQYAKLEL 757
Cdd:PTZ00121 1600 -LYEEEKKMKA---------EEAKKAEEAkikaEELKKAEEEKKKVEQLKKKEAEEK----KKAEELKKAEEENKIKAAE 1665

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  758 EKKRlEEQEKEQVMLVAHLEEQLREKQEmiQLLRRGE--------VQWVEEEKRDLEGIR----ESLLRVKEARAGGDED 825
Cdd:PTZ00121 1666 EAKK-AEEDKKKAEEAKKAEEDEKKAAE--ALKKEAEeakkaeelKKKEAEEKKKAEELKkaeeENKIKAEEAKKEAEED 1742

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530425792  826 GEELEKAQLRFFEFKrrqlvKLVNLEKDLVQQKDILKKEvqEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQD 902
Cdd:PTZ00121 1743 KKKAEEAKKDEEEKK-----KIAHLKKEEEKKAEEIRKE--KEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812

DUF5401

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

610-919

3.31e-13

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: 75.16 E-value: 3.31e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   610 ERQQREELEKLESKR------KLIEEMEEKQKSDKAELERmQQEVETQ--------------RKETEIVQLQIRKQE-ES 668
Cdd:pfam17380  286 ERQQQEKFEKMEQERlrqekeEKAREVERRRKLEEAEKAR-QAEMDRQaaiyaeqermamerERELERIRQEERKRElER 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   669 LKRRSFHIE-NKLKDLlaEKEKFEEERLREQQEIELQKKR----QEEETFLRVQEELQRLKELNNnEKAEKFQIfqELDQ 743
Cdd:pfam17380  365 IRQEEIAMEiSRMREL--ERLQMERQQKNERVRQELEAARkvkiLEEERQRKIQQQKVEMEQIRA-EQEEARQR--EVRR 439

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   744 LQKEKDEqyaklELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKR-----DLEGIRESLLRVKEA 818
Cdd:pfam17380  440 LEEERAR-----EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkilekELEERKQAMIEEERK 514

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   819 RAGGDEDGEELEKA-----QLRFFEFKRRQLVKLVnlEKDLVQQKdilKKEVQEEQEILECLKCEHDKESRLLEkhDESV 893
Cdd:pfam17380  515 RKLLEKEMEERQKAiyeeeRRREAEEERRKQQEME--ERRRIQEQ---MRKATEERSRLEAMEREREMMRQIVE--SEKA 587

                          330       340
                   ....*....|....*....|....*.
gi 530425792   894 TDVTEVPQDFEKIKPVeYRLQYKERQ 919
Cdd:pfam17380  588 RAEYEATTPITTIKPI-YRPRISEYQ 612

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

614-1147

5.83e-13

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.72 E-value: 5.83e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   614 REELEKLESKrklIEEMEEKQKSDKAELERMQQEVE-TQRKETEIVQLQIRKQEESLKRRS--FHIENKLKDLLAEKEKF 690
Cdd:TIGR02169  363 KEELEDLRAE---LEEVDKEFAETRDELKDYREKLEkLKREINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINEL 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   691 EEERLREQQEIELQkkrqeeetflrvQEELQRLKELNNNEKAEKFQIFQELDQLQKE---KDEQYAKLELEKKRLEEQEK 767
Cdd:TIGR02169  440 EEEKEDKALEIKKQ------------EWKLEQLAADLSKYEQELYDLKEEYDRVEKElskLQRELAEAEAQARASEERVR 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   768 EQVMLVAHLEEQLREKQEMIQLLRRGEVQW----------------VEEEKRDLEGIrESLLRVKEARAG---------- 821
Cdd:TIGR02169  508 GGRAVEEVLKASIQGVHGTVAQLGSVGERYataievaagnrlnnvvVEDDAVAKEAI-ELLKRRKAGRATflplnkmrde 586

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   822 ------GDEDG------------EELEKA---------QLRFFEFKRRQL--VKLVNLEKDLVQQ--------------- 857
Cdd:TIGR02169  587 rrdlsiLSEDGvigfavdlvefdPKYEPAfkyvfgdtlVVEDIEAARRLMgkYRMVTLEGELFEKsgamtggsraprggi 666

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   858 --KDILKKEVQEEQEILECLKCEhdkESRLLEKHDESVTdvtEVPQDFEKIKPVEYRLQYKERQLQYLLQNH--LPTLLE 933
Cdd:TIGR02169  667 lfSRSEPAELQRLRERLEGLKRE---LSSLQSELRRIEN---RLDELSQELSDASRKIGEIEKEIEQLEQEEekLKERLE 740

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   934 EKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQL---------QKLQATFEFTANIARQEEKVRKKEKEI 1004
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsriPEIQAELSKLEEEVSRIEARLREIEQK 820

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  1005 LESREkQQREALERALARLERRHSALQ-RHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQ 1083
Cdd:TIGR02169  821 LNRLT-LEKEYLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530425792  1084 QLKQKIYEV----------DGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDLHRV 1147
Cdd:TIGR02169  900 ELERKIEELeaqiekkrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

613-944

6.14e-13

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.33 E-value: 6.14e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   613 QREELEKLESKRKLIEEMeekqksdKAELERMQQEVEtqRKETEIVQLQIRKQEESlkRRSFHIENKLKDLLAEKEKFEE 692
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGL-------KRELSSLQSELR--RIENRLDELSQELSDAS--RKIGEIEKEIEQLEQEEEKLKE 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   693 ERLREQQEI-ELQKKRQEEETFL-RVQEELQRLKELNNNEKAEKFQIFQELDQLQ-KEKDEQYAKLELEKKRLEE--QEK 767
Cdd:TIGR02169  738 RLEELEEDLsSLEQEIENVKSELkELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEArlREI 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   768 EQVMLVAHLEEQLREK--QEMIQLLRRGEVQWVEEEKR--DLEGIRESLL-RVKEARAGGDEDGEELE---------KAQ 833
Cdd:TIGR02169  818 EQKLNRLTLEKEYLEKeiQELQEQRIDLKEQIKSIEKEieNLNGKKEELEeELEELEAALRDLESRLGdlkkerdelEAQ 897

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   834 LRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRL 913
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLA 977

                          330       340       350
                   ....*....|....*....|....*....|....
gi 530425792   914 --QYKERQLQYL-LQNHLPTLLEEKQrafEILDR 944
Cdd:TIGR02169  978 iqEYEEVLKRLDeLKEKRAKLEEERK---AILER 1008

SMC_prok_B

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

606-905

1.06e-12

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 1.06e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   606 RLEFERQQREELEKLESKRKLIEEMEEkqksdkaELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLA 685
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQKQILRERLAN----LERQLEELEA 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   686 EKEKFEEERLREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQ 765
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEE-----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   766 EKEQVMLVAHLE----EQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARaggdEDGEELEKAQLRFFEFKR 841
Cdd:TIGR02168  399 NNEIERLEARLErledRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL----ERLEEALEELREELEEAE 474

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530425792   842 RQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRlLEKHDESVTDVTEVPQDFEK 905
Cdd:TIGR02168  475 QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG-LSGILGVLSELISVDEGYEA 537

FHA_KIF13A

cd22729

forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...

456-564

1.64e-12

forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438781 [Multi-domain] Cd Length: 109 Bit Score: 65.68 E-value: 1.64e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  456 LIGIDDDLLSTGIILYHLKeGQTYVGRDdasTEQDIVLHGLDLESEHCIFE-NIGGTVTLIPLSGSQCSVNGVQIVEATH 534
Cdd:cd22729     4 LVNLNADPALNELLVYYLK-DHTRVGAD---TSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 530425792  535 LNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22729    80 LWHGDRILWGNNHFFRINLPKRKRRDWLKE 109

PRK03918

DNA double-strand break repair ATPase Rad50;

611-1109

1.77e-12

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 1.77e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  611 RQQREELEKLESKRKLIEEMEEKQKS----------DKAELERMQQEVETQRKETEIVQLQIrKQEESLKRRSFHIENKL 680
Cdd:PRK03918  269 EELKKEIEELEEKVKELKELKEKAEEyiklsefyeeYLDELREIEKRLSRLEEEINGIEERI-KELEEKEERLEELKKKL 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  681 KDLLAEKEkfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKfqIFQELDQLQKEKDEQYAKLELEKK 760
Cdd:PRK03918  348 KELEKRLE-------------ELEERHELYEEAKAKKEELERLKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITA 412

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  761 RLEEQEKEQVMLVAHLEEqLREKQEMIQLLRRgevQWVEEEKRDLegIRESLLRVKEARAGGDEDGEELEKAQLRFfefk 840
Cdd:PRK03918  413 RIGELKKEIKELKKAIEE-LKKAKGKCPVCGR---ELTEEHRKEL--LEEYTAELKRIEKELKEIEEKERKLRKEL---- 482

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  841 rRQLVKLVNLEKDLVQQKDILK--KEVQEEQEILECLKCEHDKE--SRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYK 916
Cdd:PRK03918  483 -RELEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL 561

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  917 ERQLQYL---LQNHLPTLLEEKQRAFEILDRGPLSLDnTLYQVEKEMEEKEEQLaqyQANANQLQKLQATFEFT-ANIAR 992
Cdd:PRK03918  562 EKKLDELeeeLAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKEL---EREEKELKKLEEELDKAfEELAE 637

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  993 QEEKVRKKEKEILESREK---QQREALERALARLERRHSALQRHSTlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQE 1069
Cdd:PRK03918  638 TEKRLEELRKELEELEKKyseEEYEELREEYLELSRELAGLRAELE---ELEKRREEIKKTLEKLKEELEEREKAKKELE 714

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 530425792 1070 ALEKDQERLEyeiqQLKQKIYEVDGVQKDHHGTLEGKVAS 1109
Cdd:PRK03918  715 KLEKALERVE----ELREKVKKYKALLKERALSKVGEIAS 750

PRK03918

DNA double-strand break repair ATPase Rad50;

702-1181

4.51e-12

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.63 E-value: 4.51e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  702 ELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEqekeqvmlvahLEEQLR 781
Cdd:PRK03918  173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-----------LKEEIE 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  782 EKQEMIqLLRRGEVQWVEEEKRDLE-GIRESLLRVK--EARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQK 858
Cdd:PRK03918  242 ELEKEL-ESLEGSKRKLEEKIRELEeRIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  859 DILkKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQ-YKERQLQYllqnhlptLLEEKQR 937
Cdd:PRK03918  321 EEI-NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELErLKKRLTGL--------TPEKLEK 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  938 AFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQA---------TFEFTANIARQEEKVRKKEKEILESR 1008
Cdd:PRK03918  392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEI 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792 1009 EKQQREaLERALARLER---RHSALQRHSTLGMEIEEQRQKLASLN-----SGSREQSGLQ---ASLEAEQEALEKDQER 1077
Cdd:PRK03918  472 EEKERK-LRKELRELEKvlkKESELIKLKELAEQLKELEEKLKKYNleeleKKAEEYEKLKeklIKLKGEIKSLKKELEK 550

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792 1078 ---LEYEIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMdariNAYIE--------EEVQRRLQDLHR 1146
Cdd:PRK03918  551 leeLKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY----NEYLElkdaekelEREEKELKKLEE 626

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 530425792 1147 VISEGCSTSADTMKDNEKLHNGTIQRKLKYEKRQF 1181
Cdd:PRK03918  627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEY 661

YhaN

COG4717

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

605-1091

5.06e-12

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 5.06e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  605 LRLEFERQQREELEKLESKRKlieemeEKQKSDKAELERMQQEVETQRKETEIVQlQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:COG4717    43 IRAMLLERLEKEADELFKPQG------RKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELR 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  685 AEKEKFEEERLREQQEIELQKKRQEEETF-LRVQEELQRLKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELEK---- 759
Cdd:COG4717   116 EELEKLEKLLQLLPLYQELEALEAELAELpERLEELEERLEELRELEEELE-ELEAELAELQEELEELLEQLSLATeeel 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  760 KRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIR-----ESLLRVKEARAGGDEDGEELEKAQL 834
Cdd:COG4717   195 QDLAEELEELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEErlkeaRLLLLIAAALLALLGLGGSLLSLIL 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  835 RFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKH----DESVTDVTEVPQDFEKIKPVE 910
Cdd:COG4717   274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEELQELL 353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  911 YRLQYKERQLQyllqnhlptLLEEKQRAFEILDRGPLSLDNTLYQvekemeeKEEQLAQYQANANQLQKLQATFEftani 990
Cdd:COG4717   354 REAEELEEELQ---------LEELEQEIAALLAEAGVEDEEELRA-------ALEQAEEYQELKEELEELEEQLE----- 412

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  991 arqeekvrKKEKEILESREKQQREALERALARLERRHSALQRhstlgmEIEEQRQKLaslnsgsreqsglqASLEAEQEA 1070
Cdd:COG4717   413 --------ELLGELEELLEALDEEELEEELEELEEELEELEE------ELEELREEL--------------AELEAELEQ 464

                         490       500
                  ....*....|....*....|...
gi 530425792 1071 LEKDQE--RLEYEIQQLKQKIYE 1091
Cdd:COG4717   465 LEEDGElaELLQELEELKAELRE 487

SMC_N

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

605-946

5.39e-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: 71.54 E-value: 5.39e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   605 LRLEFERQQREELEKLESK-----RKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENK 679
Cdd:pfam02463  163 AGSRLKRKKKEALKKLIEEtenlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   680 LKDLLAEKEKFEEErlreQQEIELQKKRQEEETFL-----RVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAK 754
Cdd:pfam02463  243 QELLRDEQEEIESS----KQEIEKEEEKLAQVLKEnkeeeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   755 LELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQL 834
Cdd:pfam02463  319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   835 RFFEFKRRQLVKLVNLEKDLVQQKDILKKE--VQEEQEILECLKCEHDKESRLLEKHDESVTDVTEvpQDFEKIKPVEYR 912
Cdd:pfam02463  399 LKSEEEKEAQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDE--LELKKSEDLLKE 476

                          330       340       350
                   ....*....|....*....|....*....|....
gi 530425792   913 LQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGP 946
Cdd:pfam02463  477 TQLVKLQEQLELLLSRQKLEERSQKESKARSGLK 510

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

610-870

5.60e-12

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

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 69.18 E-value: 5.60e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQI--RKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:pfam13868   30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIeeREQKRQEEYEEKLQEREQMDEIVER 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   688 EKFEEERLREQQEIELQKKRQEEETFLRVQE---ELQRLKELNNNEKAEKFqifqeldqlQKEKDEQYAKLELEKKRL-E 763
Cdd:pfam13868  110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAewkELEKEEEREEDERILEY---------LKEKAEREEEREAEREEIeE 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   764 EQEKEQVMLVAHLEEQLREKQEMIQLLRRG-----EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLR--- 835
Cdd:pfam13868  181 EKEREIARLRAQQEKAQDEKAERDELRAKLyqeeqERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEree 260

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 530425792   836 -FFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQE 870
Cdd:pfam13868  261 eEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELE 296

Smc

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

610-1030

8.49e-12

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 8.49e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  690 FEEERLREQQEIE--LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 767
Cdd:COG1196   419 LEEELEELEEALAelEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  768 EQVM--------LVAHLEEQLREKQEMIQLLRRGE---------------VQWVEEEKRDLEGIRESLLRVKEARAGGdE 824
Cdd:COG1196   499 AEADyegflegvKAALLLAGLRGLAGAVAVLIGVEaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATF-L 577

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  825 DGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFE 904
Cdd:COG1196   578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  905 kIKPVEYRLQYKERQLQYLLQNHLPTLLEEKQRAFEILDRgplSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATF 984
Cdd:COG1196   658 -AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE---EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 530425792  985 EFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSAL 1030
Cdd:COG1196   734 REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779

PTZ00121

MAEBL; Provisional

606-1248

8.50e-12

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 8.50e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  606 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLA 685
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  686 EKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELnnNEKAEKFQIFQELdqlqKEKDEQYAKLELEKKRLEEQ 765
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA--KKKAEEKKKADEA----KKKAEEAKKADEAKKKAEEA 1456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  766 EKEQvmlvaHLEEQLREKQEMIQLLRRG-EVQWVEEEKRDLEGIR---ESLLRVKEARAGGDE--DGEELEKA-QLRFFE 838
Cdd:PTZ00121 1457 KKAE-----EAKKKAEEAKKADEAKKKAeEAKKADEAKKKAEEAKkkaDEAKKAAEAKKKADEakKAEEAKKAdEAKKAE 1531

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  839 FKRrqlvKLVNLEK-DLVQQKDILKK--EVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQY 915
Cdd:PTZ00121 1532 EAK----KADEAKKaEEKKKADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  916 KERQLQyllqnhlpTLLEEKQRAFEIldrgplsldNTLYQVEKEMEEKEEQLAQYQANANQLQKlqatfeftaniARQEE 995
Cdd:PTZ00121 1608 KAEEAK--------KAEEAKIKAEEL---------KKAEEEKKKVEQLKKKEAEEKKKAEELKK-----------AEEEN 1659

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  996 KVRKKEKEILESREKQQREALERALARLERRHSALQRHstlgmeiEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQ 1075
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-------AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792 1076 ERLEYEIQQLKQKIYEVDGVQKDhhgtlEGKVASSSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDLHRVISEGCSTS 1155
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEEE-----KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792 1156 ADTMKDNEKlhnGTIQrkLKYEKRQFCPAwyldpllPRDATDTSSLIKEERREVDQNDHWDHpmlwSVSGPKTTSSA--S 1233
Cdd:PTZ00121 1808 ANIIEGGKE---GNLV--INDSKEMEDSA-------IKEVADSKNMQLEEADAFEKHKFNKN----NENGEDGNKEAdfN 1871

                         650
                  ....*....|....*
gi 530425792 1234 QERTHQQRDQSSVPE 1248
Cdd:PTZ00121 1872 KEKDLKEDDEEEIEE 1886

Kinesin_assoc

pfam16183

Kinesin-associated;

364-476

1.11e-11

Kinesin-associated;

Pssm-ID: 465047 [Multi-domain] Cd Length: 177 Bit Score: 65.25 E-value: 1.11e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   395 ---LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183   83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162

                          170
                   ....*....|....
gi 530425792   463 LLSTGIILYHLKEG 476
Cdd:pfam16183  163 PLMSECLLYYIKDG 176

PTZ00121

MAEBL; Provisional

555-825

2.76e-11

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 2.76e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  555 KEAAKLREKRKSGLLSSFSLSMTDLSKSREN--LSAVMLYNPGLFPIKGPICLRLEFERQQREELEKLESKRKLIEEMEE 632
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  633 KQKSDKAELERMQQEVEtqrkETEIVQLQIRKQEESLKRrsfhienKLKDLLAEKEKfeeerlreqqeielqkKRQEEET 712
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEE----ENKIKAAEEAKKAEEDKK-------KAEEAKKAEED----------------EKKAAEA 1693

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  713 FLRVQEELQRLKELNNNEKAEKfqifQELDQLQKEKDEQYAKLElEKKRLEEQEKEQVmlvahleEQLR---EKQEMIQL 789
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEK----KKAEELKKAEEENKIKAE-EAKKEAEEDKKKA-------EEAKkdeEEKKKIAH 1761

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 530425792  790 LRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDED 825
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797

SMC_prok_B

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

612-925

4.24e-11

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 4.24e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   612 QQREELEKLESKRKLIE----EMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEN--------- 678
Cdd:TIGR02168  674 ERRREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeriaqls 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   679 -KLKDLLAEKEKFEEERLREQQEIE--LQKKRQEEETFLRVQEELQ----RLKELN---NNEKAEKFQIFQELDQLQKEK 748
Cdd:TIGR02168  754 kELTELEAEIEELEERLEEAEEELAeaEAEIEELEAQIEQLKEELKalreALDELRaelTLLNEEAANLRERLESLERRI 833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   749 DEQYAKLELEKKRLEEQEKEQVML---VAHLEEQLREKQEMIQLL---RRGEVQWVEEEKRDLE----GIRESLLRVKEA 818
Cdd:TIGR02168  834 AATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALlneRASLEEALALLRSELEelseELRELESKRSEL 913

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   819 RAGGDEDGEELEKAQLRffefkrrqlvkLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHdesvtdVTE 898
Cdd:TIGR02168  914 RRELEELREKLAQLELR-----------LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR------LKR 976

                          330       340       350
                   ....*....|....*....|....*....|...
gi 530425792   899 VPQDFEKIKPV------EYRlQYKERqLQYLLQ 925
Cdd:TIGR02168  977 LENKIKELGPVnlaaieEYE-ELKER-YDFLTA 1007

FHA_KIF13B

cd22730

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...

456-554

7.10e-11

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438782 [Multi-domain] Cd Length: 99 Bit Score: 60.70 E-value: 7.10e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  456 LIGIDDDLLSTGIILYHLKEgQTYVGRDDAsteQDIVLHGLDLESEHCIFE-NIGGTVTLIPLSGSQCSVNGVQIVEATH 534
Cdd:cd22730     4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79

                          90       100
                  ....*....|....*....|
gi 530425792  535 LNQGAVILLGRTNMFRFNHP 554
Cdd:cd22730    80 LHHGDRILWGNNHFFRINLP 99

SMC_prok_B

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

706-1087

7.48e-11

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 7.48e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   706 KRQEEETFLR---VQEELQRL----KELNNN--------EKAEKFQ-IFQELDQLQ--------KEKDEQYAKLELEKKR 761
Cdd:TIGR02168  171 KERRKETERKlerTRENLDRLedilNELERQlkslerqaEKAERYKeLKAELRELElallvlrlEELREELEELQEELKE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   762 LEEQEKEqvmlvahLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEaraggdedgeELEKaQLRFFEFKR 841
Cdd:TIGR02168  251 AEEELEE-------LTAELQELEEKLEELRL-EVSELEEEIEELQKELYALANEIS----------RLEQ-QKQILRERL 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   842 RQLV-KLVNLEKDLV---QQKDILKKEVQEEQEILECLKCEHDkesRLLEKHDESVtdvtevpqdfEKIKPVEYRLQYKE 917
Cdd:TIGR02168  312 ANLErQLEELEAQLEeleSKLDELAEELAELEEKLEELKEELE---SLEAELEELE----------AELEELESRLEELE 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   918 RQLQYLlqnhlptlleeKQRAFEILdrgplsldntlyqvekemeekeeqlAQYQANANQLQKLQATFEftaNIARQEEKV 997
Cdd:TIGR02168  379 EQLETL-----------RSKVAQLE-------------------------LQIASLNNEIERLEARLE---RLEDRRERL 419

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   998 RKKEKEILESREKQQREALERALARLER-RHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1076
Cdd:TIGR02168  420 QQEIEELLKKLEEAELKELQAELEELEEeLEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499

                          410
                   ....*....|.
gi 530425792  1077 RLEYEIQQLKQ 1087
Cdd:TIGR02168  500 NLEGFSEGVKA 510

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

612-1098

8.02e-11

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: 67.44 E-value: 8.02e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   612 QQREELEKLESKRKL----IEEMEEKQKSDKAELE----RMQQEVETQRKETEIVQLQIR-----------KQEESLKRR 672
Cdd:pfam05483  265 ESRDKANQLEEKTKLqdenLKELIEKKDHLTKELEdikmSLQRSMSTQKALEEDLQIATKticqlteekeaQMEELNKAK 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   673 SFH--IENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEEtFLRVQEELQRLKELNNNEKAEkfqiFQELDQLQKEKDe 750
Cdd:pfam05483  345 AAHsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME-LQKKSSELEEMTKFKNNKEVE----LEELKKILAEDE- 418

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   751 qyaKLELEKKRLEEqekeqvmlvahLEEQLREK-QEMIQLLrrgevQWVEEEKRDLEgIRESLLRVKEARAGGD--EDGE 827
Cdd:pfam05483  419 ---KLLDEKKQFEK-----------IAEELKGKeQELIFLL-----QAREKEIHDLE-IQLTAIKTSEEHYLKEveDLKT 478

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   828 ELEKAQLRFFEFKRRQlVKLVNLEKDLVQQKDILKKEVQEEQE-ILECLKCEHD--KESRLLEKHDESVTDVTE-VPQDF 903
Cdd:pfam05483  479 ELEKEKLKNIELTAHC-DKLLLENKELTQEASDMTLELKKHQEdIINCKKQEERmlKQIENLEEKEMNLRDELEsVREEF 557

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   904 ---------------EKIKPVEYRLQYKERQLQYLLQ--NHLPTLLEEKQRAFEILDRGPLSLdntlyqvEKEMEEKEEQ 966
Cdd:pfam05483  558 iqkgdevkckldkseENARSIEYEVLKKEKQMKILENkcNNLKKQIENKNKNIEELHQENKAL-------KKKGSAENKQ 630

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   967 LAQYQANANQLQ-KLQATF----EFTANIARQEEKVRKKEKEILESREKQ----------QREALERALARLERRHSALQ 1031
Cdd:pfam05483  631 LNAYEIKVNKLElELASAKqkfeEIIDNYQKEIEDKKISEEKLLEEVEKAkaiadeavklQKEIDKRCQHKIAEMVALME 710

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530425792  1032 RHS-TLGMEIEEQRQKLASLNSGSREQSGLQASLE-------AEQEALEKDQERLEYEIQQLKQKIYEVDGVQKD 1098
Cdd:pfam05483  711 KHKhQYDKIIEERDSELGLYKNKEQEQSSAKAALEielsnikAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

706-1090

8.18e-11

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 8.18e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   706 KRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAK---LELEKKRLEEQEKEQVMLVAHLEEQLRE 782
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeIEKEIEQLEQEEEKLKERLEELEEDLSS 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   783 KQEMIQLLRRgEVQWVEEEKRDLEgirESLLRVKEARAG--GDEDGEELEK--AQLRFFEFKRRQLVKLVN-LEKDL--- 854
Cdd:TIGR02169  749 LEQEIENVKS-ELKELEARIEELE---EDLHKLEEALNDleARLSHSRIPEiqAELSKLEEEVSRIEARLReIEQKLnrl 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   855 VQQKDILKKEVQEEQEILECLKcehDKESRLLEKHDESVTDVtevpqdfEKIKPVEYRLQYKERQLQYLLQNhlptllee 934
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLK---EQIKSIEKEIENLNGKK-------EELEEELEELEAALRDLESRLGD-------- 886

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   935 kqrafeiLDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQ-KLQATFEFTANIARQEEKVRKKEKEILESRE-KQQ 1012
Cdd:TIGR02169  887 -------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKaKLEALEEELSEIEDPKGEDEEIPEEELSLEDvQAE 959

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530425792  1013 REALERALARLERRHSAlqrhstlgmEIEEQRQKLASLNsgsrEQSGLQASLEAEQEALekdQERLEyEIQQLKQKIY 1090
Cdd:TIGR02169  960 LQRVEEEIRALEPVNML---------AIQEYEEVLKRLD----ELKEKRAKLEEERKAI---LERIE-EYEKKKREVF 1020

DUF4670

pfam15709

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...

606-785

9.22e-11

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

Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 66.51 E-value: 9.22e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   606 RLEFERQQREEleklESKRKLIEEMEEKQKSDKAELERMQQevetqrKETEIVQLQIRKQEESLKRRSFHIENKLKDLLA 685
Cdd:pfam15709  347 RLEVERKRREQ----EEQRRLQQEQLERAEKMREELELEQQ------RRFEEIRLRKQRLEEERQRQEEEERKQRLQLQA 416

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   686 EKEKFEEERLREQQEI-ELQKKRQEEETfLRVQEELQRLKELnNNEKAEKFQIFQELD-------QLQKEKDEQYAKLEL 757
Cdd:pfam15709  417 AQERARQQQEEFRRKLqELQRKKQQEEA-ERAEAEKQRQKEL-EMQLAEEQKRLMEMAeeerleyQRQKQEAEEKARLEA 494

                          170       180
                   ....*....|....*....|....*...
gi 530425792   758 EKKRleEQEKEQVMLVahLEEQLREKQE 785
Cdd:pfam15709  495 EERR--QKEEEAARLA--LEEAMKQAQE 518

PRK03918

DNA double-strand break repair ATPase Rad50;

607-1095

9.47e-11

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 9.47e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  607 LEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVetqrKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAE 686
Cdd:PRK03918  168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEKLEKEVKELE-ELKEEIEE 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  687 KEKFEEERLREQQEIElQKKRQEEEtflRVQEELQRLKELNNNEKaekfqifqELDQLqKEKDEQYAKLELE----KKRL 762
Cdd:PRK03918  243 LEKELESLEGSKRKLE-EKIRELEE---RIEELKKEIEELEEKVK--------ELKEL-KEKAEEYIKLSEFyeeyLDEL 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  763 EEQEKEqvmlVAHLEEQLREKQEMIQLL--RRGEVQWVEEE----KRDLEGIRESLLRVKEARAGGDE--------DGEE 828
Cdd:PRK03918  310 REIEKR----LSRLEEEINGIEERIKELeeKEERLEELKKKlkelEKRLEELEERHELYEEAKAKKEElerlkkrlTGLT 385

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  829 LEKAQLRFFEFKRRQLvKLVNLEKDLVQQKDILKKEVQEEQEILECLK-----C--------EHDKEsRLLEKHDESVTD 895
Cdd:PRK03918  386 PEKLEKELEELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEELKkakgkCpvcgreltEEHRK-ELLEEYTAELKR 463

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  896 VTEvpqDFEKIKPVEYRLQYKERQLQYLLQNHlPTLLEEKQRAFEIldrgpLSLDNTLYQVekemeekeeqlaqyqaNAN 975
Cdd:PRK03918  464 IEK---ELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQL-----KELEEKLKKY----------------NLE 518

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  976 QLQKLQATFEFTANIARQEEKVRKKEKEILESRE--KQQREALERALARLERRHSALQRH-STLGME-IEEQRQKLASLN 1051
Cdd:PRK03918  519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELLKElEELGFEsVEELEERLKELE 598

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 530425792 1052 SGSREQSGLQASlEAEQEALEKDQERLEYEIQQLKQKIYEVDGV 1095
Cdd:PRK03918  599 PFYNEYLELKDA-EKELEREEKELKKLEEELDKAFEELAETEKR 641

SMC_prok_B

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

608-927

9.55e-11

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 9.55e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   608 EFERQqreeLEKLESKRKLIEEMEEKqksdKAELERMQQEVETQRKETEIVQL-QIRKQEESLKRRSFHIENKLKDLLAE 686
Cdd:TIGR02168  197 ELERQ----LKSLERQAEKAERYKEL----KAELRELELALLVLRLEELREELeELQEELKEAEEELEELTAELQELEEK 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   687 KEkfeeerlreqqeiELQKKRQE-EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQ 765
Cdd:TIGR02168  269 LE-------------ELRLEVSElEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   766 EKEQVML----------VAHLEEQLREKQEMIQLLRRGEVQW---VEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKA 832
Cdd:TIGR02168  336 AEELAELeekleelkeeLESLEAELEELEAELEELESRLEELeeqLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   833 QLRFFEFKRRQLVKLVNLEKDLVQQkdilkkEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKikpVEYR 912
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAELKELQA------ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER---ELAQ 486

                          330
                   ....*....|....*
gi 530425792   913 LQYKERQLQYLLQNH 927
Cdd:TIGR02168  487 LQARLDSLERLQENL 501

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

606-920

1.30e-10

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.02 E-value: 1.30e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   606 RLEFERQQREELEKLEskrklieemEEKQKSDKAELERMQQEVETQRKeteivqlQIRKQEESLKRrsfHIEnKLKDLLA 685
Cdd:TIGR02169  202 RLRREREKAERYQALL---------KEKREYEGYELLKEKEALERQKE-------AIERQLASLEE---ELE-KLTEEIS 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   686 EKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLK-ELNNNEK--AEKFQIFQELDQLQKEKDEQYAKLELEKKRL 762
Cdd:TIGR02169  262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERsiAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   763 EEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLegiRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRR 842
Cdd:TIGR02169  342 EREIEEERKRRDKLTEEYAELKEELEDLRA-ELEEVDKEFAET---RDELKDYREKLEKLKREINELKRELDRLQEELQR 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   843 QLVKLVNLE---KDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTevpqdfEKIKPVEYRLQYKERQ 919
Cdd:TIGR02169  418 LSEELADLNaaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK------EEYDRVEKELSKLQRE 491


                   .
gi 530425792   920 L 920
Cdd:TIGR02169  492 L 492

YhaN

COG4717

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

611-1083

1.74e-10

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 1.74e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSfhIENKLKDLLAEKEKF 690
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA--LEAELAELPERLEEL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  691 EEERLREQQEIELQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIF----QELDQLQKEKDEQYAKLELEKKRLEEQE 766
Cdd:COG4717   152 EERLEELRELEEELEELEAELA--ELQEELEELLEQLSLATEEELQDLaeelEELQQRLAELEEELEEAQEELEELEEEL 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  767 K--EQVMLVAHLEEQLREKQEMIQLLRRGEVqwveeekrdLEGIRESLLRVKEARAGgdedgeeLEKAQLRFFefkrrQL 844
Cdd:COG4717   230 EqlENELEAAALEERLKEARLLLLIAAALLA---------LLGLGGSLLSLILTIAG-------VLFLVLGLL-----AL 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  845 VKLVNLEKDLVQQKDILKKEVQEEQEILEclkcEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLL 924
Cdd:COG4717   289 LFLLLAREKASLGKEAEELQALPALEELE----EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  925 QNHLptlleEKQRAfEILDRGPLSLDNTLYQvekemeeKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEI 1004
Cdd:COG4717   365 LEEL-----EQEIA-ALLAEAGVEDEEELRA-------ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE 431

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792 1005 LESRE--------KQQREALERALARLERRHSALQRhstlGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1076
Cdd:COG4717   432 EELEEleeeleelEEELEELREELAELEAELEQLEE----DGELAELLQELEELKAELRELAEEWAALKLALELLEEARE 507


                  ....*..
gi 530425792 1077 RLEYEIQ 1083
Cdd:COG4717   508 EYREERL 514

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

623-1042

2.02e-10

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 2.02e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   623 KRKLIEEM-------EEKQKSdKAELErmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAEKEKFeeerl 695
Cdd:TIGR02169  155 RRKIIDEIagvaefdRKKEKA-LEELE----EVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREY----- 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   696 reqqeielqkkrqeeetflrvqEELQRLKELNNNEKaEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEqekeqvmlvah 775
Cdd:TIGR02169  224 ----------------------EGYELLKEKEALER-QKEAIERQLASLEEELEKLTEEISELEKRLEE----------- 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   776 LEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAggdEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLV 855
Cdd:TIGR02169  270 IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEIEELEREIE 346

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   856 QQ---KDILKKEVQEEQEILECLKCEHDKESrllEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLL 932
Cdd:TIGR02169  347 EErkrRDKLTEEYAELKEELEDLRAELEEVD---KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   933 EEKQRAFEILDRgplsldntLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeftaniARQEEKVRKKEKEILESRekqq 1012
Cdd:TIGR02169  424 DLNAAIAGIEAK--------INELEEEKEDKALEIKKQEWKLEQLAADLSK-------YEQELYDLKEEYDRVEKE---- 484

                          410       420       430
                   ....*....|....*....|....*....|
gi 530425792  1013 REALERALARLERRHSALQRHSTLGMEIEE 1042
Cdd:TIGR02169  485 LSKLQRELAEAEAQARASEERVRGGRAVEE 514

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

611-820

1.04e-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: 62.47 E-value: 1.04e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  611 RQQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:COG4942    26 EAELEQLQQeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  690 FEEERlreqqeIELQKKRQEE--------ETFLRVQEELQRLKELNNNEKAEKFQIFQELDQL----------QKEKDEQ 751
Cdd:COG4942   106 LAELL------RALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELaalraeleaeRAELEAL 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425792  752 YAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgevqwveeEKRDLEGIRESLLRVKEARA 820
Cdd:COG4942   180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ--------EAEELEALIARLEAEAAAAA 240

FHA

cd00060

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...

455-551

1.35e-09

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.

Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 56.51 E-value: 1.35e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  455 HLIGIDDDllsTGIILYHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQ-CSVNGVQIVEAT 533
Cdd:cd00060     1 RLIVLDGD---GGGREFPLTKGVVTIGRSPDC---DIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNgTFVNGKRITPPV 74

                          90
                  ....*....|....*...
gi 530425792  534 HLNQGAVILLGRTNmFRF 551
Cdd:cd00060    75 PLQDGDVIRLGDTT-FRF 91

SMC_prok_B

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

753-1089

1.39e-09

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 1.39e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   753 AKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEvqwvEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKA 832
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL----EELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   833 QLRFFEFK---RRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKikpv 909
Cdd:TIGR02168  756 LTELEAEIeelEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER---- 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   910 eyRLQYKERQLQYLLQNhlptlLEEKQRAFEILdrgplsldntlyqvekemeekEEQLAQYQAnanQLQKLQATFEFTAN 989
Cdd:TIGR02168  832 --RIAATERRLEDLEEQ-----IEELSEDIESL---------------------AAEIEELEE---LIEELESELEALLN 880

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   990 IARQEEKVRKKEKEILESREKQQREaLERALARLERRHSALQ-RHSTLGMEIEEQRQKLASLNSGSREQSGLQAS-LEAE 1067
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRE-LESKRSELRRELEELReKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeAEAL 959

                          330       340
                   ....*....|....*....|..
gi 530425792  1068 QEALEKDQERLEYEIQQLKQKI 1089
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKI 981

Smc

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

706-1094

1.76e-09

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.76e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  706 KRQEEETFLR---VQEELQRLK----ELNNN--------EKAEKFQifqELDQLQKEKDEQYAKLELEKKRLEEQEKEQV 770
Cdd:COG1196   171 KERKEEAERKleaTEENLERLEdilgELERQleplerqaEKAERYR---ELKEELKELEAELLLLKLRELEAELEELEAE 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  771 mlVAHLEEQLREKQEMIQLLRRgevqwveeekrdlegiresllRVKEARAGGDEDGEELEKAQLRFFEFKRRQLvklvnl 850
Cdd:COG1196   248 --LEELEAELEELEAELAELEA---------------------ELEELRLELEELELELEEAQAEEYELLAELA------ 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  851 ekDLVQQKDILKKEVQEEQEILEclkcEHDKESRLLEKHDESVTDVTEvpqdfekikpvEYRLQYKErqlqyllqnhlpt 930
Cdd:COG1196   299 --RLEQDIARLEERRRELEERLE----ELEEELAELEEELEELEEELE-----------ELEEELEE------------- 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  931 lLEEKQRAFEildrgplsldntlyqvekemeekeEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREK 1010
Cdd:COG1196   349 -AEEELEEAE------------------------AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792 1011 QQREALERALARLERRHSALQRHSTlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIY 1090
Cdd:COG1196   404 ELEEAEEALLERLERLEEELEELEE---ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480


                  ....
gi 530425792 1091 EVDG 1094
Cdd:COG1196   481 ELLE 484

SMC_N

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

605-891

2.12e-09

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 62.68 E-value: 2.12e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   605 LRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQeeSLKRRSFHIENKLKDLL 684
Cdd:pfam02463  726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKL--KVEEEKEEKLKAQEEEL 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   685 AEKEKFEEERLREQQEIELQKKRQEEEtflrvQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQ--YAKLELEKKRL 762
Cdd:pfam02463  804 RALEEELKEEAELLEEEQLLIEQEEKI-----KEEELEELALELKEEQKLEKLAEEELERLEEEITKeeLLQELLLKEEE 878

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   763 EEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQ---------WVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 833
Cdd:pfam02463  879 LEEQKLKDELESKEEKEKEEKKELEEESQKLNLLeekeneieeRIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEE 958

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 530425792   834 LRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDE 891
Cdd:pfam02463  959 EERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016

PRK03918

DNA double-strand break repair ATPase Rad50;

606-1025

2.46e-09

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 2.46e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  606 RLEFERQQ-REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRketEIVQLQIRKQEESLKRRSFHIEnKLKDLL 684
Cdd:PRK03918  318 RLEEEINGiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE---EAKAKKEELERLKKRLTGLTPE-KLEKEL 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  685 AEKEKFEEERLREQQEI-----ELQKKRQEEETFLrvqEELQRLK--------ELNNNEKAEKFQIF-QELDQLQKEK-- 748
Cdd:PRK03918  394 EELEKAKEEIEEEISKItarigELKKEIKELKKAI---EELKKAKgkcpvcgrELTEEHRKELLEEYtAELKRIEKELke 470

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  749 -DEQYAKLELEKKRLEEQEKEQVMLVAHLE--EQLREKQEMiqlLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDED 825
Cdd:PRK03918  471 iEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEK---LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  826 GEELE--KAQLRFFEFKRRQL-VKLVNLEKDL----VQQKDILKKEVQEEQEI----LECLKCEHDKESRLLEKHDESvt 894
Cdd:PRK03918  548 LEKLEelKKKLAELEKKLDELeEELAELLKELeelgFESVEELEERLKELEPFyneyLELKDAEKELEREEKELKKLE-- 625

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  895 dvTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDntlyqvekemeekeeqlAQYQANA 974
Cdd:PRK03918  626 --EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLR-----------------AELEELE 686

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530425792  975 NQLQKLQATFEftaNIARQeekvrkkekeiLESREKQQRE--ALERALARLER 1025
Cdd:PRK03918  687 KRREEIKKTLE---KLKEE-----------LEEREKAKKEleKLEKALERVEE 725

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

608-1088

2.47e-09

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: 62.68 E-value: 2.47e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   608 EFERQQREELEKLESKRKLIEEMEEKQKSDK-------------AELERMQQEVETQRKETEIVQLQirkqeeslkRRSF 674
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrarieelraqeAVLEETQERINRARKAAPLAAHI---------KAVT 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   675 HIENKLKDLLAE-KEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQlQKEKDEQYA 753
Cdd:TIGR00618  304 QIEQQAQRIHTElQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ-QHTLTQHIH 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   754 KLELEKKRLEEQEKeqvmLVAHLEEQLREkqemiqllrrgevqwvEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 833
Cdd:TIGR00618  383 TLQQQKTTLTQKLQ----SLCKELDILQR----------------EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   834 LRFFEFKRRQLVKLVNLEKDLVQQKdilkkeVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPqdfekiKPVEYRL 913
Cdd:TIGR00618  443 CAAAITCTAQCEKLEKIHLQESAQS------LKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP------CPLCGSC 510

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   914 QYKERQLQYLLqnhlptLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQanaNQLQKLQATFEFTA----- 988
Cdd:TIGR00618  511 IHPNPARQDID------NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK---EQMQEIQQSFSILTqcdnr 581

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   989 -----NIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLnsgSREQSGLQAS 1063
Cdd:TIGR00618  582 skediPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL---HALQLTLTQE 658

                          490       500
                   ....*....|....*....|....*
gi 530425792  1064 LEAEQEALEKDQERLEYEIQQLKQK 1088
Cdd:TIGR00618  659 RVREHALSIRVLPKELLASRQLALQ 683

PRK02224

DNA double-strand break repair Rad50 ATPase;

605-1091

3.01e-09

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 3.01e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  605 LRLEFERQQREELEKLESKrklIEEMEEKQKSDKAELERMQQEVETQRKETEivqlqirkqeeslkrrsfHIENKLKDLL 684
Cdd:PRK02224  241 EVLEEHEERREELETLEAE---IEDLRETIAETEREREELAEEVRDLRERLE------------------ELEEERDDLL 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  685 AEKEKFEEERLREQQEIELQKKRqEEETFLRVQEELQRLKELNNNEKAEKFQIfQELDQLQKEKDEQYAKLELEKKRLEE 764
Cdd:PRK02224  300 AEAGLDDADAEAVEARREELEDR-DEELRDRLEECRVAAQAHNEEAESLREDA-DDLEERAEELREEAAELESELEEARE 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  765 QEKEQVMLVAHLEEQLREKqemiqllrRGEVQWVEEEKRDLEGIRESLLrvkEARAGGDEDGEELEkaqlrffefkrrql 844
Cdd:PRK02224  378 AVEDRREEIEELEEEIEEL--------RERFGDAPVDLGNAEDFLEELR---EERDELREREAELE-------------- 432

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  845 VKLVNLEKDlvqqkdilkkeVQEEQEILE---CLKCEHD-KESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQL 920
Cdd:PRK02224  433 ATLRTARER-----------VEEAEALLEagkCPECGQPvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  921 QYL--LQNHLPTLLEEKQRAFEILDRGPLSLDNTlyqvekemeekEEQLAQYQANANQLQKLQATFEFTANIARQEEKVR 998
Cdd:PRK02224  502 EDLveAEDRIERLEERREDLEELIAERRETIEEK-----------RERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  999 KKEKEILESRE---KQQREALERALARLERRHSALQRHSTLgmeiEEQRQKLASLNSGSREQ--------SGLQASLEAE 1067
Cdd:PRK02224  571 REEVAELNSKLaelKERIESLERIRTLLAAIADAEDEIERL----REKREALAELNDERRERlaekrerkRELEAEFDEA 646

                         490       500
                  ....*....|....*....|....*
gi 530425792 1068 Q-EALEKDQERLEYEIQQLKQKIYE 1091
Cdd:PRK02224  647 RiEEAREDKERAEEYLEQVEEKLDE 671

COG4913

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

624-1185

5.05e-09

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 5.05e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  624 RKLIEEMEEkqksdkaeLERMQQEVETQRKETEIVQlQIRKQEESLKRrsfhienkLKDLLAEKEKFEEERLREQQEIEL 703
Cdd:COG4913   228 DALVEHFDD--------LERAHEALEDAREQIELLE-PIRELAERYAA--------ARERLAELEYLRAALRLWFAQRRL 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  704 QKKRQEEEtflRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE----QYAKLELEKKRLEEQEKEQVMLVAHLEEQ 779
Cdd:COG4913   291 ELLEAELE---ELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEAL 367

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  780 LR-------EKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEkAQLRffEFKRRQlvklVNLEK 852
Cdd:COG4913   368 LAalglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEIA--SLERRK----SNIPA 440

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  853 DLVQQKDILKK----------------EVQEEQEI----LEclKCEHDKESRLL--EKHDESVTD--------------- 895
Cdd:COG4913   441 RLLALRDALAEalgldeaelpfvgeliEVRPEEERwrgaIE--RVLGGFALTLLvpPEHYAAALRwvnrlhlrgrlvyer 518

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  896 VTEVPQDFEKIKPVE----YRLQYKERQLQYLLQNHL-----------PTLLEEKQRA-------------FEILDRGPL 947
Cdd:COG4913   519 VRTGLPDPERPRLDPdslaGKLDFKPHPFRAWLEAELgrrfdyvcvdsPEELRRHPRAitragqvkgngtrHEKDDRRRI 598

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  948 S------LDNTlyqvekemeekeEQLAQYQAnanQLQKLQATFEFTANIARQEekvrkkekeileSREKQQREALERALA 1021
Cdd:COG4913   599 RsryvlgFDNR------------AKLAALEA---ELAELEEELAEAEERLEAL------------EAELDALQERREALQ 651

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792 1022 RLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLE---AEQEALEKDQERLEYEIQQLKQKIYEVDGVQKD 1098
Cdd:COG4913   652 RLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEeleAELEELEEELDELKGEIGRLEKELEQAEEELDE 731

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792 1099 HHGTLEGKVAssslpvsAEKSHLVPLMDARINAYIEEEVQRRLQDlhrvisegcSTSADTMKDNEKLHNgtIQRKLKYEK 1178
Cdd:COG4913   732 LQDRLEAAED-------LARLELRALLEERFAAALGDAVERELRE---------NLEERIDALRARLNR--AEEELERAM 793


                  ....*..
gi 530425792 1179 RQFCPAW 1185
Cdd:COG4913   794 RAFNREW 800

PTZ00121

MAEBL; Provisional

609-1180

9.09e-09

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 9.09e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  609 FERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEV---ETQRKETEIVQLQIRKQEESLKRrsfhIENKLKdllA 685
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaEEARKAEDAKRVEIARKAEDARK----AEEARK---A 1172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  686 EKEKfeeerlreqqeiELQKKRQEEEtfLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKL--ELEKKRLE 763
Cdd:PTZ00121 1173 EDAK------------KAEAARKAEE--VRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkKAEEAKKD 1238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  764 EQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQ 843
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  844 LVKlvNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESvTDVTEVPQDFEKIKPVEYRLQYKERQLQYL 923
Cdd:PTZ00121 1319 EAK--KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  924 LQNHLPtllEEKQRAFEILDRgplsldntlyQVEKEMEEKEEQLAQYQANANQLQKlqatfefTANIARQEEKVRKKEKE 1003
Cdd:PTZ00121 1396 AKKKAE---EDKKKADELKKA----------AAAKKKADEAKKKAEEKKKADEAKK-------KAEEAKKADEAKKKAEE 1455

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792 1004 ILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQ----EALEKDQERLE 1079
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEakkaDEAKKAEEAKK 1535

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792 1080 YEIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMDARINAYIEEevqRRLQDLHRVISEGCSTSADTM 1159
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE---ARIEEVMKLYEEEKKMKAEEA 1612

                         570       580
                  ....*....|....*....|.
gi 530425792 1160 KDNEKLHNGTIQRKLKYEKRQ 1180
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKK 1633

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

607-873

9.45e-09

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 59.16 E-value: 9.45e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   607 LEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsfhIENKLKDLLAE 686
Cdd:pfam13868   91 EEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDER---ILEYLKEKAER 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   687 KEKFeeerlreqqeiELQKKRQEEEtFLRVQEELQRLKELNNNEKAEKFQIFQELdqLQKEKDEQYAKLELEKKrlEEQE 766
Cdd:pfam13868  168 EEER-----------EAEREEIEEE-KEREIARLRAQQEKAQDEKAERDELRAKL--YQEEQERKERQKEREEA--EKKA 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   767 KEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAggdEDGEELEKAQLRFFEFKRRQLVK 846
Cdd:pfam13868  232 RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRR---MKRLEHRRELEKQIEEREEQRAA 308

                          250       260
                   ....*....|....*....|....*..
gi 530425792   847 LVNLEkdlVQQKDILKKEVQEEQEILE 873
Cdd:pfam13868  309 EREEE---LEEGERLREEEAERRERIE 332

Myosin_tail_1

pfam01576

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

612-1105

1.25e-08

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: 60.19 E-value: 1.25e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   612 QQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVEtqrKETEIVQLQIRKQEEslkrrsfhienklkdLLAEKEKFe 691
Cdd:pfam01576    2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLC---EEKNALQEQLQAETE---------------LCAEAEEM- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   692 eerlreqqEIELQKKRQEEETFL-----RVQEELQRLKELnNNEKAEKFQIFQELDQ-----------LQKEK------- 748
Cdd:pfam01576   63 --------RARLAARKQELEEILhelesRLEEEEERSQQL-QNEKKKMQQHIQDLEEqldeeeaarqkLQLEKvtteaki 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   749 ----------DEQYAKLELEKKRLEEQEKEQVMLVAHLEE------QLREKQEMI-----QLLRRGEVQWVEEEK--RDL 805
Cdd:pfam01576  134 kkleedilllEDQNSKLSKERKLLEERISEFTSNLAEEEEkakslsKLKNKHEAMisdleERLKKEEKGRQELEKakRKL 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   806 EG--------IRESLLRVKEARAGGDEDGEELEKAQLRFFE--FKRRQLVK--------LVNLEKDLVQQKDILKKEVQE 867
Cdd:pfam01576  214 EGestdlqeqIAELQAQIAELRAQLAKKEEELQAALARLEEetAQKNNALKkireleaqISELQEDLESERAARNKAEKQ 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   868 EQ---EILECLKCE----HDKESRLLEKHDESVTDVTEVPqdfekiKPVEYRLQYKERQLQYLLQNHlPTLLEEKQRAFE 940
Cdd:pfam01576  294 RRdlgEELEALKTEledtLDTTAAQQELRSKREQEVTELK------KALEEETRSHEAQLQEMRQKH-TQALEELTEQLE 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   941 ILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANAN-----------QLQKLQATFEFTANIARQEEKVRKKEKEILESRE 1009
Cdd:pfam01576  367 QAKRNKANLEKAKQALESENAELQAELRTLQQAKQdsehkrkklegQLQELQARLSESERQRAELAEKLSKLQSELESVS 446

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  1010 KQQREAlERALARLERRHSAL--QRHSTLGMEIEEQRQKLA---SLNSGSREQSGLQASLEAEQEAlekdQERLEYEIQQ 1084
Cdd:pfam01576  447 SLLNEA-EGKNIKLSKDVSSLesQLQDTQELLQEETRQKLNlstRLRQLEDERNSLQEQLEEEEEA----KRNVERQLST 521

                          570       580
                   ....*....|....*....|.
gi 530425792  1085 LKQKIYEVDGVQKDHHGTLEG 1105
Cdd:pfam01576  522 LQAQLSDMKKKLEEDAGTLEA 542

CwlO1

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

619-833

1.59e-08

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 1.59e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  619 KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKrrsfhienKLKDLLAEKEKfeeerlreq 698
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------KLQAEIAEAEA--------- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  699 qeiELQKKRQEEETFLRVQEE--------------------LQRLKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELE 758
Cdd:COG3883    80 ---EIEERREELGERARALYRsggsvsyldvllgsesfsdfLDRLSALSKIADADA-DLLEELKADKAELEAKKAELEAK 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530425792  759 KKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 833
Cdd:COG3883   156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSA-EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

611-787

1.74e-08

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: 57.24 E-value: 1.74e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAEKEKF 690
Cdd:COG1579     3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  691 EEERLREQQE---------IELQKKRQE--EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEK 759
Cdd:COG1579    79 EEQLGNVRNNkeyealqkeIESLKRRISdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158

                         170       180
                  ....*....|....*....|....*...
gi 530425792  760 KRLEEQEKEqvmLVAHLEEQLREKQEMI 787
Cdd:COG1579   159 EELEAEREE---LAAKIPPELLALYERI 183

SMC_prok_B

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

606-818

3.38e-08

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 3.38e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   606 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVqlqiRKQEESLKRRSFHIENKLKDLLA 685
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLER 831

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   686 EkekfeeerlreqqeIELQKKRQE--EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:TIGR02168  832 R--------------IAATERRLEdlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530425792   764 EQEKEqvmlVAHLEEQLREKQEMIQLLRrgevQWVEEEKRDLEGIRESLLRVKEA 818
Cdd:TIGR02168  898 ELSEE----LRELESKRSELRRELEELR----EKLAQLELRLEGLEVRIDNLQER 944

DUF4659

pfam15558

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...

613-870

4.00e-08

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

Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 57.74 E-value: 4.00e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   613 QREELEKLESKRKLIEEmEEKQKSDKAELERMQQEVETQRKETEivqlqiRKQEESLKRRSFHI---ENKLKDLLAEKEK 689
Cdd:pfam15558   33 AWEELRRRDQKRQETLE-RERRLLLQQSQEQWQAEKEQRKARLG------REERRRADRREKQViekESRWREQAEDQEN 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   690 FEEERLREQQEIELQKKRQEEETfLRVQEE-LQRLKELNNNEKAEKFQI---------------FQELDQ---------- 743
Cdd:pfam15558  106 QRQEKLERARQEAEQRKQCQEQR-LKEKEEeLQALREQNSLQLQERLEEachkrqlkereeqkkVQENNLsellnhqark 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   744 ----LQKEKDEQYAKLELEKKRLEEQEK-EQVMLVAHLEEQLREKQEMIQLLRrgeVQWVEEEK-RDLEGIRESLLRVKE 817
Cdd:pfam15558  185 vlvdCQAKAEELLRRLSLEQSLQRSQENyEQLVEERHRELREKAQKEEEQFQR---AKWRAEEKeEERQEHKEALAELAD 261

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530425792   818 ARAGGDEDGEELEKAQlrffefkRRQLVKLVNLEKDLVQQkdILKKEVQEEQE 870
Cdd:pfam15558  262 RKIQQARQVAHKTVQD-------KAQRARELNLEREKNHH--ILKLKVEKEEK 305

SMC_prok_B

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

608-1089

1.32e-07

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 1.32e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVetqrketeivqLQIRKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-----------AQLELQIASLNNEIERLEARLERLEDRR 416

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   688 EKFeeerlreQQEIELQKKRQEEETFLRVQEELQRLKelnnnekaekfqifQELDQLQKEKDEQYAKLELEKKRLEEQEK 767
Cdd:TIGR02168  417 ERL-------QQEIEELLKKLEEAELKELQAELEELE--------------EELEELQEELERLEEALEELREELEEAEQ 475

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   768 EQVMLVAHLeEQLREKQEMIQ-LLRRGE-----VQWVEEEKRDLEGIRE---SLLRVK-------EARAGGDED---GEE 828
Cdd:TIGR02168  476 ALDAAEREL-AQLQARLDSLErLQENLEgfsegVKALLKNQSGLSGILGvlsELISVDegyeaaiEAALGGRLQavvVEN 554

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   829 LEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDkesrlLEKHDESVTDVtevpqdfekikp 908
Cdd:TIGR02168  555 LNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD-----LVKFDPKLRKA------------ 617

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   909 VEYRL----------QYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQ 978
Cdd:TIGR02168  618 LSYLLggvlvvddldNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELE 697

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   979 KLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERrhsALQRHSTLGMEIEEQRQKLASLNSGSREQS 1058
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKELTELEAEIEELEERLEEAE 774

                          490       500       510
                   ....*....|....*....|....*....|.
gi 530425792  1059 GLQASLEAEQEALEKDQERLEYEIQQLKQKI 1089
Cdd:TIGR02168  775 EELAEAEAEIEELEAQIEQLKEELKALREAL 805

PTZ00121

MAEBL; Provisional

606-1178

1.34e-07

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 1.34e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  606 RLEFERQQrEELEKLESKRKLIE--EMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDl 683
Cdd:PTZ00121 1165 KAEEARKA-EDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK----AEEAKKD- 1238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  684 lAEKEKfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:PTZ00121 1239 -AEEAK------------KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD 1305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  764 EQEK--EQVMLVAHLEEQLREKQEMIQLLRRG--EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEF 839
Cdd:PTZ00121 1306 EAKKkaEEAKKADEAKKKAEEAKKKADAAKKKaeEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  840 KRRQLVKLVNLEKDLVQQK---DILKKEVQEEQEILEC-LKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQY 915
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKkkaDELKKAAAAKKKADEAkKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  916 KERQLQyllQNHLPTLLEEKQRAFEI---LDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIAR 992
Cdd:PTZ00121 1466 AEEAKK---ADEAKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  993 QEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLgMEIEEQR-QKLASLNSGSREQSGLQASLEAEQ--- 1068
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA-KKAEEARiEEVMKLYEEEKKMKAEEAKKAEEAkik 1621

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792 1069 -EALEKDQERLEYEIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAE--KSHLVPLMDARINAYIEEEVQRRLQDLH 1145
Cdd:PTZ00121 1622 aEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701

                         570       580       590
                  ....*....|....*....|....*....|...
gi 530425792 1146 RVISEGCSTSADTMKDNEKLHNGTIQRKLKYEK 1178
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734

DUF4670

pfam15709

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...

608-806

2.21e-07

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

Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 55.73 E-value: 2.21e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMqqEVETQRKETEivqLQIRKQEESLKRrsfhiENKLKDLLaEK 687
Cdd:pfam15709  312 EEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRL--EVERKRREQE---EQRRLQQEQLER-----AEKMREEL-EL 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   688 EKfeeerLREQQEIELQKKRQEEETFLRVQEEL-QRLKELNNNEKAEKFQ--IFQELDQLQKEKDEQYA-KLELEKKRLE 763
Cdd:pfam15709  381 EQ-----QRRFEEIRLRKQRLEEERQRQEEEERkQRLQLQAAQERARQQQeeFRRKLQELQRKKQQEEAeRAEAEKQRQK 455

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 530425792   764 EQE----KEQVMLVAHLEEQ----LREKQEMIQllrrgEVQWVEEEKRDLE 806
Cdd:pfam15709  456 ELEmqlaEEQKRLMEMAEEErleyQRQKQEAEE-----KARLEAEERRQKE 501

SMC_N

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

354-1024

2.29e-07

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.13 E-value: 2.29e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   354 RAKNIINKPTINEDANVKLIRELRAEIARLKtlLAQGNQIALLDSPTALSMEEKLQQNEARVQELTK----EWTNKWNET 429
Cdd:pfam02463  415 RQLEDLLKEEKKEELEILEEEEESIELKQGK--LTEEKEELEKQELKLLKDELELKKSEDLLKETQLvklqEQLELLLSR 492

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   430 QNILKEQTLALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIG 509
Cdd:pfam02463  493 QKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTE 572

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   510 GTVTLIPLSG--SQCSVNGVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLREKRKSGLLSSFSLSMTDLSKSRENLS 587
Cdd:pfam02463  573 LPLGARKLRLliPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGV 652

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   588 AVMlynPGLFPIKGPICLRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEE 667
Cdd:pfam02463  653 SLE---EGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQE 729

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   668 SLKRRSFHIENKLKDLLAEKEKfeeerlreqQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKE 747
Cdd:pfam02463  730 AQDKINEELKLLKQKIDEEEEE---------EEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQE 800

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   748 KDEQyAKLELEKKRLEEQEKEQVmlvahLEEQLREKQEmiqllrrgevqwvEEEKRDLEGIRESLLRVKEARAGGDEDGE 827
Cdd:pfam02463  801 EELR-ALEEELKEEAELLEEEQL-----LIEQEEKIKE-------------EELEELALELKEEQKLEKLAEEELERLEE 861

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   828 ELEKAQLrffefKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKEsrLLEKHDESVTDVTEVPQDFEKIK 907
Cdd:pfam02463  862 EITKEEL-----LQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL--LEEKENEIEERIKEEAEILLKYE 934

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   908 PVEYRLQYKERQLQYLLQNHLPTLLEEkqrafeildrgplsldntlyqvekemeekeEQLAQYQANANQLQKLQATFEFT 987
Cdd:pfam02463  935 EEPEELLLEEADEKEKEENNKEEEEER------------------------------NKRLLLAKEELGKVNLMAIEEFE 984

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 530425792   988 ANIARQEEKVRKKEKEILESREKQQREALERALARLE 1024
Cdd:pfam02463  985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021

COG4913

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

605-1091

2.96e-07

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 2.96e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  605 LRLEFERQQREELEKLeskrklIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIR----KQEESLKRRSFHIENKL 680
Cdd:COG4913   281 LRLWFAQRRLELLEAE------LEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLEREL 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  681 KDLLAEKEKFEEERLREQQEIELqkkrqEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKK 760
Cdd:COG4913   355 EERERRRARLEALLAALGLPLPA-----SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  761 RLEEQ----EKEQVMLVAHLEEQLREKQ-------EMIQLlRRGEVQW----------------VEEE----------KR 803
Cdd:COG4913   430 SLERRksniPARLLALRDALAEALGLDEaelpfvgELIEV-RPEEERWrgaiervlggfaltllVPPEhyaaalrwvnRL 508

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  804 DL------EGIRESLLRVKEARAGGD------------------------------EDGEELE------------KAQLR 835
Cdd:COG4913   509 HLrgrlvyERVRTGLPDPERPRLDPDslagkldfkphpfrawleaelgrrfdyvcvDSPEELRrhpraitragqvKGNGT 588

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  836 FFE-----FKRRQLV-------KLVNLEKDLVQqkdiLKKEVQEEQEILEclkcEHDKESRLLEKHDESVTDVTEVPQDF 903
Cdd:COG4913   589 RHEkddrrRIRSRYVlgfdnraKLAALEAELAE----LEEELAEAEERLE----ALEAELDALQERREALQRLAEYSWDE 660

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  904 EKIKPVEYRLQYKERQLQYLLQNH--LPTLLEEKQRAFEILDRgplsLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQ 981
Cdd:COG4913   661 IDVASAEREIAELEAELERLDASSddLAALEEQLEELEAELEE----LEEELDELKGEIGRLEKELEQAEEELDELQDRL 736

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  982 ATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGME-------------------IEE 1042
Cdd:COG4913   737 EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldadlesLPE 816

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 530425792 1043 QRQKLASLnsgsrEQSGLqasLEAEQEALEKDQERLEYEIQQLKQKIYE 1091
Cdd:COG4913   817 YLALLDRL-----EEDGL---PEYEERFKELLNENSIEFVADLLSKLRR 857

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

611-988

3.34e-07

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: 55.41 E-value: 3.34e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQ------------EVETQRKETEIVQLQIRKQEESLKRrsfhIEN 678
Cdd:TIGR04523  267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkeqdwnkelksELKNQEKKLEEIQNQISQNNKIISQ----LNE 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   679 KLKDLlaEKEKFEEERLREQQEIELQKKRQEEETFLRVQEE-LQRLKELNNNEKAEKFQIfQELDQLQKEKDEQYAKLEL 757
Cdd:TIGR04523  343 QISQL--KKELTNSESENSEKQRELEEKQNEIEKLKKENQSyKQEIKNLESQINDLESKI-QNQEKLNQQKDEQIKKLQQ 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   758 EKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLrrgevqwvEEEKRDLEGIRESL-LRVKEARAGGDEDGEELEKAQlRF 836
Cdd:TIGR04523  420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVK--------ELIIKNLDNTRESLeTQLKVLSRSINKIKQNLEQKQ-KE 490

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   837 FEFKRRQLVKLVNLEKDLVQQKDILKKEVQE---EQEILECLKCEhdKESRLLEKHDESVTDVTEVpqDFEKIKPVeyrL 913
Cdd:TIGR04523  491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSlkeKIEKLESEKKE--KESKISDLEDELNKDDFEL--KKENLEKE---I 563

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530425792   914 QYKERQLQYLLQNHlpTLLEEKQRAFEILdrgplsldntlyqvekemeekeeqLAQYQANANQLQKLQATFEFTA 988
Cdd:TIGR04523  564 DEKNKEIEELKQTQ--KSLKKKQEEKQEL------------------------IDQKEKEKKDLIKEIEEKEKKI 612

SMC_prok_B

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

799-1106

4.91e-07

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 4.91e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   799 EEEKRDLEGIRESLLRVKEARaggdedgEELEKaQLRFFEFKRRQLVKLVNLEKDLVQ-QKDILKKEVQEEQEILECLKc 877
Cdd:TIGR02168  175 KETERKLERTRENLDRLEDIL-------NELER-QLKSLERQAEKAERYKELKAELRElELALLVLRLEELREELEELQ- 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   878 ehDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQ---YLLQNHLPTLLEEKQRA---FEILDRGPLSLDN 951
Cdd:TIGR02168  246 --EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelYALANEISRLEQQKQILrerLANLERQLEELEA 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   952 TLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEftaniarqeekvrkkekeILESREKQQREALERALARLERrhsalq 1031
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLE------------------AELEELEAELEELESRLEELEE------ 379

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530425792  1032 rhstlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDgvQKDHHGTLEGK 1106
Cdd:TIGR02168  380 -------QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEEL 445

FHA

COG1716

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];

471-551

5.00e-07

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];

Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 49.57 E-value: 5.00e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  471 YHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLsGSQ--CSVNGVQIVEATHLNQGAVILLGRTnM 548
Cdd:COG1716    16 FPLDGGPLTIGRAPDN---DIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90


                  ...
gi 530425792  549 FRF 551
Cdd:COG1716    91 LRF 93

COG1340

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

611-803

5.08e-07

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.38 E-value: 5.08e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  611 RQQREELEKLESKRKLIEEMEEKQksdkAELERMQQ-EVETQRKETEIVQlQIRKQEESLKRR--SFHIENKLKDLLAEk 687
Cdd:COG1340    95 DELRKELAELNKAGGSIDKLRKEI----ERLEWRQQtEVLSPEEEKELVE-KIKELEKELEKAkkALEKNEKLKELRAE- 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  688 ekfeeerlreqqeieLQKKRQEEETFlrvQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 767
Cdd:COG1340   169 ---------------LKELRKEAEEI---HKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 530425792  768 EQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKR 803
Cdd:COG1340   231 EIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

611-803

5.81e-07

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

Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 5.81e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETE----IVQLQIRKQEESLKRRSFHIENKLK----- 681
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEaelaELEKEIAELRAELEAQKEELAELLRalyrl 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  682 ------DLLAEKEKFEEERLREQQEIELQKKRQEE-ETFLRVQEELQRLKELNNNEKAEKFQIFQE-------LDQLQKE 747
Cdd:COG4942   117 grqpplALLLSPEDFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELEALLAEleeeraaLEALKAE 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530425792  748 KDEQYAKLELEKKRLEEQekeqvmlvahLEEQLREKQEMIQLLRRGEVQWVEEEKR 803
Cdd:COG4942   197 RQKLLARLEKELAELAAE----------LAELQQEAEELEALIARLEAEAAAAAER 242

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

615-1089

7.88e-07

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 7.88e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   615 EELEKLESKRKLI--EEMEEKQKSDK--AELERMQQEVETQR-----KETEIVQL--QIRKQEESLKRRSFHIENKLKDL 683
Cdd:TIGR04523   75 NKIKILEQQIKDLndKLKKNKDKINKlnSDLSKINSEIKNDKeqknkLEVELNKLekQKKENKKNIDKFLTEIKKKEKEL 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   684 LAEKEKFEeerlreqqeiELQKKRQEEETFL-RVQEELQRLKELNNNEKAEKFQIFQELDQLQKeKDEQYAKLELEKKRL 762
Cdd:TIGR04523  155 EKLNNKYN----------DLKKQKEELENELnLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKK-KIQKNKSLESQISEL 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   763 EEQEKEqvmlvahLEEQLREKQEMIQllrrgevqwveEEKRDLEGIRESLLRVKEARaggDEDGEELEKAQLRFFEFKRr 842
Cdd:TIGR04523  224 KKQNNQ-------LKDNIEKKQQEIN-----------EKTTEISNTQTQLNQLKDEQ---NKIKKQLSEKQKELEQNNK- 281

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   843 qlvKLVNLEKDLVQQK-DILKKEVQEEQEILECLKCEHDKESRLLE-------KHDESVTDVTEVPQDFEK-IKPVEYRL 913
Cdd:TIGR04523  282 ---KIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLEeiqnqisQNNKIISQLNEQISQLKKeLTNSESEN 358

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   914 QYKERQLQYLlQNHLPTLLEEKQRAFEI---LDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQK----LQATFEF 986
Cdd:TIGR04523  359 SEKQRELEEK-QNEIEKLKKENQSYKQEiknLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKeierLKETIIK 437

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   987 TANIARQEEKVRKKEKEILESRE------KQQREALERALARLERRHSALQRhstlgmEIEEQRQKLASLNSGSREQSGL 1060
Cdd:TIGR04523  438 NNSEIKDLTNQDSVKELIIKNLDntreslETQLKVLSRSINKIKQNLEQKQK------ELKSKEKELKKLNEEKKELEEK 511

                          490       500
                   ....*....|....*....|....*....
gi 530425792  1061 QASLEAEQEALEKDQERLEYEIQQLKQKI 1089
Cdd:TIGR04523  512 VKDLTKKISSLKEKIEKLESEKKEKESKI 540

FHA_RADIL-like

cd22712

forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...

451-554

9.88e-07

forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438764 [Multi-domain] Cd Length: 120 Bit Score: 49.61 E-value: 9.88e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  451 SELPHLIGI-----DDDLLstgiiLYHLKEGQTYVGRDDASTEQ-DIVLHGLDLESEHCI-----------FENIGGT-- 511
Cdd:cd22712     1 SDYPYLLTLrgfspKQDLL-----VYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCWirrkpeplsddEDSDKESad 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 530425792  512 --VTLIPLSGSQCSVNGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22712    76 yrVVLSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120

SMC_prok_B

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

606-1144

1.34e-06

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 1.34e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   606 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQ--------IRKQEESLKRRSFHIE 677
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeleeLEEELEELQEELERLE 460

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   678 NKLKDLLAEKEKFEEERLREQQeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQK--EKDEQYaKL 755
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAER--ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEliSVDEGY-EA 537

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   756 ELEK---KRLE----EQEKEQVMLVAHLEE-----------------QLREKQEMIQLLRRGEVQW---VEEEKRDLEGI 808
Cdd:TIGR02168  538 AIEAalgGRLQavvvENLNAAKKAIAFLKQnelgrvtflpldsikgtEIQGNDREILKNIEGFLGVakdLVKFDPKLRKA 617

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   809 RESLL-------RVKEA---------------------RAGGDEDGEELEKAQLRFfeFKRRQLVKLVNLEKDLVQQKDI 860
Cdd:TIGR02168  618 LSYLLggvlvvdDLDNAlelakklrpgyrivtldgdlvRPGGVITGGSAKTNSSIL--ERRREIEELEEKIEELEEKIAE 695

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   861 LKKEVQE-EQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQ--NHLPTLLEEKQR 937
Cdd:TIGR02168  696 LEKALAElRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAeiEELEERLEEAEE 775

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   938 AFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALE 1017
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  1018 RALARLE-------RRHSALQRHSTLGMEIEEQRQKL--------ASLNSGSREQSGLQASLEAEQEALEK---DQERLE 1079
Cdd:TIGR02168  856 SLAAEIEeleelieELESELEALLNERASLEEALALLrseleelsEELRELESKRSELRRELEELREKLAQlelRLEGLE 935

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  1080 YEIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMDA--RIN-AYIEE--EVQRRLQDL 1144
Cdd:TIGR02168  936 VRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgPVNlAAIEEyeELKERYDFL 1005

COG2433

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

627-800

1.48e-06

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

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 53.32 E-value: 1.48e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  627 IEEMEEKQKSDkaELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAEKEKfeeerLREQQEIELQKK 706
Cdd:COG2433   382 LEELIEKELPE--EEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-ELEAELEEKDE-----RIERLERELSEA 453

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  707 RQEEETFLRVQEELQRLKELNNNEKAEkfqifqeLDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLE----EQLRE 782
Cdd:COG2433   454 RSEERREIRKDREISRLDREIERLERE-------LEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEkftkEAIRR 526

                         170
                  ....*....|....*...
gi 530425792  783 KQEMIqLLRRGEVQWVEE 800
Cdd:COG2433   527 LEEEY-GLKEGDVVYLRD 543

MAP7

pfam05672

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...

605-764

2.20e-06

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

Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 49.27 E-value: 2.20e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   605 LRLEFERQQREELEKLESKRKLIEEMEEkqksdKAELERMQQEVETQRKETEivqlqiRKQEESLKRRSfHIENKLKDLL 684
Cdd:pfam05672   23 AREQREREEQERLEKEEEERLRKEELRR-----RAEEERARREEEARRLEEE------RRREEEERQRK-AEEEAEEREQ 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   685 AEKEKfeeerlreqqEIELQKKRQEEETFLRVQEELQRLkelnnnekaEKFQIFQELDQLQKEKdeqyakleleKKRLEE 764
Cdd:pfam05672   91 REQEE----------QERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER----------KKRIEE 141

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

611-940

3.77e-06

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.07 E-value: 3.77e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   611 RQQREELEKLESKRKL----------IEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQE-ESLKRRSFHIENK 679
Cdd:pfam13868    2 RENSDELRELNSKLLAakcnkerdaqIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERkEERKRYRQELEEQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   680 LKDLLAEKEKfeeerlreqqeiELQKKRQEEETFLRVQEELQRlkelnnNEKAEKFQIFQELDQLQKEKDEQYAKLELEK 759
Cdd:pfam13868   82 IEEREQKRQE------------EYEEKLQEREQMDEIVERIQE------EDQAEAEEKLEKQRQLREEIDEFNEEQAEWK 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   760 KRLEEQEKEQVMLVahlEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLrffEF 839
Cdd:pfam13868  144 ELEKEEEREEDERI---LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQ---ER 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   840 KRRQlvklvnLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESvtdvtEVPQDFEKIKPVEYRLQYKERQ 919
Cdd:pfam13868  218 KERQ------KEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFE-----RMLRKQAEDEEIEQEEAEKRRM 286

                          330       340
                   ....*....|....*....|.
gi 530425792   920 LQYLLQNHLPTLLEEKQRAFE 940
Cdd:pfam13868  287 KRLEHRRELEKQIEEREEQRA 307

DUF5401

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

720-1091

4.22e-06

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

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.66 E-value: 4.22e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   720 LQRLKELNNNEKAEKFQIFQElDQLQKEKDEQYAKLElEKKRLEEQEKEQVmlvAHLEEQ--LREKQEMIQLLRRGEVQW 797
Cdd:pfam17380  278 VQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVE-RRRKLEEAEKARQ---AEMDRQaaIYAEQERMAMERERELER 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   798 V--EEEKRDLEGIRESLLRVKEARAggdedgEELEKAQLrffefKRRQLVKLVNLEKDLVQQKDILKKEVQEEqeilecl 875
Cdd:pfam17380  353 IrqEERKRELERIRQEEIAMEISRM------RELERLQM-----ERQQKNERVRQELEAARKVKILEEERQRK------- 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   876 kcehdkesrllekhdesvtdVTEVPQDFEKIKpveyRLQYKERQLQyllqnhLPTLLEEKQRAFEILDRgplsldntlyq 955
Cdd:pfam17380  415 --------------------IQQQKVEMEQIR----AEQEEARQRE------VRRLEEERAREMERVRL----------- 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   956 vekemeekeeqlaQYQANANQLQKLqatfeftaniaRQEEKVRKKEKEILESREKQQREALEralarlerrhsalQRHST 1035
Cdd:pfam17380  454 -------------EEQERQQQVERL-----------RQQEEERKRKKLELEKEKRDRKRAEE-------------QRRKI 496

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 530425792  1036 LGMEIEEQRQKLAslnSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYE 1091
Cdd:pfam17380  497 LEKELEERKQAMI---EEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME 549

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

576-1088

4.30e-06

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 4.30e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   576 MTDLSKSRENL-SAVMLYNPGLFPIKGPICLRLEFERQQ---------REELEKLESK-RKLIEEMEEKQKSDKAELERM 644
Cdd:pfam05483   25 KSNLSKNGENIdSDPAFQKLNFLPMLEQVANSGDCHYQEglkdsdfenSEGLSRLYSKlYKEAEKIKKWKVSIEAELKQK 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   645 QQEVETQRKETE-----IVQLQIRKQEESLKRRSFHIENklKDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRvQEE 719
Cdd:pfam05483  105 ENKLQENRKIIEaqrkaIQELQFENEKVSLKLEEEIQEN--KDLIKENNATRHLCNLLKETCARSAEKTKKYEYER-EET 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   720 LQRLKELNNNekAEKFQI-FQELdQLQKEKdeqyAKLELEKKRLEEQEKEQvmlvaHLEE----QLREKQEMIQLLRrge 794
Cdd:pfam05483  182 RQVYMDLNNN--IEKMILaFEEL-RVQAEN----ARLEMHFKLKEDHEKIQ-----HLEEeykkEINDKEKQVSLLL--- 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   795 VQWVEEEKRdlegIRESLLRVKEAR--AGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEIL 872
Cdd:pfam05483  247 IQITEKENK----MKDLTFLLEESRdkANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIA 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   873 ECLKCE--HDKESRLLE------KHDESVTDVTEVPQDFEKIKPVE-YRLQYKERQLQYLlqnhlptLLEEKQRAFEild 943
Cdd:pfam05483  323 TKTICQltEEKEAQMEElnkakaAHSFVVTEFEATTCSLEELLRTEqQRLEKNEDQLKII-------TMELQKKSSE--- 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   944 rgplsldntLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARL 1023
Cdd:pfam05483  393 ---------LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIK 463

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425792  1024 ERRHSALQRHSTLGMEIEEQRQKLASLNSGS-----------REQSGLQASLEAEQEAL---EKDQERLEYEIQQLKQK 1088
Cdd:pfam05483  464 TSEEHYLKEVEDLKTELEKEKLKNIELTAHCdklllenkeltQEASDMTLELKKHQEDIincKKQEERMLKQIENLEEK 542

DUF3584

pfam12128

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...

605-1149

4.58e-06

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: 51.76 E-value: 4.58e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   605 LRLEFERQQREELEKLESKRKLIEEMEEKQKsdkAELERMQQEVETQ-RKETEIVQLQIRKQEESLKRRSFHIENKLKDL 683
Cdd:pfam12128  380 RRSKIKEQNNRDIAGIKDKLAKIREARDRQL---AVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQA 456

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   684 LAEKEkfeeerlreqqeiELQKKRQEEETFLRVQEELQRlkelnNNEKAEKFQifQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:pfam12128  457 TATPE-------------LLLQLENFDERIERAREEQEA-----ANAEVERLQ--SELRQARKRRDQASEALRQASRRLE 516

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   764 EQEKEqvmlVAHLEEQLREKQ-EMIQLLRRGEVQWVEEEKRDLEgiRESLLR---VKEARAGGDEDGEELEKAQLRffeF 839
Cdd:pfam12128  517 ERQSA----LDELELQLFPQAgTLLHFLRKEAPDWEQSIGKVIS--PELLHRtdlDPEVWDGSVGGELNLYGVKLD---L 587

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   840 KRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTevpQDFEKIKPVEYRLQYKERQ 919
Cdd:pfam12128  588 KRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR---TALKNARLDLRRLFDEKQS 664

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   920 LQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNT----LYQVEKEMEEKEEQLAQY-----QANANQLQKLQATFE-FTAN 989
Cdd:pfam12128  665 EKDKKNKALAERKDSANERLNSLEAQLKQLDKKhqawLEEQKEQKREARTEKQAYwqvveGALDAQLALLKAAIAaRRSG 744

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   990 IARQEEKVRKKEKEILESRE---------KQQREALERALARLE-RRHSALQRH------------------STLGMEIE 1041
Cdd:pfam12128  745 AKAELKALETWYKRDLASLGvdpdviaklKREIRTLERKIERIAvRRQEVLRYFdwyqetwlqrrprlatqlSNIERAIS 824

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  1042 EQRQKLASLNSGSREQsglQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQKDhhgtleGKVASSSLPVSAEKSHL 1121
Cdd:pfam12128  825 ELQQQLARLIADTKLR---RAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED------ANSEQAQGSIGERLAQL 895

                          570       580
                   ....*....|....*....|....*...
gi 530425792  1122 VPLMDarINAYIEEEVQRRLQDLHRVIS 1149
Cdd:pfam12128  896 EDLKL--KRDYLSESVKKYVEHFKNVIA 921

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

615-831

7.05e-06

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 7.05e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   615 EELEKLESKRKLIEEMEEKQKsdkAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEER 694
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   695 LREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEqyaklelekkrlEEQEKEQVMLVA 774
Cdd:TIGR02169  892 DELEAQLRELERKIEE-----LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE------------DEEIPEEELSLE 954

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530425792   775 HLEEQLREKQEMIQLLrrGEV-----QWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEK 831
Cdd:TIGR02169  955 DVQAELQRVEEEIRAL--EPVnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014

rad50

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

608-912

7.60e-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: 51.20 E-value: 7.60e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   608 EFERQQREELEKLESKRKLIEEMEEK----------QKSDKAELERMQQEVETQRKET-EIVQLQIRKQEESLKRRSFHI 676
Cdd:TIGR00606  238 EIVKSYENELDPLKNRLKEIEHNLSKimkldneikaLKSRKKQMEKDNSELELKMEKVfQGTDEQLNDLYHNHQRTVREK 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   677 ENKLKDLLAEKEKFEEERLreqqeiELQKKRQE---EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKD---E 750
Cdd:TIGR00606  318 ERELVDCQRELEKLNKERR------LLNQEKTEllvEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFserQ 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   751 QYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLR---RGEVQWVEEEKRDLEGIRESLLRVKearaggdEDGE 827
Cdd:TIGR00606  392 IKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRdekKGLGRTIELKKEILEKKQEELKFVI-------KELQ 464

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   828 ELEKAQLRFFEFK---RRQLVKLVNLEKD-LVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQD- 902
Cdd:TIGR00606  465 QLEGSSDRILELDqelRKAERELSKAEKNsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDk 544

                          330
                   ....*....|...
gi 530425792   903 ---FEKIKPVEYR 912
Cdd:TIGR00606  545 mdkDEQIRKIKSR 557

TolA

COG3064

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

610-873

8.94e-06

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

Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 50.42 E-value: 8.94e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  610 ERQQREELEKLESKRKLIEEMEEKQKsDKAELERMQQEVETQRKETEIVQLQIRKQEeslkrrsfhienKLKDLLAEKEK 689
Cdd:COG3064    11 EAAAQERLEQAEAEKRAAAEAEQKAK-EEAEEERLAELEAKRQAEEEAREAKAEAEQ------------RAAELAAEAAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  690 feeerlreqqeielqKKRQEEETFLRVQEELQRlKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQ 769
Cdd:COG3064    78 ---------------KLAEAEKAAAEAEKKAAA-EKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEER 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  770 VMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVN 849
Cdd:COG3064   142 KAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAV 221

                         250       260
                  ....*....|....*....|....
gi 530425792  850 LEKDLVQQKDILKKEVQEEQEILE 873
Cdd:COG3064   222 AARAAAASREAALAAVEATEEAAL 245

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

610-844

1.06e-05

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 1.06e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   610 ERQQREELEKLESK-RKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsfhiENKLKDLLAEKE 688
Cdd:pfam13868  108 ERIQEEDQAEAEEKlEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER----EAEREEIEEEKE 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   689 KfEEERLREQQEIELQKKRQEEE-TFLRVQEELQ---RLKELNNNEKAEKFQifQELDQLQKEKDEQYAKLELEKKRLEE 764
Cdd:pfam13868  184 R-EIARLRAQQEKAQDEKAERDElRAKLYQEEQErkeRQKEREEAEKKARQR--QELQQAREEQIELKERRLAEEAEREE 260

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   765 QEKEQVMLV----AHLEEQLREKQEMIQLLRRGEVQWVEEEKRdlegiRESLLRVKEARAGGDEDGEELEKAQLRFFEFK 840
Cdd:pfam13868  261 EEFERMLRKqaedEEIEQEEAEKRRMKRLEHRRELEKQIEERE-----EQRAAEREEELEEGERLREEEAERRERIEEER 335


                   ....
gi 530425792   841 RRQL 844
Cdd:pfam13868  336 QKKL 339

PRK12704

phosphodiesterase; Provisional

613-768

1.25e-05

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 1.25e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  613 QREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEE 692
Cdd:PRK12704   45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530425792  693 ERLreqqeiELQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIFqeLDQLQKEKDEQYAKL--ELEKKRLEEQEKE 768
Cdd:PRK12704  122 KQQ------ELEKKEEELEE--LIEEQLQELERISGLTAEEAKEIL--LEKVEEEARHEAAVLikEIEEEAKEEADKK 189

Myosin_tail_1

pfam01576

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

608-1109

1.28e-05

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 1.28e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   608 EFERQQREELEKLESKRKL-------IEEMEEKQKsdKAELERMQQEVETQRKETEIVQLQ-----IRKQEESLKRRSFH 675
Cdd:pfam01576  163 EFTSNLAEEEEKAKSLSKLknkheamISDLEERLK--KEEKGRQELEKAKRKLEGESTDLQeqiaeLQAQIAELRAQLAK 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   676 IENKLKDLLAEKEKfeeerlREQQEIELQKK-RQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKE----KDE 750
Cdd:pfam01576  241 KEEELQAALARLEE------ETAQKNNALKKiRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtLDT 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   751 QYAKLELEKKRleeqEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELe 830
Cdd:pfam01576  315 TAAQQELRSKR----EQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAEL- 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   831 KAQLRFF-------EFKRRQLVKLVNlekDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLE----KHDESVTDVTEV 899
Cdd:pfam01576  390 QAELRTLqqakqdsEHKRKKLEGQLQ---ELQARLSESERQRAELAEKLSKLQSELESVSSLLNeaegKNIKLSKDVSSL 466

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   900 P---QDFEKIKPVEYR----LQYKERQLQYlLQNHLPTLLEEKQRAFEILDRgplsldntlyqvekemeekeeQLAQYQA 972
Cdd:pfam01576  467 EsqlQDTQELLQEETRqklnLSTRLRQLED-ERNSLQEQLEEEEEAKRNVER---------------------QLSTLQA 524

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   973 nanQLQKLQATFEFTANIARQEEKVRKKEKEILESReKQQREALERALARLERRHSALQRH-STLGMEIEEQRQKLASLN 1051
Cdd:pfam01576  525 ---QLSDMKKKLEEDAGTLEALEEGKKRLQRELEAL-TQQLEEKAAAYDKLEKTKNRLQQElDDLLVDLDHQRQLVSNLE 600

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530425792  1052 SGSR-------EQSGLQASL-----EAEQEALEKDQE--RLEYEIQQLKQKIYEVDGVQKDHHGTLEGKVAS 1109
Cdd:pfam01576  601 KKQKkfdqmlaEEKAISARYaeerdRAEAEAREKETRalSLARALEEALEAKEELERTNKQLRAEMEDLVSS 672

PRK02224

DNA double-strand break repair Rad50 ATPase;

598-898

1.43e-05

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.43e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  598 PIKG-PICLRLEFERQQREELE-KLESKRKLIEEMEEK--QKSDKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRS 673
Cdd:PRK02224  460 PVEGsPHVETIEEDRERVEELEaELEDLEEEVEEVEERleRAEDLVEAED---RIERLEERREDLEELIAERRETIEEKR 536

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  674 FHIENKLK---DLLAEKEkfeeerlreqqeielQKKRQEEETFLRVQEELQRLKELNnnekAEKFQIFQELDQLQKEKDE 750
Cdd:PRK02224  537 ERAEELREraaELEAEAE---------------EKREAAAEAEEEAEEAREEVAELN----SKLAELKERIESLERIRTL 597

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  751 QYAKLELEKKRLEEQEKEqvmlvAHLEEQLREKQEMIQLLRrgevqwveEEKRDLEG-IRESllRVKEARaggdEDGEEL 829
Cdd:PRK02224  598 LAAIADAEDEIERLREKR-----EALAELNDERRERLAEKR--------ERKRELEAeFDEA--RIEEAR----EDKERA 658

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530425792  830 EKAQLRFFEfkrrqlvKLvnleKDLVQQKDILKKE---VQEEQEILECLKCEHDkesRLLEKHD--ESVTDVTE 898
Cdd:PRK02224  659 EEYLEQVEE-------KL----DELREERDDLQAEigaVENELEELEELRERRE---ALENRVEalEALYDEAE 718

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

605-926

1.70e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.70e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  605 LRLEFERQQREELEKL--ESKRKLIEEMEEKQKsdkaELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhienkLKD 682
Cdd:COG4372    13 LSLFGLRPKTGILIAAlsEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQ--------LEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  683 LLAEKEKfeeerlreqqeiELQKKRQEEEtflRVQEELQRLKElnnnekaEKFQIFQELDQLQKEK---DEQYAKLELEK 759
Cdd:COG4372    81 ELEELNE------------QLQAAQAELA---QAQEELESLQE-------EAEELQEELEELQKERqdlEQQRKQLEAQI 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  760 KRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRG-EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFE 838
Cdd:COG4372   139 AELQSEIAEREEELKELEEQLESLQEELAALEQElQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAE 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  839 FKRRQLVKL-----VNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRL 913
Cdd:COG4372   219 ELLEAKDSLeaklgLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLL 298

                         330
                  ....*....|...
gi 530425792  914 QYKERQLQYLLQN 926
Cdd:COG4372   299 ALLLNLAALSLIG 311

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

605-938

1.73e-05

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: 49.82 E-value: 1.73e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   605 LRLEFERQQReeleKLESKRKLIEEMEEKQKSDKAELERMQQEVETQ-------RKETEIVQLQIR---KQEESLKRRSF 674
Cdd:pfam10174  350 LRLRLEEKES----FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKerkinvlQKKIENLQEQLRdkdKQLAGLKERVK 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   675 HIEN----------KLKDLLAEKEKFEEERLREqQEIELQKKRQEEETFlrvQEELQRLKELNNNEKAEKFQIFQELDQL 744
Cdd:pfam10174  426 SLQTdssntdtaltTLEEALSEKERIIERLKEQ-REREDRERLEELESL---KKENKDLKEKVSALQPELTEKESSLIDL 501

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   745 QK----------EKDEQYAKLE--LEKKRLEEQEKEQVMLVAH-LEEQLREKQEM---IQLLRRgEVQWVEEEKR----D 804
Cdd:pfam10174  502 KEhasslassglKKDSKLKSLEiaVEQKKEECSKLENQLKKAHnAEEAVRTNPEIndrIRLLEQ-EVARYKEESGkaqaE 580

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   805 LEGIRESLLRVKEARAGGDEDGEELEKAQLRFFefkRRQLVKLVNLEkdLVQQKDiLKKEVQEEQEILECLKCEHDKESR 884
Cdd:pfam10174  581 VERLLGILREVENEKNDKDKKIAELESLTLRQM---KEQNKKVANIK--HGQQEM-KKKGAQLLEEARRREDNLADNSQQ 654

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530425792   885 LleKHDESVTDVTEVPQDFEKIK----PVEYRLQYKERQLQYLLQN---HLPTLLEEKQRA 938
Cdd:pfam10174  655 L--QLEELMGALEKTRQELDATKarlsSTQQSLAEKDGHLTNLRAErrkQLEEILEMKQEA 713

Yop-YscD_cpl

pfam16697

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...

471-555

1.78e-05

Pssm-ID: 465238 [Multi-domain] Cd Length: 94 Bit Score: 44.94 E-value: 1.78e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   471 YHLKEGQTYVGRDDastEQDIVLHGLDLESEHCIFENIGGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILLGRTnM 548
Cdd:pfam16697   12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLgSGNGTLVNGQRVTELGIaLRPGDRIELGQT-E 87


                   ....*..
gi 530425792   549 FRFNHPK 555
Cdd:pfam16697   88 FCLVPAD 94

MAD

pfam05557

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...

607-1089

2.08e-05

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

Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 49.35 E-value: 2.08e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   607 LEFERQQREELEKleSKRKLIEEMEEKQKSDKAELERMQQevetqRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAE 686
Cdd:pfam05557   43 LDRESDRNQELQK--RIRLLEKREAEAEEALREQAELNRL-----KKKYLEALNKKLNEKESQLADAREVISCLKNELSE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   687 kekfeeerlreqqeieLQKKRQEEETFLRVQE-ELQRLKELNNNEKA------EKFQIFQELDQLQKEKDEQYAKLELEk 759
Cdd:pfam05557  116 ----------------LRRQIQRAELELQSTNsELEELQERLDLLKAkaseaeQLRQNLEKQQSSLAEAEQRIKELEFE- 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   760 krLEEQE---------KEQVMLVAHLEEQLREKQEMIQLLR--RGEVQWVEEEKrdlEGIRESLLRVKEARAGGDEDGEE 828
Cdd:pfam05557  179 --IQSQEqdseivknsKSELARIPELEKELERLREHNKHLNenIENKLLLKEEV---EDLKRKLEREEKYREEAATLELE 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   829 LEKAQLRFFEFK----------------RRQLVKLVNLEKDLVQQKDILKKEVQEEQEILeclkcehdkeSRLLEKHDES 892
Cdd:pfam05557  254 KEKLEQELQSWVklaqdtglnlrspedlSRRIEQLQQREIVLKEENSSLTSSARQLEKAR----------RELEQELAQY 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   893 VTDVTEVPQDFEKIKPVEYRLQ------YKERQL--QYL--------LQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQV 956
Cdd:pfam05557  324 LKKIEDLNKKLKRHKALVRRLQrrvlllTKERDGyrAILesydkeltMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQL 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   957 EKEMEEKEEQLAQYQANANQLQKLQatfeftaniaRQEEKVRKKEKEILESREKQQREALERALARLERRHSALQrhstl 1036
Cdd:pfam05557  404 SVAEEELGGYKQQAQTLERELQALR----------QQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELE----- 468

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530425792  1037 gMEIEEQR-QKLASLNSGSREQSGLQASLEAEQEALEkDQERLEYEIQQLKQKI 1089
Cdd:pfam05557  469 -MELERRClQGDYDPKKTKVLHLSMNPAAEAYQQRKN-QLEKLQAEIERLKRLL 520

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

607-940

2.54e-05

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 2.54e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   607 LEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAE 686
Cdd:TIGR04523  359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL----LEKEIERLKET 434

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   687 KEKFEEERLREQQEI--------ELQKKRQEEETFLRV---------------QEEL-QRLKELN--NNEKAEKFQIFQE 740
Cdd:TIGR04523  435 IIKNNSEIKDLTNQDsvkeliikNLDNTRESLETQLKVlsrsinkikqnleqkQKELkSKEKELKklNEEKKELEEKVKD 514

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   741 LDQLQKEKDEQYAKLELEKKRLEEQ---------EKEQVMLVAHLEEQLREKQEMIqllrrgeVQWVEEEKRDLEGIRES 811
Cdd:TIGR04523  515 LTKKISSLKEKIEKLESEKKEKESKisdledelnKDDFELKKENLEKEIDEKNKEI-------EELKQTQKSLKKKQEEK 587

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   812 LLRVKEARAGGDEDGEELEK-----AQL-RFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKcehDKESRL 885
Cdd:TIGR04523  588 QELIDQKEKEKKDLIKEIEEkekkiSSLeKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR---NKWPEI 664

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530425792   886 LEKHDESVTDVTEVPQDFEKIKPvEYRLQYKERQLQYLLQNHLPtLLEEKQRAFE 940
Cdd:TIGR04523  665 IKKIKESKTKIDDIIELMKDWLK-ELSLHYKKYITRMIRIKDLP-KLEEKYKEIE 717

SMC_N

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

605-1150

2.61e-05

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 2.61e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   605 LRLEFERQQREELEKLESKRKLIEEMEEK--QKSDKAELERMQQEVETQRKETEIVQLQIRKQEES----------LKRR 672
Cdd:pfam02463  444 GKLTEEKEELEKQELKLLKDELELKKSEDllKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLkvllalikdgVGGR 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   673 SFHIENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQY 752
Cdd:pfam02463  524 IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIL 603

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   753 AKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKA 832
Cdd:pfam02463  604 NLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE 683

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   833 QLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKceHDKESRLLEKHDESVTDVTEVPQDFEKIKP-VEY 911
Cdd:pfam02463  684 KAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRV--QEAQDKINEELKLLKQKIDEEEEEEEKSRLkKEE 761

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   912 RLQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKlqatfeftania 991
Cdd:pfam02463  762 KEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK------------ 829

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   992 RQEEKVRKKEKEILES------REKQQREALERALARLERRHSALQRHSTL---------GMEIEEQRQKLASLNSGSRE 1056
Cdd:pfam02463  830 IKEEELEELALELKEEqkleklAEEELERLEEEITKEELLQELLLKEEELEeqklkdeleSKEEKEKEEKKELEEESQKL 909

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  1057 QSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMDARINAYIEEE 1136
Cdd:pfam02463  910 NLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989

                          570
                   ....*....|....
gi 530425792  1137 VQRRLQDLHRVISE 1150
Cdd:pfam02463  990 YNKDELEKERLEEE 1003

GumC

COG3206

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

909-1096

2.79e-05

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.79e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  909 VEYRLQYKERQLQY---LLQNHLPTL---LEEKQRAFEILDR--GPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 980
Cdd:COG3206   162 LEQNLELRREEARKaleFLEEQLPELrkeLEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  981 QATFEftANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSAlqRHStlgmEIEEQRQKLASLNSG-SREQSG 1059
Cdd:COG3206   242 LAALR--AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTP--NHP----DVIALRAQIAALRAQlQQEAQR 313

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 530425792 1060 LQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQ 1096
Cdd:COG3206   314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

614-924

2.87e-05

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: 49.35 E-value: 2.87e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   614 REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQrkETEIVQLQIR-----KQEESLKRRSFHIEN------KLKD 682
Cdd:pfam15921  478 RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT--NAEITKLRSRvdlklQELQHLKNEGDHLRNvqteceALKL 555

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   683 LLAEKEKFeeerlreqqeIELQKKRQEEETFLRVQ----------EELQRLKELNNNEkaekfqifQELDQLQKEKDEQY 752
Cdd:pfam15921  556 QMAEKDKV----------IEILRQQIENMTQLVGQhgrtagamqvEKAQLEKEINDRR--------LELQEFKILKDKKD 617

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   753 AKLELEKKRLEEQEKEQVMLVAHLEEQLRE----KQEMIQLLR-----RGEVQWVEEE----KRDLEGIRESL------- 812
Cdd:pfam15921  618 AKIRELEARVSDLELEKVKLVNAGSERLRAvkdiKQERDQLLNevktsRNELNSLSEDyevlKRNFRNKSEEMetttnkl 697

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   813 -LRVKEARAggdedgeELEKAQ--LRFFEFKRRQLVKL-VNLEKDLVQQK---DILKKEVQ-EEQEILECLKCEH---DK 881
Cdd:pfam15921  698 kMQLKSAQS-------ELEQTRntLKSMEGSDGHAMKVaMGMQKQITAKRgqiDALQSKIQfLEEAMTNANKEKHflkEE 770

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 530425792   882 ESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLL 924
Cdd:pfam15921  771 KNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

852-1089

3.78e-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: 48.22 E-value: 3.78e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  852 KDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEvpqdfeKIKPVEYRLQYKERQLQyllqnhlpTL 931
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR------RIRALEQELAALEAELA--------EL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  932 LEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREK- 1010
Cdd:COG4942    89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAe 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792 1011 --QQREALERALARLERRHSALQRhstlgmEIEEQRQKLASLNSGsreqsglQASLEAEQEALEKDQERLEYEIQQLKQK 1088
Cdd:COG4942   169 leAERAELEALLAELEEERAALEA------LKAERQKLLARLEKE-------LAELAAELAELQQEAEELEALIARLEAE 235


                  .
gi 530425792 1089 I 1089
Cdd:COG4942   236 A 236

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

605-782

5.08e-05

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 5.08e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   605 LRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLL 684
Cdd:TIGR02169  841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE-KKRKRL 919

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   685 AEKEKFEEERLREQQEIELQKKRQEE------------ETFLRVQEELQRLKELNNneKAEkfQIFQELDQLQKEKDEQY 752
Cdd:TIGR02169  920 SELKAKLEALEEELSEIEDPKGEDEEipeeelsledvqAELQRVEEEIRALEPVNM--LAI--QEYEEVLKRLDELKEKR 995

                          170       180       190
                   ....*....|....*....|....*....|
gi 530425792   753 AKLELEKKRLEEqekeqvmLVAHLEEQLRE 782
Cdd:TIGR02169  996 AKLEEERKAILE-------RIEEYEKKKRE 1018

rad50

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

602-891

5.24e-05

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 5.24e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   602 PICLR-LEFERQQREELEKLESKRKL----IEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHI 676
Cdd:TIGR00606  681 PVCQRvFQTEAELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   677 EnKLKDLLAEKEKfeeERLREQQEIELQKKRQEEETFL-RVQEELQRLKELNNNEKAEKFQI-----FQELDQLQKEKDE 750
Cdd:TIGR00606  761 Q-RLKNDIEEQET---LLGTIMPEEESAKVCLTDVTIMeRFQMELKDVERKIAQQAAKLQGSdldrtVQQVNQEKQEKQH 836

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   751 QY----AKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEvQWVEEEKRDLEGIRESLLRVKEARAGGDEDG 826
Cdd:TIGR00606  837 ELdtvvSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ-QFEEQLVELSTEVQSLIREIKDAKEQDSPLE 915

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530425792   827 EELEKAQLRffefkRRQLVKLVNLEKDLVQQK-DILKKEVQEEQEILECL--KCEHDKESRLLEKHDE 891
Cdd:TIGR00606  916 TFLEKDQQE-----KEELISSKETSNKKAQDKvNDIKEKVKNIHGYMKDIenKIQDGKDDYLKQKETE 978

Caldesmon

pfam02029

Caldesmon;

608-890

5.26e-05

Caldesmon;

Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.94 E-value: 5.26e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRK----ETEIVQLQIRKQEESLKRRsfhienkLKDL 683
Cdd:pfam02029   10 ERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQggldEEEAFLDRTAKREERRQKR-------LQEA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   684 LAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNN--------NEKAEKFQIFQELDQLQKEKDEQYAKL 755
Cdd:pfam02029   83 LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRykeeeteiREKEYQENKWSTEVRQAEEEGEEEEDK 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   756 ELEKKRLEEQE--KEQVMLVAHLEEqLREKQEMIQLLRRGEV------QWVEEEKRDLEGIRESLLRVKEARAGGDEDGE 827
Cdd:pfam02029  163 SEEAEEVPTENfaKEEVKDEKIKKE-KKVKYESKVFLDQKRGhpevksQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530425792   828 ELEKAQLRfFEFKRRQLVKLVNLEKDLVQQKdilkkevQEEQEI-LECLKCEHDKESRLLEKHD 890
Cdd:pfam02029  242 VFLEAEQK-LEELRRRRQEKESEEFEKLRQK-------QQEAELeLEELKKKREERRKLLEEEE 297

HEC1

COG5185

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...

605-914

6.63e-05

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

Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 47.64 E-value: 6.63e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  605 LRLEFERQQREELEKLEsKRKLIEEMEEKQKSDKAELERMQQEVE-TQRKETEIVQLQIRKQEESLKRRSFHIEN----- 678
Cdd:COG5185   213 GNLGSESTLLEKAKEII-NIEEALKGFQDPESELEDLAQTSDKLEkLVEQNTDLRLEKLGENAESSKRLNENANNlikqf 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  679 -KLKDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEE----LQRLKELNNNE-----------KAEKFQIFQELD 742
Cdd:COG5185   292 eNTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKREtetgIQNLTAEIEQGqesltenleaiKEEIENIVGEVE 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  743 QLQKEKDEQYAKLELEKKRLE------EQEKEQVMLVAHLEEQLREKQEMIQLLRR---GEVQWVEEEKRDLEGIRESLL 813
Cdd:COG5185   372 LSKSSEELDSFKDTIESTKESldeipqNQRGYAQEILATLEDTLKAADRQIEELQRqieQATSSNEEVSKLLNELISELN 451

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  814 RVKEaraggDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQqkdiLKKEVQEEQEILECLKcehDKESRLLEKHDESV 893
Cdd:COG5185   452 KVMR-----EADEESQSRLEEAYDEINRSVRSKKEDLNEELTQ----IESRVSTLKATLEKLR---AKLERQLEGVRSKL 519

                         330       340
                  ....*....|....*....|.
gi 530425792  894 TDVTEVPQDFEKIKPVEYRLQ 914
Cdd:COG5185   520 DQVAESLKDFMRARGYAHILA 540

PRK12704

phosphodiesterase; Provisional

676-820

6.68e-05

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 6.68e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  676 IENKLKDLLAEKEKfeeerlreqqeiELQKKRQEEEtfLRVQEELQRLKELNNNEKAEKFQIFQELDQ--LQKEK--DEQ 751
Cdd:PRK12704   36 AEEEAKRILEEAKK------------EAEAIKKEAL--LEAKEEIHKLRNEFEKELRERRNELQKLEKrlLQKEEnlDRK 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425792  752 YAKLELEKKRLEEQEKEqvmlVAHLEEQLREKQEMIQLLrrgevqwVEEEKRDLEGIreSLLRVKEARA 820
Cdd:PRK12704  102 LELLEKREEELEKKEKE----LEQKQQELEKKEEELEEL-------IEEQLQELERI--SGLTAEEAKE 157

Borrelia_P83

pfam05262

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.

703-908

7.05e-05

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.

Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.69 E-value: 7.05e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   703 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIF-QELDQLQKEKDEQYAKLELEKKRLEEQEKEqvmlvahLEEQLR 781
Cdd:pfam05262  183 VEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLkEELDKKQIDADKAQQKADFAQDNADKQRDE-------VRQKQQ 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   782 EKQemiQLLRRGEVQWVEEEKRDLEgiresllrvkearaggdEDGEELEKAQLrffEFKRrqlvKLVNLEKDLVQQKDIL 861
Cdd:pfam05262  256 EAK---NLPKPADTSSPKEDKQVAE-----------------NQKREIEKAQI---EIKK----NDEEALKAKDHKAFDL 308

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 530425792   862 KKEVQEEQEILEclkcehdkesrllEKHDESVTDVTEVPQDFEKIKP 908
Cdd:pfam05262  309 KQESKASEKEAE-------------DKELEAQKKREPVAEDLQKTKP 342

COG5022

Myosin heavy chain [General function prediction only];

611-867

9.23e-05

Myosin heavy chain [General function prediction only];

Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.77 E-value: 9.23e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  611 RQQREELekleskRKLIEEMEEKQKSDKAELERMQ-QEVETQRKETEIVQ-----LQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:COG5022   806 LGSRKEY------RSYLACIIKLQKTIKREKKLREtEEVEFSLKAEVLIQkfgrsLKAKKRFSLLKKETIYLQSAQRVEL 879

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  685 AEKEKF-------------EEERLREQQEIELQKKRQE---EETFLRVqEELQRLKELNNNEKAEkfqifqELDQLQKEK 748
Cdd:COG5022   880 AERQLQelkidvksisslkLVNLELESEIIELKKSLSSdliENLEFKT-ELIARLKKLLNNIDLE------EGPSIEYVK 952

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  749 DEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEARAGGDedgeE 828
Cdd:COG5022   953 LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKN-FKKELAELSKQYGALQESTKQLKELPVEVA----E 1027

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 530425792  829 LEKAQLRFFE--FKRRQLVKLVNLEKDLVQQKDILKKEVQE 867
Cdd:COG5022  1028 LQSASKIISSesTELSILKPLQKLKGLLLLENNQLQARYKA 1068

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

606-895

1.04e-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: 47.20 E-value: 1.04e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   606 RLEFERQQRE------ELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQE------------ 666
Cdd:pfam07888   68 REQWERQRRElesrvaELKEeLRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEediktltqrvle 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   667 -----ESLKRRSFHIENKLKDLLAEKEKFEEERLREQQEI-----ELQKKR----QEEETFLRVQEELQRLKELNNN--- 729
Cdd:pfam07888  148 retelERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslskEFQELRnslaQRDTQVLQLQDTITTLTQKLTTahr 227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   730 EKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEE-QLREKQEMIQL------LRRGEVQW----- 797
Cdd:pfam07888  228 KEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQaRLQAAQLTLQLadaslaLREGRARWaqere 307

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   798 -----VEEEKRDLEGIRESLLRVKEARaggDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKeVQEEQEIL 872
Cdd:pfam07888  308 tlqqsAEADKDRIEKLSAELQRLEERL---QEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV-AQKEKEQL 383

                          330       340
                   ....*....|....*....|...
gi 530425792   873 ECLKCEHDKESRLLEKHDESVTD 895
Cdd:pfam07888  384 QAEKQELLEYIRQLEQRLETVAD 406

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

615-1092

1.31e-04

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 1.31e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   615 EELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKD---LLAEKEKFE 691
Cdd:TIGR04523  145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKnksLESQISELK 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   692 EERLREQQEIEL--QKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQ---LQKEKDEQYAKLELEKKRLEeQE 766
Cdd:TIGR04523  225 KQNNQLKDNIEKkqQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLN-NQ 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   767 KEQVmLVAHLEEQLREKQEMIQLLR---RGEVQWVEEEKRDLEGIRESLlrvKEARAGGDEDGEELEKAQLRFFEFKRRQ 843
Cdd:TIGR04523  304 KEQD-WNKELKSELKNQEKKLEEIQnqiSQNNKIISQLNEQISQLKKEL---TNSESENSEKQRELEEKQNEIEKLKKEN 379

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   844 LVKLVNLEK------DLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKiKPVEYRLQYKE 917
Cdd:TIGR04523  380 QSYKQEIKNlesqinDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN-QDSVKELIIKN 458

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   918 rqlqyllqnhLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEftaniarQEEKV 997
Cdd:TIGR04523  459 ----------LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT-------KKISS 521

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   998 RKKEKEILESREKQQREALERALARLERRHSALQRhSTLGMEIEEQRQKLaslnsgsrEQsglqasLEAEQEALEKDQER 1077
Cdd:TIGR04523  522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKK-ENLEKEIDEKNKEI--------EE------LKQTQKSLKKKQEE 586

                          490
                   ....*....|....*
gi 530425792  1078 LEYEIQQLKQKIYEV 1092
Cdd:TIGR04523  587 KQELIDQKEKEKKDL 601

RNase_Y_N

pfam12072

RNase Y N-terminal region;

623-768

1.44e-04

RNase Y N-terminal region;

Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 44.88 E-value: 1.44e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   623 KRKLIEEMEEKQKSdKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIENKlKDLLAEKEKfeeerlrEQQEIE 702
Cdd:pfam12072   52 KEALLEAKEEIHKL-RAEAER---ELKERRNELQRQERRLLQKEETLDRKDESLEKK-EESLEKKEK-------ELEAQQ 119

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530425792   703 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFqeLDQLQKEKDEQYAKL--ELEKKRLEEQEKE 768
Cdd:pfam12072  120 QQLEEKEEELEELIEEQRQELERISGLTSEEAKEIL--LDEVEEELRHEAAVMikEIEEEAKEEADKK 185

COG1340

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

622-894

1.55e-04

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 1.55e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  622 SKRKLIEEMEEKQKSDKAELERMQQEVETQRKEteivqlqIRKQEESLKRRSFHIENKLKDLLAEKEkfeeerlreqqei 701
Cdd:COG1340     1 SKTDELSSSLEELEEKIEELREEIEELKEKRDE-------LNEELKELAEKRDELNAQVKELREEAQ------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  702 ELQKKRQEeetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE------QYAKLELEKKRLE----------EQ 765
Cdd:COG1340    61 ELREKRDE------LNEKVKELKEERDELNEKLNELREELDELRKELAElnkaggSIDKLRKEIERLEwrqqtevlspEE 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  766 EKEQVMLVAHLEEQLREKQEMiqllrrgevqwvEEEKRDLEGIRESLLRVK-EARAGGDEDGEELEKAQLrffefKRRQL 844
Cdd:COG1340   135 EKELVEKIKELEKELEKAKKA------------LEKNEKLKELRAELKELRkEAEEIHKKIKELAEEAQE-----LHEEM 197

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 530425792  845 VKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVT 894
Cdd:COG1340   198 IELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247

DUF5401

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

608-763

1.65e-04

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

Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 1.65e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   608 EFERQQREELEKLESKRKLiEEMEEKQKSDKAELERMQQEvetqRKETEIVQLQIRKQE-ESLKRRSFHIENKLKDLLAE 686
Cdd:pfam17380  447 EMERVRLEEQERQQQVERL-RQQEEERKRKKLELEKEKRD----RKRAEEQRRKILEKElEERKQAMIEEERKRKLLEKE 521

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   687 KEKFEEERLREQQEIELQKKR---QEEETFLRVQEELQRLKElnnnEKAekfqifqELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:pfam17380  522 MEERQKAIYEEERRREAEEERrkqQEMEERRRIQEQMRKATE----ERS-------RLEAMEREREMMRQIVESEKARAE 590

rad50

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

604-921

1.81e-04

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 1.81e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   604 CLRLEFERQQREELEKLESKRKLIEEMEEKqksDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRS----FHIENK 679
Cdd:TIGR00606  498 TLKKEVKSLQNEKADLDRKLRKLDQEMEQL---NHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSllgyFPNKKQ 574

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   680 LKDLLAEKEKfeeerlreqqeielqKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKE-------KDEQy 752
Cdd:TIGR00606  575 LEDWLHSKSK---------------EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgsQDEE- 638

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   753 AKLELEKKRLEEQEKEQVMLVA-------HLEEQLREKQEMIQLLRRgeVQWVEEEKRDLEGIRESLLRVKEARAggded 825
Cdd:TIGR00606  639 SDLERLKEEIEKSSKQRAMLAGatavysqFITQLTDENQSCCPVCQR--VFQTEAELQEFISDLQSKLRLAPDKL----- 711

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   826 gEELEKaQLRFFEFKRRQLVKLVNLEKDLVQQKDilkKEVQEEQEILECLKCEHDKESRLLEKHDESV------------ 893
Cdd:TIGR00606  712 -KSTES-ELKKKEKRRDEMLGLAPGRQSIIDLKE---KEIPELRNKLQKVNRDIQRLKNDIEEQETLLgtimpeeesakv 786

                          330       340       350
                   ....*....|....*....|....*....|
gi 530425792   894 --TDVTEVPQDFEKIKPVEYRLQYKERQLQ 921
Cdd:TIGR00606  787 clTDVTIMERFQMELKDVERKIAQQAAKLQ 816

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

611-1147

2.08e-04

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: 46.65 E-value: 2.08e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   611 RQQREELEKLESKRKL-IEEMEEKQKSDKAELERMQQEVEtqrketeIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEk 689
Cdd:pfam15921  263 QQHQDRIEQLISEHEVeITGLTEKASSARSQANSIQSQLE-------IIQEQARNQNSMYMRQLSDLESTVSQLRSELR- 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   690 feeerlreqqeielQKKRQEEETFlrvqEELQRLKELNNNE----KAEKFQIFQEL----DQLQK-----EKDEQYAKLE 756
Cdd:pfam15921  335 --------------EAKRMYEDKI----EELEKQLVLANSElteaRTERDQFSQESgnldDQLQKlladlHKREKELSLE 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   757 LEK-KRLEEQEKEQVMLVAHLEEQLREKQEMIQLLrrgevqwveeekrdlegirESLLRVKEARAGGdedgeELEKaQLR 835
Cdd:pfam15921  397 KEQnKRLWDRDTGNSITIDHLRRELDDRNMEVQRL-------------------EALLKAMKSECQG-----QMER-QMA 451

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   836 FFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQeileclkcehdKESRLLEKHDESVTDVTevpqdfekikpveyrlqy 915
Cdd:pfam15921  452 AIQGKNESLEKVSSLTAQLESTKEMLRKVVEELT-----------AKKMTLESSERTVSDLT------------------ 502

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   916 kerqlqyllqnhlpTLLEEKQRAFEildrgplSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQAtfeftaniarqee 995
Cdd:pfam15921  503 --------------ASLQEKERAIE-------ATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQT------------- 548

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   996 kvrkkekeilesrekqQREALERALARLERrhsalqrhstlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQ 1075
Cdd:pfam15921  549 ----------------ECEALKLQMAEKDK-------------VIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI 599

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530425792  1076 ERLEYEIQQLKqkiyevdgVQKDHHGT----LEGKVASSSLpvsaEKSHLVPLMDARINAyIEEEVQRRLQDLHRV 1147
Cdd:pfam15921  600 NDRRLELQEFK--------ILKDKKDAkireLEARVSDLEL----EKVKLVNAGSERLRA-VKDIKQERDQLLNEV 662

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

757-1091

2.09e-04

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 2.09e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   757 LEKKRLEEQEKEQVMLV--------AHLEEQLREKQEMIQLLRRGEVQwVEEEKRDLEGIRESL-LRVKEARAGGDEDGE 827
Cdd:pfam07888    9 LEEESHGEEGGTDMLLVvpraellqNRLEECLQERAELLQAQEAANRQ-REKEKERYKRDREQWeRQRRELESRVAELKE 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   828 ELEKAQLRFFEFKRRQlVKLVNLEKDLVQQKDILKKEVQE-EQEILEclkCEHDKESrLLEKHDESVTDVTEVPQDFEKI 906
Cdd:pfam07888   88 ELRQSREKHEELEEKY-KELSASSEELSEEKDALLAQRAAhEARIRE---LEEDIKT-LTQRVLERETELERMKERAKKA 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   907 KPVEYRLQYKERQLQYLLQ------NHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 980
Cdd:pfam07888  163 GAQRKEEEAERKQLQAKLQqteeelRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSL 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   981 QATFeftaNIARQEEKVRKKEKEILESREKQQREALERalARLERRHSALQRhSTLGMEIEEQRQKLAslnsgsREQSGL 1060
Cdd:pfam07888  243 QERL----NASERKVEGLGEELSSMAAQRDRTQAELHQ--ARLQAAQLTLQL-ADASLALREGRARWA------QERETL 309

                          330       340       350
                   ....*....|....*....|....*....|.
gi 530425792  1061 QASLEAEQEALEKdqerLEYEIQQLKQKIYE 1091
Cdd:pfam07888  310 QQSAEADKDRIEK----LSAELQRLEERLQE 336

CCDC158

pfam15921

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...

706-1096

2.12e-04

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: 46.26 E-value: 2.12e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   706 KRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQ-------ELDQLQKEKDeqyAKLELEKKRLEEQE--KEQVMLVAH- 775
Cdd:pfam15921   77 ERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidlqtKLQEMQMERD---AMADIRRRESQSQEdlRNQLQNTVHe 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   776 -------LEEQLREKQEMIQLLRRGEVQwveeEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLV 848
Cdd:pfam15921  154 leaakclKEDMLEDSNTQIEQLRKMMLS----HEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILREL 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   849 NLEKDLVQ--------QKDILKKEVQEEQEILecLKCEHDKESRLLEKHDESVTDVTEVPQDFE-KIKPVEYRLQYKERQ 919
Cdd:pfam15921  230 DTEISYLKgrifpvedQLEALKSESQNKIELL--LQQHQDRIEQLISEHEVEITGLTEKASSARsQANSIQSQLEIIQEQ 307

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   920 LQ-----YLLQ--------NHLPTLLEEKQRAFEI----LDRGPLSLDNTLYQVEKEMEekeeQLAQYQANAN-QLQKLQ 981
Cdd:pfam15921  308 ARnqnsmYMRQlsdlestvSQLRSELREAKRMYEDkieeLEKQLVLANSELTEARTERD----QFSQESGNLDdQLQKLL 383

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   982 ATFE------------------------FTANIARQEEKVRKKEKEILESREKQQRE----ALERALARLERRHSALQRH 1033
Cdd:pfam15921  384 ADLHkrekelslekeqnkrlwdrdtgnsITIDHLRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEKV 463

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  1034 STLGMEIEEQRQKL-----------ASLNSGSREQSGLQASLEAEQEALE-------KDQERLEYEIQQLKQKIYEVDGV 1095
Cdd:pfam15921  464 SSLTAQLESTKEMLrkvveeltakkMTLESSERTVSDLTASLQEKERAIEatnaeitKLRSRVDLKLQELQHLKNEGDHL 543


                   .
gi 530425792  1096 Q 1096
Cdd:pfam15921  544 R 544

PRK05771

V-type ATP synthase subunit I; Validated

551-820

2.37e-04

V-type ATP synthase subunit I; Validated

Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.37e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  551 FNHPKEAAKLREKRKSgllssfslsMTDLSKSRENLSAVMLYNPGLFPIKGPICLR--LEFERQQREELEKLESKrklIE 628
Cdd:PRK05771   36 LKEELSNERLRKLRSL---------LTKLSEALDKLRSYLPKLNPLREEKKKVSVKslEELIKDVEEELEKIEKE---IK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  629 EMEEKqksdKAELERMQQEVETQRKETEI-----VQLQIRKQEESLKRRSFHI-ENKLKDLLAEKEKFEEERLREQQE-- 700
Cdd:PRK05771  104 ELEEE----ISELENEIKELEQEIERLEPwgnfdLDLSLLLGFKYVSVFVGTVpEDKLEELKLESDVENVEYISTDKGyv 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  701 --IELQKKRQEEEtflrVQEELQRLkELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEE 778
Cdd:PRK05771  180 yvVVVVLKELSDE----VEEELKKL-GFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYE 254

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 530425792  779 QL---REKQEM-IQLLRRGEV----QWVEEEkrDLEGIRESLLRVKEARA 820
Cdd:PRK05771  255 YLeieLERAEAlSKFLKTDKTfaieGWVPED--RVKKLKELIDKATGGSA 302

Caldesmon

pfam02029

Caldesmon;

608-786

2.50e-04

Caldesmon;

Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 2.50e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   608 EFERQQREELEKLESKRKLIEEMEeKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSfhiENKLKDLLAEK 687
Cdd:pfam02029  147 TEVRQAEEEGEEEEDKSEEAEEVP-TENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQN---GEEEVTKLKVT 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   688 EKFEEERLREQQEIELQKKRQEEeTFLRVQEELQRLKELNNNE----KAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:pfam02029  223 TKRRQGGLSQSQEREEEAEVFLE-AEQKLEELRRRRQEKESEEfeklRQKQQEAELELEELKKKREERRKLLEEEEQRRK 301

                          170       180
                   ....*....|....*....|...
gi 530425792   764 EQEKEQvmLVAHLEEQLREKQEM 786
Cdd:pfam02029  302 QEEAER--KLREEEEKRRMKEEI 322

CAF-1_p150

pfam11600

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...

703-821

2.71e-04

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

Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 43.52 E-value: 2.71e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   703 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAhlEEQLRE 782
Cdd:pfam11600   18 LEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEKEKAEKLRLK--EEKRKE 95

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 530425792   783 KQEMIQlLRRGEVQWVEEEKRdlegIRESLLRVKEARAG 821
Cdd:pfam11600   96 KQEALE-AKLEEKRKKEEEKR----LKEEEKRIKAEKAE 129

PRK12704

phosphodiesterase; Provisional

624-788

2.81e-04

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.81e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  624 RKLIEEMEEKQKSDKAELERmqqEVETQRKETEIVQlqirkQEESLKRRSfHIENKLKDLLAEkekfeeerlreQQEIEl 703
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEAKK---EAEAIKKEALLEA-----KEEIHKLRN-EFEKELRERRNE-----------LQKLE- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  704 QKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKlelEKKRLEE-----QEKEQVMLVAHLEE 778
Cdd:PRK12704   89 KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELERisgltAEEAKEILLEKVEE 165

                         170
                  ....*....|.
gi 530425792  779 QLR-EKQEMIQ 788
Cdd:PRK12704  166 EARhEAAVLIK 176

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

704-888

2.98e-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: 45.14 E-value: 2.98e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  704 QKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE---QYAKLELEKKRLEEQEKEQVMLVAHLEEQL 780
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAlarRIRALEQELAALEAELAELEKEIAELRAEL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  781 REKQEMI--------------------------QLLRRGEV--QWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEkA 832
Cdd:COG4942   100 EAQKEELaellralyrlgrqpplalllspedflDAVRRLQYlkYLAPARREQAEELRADLAELAALRAELEAERAELE-A 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530425792  833 QLRFFEFKRRQLVKLVNLEKDLVQQkdiLKKEVQEEQEILECLKCEHDKESRLLEK 888
Cdd:COG4942   179 LLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIAR 231

PTZ00121

MAEBL; Provisional

623-910

3.64e-04

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 3.64e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  623 KRKLIEEMEEKQKSDKA-ELERMQQEVETQRKETEivqlqIRKQEESLKRRSFHIENKLKDLLAEKEKfeeerlreqqei 701
Cdd:PTZ00121 1062 AKAHVGQDEGLKPSYKDfDFDAKEDNRADEATEEA-----FGKAEEAKKTETGKAEEARKAEEAKKKA------------ 1124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  702 elQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKlelEKKRLEEQEKEQVMLVAhleEQLR 781
Cdd:PTZ00121 1125 --EDARKAEEA--RKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE---DAKKAEAARKAEEVRKA---EELR 1194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  782 EKQEM--IQLLRRGEVQWVEEEKRDLEGIR--ESLLRVKEARaggdEDGEELEKAQ--LRFFEFKRRQLVKLVNLEKDLV 855
Cdd:PTZ00121 1195 KAEDArkAEAARKAEEERKAEEARKAEDAKkaEAVKKAEEAK----KDAEEAKKAEeeRNNEEIRKFEEARMAHFARRQA 1270

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530425792  856 QQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVE 910
Cdd:PTZ00121 1271 AIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325

FHA

pfam00498

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.

478-543

3.73e-04

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.

Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 40.25 E-value: 3.73e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425792   478 TYVGRDDastEQDIVLHGLDLESEHCIFENI-GGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILL 543
Cdd:pfam00498    1 VTIGRSP---DCDIVLDDPSVSRRHAEIRYDgGGRFYLEDLgSTNGTFVNGQRLGPEPVrLKDGDVIRL 66

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

608-872

3.74e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 3.74e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKEteivQLQIRKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:COG4372    77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE----RQDLEQQRKQLEAQIAELQSEIAEREEEL 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  688 EKFEEERLREQQEIELQKKRQEEETFLRVQEELQRL-KELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEK-KRLEEQ 765
Cdd:COG4372   153 KELEEQLESLQEELAALEQELQALSEAEAEQALDELlKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDsLEAKLG 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  766 EKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLV 845
Cdd:COG4372   233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312

                         250       260
                  ....*....|....*....|....*..
gi 530425792  846 KLVNLEKDLVQQKDILKKEVQEEQEIL 872
Cdd:COG4372   313 LEDALLAALLELAKKLELALAILLAEL 339

FHA_Ki67

cd22673

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...

473-551

3.80e-04

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.

Pssm-ID: 438725 [Multi-domain] Cd Length: 95 Bit Score: 41.43 E-value: 3.80e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  473 LKEGQTYVGRDDASteqDIVLHGLDLESEHC-IFENIGGTVTLIPLSGS-QCSVNGVQIVEATHLNQGAVILLGrTNMFR 550
Cdd:cd22673    18 LTKKSCTFGRDLSC---DIRIQLPGVSREHCrIEVDENGKAYLENLSTTnPTLVNGKAIEKSAELKDGDVITIG-GRSFR 93


                  .
gi 530425792  551 F 551
Cdd:cd22673    94 F 94

Caldesmon

pfam02029

Caldesmon;

621-772

4.29e-04

Caldesmon;

Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 4.29e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   621 ESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEiVQLQIRKQEESLKRRSFHIENklkdllAEKEKFEEERLREQQE 700
Cdd:pfam02029  206 EVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE-VFLEAEQKLEELRRRRQEKES------EEFEKLRQKQQEAELE 278

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530425792   701 IELQKKRQEEETFLRVQEELQRlkelnNNEKAEKfqifqeldQLQKEKDEQYAKLELEKKRLEEQEKEQVML 772
Cdd:pfam02029  279 LEELKKKREERRKLLEEEEQRR-----KQEEAER--------KLREEEEKRRMKEEIERRRAEAAEKRQKLP 337

PHA02562

endonuclease subunit; Provisional

618-861

5.34e-04

endonuclease subunit; Provisional

Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 5.34e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  618 EKLESKRKLIEEMEEKQKSDKAELERMqqeVETQRKETEivqlQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLRE 697
Cdd:PHA02562  195 QQIKTYNKNIEEQRKKNGENIARKQNK---YDELVEEAK----TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKI 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  698 QQEIELQKKrqeEETFLRVQEE----LQRLKElnNNEKAEKfqIFQELDQLQKekdeqyaKLELEKKRLEEQEKeqvmlv 773
Cdd:PHA02562  268 KSKIEQFQK---VIKMYEKGGVcptcTQQISE--GPDRITK--IKDKLKELQH-------SLEKLDTAIDELEE------ 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  774 ahLEEQLREKQEMIQLLRRGevqwVEEEKRDLEGIRESLLRVK----EARAGGDEDGEELEKAQlrffefkrRQLVKLVN 849
Cdd:PHA02562  328 --IMDEFNEQSKKLLELKNK----ISTNKQSLITLVDKAKKVKaaieELQAEFVDNAEELAKLQ--------DELDKIVK 393

                         250
                  ....*....|..
gi 530425792  850 LEKDLVQQKDIL 861
Cdd:PHA02562  394 TKSELVKEKYHR 405

EnvC

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

608-713

6.06e-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: 44.37 E-value: 6.06e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:COG4942   143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222

                          90       100
                  ....*....|....*....|....*.
gi 530425792  688 EKFEEERLREQQEIELQKKRQEEETF 713
Cdd:COG4942   223 EELEALIARLEAEAAAAAERTPAAGF 248

GBP_C

cd16269

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...

618-818

6.09e-04

Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.11 E-value: 6.09e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  618 EKLESKRKLIEEMEEKqksdKAELERMQQEVETQRKETEIVQLqIRKQEESLKRRSFHIENKLKDLLAEKEKFeeerlre 697
Cdd:cd16269    87 EDQKFQKKLMEQLEEK----KEEFCKQNEEASSKRCQALLQEL-SAPLEEKISQGSYSVPGGYQLYLEDREKL------- 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  698 qqeieLQKKRQEEETFLRVQEELQR-LKELNNNEKAEKfQIFQELDQLQKEKDEQYAK---LELEKKRLEEQEKEQVMLv 773
Cdd:cd16269   155 -----VEKYRQVPRKGVKAEEVLQEfLQSKEAEAEAIL-QADQALTEKEKEIEAERAKaeaAEQERKLLEEQQRELEQK- 227

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 530425792  774 ahLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEA 818
Cdd:cd16269   228 --LEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEA 270

MAD

pfam05557

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...

610-867

7.47e-04

Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.35 E-value: 7.47e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQ--LQIRKQEESLKRRSfhieNKLKDLLAEK 687
Cdd:pfam05557  310 EKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRaiLESYDKELTMSNYS----PQLLERIEEA 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   688 EKFEEERLREQQEIELQKKRQEEETFLRVQE------ELQRLKElnNNEKAEKFQIFQELDQLQKEKDEqyakLELEKKR 761
Cdd:pfam05557  386 EDMTQKMQAHNEEMEAQLSVAEEELGGYKQQaqtlerELQALRQ--QESLADPSYSKEEVDSLRRKLET----LELERQR 459

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   762 LEEQEKEQVMLVAHLEeqLREKQEM-----IQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRF 836
Cdd:pfam05557  460 LREQKNELEMELERRC--LQGDYDPkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETT 537

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 530425792   837 FEFKRRQLVKL----VNLEKDLVQQKDILKKEVQE 867
Cdd:pfam05557  538 STMNFKEVLDLrkelESAELKNQRLKEVFQAKIQE 572

DUF4515

pfam14988

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...

607-790

9.56e-04

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.

Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 42.45 E-value: 9.56e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   607 LEFERQQREELEKLESK-----RKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESL---KRRSFHIEN 678
Cdd:pfam14988    6 LEYLAKKTEEKQKKIEKlwnqyVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALrpfAKLKESQER 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   679 KLKDLLAEKEKFEEERLREQQEIELQkkRQEEETFLRVQEELQRLKEL---NNNEKAEKFQ----------------IFQ 739
Cdd:pfam14988   86 EIQDLEEEKEKVRAETAEKDREAHLQ--FLKEKALLEKQLQELRILELgerATRELKRKAQalklaakqalsefcrsIKR 163

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530425792   740 ELDQLQKE---KDEQYAKLELEKKRLEEQEKeqvmlvahleeQLREKQEMIQLL 790
Cdd:pfam14988  164 ENRQLQKEllqLIQETQALEAIKSKLENRKQ-----------RLKEEQWYLEAL 206

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

605-807

1.18e-03

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 1.18e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   605 LRLEFERQQRE---ELEKLESKRKLIEEMEEKQKSDKAELER----MQQEVETQRKETEIVQ-----LQIRKQEESLKRR 672
Cdd:pfam05483  553 VREEFIQKGDEvkcKLDKSEENARSIEYEVLKKEKQMKILENkcnnLKKQIENKNKNIEELHqenkaLKKKGSAENKQLN 632

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   673 SFHIE-NKLK-DLLAEKEKFEEERLREQQEIELQKKRQE------EETFLRVQEELQRLKELnnnEKAEKFQIFQELDQL 744
Cdd:pfam05483  633 AYEIKvNKLElELASAKQKFEEIIDNYQKEIEDKKISEEklleevEKAKAIADEAVKLQKEI---DKRCQHKIAEMVALM 709

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530425792   745 QKEKdEQYAKLELEKKR----LEEQEKEQVMLVAHLEEQLRE-KQEMIQLLRRGEVQWVEEEKRDLEG 807
Cdd:pfam05483  710 EKHK-HQYDKIIEERDSelglYKNKEQEQSSAKAALEIELSNiKAELLSLKKQLEIEKEEKEKLKMEA 776

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

716-1085

1.27e-03

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 1.27e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   716 VQEELQRLKELN--------NNEKAEKFQIFQELDQLQKEKDEQYAKLeLEKKRLEEQEKEQVMLVAHLEEQLREKQEMI 787
Cdd:pfam13868    1 LRENSDELRELNskllaakcNKERDAQIAEKKRIKAEEKEEERRLDEM-MEEERERALEEEEEKEEERKEERKRYRQELE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   788 QLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAggdedgEELEKAQLRFFEFKR-RQLVKLVNLEKDLVQQKDIlKKEVQ 866
Cdd:pfam13868   80 EQIEEREQKRQEEYEEKLQEREQMDEIVERIQE------EDQAEAEEKLEKQRQlREEIDEFNEEQAEWKELEK-EEERE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   867 EEQEILECLKcehDKESRLLEKHDESvtdvtevpqdfekikpveyRLQYKERQLqylLQNHLPTLLEEKQRAFEILDRgp 946
Cdd:pfam13868  153 EDERILEYLK---EKAEREEEREAER-------------------EEIEEEKER---EIARLRAQQEKAQDEKAERDE-- 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   947 lsLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATF-EFTANIARQEEKVRKKEKEILESREKQQREALERALARLER 1025
Cdd:pfam13868  206 --LRAKLYQEEQERKERQKEREEAEKKARQRQELQQAReEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEK 283

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530425792  1026 RHSALQRHST-LGMEIEEQRQKLAslnsgsREQSGLQASLEAEQEALEKDQERLEYEIQQL 1085
Cdd:pfam13868  284 RRMKRLEHRReLEKQIEEREEQRA------AEREEELEEGERLREEEAERRERIEEERQKK 338

Mitofilin

pfam09731

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...

611-727

1.89e-03

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: 43.21 E-value: 1.89e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   611 RQQREELEKLEskRKLIEEMEEKQKSDKAELERMQQ-EVETQRKETE-IVQLQIRKQEESlkrrsfhIENKLKDLLAEKE 688
Cdd:pfam09731  319 EKQKEELDKLA--EELSARLEEVRAADEAQLRLEFErEREEIRESYEeKLRTELERQAEA-------HEEHLKDVLVEQE 389

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 530425792   689 kfeeerlreqqeIELQKKRQEEETFLRVQEELQRLKELN 727
Cdd:pfam09731  390 ------------IELQREFLQDIKEKVEEERAGRLLKLN 416

CwlO1

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

611-689

1.89e-03

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.89e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425792  611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:COG3883   129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207

TACC_C

pfam05010

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...

632-792

2.12e-03

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: 41.59 E-value: 2.12e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   632 EKQKSDKAELERMQQEVETqrKETEIVQLQIRKQEEslkrrsfHIEN-KLKDLLAEKEKfeeeRLREQQEIELQKKRQEE 710
Cdd:pfam05010    1 YSQKDMDAALEKARNEIEE--KELEINELKAKYEEL-------RRENlEMRKIVAEFEK----TIAQMIEEKQKQKELEH 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   711 ETFLRVQEELQRLK-ELNNNEKAeKFQIFQELDQlQKEKDEQYAKLELEKK--------RLEEQEKEQVMLVAHLEEQLR 781
Cdd:pfam05010   68 AEIQKVLEEKDQALaDLNSVEKS-FSDLFKRYEK-QKEVISGYKKNEESLKkcaqdylaRIKKEEQRYQALKAHAEEKLD 145

                          170
                   ....*....|.
gi 530425792   782 EKQEMIQLLRR 792
Cdd:pfam05010  146 QANEEIAQVRS 156

COG4026

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...

624-782

2.48e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];

Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 42.02 E-value: 2.48e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  624 RKLIEEMEEKQKSDKAELERMQ---------QEVETQRKETE--IVQ-----LQIRKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:COG4026    72 RELAEKFFEELKGMVGHVERMKlplghdveyVDVELVRKEIKnaIIRaglksLQNIPEYNELREELLELKEKIDEIAKEK 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  688 EKFEEERLreqqeiELQKKRQEeetflrVQEELQRLKElnnnekaekfqifqELDQLQKEKDEQYAKLELEKKRLEEQEK 767
Cdd:COG4026   152 EKLTKENE------ELESELEE------LREEYKKLRE--------------ENSILEEEFDNIKSEYSDLKSRFEELLK 205

                         170
                  ....*....|....*
gi 530425792  768 EQVMLVAHLEEQLRE 782
Cdd:COG4026   206 KRLLEVFSLEELWKE 220

DUF5401

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

605-689

2.50e-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: 42.80 E-value: 2.50e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   605 LRLEFERQQREELEKlESKRKLIE-EMEEKQKSDKAELERMQQEvETQRKETEI-----VQLQIRK-QEESLKRRSFHIE 677
Cdd:pfam17380  497 LEKELEERKQAMIEE-ERKRKLLEkEMEERQKAIYEEERRREAE-EERRKQQEMeerrrIQEQMRKaTEERSRLEAMERE 574

                           90
                   ....*....|..
gi 530425792   678 NKLKDLLAEKEK 689
Cdd:pfam17380  575 REMMRQIVESEK 586

PRK12704

phosphodiesterase; Provisional

966-1091

2.92e-03

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.92e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  966 QLAQYQANaNQLQKLQATFEFTANIARQEEKVrkkekeiLESREKQQREALERALARLERRHSALQRH----STLGMEIE 1041
Cdd:PRK12704   56 KEALLEAK-EEIHKLRNEFEKELRERRNELQK-------LEKRLLQKEENLDRKLELLEKREEELEKKekelEQKQQELE 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530425792 1042 EQRQKLASLNSGSREQ----SGLQASlEAEQEALEKDQERLEYEIQQLKQKIYE 1091
Cdd:PRK12704  128 KKEEELEELIEEQLQEleriSGLTAE-EAKEILLEKVEEEARHEAAVLIKEIEE 180

rad50

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

621-1096

3.15e-03

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 3.15e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   621 ESKRKLIEEMEEKQKSDK--------AELERMQQEVETQRKETEIVQLQiRKQEESLKRRSFHIENKLKDLLAEKEKFEE 692
Cdd:TIGR00606  160 DSNWPLSEGKALKQKFDEifsatryiKALETLRQVRQTQGQKVQEHQME-LKYLKQYKEKACEIRDQITSKEAQLESSRE 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   693 ERLREQQEIELQKKRQEE-----ETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKR-LEEQE 766
Cdd:TIGR00606  239 IVKSYENELDPLKNRLKEiehnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRtVREKE 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   767 KEQVMLVAHLEEQLREKQEMIQ-----LLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGD--EDGEELEKAQLRFFEF 839
Cdd:TIGR00606  319 RELVDCQRELEKLNKERRLLNQektelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDgfERGPFSERQIKNFHTL 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   840 KRRQL---VKLVNLEKDLVQQKDILKKEVQEEQEI-LECLKCEHDKESRLLEKHDESVTDVTEVPQDFE----KIKPVEY 911
Cdd:TIGR00606  399 VIERQedeAKTAAQLCADLQSKERLKQEQADEIRDeKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgssdRILELDQ 478

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   912 RLQYKERQLQYLLQNhlpTLLEEKQRAFEILDRGPLSLDNTLyqvekemeekeEQLAQYQAnanQLQKLQATFEFTANIA 991
Cdd:TIGR00606  479 ELRKAERELSKAEKN---SLTETLKKEVKSLQNEKADLDRKL-----------RKLDQEME---QLNHHTTTRTQMEMLT 541

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   992 RQEEKVRKKEKEIlesrEKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSreqsglqASLEAEQEAL 1071
Cdd:TIGR00606  542 KDKMDKDEQIRKI----KSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKEL-------ASLEQNKNHI 610

                          490       500
                   ....*....|....*....|....*
gi 530425792  1072 EKDQERLEYEIQQLKQKIYEVDGVQ 1096
Cdd:TIGR00606  611 NNELESKEEQLSSYEDKLFDVCGSQ 635

PRK00409

recombination and DNA strand exchange inhibitor protein; Reviewed

626-794

3.28e-03

recombination and DNA strand exchange inhibitor protein; Reviewed

Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.28e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  626 LIEEMEEKQKSDKAELERMQQEVETQRKETEivqlQIRKQEESLKRRsfhIENKLKDLLAEKEKFEEErlreqqeIELQK 705
Cdd:PRK00409  503 IIEEAKKLIGEDKEKLNELIASLEELERELE----QKAEEAEALLKE---AEKLKEELEEKKEKLQEE-------EDKLL 568

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  706 KRQEEEtflrVQEELQRLKElnnnekaEKFQIFQELDQLQKEKDEQYAKLELE--KKRLEEQEKEqvmlvahLEEQLREK 783
Cdd:PRK00409  569 EEAEKE----AQQAIKEAKK-------EADEIIKELRQLQKGGYASVKAHELIeaRKRLNKANEK-------KEKKKKKQ 630

                         170
                  ....*....|.
gi 530425792  784 QEMIQLLRRGE 794
Cdd:PRK00409  631 KEKQEELKVGD 641

ATG16

pfam08614

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...

707-806

3.42e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.

Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 40.30 E-value: 3.42e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   707 RQEEETFLRVQEEL-QRLKELNNnekaekfqifqELDQLQKekdeqyaKLELEKKRLEEQEKEQVML---VAHLEEQLRE 782
Cdd:pfam08614   63 REELAELYRSRGELaQRLVDLNE-----------ELQELEK-------KLREDERRLAALEAERAQLeekLKDREEELRE 124

                           90       100       110
                   ....*....|....*....|....*....|
gi 530425792   783 KQEMIQLLR------RGEVQWVEEEKRDLE 806
Cdd:pfam08614  125 KRKLNQDLQdelvalQLQLNMAEEKLRKLE 154

PRK12704

phosphodiesterase; Provisional

612-689

3.81e-03

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.81e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425792  612 QQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:PRK12704   68 KLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

612-921

3.89e-03

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 3.89e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   612 QQREELEklESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEkfe 691
Cdd:TIGR00618  577 QCDNRSK--EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL--- 651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   692 eerlreqqEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQ------ELDQLQKEKDEQYAKLELEKKRLEEQ 765
Cdd:TIGR00618  652 --------QLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQltywkeMLAQCQTLLRELETHIEEYDREFNEI 723

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   766 EKEQVMLVAHLEEQLREKQEMIQLLRRgevqwveEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQlRFFEFKRRQLV 845
Cdd:TIGR00618  724 ENASSSLGSDLAAREDALNQSLKELMH-------QARTVLKARTEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLRE 795

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425792   846 KLVNLEKDLVQQKDILKKEVQEEQEiLECLKCEHDKE---SRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQ 921
Cdd:TIGR00618  796 EDTHLLKTLEAEIGQEIPSDEDILN-LQCETLVQEEEqflSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQ 873

SMC_prok_A

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

778-1086

4.19e-03

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 4.19e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   778 EQLREKQEMIQLlRRGEVQWVEEEKRD----LEGIRESLLRVKEARaggDEDGEELEKAQLRFFEFKRRQLVKLVNLEKD 853
Cdd:TIGR02169  173 EKALEELEEVEE-NIERLDLIIDEKRQqlerLRREREKAERYQALL---KEKREYEGYELLKEKEALERQKEAIERQLAS 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   854 LVQQKDILKKEVQE-EQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFE-KIKPVEYRLQYKERQLQyllqnhlpTL 931
Cdd:TIGR02169  249 LEEELEKLTEEISElEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELE--------DA 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   932 LEEKQRAFEILDRgplsldntlyqVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQ 1011
Cdd:TIGR02169  321 EERLAKLEAEIDK-----------LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425792  1012 QREALE---RALARLERRHSALQ-RHSTLGMEIEEQRQKLASLNSGSREqsgLQASLEAEQEALEKDQERLEYEIQQLK 1086
Cdd:TIGR02169  390 YREKLEklkREINELKRELDRLQeELQRLSEELADLNAAIAGIEAKINE---LEEEKEDKALEIKKQEWKLEQLAADLS 465

FHA_RADIL

cd22733

forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...

452-554

4.30e-03

forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.

Pssm-ID: 438785 Cd Length: 113 Bit Score: 39.01 E-value: 4.30e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  452 ELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGT-------VTLIPLSGSQCSV 524
Cdd:cd22733     4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRRVRLPkhrseekLVLEPIPGAHVSV 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 530425792  525 NGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22733    84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113

Filament

pfam00038

Intermediate filament protein;

605-791

4.48e-03

Intermediate filament protein;

Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 4.48e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   605 LRLEFERQQREELE-KLESKRKLIEEmEEKQKSD-KAELERMQQEVETQRK--ETEIVQLQIRKQEESL-----KRRSFH 675
Cdd:pfam00038   89 QKYEDELNLRTSAEnDLVGLRKDLDE-ATLARVDlEAKIESLKEELAFLKKnhEEEVRELQAQVSDTQVnvemdAARKLD 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   676 IENKLKDLLAEKEKFEeerlreqqeielQKKRQE-EETFLRVQEELQRLKELNNNE-KAEKFQIFQ----------ELDQ 743
Cdd:pfam00038  168 LTSALAEIRAQYEEIA------------AKNREEaEEWYQSKLEELQQAAARNGDAlRSAKEEITElrrtiqsleiELQS 235

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 530425792   744 LQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLRE-KQEMIQLLR 791
Cdd:pfam00038  236 LKKQKASLERQLAETEERYELQLADYQELISELEAELQEtRQEMARQLR 284

mukB

PRK04863

chromosome partition protein MukB;

620-1098

4.49e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 4.49e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  620 LESKRKLIEEMEEKQKSDKA-ELERmqqEVETQRKETEIVQlQIRKQEESLKRRSfHIENKLKDLLAEKEKfeeerlreq 698
Cdd:PRK04863  479 YQLVRKIAGEVSRSEAWDVArELLR---RLREQRHLAEQLQ-QLRMRLSELEQRL-RQQQRAERLLAEFCK--------- 544

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  699 qeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLE-LEKKRLEEQEKeqvmlVAHLE 777
Cdd:PRK04863  545 ---RLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAaRAPAWLAAQDA-----LARLR 616

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  778 EQLREKQE--------MIQLLRR-----GEVQWVEEEKRDLEGIRESLlrvkeARAGGDEDGE----------------- 827
Cdd:PRK04863  617 EQSGEEFEdsqdvteyMQQLLERereltVERDELAARKQALDEEIERL-----SQPGGSEDPRlnalaerfggvllseiy 691

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  828 ---ELEKA--------QLRF------FEFKRRQLVKLVNLEKDLvqqkdilkkevqeeqeilecLKCEHDKESrllekHD 890
Cdd:PRK04863  692 ddvSLEDApyfsalygPARHaivvpdLSDAAEQLAGLEDCPEDL--------------------YLIEGDPDS-----FD 746

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  891 ESVTDVTEvpqdFEKIKPVeyrlQYKERQLQYLLQNHLPtLLEEKQRafeildrgplslDNTLYQVEKEMEEKEEQLAQY 970
Cdd:PRK04863  747 DSVFSVEE----LEKAVVV----KIADRQWRYSRFPEVP-LFGRAAR------------EKRIEQLRAEREELAERYATL 805

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  971 QANANQLQKLQATFE----------FTAN------IARQEEKVRKKEKEILESREKQQREALERALARLerrhSALQRH- 1033
Cdd:PRK04863  806 SFDVQKLQRLHQAFSrfigshlavaFEADpeaelrQLNRRRVELERALADHESQEQQQRSQLEQAKEGL----SALNRLl 881

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530425792 1034 --------STLGMEIEEQRQKLASLNSGSR---EQSGLQASLEAEQEALEKDQERLEyeiqQLKQKIYEVDGVQKD 1098
Cdd:PRK04863  882 prlnlladETLADRVEEIREQLDEAEEAKRfvqQHGNALAQLEPIVSVLQSDPEQFE----QLKQDYQQAQQTQRD 953

PRK02224

DNA double-strand break repair Rad50 ATPase;

606-898

4.60e-03

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 4.60e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  606 RLEFERQQ----REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsF------- 674
Cdd:PRK02224  329 RLEECRVAaqahNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER-Fgdapvdl 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  675 -HIENKLKDLLAEKEKFEEERLREQQEI-ELQKKRQEEETFL-------------------RVQEELQRLKELnnneKAE 733
Cdd:PRK02224  408 gNAEDFLEELREERDELREREAELEATLrTARERVEEAEALLeagkcpecgqpvegsphveTIEEDRERVEEL----EAE 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  734 KFQIFQELDQLQK--EKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLR-------------------- 791
Cdd:PRK02224  484 LEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELReraaeleaeaeekreaaaea 563

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  792 -------RGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKaqLRffeFKRRQLVKLVNLEKDLVQQKDILKKE 864
Cdd:PRK02224  564 eeeaeeaREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIER--LR---EKREALAELNDERRERLAEKRERKRE 638

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 530425792  865 VQEE--QEILECLKCEHDKESRLLEKHDESVTDVTE 898
Cdd:PRK02224  639 LEAEfdEARIEEAREDKERAEEYLEQVEEKLDELRE 674

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

605-1078

4.82e-03

Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 4.82e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   605 LRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERM---------------------------QQEV--------- 648
Cdd:pfam10174  209 IHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNirdledevqmlktngllhtedreeeikQMEVykshskfmk 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   649 --------ETQRKETEIVQLQIR-----KQEESLKRrsfHIEnKLKDLLAEKEKfeEERLREQQEIELQKKRQEEETFL- 714
Cdd:pfam10174  289 nkidqlkqELSKKESELLALQTKletltNQNSDCKQ---HIE-VLKESLTAKEQ--RAAILQTEVDALRLRLEEKESFLn 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   715 RVQEELQRLKElnnnekaEKFQIFQELDQLQKEKDEQYAKLELEKKRLEeqekeqvmlvaHLEEQLREKQEMIQLLRRGe 794
Cdd:pfam10174  363 KKTKQLQDLTE-------EKSTLAGEIRDLKDMLDVKERKINVLQKKIE-----------NLQEQLRDKDKQLAGLKER- 423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   795 vqwVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQE-EQEILE 873
Cdd:pfam10174  424 ---VKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEkESSLID 500

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   874 CLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQyKERQLQY-------------LLQNHLPTLLEEKQRAFE 940
Cdd:pfam10174  501 LKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK-KAHNAEEavrtnpeindrirLLEQEVARYKEESGKAQA 579

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   941 ILDRgplsLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeFTANI-ARQEEKVRKKEKEILESREKQQREALERA 1019
Cdd:pfam10174  580 EVER----LLGILREVENEKNDKDKKIAELESLTLRQMKEQNK--KVANIkHGQQEMKKKGAQLLEEARRREDNLADNSQ 653

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530425792  1020 LARLERRHSALQRHStlgMEIEEQRQKLASLNSGSREQSGLQASLEAE-----QEALEKDQERL 1078
Cdd:pfam10174  654 QLQLEELMGALEKTR---QELDATKARLSSTQQSLAEKDGHLTNLRAErrkqlEEILEMKQEAL 714

CwlO1

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

1010-1119

5.01e-03

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.01e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792 1010 KQQREALERALARLERRHSALQRhstlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKI 1089
Cdd:COG3883   139 KADKAELEAKKAELEAKLAELEA------LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212

                          90       100       110
                  ....*....|....*....|....*....|
gi 530425792 1090 YEVDGVQKDHHGTLEGKVASSSLPVSAEKS 1119
Cdd:COG3883   213 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242

ClpA

COG0542

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...

739-869

5.21e-03

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

Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 5.21e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792  739 QELDQLqkekDEQYAKLELEKKRLE-EQEKEQVMLVAHLEEQLREKQEMIQLLRRgevQWvEEEKRDLEGIREsllrVKE 817
Cdd:COG0542   411 EELDEL----ERRLEQLEIEKEALKkEQDEASFERLAELRDELAELEEELEALKA---RW-EAEKELIEEIQE----LKE 478

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530425792  818 ARAGGDEDGEELEKaqlrffefkrrqlvKLVNLEKDLVQQKDILKKEVQEEQ 869
Cdd:COG0542   479 ELEQRYGKIPELEK--------------ELAELEEELAELAPLLREEVTEED 516

Golgin_A5

pfam09787

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...

620-791

5.59e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.

Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 5.59e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   620 LESKRKLIEEMEEKQKSD--------KAELERMQQEVETQRKETEivqlQIRKQEESLKRRSFHIENklkdllaekekfe 691
Cdd:pfam09787   20 LQSKEKLIASLKEGSGVEgldsstalTLELEELRQERDLLREEIQ----KLRGQIQQLRTELQELEA------------- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425792   692 eerlreqqeielqkkrQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKdeQYAKLELEKKRleeqekeqvm 771
Cdd:pfam09787   83 ----------------QQQEEAESSREQLQELEEQLATERSARREAEAELERLQEEL--RYLEEELRRSK---------- 134

                          170       180
                   ....*....|....*....|
gi 530425792   772 lvAHLEEQLREKQEMIQLLR 791
Cdd:pfam09787  135 --ATLQSRIKDREAEIEKLR 152

CwlO1